Details of the Researcher

PHOTO

Kazutaka Murayama
Section
Graduate School of Biomedical Engineering
Job title
Associate Professor
Degree

  • 博士（工学）（豊橋技術科学大学）

  • 修士（工学）（豊橋技術科学大学）

Research History 4

  • 2005/01 - 2008/03
    東北大学先進医工学研究機構

  • 2001/09 - 2004/12
    理化学研究所ゲノム科学総合研究センター

  • 1998/04 - 2001/08
    Free University of Berlin

  • 2008/04 -
    Graduate School of Biomedical Engineering, Tohoku University　Associate Professor

Education 1

  • Toyohashi University of Technology　Graduate School, Division of Engineering　機能材料工学

    - 1998/03/31

Professional Memberships 3

  • 日本生物物理学会

  • 蛋白質科学会

  • 日本結晶学会

Research Interests 3

  • 生物物理化学

  • 生体高分子

  • 構造解析

Research Areas 1

  • Life sciences / Structural biochemistry /

Papers 148

  1. Inhibition of methionine aminopeptidase in C2C12 myoblasts disrupts cell integrity via increasing endoplasmic reticulum stress. International-journal

    Shion Osana, Cheng-Ta Tsai, Naoki Suzuki, Kazutaka Murayama, Masaki Kaneko, Katsuhiko Hata, Hiroaki Takada, Yutaka Kano, Ryoichi Nagatomi

    Biochimica et biophysica acta. Molecular cell research　119901-119901　2025/01/13

    DOI： 10.1016/j.bbamcr.2025.119901 　

    More details Close

    Proteasome-dependent protein degradation and the digestion of peptides by aminopeptidases are essential for myogenesis. Methionine aminopeptidases (MetAPs) are uniquely involved in, both, the proteasomal degradation of proteins and in the regulation of translation (via involvement in post-translational modification). Suppressing MetAP1 and MetAP2 expression inhibits the myogenic differentiation of C2C12 myoblasts. However, the molecular mechanism by which inhibiting MetAPs impairs cellular function remains to be elucidated. Here, we provide evidence for our hypothesis that MetAPs regulate proteostasis and that their inhibition increases ER stress by disrupting the post-translational modification, and thereby compromises cell integrity. Thus, using C2C12 myoblasts, we investigate the effect of inhibiting MetAPs on cell proliferation and the molecular mechanisms underpinning its effects. We found that exposure to bengamide B (a MetAP inhibitor) caused C2C12 myoblasts to lose their proliferative abilities via cell cycle arrest. The underlying mechanism involved the accumulation of abnormal proteins (due to the decrease in the N-terminal methionine removal function) which led to increased endoplasmic reticulum stress, decreased protein synthesis, and a protective activation of the autophagy pathway. To identify the MetAP involved in these effects, we use siRNAs to specifically knockdown MetAP1 and MetAP2 expressions. We found that only MetAP2 knockdown mimicked the effects seen with bengamide B treatment. Thus, we suggest that MetAP2, rather than MetAP1, is involved in maintaining the integrity of C2C12 myoblasts. Our results are useful in understanding muscle regeneration, obesity, and overeating disorders. It will help guide new treatment strategies for these disorders.

  2. An orally available P1'-5-fluorinated Mpro inhibitor blocks SARS-CoV-2 replication without booster and exhibits high genetic barrier. International-journal

    Nobuyo Higashi-Kuwata, Haydar Bulut, Hironori Hayashi, Kohei Tsuji, Hiromi Ogata-Aoki, Maki Kiso, Nobutoki Takamune, Naoki Kishimoto, Shin-Ichiro Hattori, Takahiro Ishii, Takuya Kobayakawa, Kenta Nakano, Yukiko Shimizu, Debananda Das, Junji Saruwatari, Kazuya Hasegawa, Kazutaka Murayama, Yoshikazu Sukenaga, Yuki Takamatsu, Kazuhisa Yoshimura, Manabu Aoki, Yuri Furusawa, Tadashi Okamura, Seiya Yamayoshi, Yoshihiro Kawaoka, Shogo Misumi, Hirokazu Tamamura, Hiroaki Mitsuya

    PNAS nexus　4　(1)　pgae578　2025/01

    DOI： 10.1093/pnasnexus/pgae578 　

    More details Close

    We identified a 5-fluoro-benzothiazole-containing small molecule, TKB272, through fluorine-scanning of the benzothiazole moiety, which more potently inhibits the enzymatic activity of SARS-CoV-2's main protease (Mpro) and more effectively blocks the infectivity and replication of all SARS-CoV-2 strains examined including Omicron variants such as SARS-CoV-2XBB1.5 and SARS-CoV-2EG.5.1 than two Mpro inhibitors: nirmatrelvir and ensitrelvir. Notably, the administration of ritonavir-boosted nirmatrelvir and ensitrelvir causes drug-drug interactions warranting cautions due to their CYP3A4 inhibition, thereby limiting their clinical utility. When orally administered, TKB272 blocked SARS-CoV-2XBB1.5 replication without ritonavir in B6.Cg-Tg(K18-hACE2)2-Prlmn/J-transgenic mice, comparably as did ritonavir-boosted nirmatrelvir. When the ancestral SARS-CoV-2 was propagated with nirmatrelvir in vitro, a highly nirmatrelvir-resistant E166V-carrying variant (SARS-CoV-2E166V-P14) readily emerged by passage 14; however, when propagated with TKB272, no variants emerged by passage 25. SARS-CoV-2E166V showed some cross-resistance to TKB272 but was substantially sensitive to the compound. X-ray structural analyses and mass-spectrometric data showed that the E166V substitution disrupts the critical dimerization-initiating Ser1'-E166 interactions, thereby limiting nirmatrelvir's Mpro inhibition but that TKB272 nevertheless forms a tight binding with Mpro's catalytic active sight even in the presence of the E166V substitution. TKB272 shows no apparent genotoxicity as tested in the micro-Ames test. Highly potent TKB272 may serve as a COVID-19 therapeutic, overcome resistance to existing Mpro inhibitors.

  3. Heme regulates protein interactions and phosphorylation of BACH2 intrinsically disordered region in humoral response

    Miki Watanabe-Matsui, Shun Kadoya, Kei Segawa, Hiroki Shima, Tadashi Nakagawa, Yuko Nagasawa, Shuichiro Hayashi, Mitsuyo Matsumoto, Mariko Ikeda, Akihiko Muto, Kyoko Ochiai, Long C. Nguyen, Katsumi Doh-Ura, Mikako Shirouzu, Keiko Nakayama, Kazutaka Murayama, Kazuhiko Igarashi

    iScience　28　(1)　111529-111529　2025/01

    Publisher: Elsevier BV

    DOI： 10.1016/j.isci.2024.111529 　

    ISSN： 2589-0042

  4. Structural basis for the effects of Ser387 phosphorylation of MgcRacGAP on its GTPase-activating activities for CDC42 and RHOA. International-journal

    Kazutaka Murayama, Miyuki Kato-Murayama, Toshiaki Hosaka, Toshio Kitamura, Shigeyuki Yokoyama, Mikako Shirouzu

    Journal of structural biology　108151-108151　2024/11/08

    DOI： 10.1016/j.jsb.2024.108151 　

    More details Close

    MgcRacGAP is a GTPase-activating protein (GAP) for the Rho family GTPases. During cytokinesis, MgcRacGAP localizes to the midbody, where it activates the GTPase activity of Rho family GTPases to facilitate cytokinesis. In the midbody, Aurora B phosphorylates Ser387 within the GAP domain of human MgcRacGAP, a modification that is suggested to influence GTPase preference. However, there are conflicting reports, with some studies indicating that Ser387 phosphorylation does not alter the GTPase preference of MgcRacGAP. This controversy highlights the need for a deeper understanding of the molecular interactions involved, which can be clarified through structural analyses. In the present study, we determined the crystal structures of the wild-type MgcRacGAP GAP domain complexed with CDC42•GDP•AlF4- and the S378D phosphomimetic mutant GAP domain fused with RHOA•GDP•AlF4-. Additionally, crystal structures of the GAP domains were determined for the S387D and S387A mutants. Our analysis revealed that neither GTPase binding nor S387D mutation affected the overall structure of the GAP domain. However, comparison of the CDC42•MgcRacGAP (wild-type) complex with the RHOA-MgcRacGAP(S378D) fusion protein structure indicated that the S387D mutation caused positional shifts in both CDC42 and RHOA relative to MgcRacGAP. These shifts reduced interactions with CDC42 more severely than those with RHOA. In fact, the S387D mutation decreased the GTPase-activating activity of MgcRacGAP toward CDC42, while its impact on RHOA was only moderate. This difference in the rate of activity reduction may play an important role in GTPase preference.

  5. Absolute quantification of BACH1 and BACH2 transcription factors in B and plasma cells reveals their dynamic changes and unique roles

    Takeshi Kurasawa, Akihiko Muto, Mitsuyo Matsumoto, Kyoko Ochiai, Kazutaka Murayama, Kazuhiko Igarashi

    The Journal of Biochemistry　176　(6)　449-459　2024/09/25

    Publisher: Oxford University Press (OUP)

    DOI： 10.1093/jb/mvae065 　

    ISSN： 0021-924X

    eISSN： 1756-2651

    More details Close

    Abstract Changes in the absolute protein amounts of transcription factors are important for regulating gene expression during cell differentiation and in responses to changes in the cellular and extracellular environment. However, few studies have focused on the absolute quantification of mammalian transcription factors. In this study, we established an absolute quantification method for the transcription factors BACH1 and BACH2, which are expressed in B cells and regulated by direct heme binding. The method used purified recombinant proteins as controls in western blotting and was applied to mouse naïve B cells in the spleen, as well as activated B cells and plasma cells. BACH1 was present in naïve B cells at approximately half the levels of BACH2. In activated B cells, BACH1 decreased compared to naïve B cells, whilst BACH2 increased. In plasma cells, BACH1 increased back to the same extent as in naïve B cells, whilst BACH2 was not detected. Their target genes, Prdm1 and Hmox1, were highly induced in plasma cells. BACH1 was found to undergo degradation with lower concentrations of heme than BACH2. Therefore, BACH1 and BACH2 are similarly abundant in B cells but differ in heme sensitivity, potentially regulating gene expression differently depending on their heme responsiveness.

  6. SHIN-2 exerts potent activity against VanA-type vancomycin-resistant Enterococcus faecium in vitro by stabilizing the active site loop of serine hydroxymethyltransferase. International-journal

    Hironori Hayashi, Erika Saijo, Kazushige Hirata, Shumei Murakami, Haruka Okuda, Eiichi N Kodama, Kazuya Hasegawa, Kazutaka Murayama

    Archives of biochemistry and biophysics　110160-110160　2024/09/21

    DOI： 10.1016/j.abb.2024.110160 　

    More details Close

    Novel classes of antibiotics are needed to improve the resilience of the healthcare system to antimicrobial resistance (AMR), including vancomycin resistance. vanA gene cluster is a cause of vancomycin resistance. This gene cluster is transferred and spreads vancomycin resistance from Enterococcus spp. to Staphylococcus aureus. Therefore, novel antibacterial agents are required to combat AMR, including vanA-type vancomycin resistance. Serine hydroxymethyltransferase (SHMT) is a key target of antibacterial agents. However, the specific binding mechanisms of SHMT inhibitors remain unclear. Detailed structural information will contribute to understanding these mechanisms. In this study, we found that (+)-SHIN-2, the first in vivo active inhibitor of human SHMT, is strongly bound to the Enterococcus faecium SHMT (efmSHMT). Comparison of the crystal structures of apo- and (+)-SHIN-2-boud efmSHMT revealed that (+)-SHIN-2 stabilized the active site loop of efmSHMT via hydrogen bonds, which are critical for efmSHMT inhibition. Additionally, (+)-SHIN-2 formed hydrogen bonds with serine, forming the Schiff's base with pyridoxal 5'-phosphate, which is a co-factor of SHMT. Furthermore, (+)-SHIN-2 exerted biostatic effects on vancomycin-susceptible and vanA-type vancomycin-resistant E. faecium in vitro, indicating that SHMT inhibitors do not induce cross-resistance to vanA-type vancomycin. Overall, these findings can aid in the design of novel SHMT inhibitors to combat AMR, including vancomycin resistance.

  7. Structural and virologic mechanism of the emergence of resistance to M pro inhibitors in SARS-CoV-2

    Shin-ichiro Hattori, Haydar Bulut, Hironori Hayashi, Naoki Kishimoto, Nobutoki Takamune, Kazuya Hasegawa, Yuri Furusawa, Seiya Yamayoshi, Kazutaka Murayama, Hirokazu Tamamura, Mi Li, Alexander Wlodawer, Yoshihiro Kawaoka, Shogo Misumi, Hiroaki Mitsuya

    Proceedings of the National Academy of Sciences　121　(37)　2024/09/05

    Publisher: Proceedings of the National Academy of Sciences

    DOI： 10.1073/pnas.2404175121 　

    ISSN： 0027-8424

    eISSN： 1091-6490

    More details Close

    We generated SARS-CoV-2 variants resistant to three SARS-CoV-2 main protease (M pro ) inhibitors (nirmatrelvir, TKB245, and 5h), by propagating the ancestral SARS-CoV-2 WK521 WT in VeroE6 TMPRSS2 cells with increasing concentrations of each inhibitor and examined their structural and virologic profiles. A predominant E166V-carrying variant (SARS-CoV-2 WK521 E166V ), which emerged when passaged with nirmatrelvir and TKB245, proved to be resistant to the two inhibitors. A recombinant SARS-CoV-2 E166V was resistant to nirmatrelvir and TKB245, but sensitive to 5h. X-ray structural study showed that the dimerization of M pro was severely hindered by E166V substitution due to the disruption of the presumed dimerization-initiating Ser1’-Glu166 interactions. TKB245 stayed bound to M pro E166V , whereas nirmatrelvir failed. Native mass spectrometry confirmed that nirmatrelvir and TKB245 promoted the dimerization of M pro , and compromised the enzymatic activity; the Ki values of recombinant M pro E166V for nirmatrelvir and TKB245 were 117±3 and 17.1±1.9 µM, respectively, indicating that TKB245 has a greater (by a factor of 6.8) binding affinity to M pro E166V than nirmatrelvir. SARS-CoV-2 WK521 WT selected with 5h acquired A191T substitution in M pro (SARS-CoV-2 WK521 A191T ) and better replicated in the presence of 5h, than SARS-CoV-2 WK521 WT . However, no significant enzymatic or structural changes in M pro A191T were observed. The replicability of SARS-CoV-2 WK521 E166V proved to be compromised compared to SARS-CoV-2 WK521 WT but predominated over SARS-CoV-2 WK521 WT in the presence of nirmatrelvir. The replicability of SARS-CoV-2 WK521 A191T surpassed that of SARS-CoV-2 WK521 WT in the absence of 5h, confirming that A191T confers enhanced viral fitness. The present data should shed light on the understanding of the mechanism of SARS-CoV-2’s drug resistance acquisition and the development of resistance-repellant COVID-19 therapeutics.

  8. Structure of a phosphodiesterase from Streptomyces sanglieri with a novel C-terminal domain. International-journal

    Kazutaka Murayama, Toshiaki Hosaka, Mikako Shirouzu, Daisuke Sugimori

    Biochemical and biophysical research communications　708　149784-149784　2024/05/14

    DOI： 10.1016/j.bbrc.2024.149784 　

    More details Close

    A glycerophosphoethanolamine ethanolaminephosphodiesterase (GPE-EP) from Streptomyces sanglieri hydrolyzes glycerophosphoethanolamine to phosphoethanolamine and glycerol. The structure of GPE-EP was determined by the molecular replacement method using a search model generated with AlphaFold2. This structure includes the entire length of the mature protein and it is composed of an N-terminal domain and a novel C-terminal domain connected to a flexible linker. The N-terminal domain is the catalytic domain containing calcium ions at the catalytic site. Coordination bonds were observed between five amino acid residues and glycerol. Although the function of the C-terminal domain is currently unknown, inter-domain interactions between the N- and C-terminal domains may contribute to its relatively high thermostability.

  9. Molecular basis of ligand recognition specificity of flavone glucosyltransferases in Nemophila menziesii. International-journal

    Kazutaka Murayama, Miyuki Kato-Murayama, Toshiaki Hosaka, Naoko Okitsu, Yoshikazu Tanaka, Mikako Shirouzu

    Archives of biochemistry and biophysics　753　109926-109926　2024/03

    DOI： 10.1016/j.abb.2024.109926 　

    More details Close

    Of the more than 100 families of glycosyltransferases, family 1 glycosyltransferases catalyze glycosylation using uridine diphosphate (UDP)-sugar as a sugar donor and are thus referred to as UDP-sugar:glycosyl transferases. The blue color of the Nemophila menziesii flower is derived from metalloanthocyanin, which consists of anthocyanin, flavone, and metal ions. Flavone 7-O-β-glucoside-4'-O-β-glucoside in the plant is sequentially biosynthesized from flavons by UDP-glucose:flavone 4'-O-glucosyltransferase (NmF4'GT) and UDP-glucose:flavone 4'-O-glucoside 7-O-glucosyltransferase (NmF4'G7GT). To identify the molecular mechanisms of glucosylation of flavone, the crystal structures of NmF4'G7GT in its apo form and in complex with UDP-glucose or luteolin were determined, and molecular structure prediction using AlphaFold2 was conducted for NmF4'GT. The crystal structures revealed that the size of the ligand-binding pocket and interaction environment for the glucose moiety at the pocket entrance plays a critical role in the substrate preference in NmF4'G7GT. The substrate specificity of NmF4'GT was examined by comparing its model structure with that of NmF4'G7GT. The structure of NmF4'GT may have a smaller acceptor pocket, leading to a substrate preference for non-glucosylated flavones (or flavone aglycones).

  10. Helical peptides with disordered regions for measles viruses provide new generalized insights into fusion inhibitors. International-journal

    Kazushige Hirata, Aoi Takahara, Satoshi Suzuki, Shumei Murakami, Kumi Kawaji, Akie Nishiyama, Mina Sasano, Mariko Shoji-Ueno, Emiko Usui, Kazutaka Murayama, Hironori Hayashi, Shinya Oishi, Eiichi N Kodama

    iScience　27　(2)　108961-108961　2024/02/16

    DOI： 10.1016/j.isci.2024.108961 　

    More details Close

    Despite effective vaccines, measles virus (MeV) outbreaks occur sporadically. Therefore, developing anti-MeV agents remains important for suppressing MeV infections. We previously designed peptide-based MeV fusion inhibitors, M1 and M2, that target MeV class I fusion protein (F protein). Here, we developed a novel fusion inhibitor, MEK35, that exerts potent activity against M1/M2-resistant MeV variants. Comparing MEK35 to M1 derivatives revealed that combining disordered and helical elements was essential for overcoming M1/M2 resistance. Moreover, we propose a three-step antiviral process for peptide-based fusion inhibitors: (i) disordered peptides interact with F protein; (ii) the peptides adopt a partial helical conformation and bind to F protein through hydrophobic interactions; and (iii) subsequent interactions involving the disordered region of the peptides afford a peptide-F protein with a high-affinity peptide-F protein interaction. An M1-resistant substitution blocks the second step. These results should aid the development of novel viral fusion inhibitors targeting class I F protein.

  11. GRL-142 binds to and impairs HIV-1 integrase nuclear localization signal and potently suppresses highly INSTI-resistant HIV-1 variants. International-journal

    Manabu Aoki, Hiromi Aoki-Ogata, Haydar Bulut, Hironori Hayashi, Nobutoki Takamune, Naoki Kishimoto, Hiroki Tanaka, Nobuyo Higashi-Kuwata, Shin-Ichiro Hattori, Debananda Das, Kalapala Venkateswara Rao, Kazuya Iwama, David A Davis, Kazuya Hasegawa, Kazutaka Murayama, Robert Yarchoan, Arun K Ghosh, Alice K Pau, Shinichi Machida, Shogo Misumi, Hiroaki Mitsuya

    Science advances　9　(28)　eadg2955　2023/07/14

    DOI： 10.1126/sciadv.adg2955 　

    More details Close

    Nuclear localization signal (NLS) of HIV-1 integrase (IN) is implicated in nuclear import of HIV-1 preintegration complex (PIC). Here, we established a multiclass drug-resistant HIV-1 variant (HIVKGD) by consecutively exposing an HIV-1 variant to various antiretroviral agents including IN strand transfer inhibitors (INSTIs). HIVKGD was extremely susceptible to a previously reported HIV-1 protease inhibitor, GRL-142, with IC50 of 130 femtomolar. When cells were exposed to HIVKGD IN-containing recombinant HIV in the presence of GRL-142, significant decrease of unintegrated 2-LTR circular cDNA was observed, suggesting that nuclear import of PIC was severely compromised by GRL-142. X-ray crystallographic analyses revealed that GRL-142 interacts with NLS's putative sequence (DQAEHLK) and sterically blocks the nuclear transport of GRL-142-bound HIVKGD's PIC. Highly INSTI-resistant HIV-1 variants isolated from heavily INSTI-experienced patients proved to be susceptible to GRL-142, suggesting that NLS-targeting agents would serve as salvage therapy agents for highly INSTI-resistant variant-harboring individuals. The data should offer a new modality to block HIV-1 infectivity and replication and shed light on developing NLS inhibitors for AIDS therapy.

  12. The aminopeptidase LAP3 suppression accelerates myogenic differentiation via the AKT-TFE3 pathway in C2C12 myoblasts. International-journal

    Shion Osana, Yasuo Kitajima, Suzuki Naoki, Kazutaka Murayama, Hiroaki Takada, Ayaka Tabuchi, Yutaka Kano, Ryoichi Nagatomi

    Journal of cellular physiology　2023/07/12

    DOI： 10.1002/jcp.31070 　

    More details Close

    Skeletal muscle maintenance depends largely on muscle stem cells (satellite cells) that supply myoblasts required for muscle regeneration and growth. The ubiquitin-proteasome system is the major intracellular protein degradation pathway. We previously reported that proteasome dysfunction in skeletal muscle significantly impairs muscle growth and development. Furthermore, the inhibition of aminopeptidase, a proteolytic enzyme that removes amino acids from the termini of peptides derived from proteasomal proteolysis, impairs the proliferation and differentiation ability of C2C12 myoblasts. However, no evidence has been reported on the role of aminopeptidases with different substrate specificities on myogenesis. In this study, therefore, we investigated whether the knockdown of aminopeptidases in differentiating C2C12 myoblasts affects myogenesis. The knockdown of the X-prolyl aminopeptidase 1, aspartyl aminopeptidase, leucyl-cystinyl aminopeptidase, methionyl aminopeptidase 1, methionyl aminopeptidase 2, puromycine-sensitive aminopeptidase, and arginyl aminopeptidase like 1 gene in C2C12 myoblasts resulted in defective myogenic differentiation. Surprisingly, the knockdown of leucine aminopeptidase 3 (LAP3) in C2C12 myoblasts promoted myogenic differentiation. We also found that suppression of LAP3 expression in C2C12 myoblasts resulted in the inhibition of proteasomal proteolysis, decreased intracellular branched-chain amino acid levels, and enhanced mTORC2-mediated AKT phosphorylation (S473). Furthermore, phosphorylated AKT induced the translocation of TFE3 from the nucleus to the cytoplasm, promoting myogenic differentiation through increased expression of myogenin. Overall, our study highlights the association of aminopeptidases with myogenic differentiation.

  13. タンパク質間相互作用を標的とするRSウイルスの新薬更補創出

    鈴木 聡志, 天野 陽斗, 薄井 友輔, 河治 久実, 笹野 美奈, 西山 瑛絵, 平松 佳樹, 橋本 浩一, 村山 和隆, 児玉 栄一, 大石 真也, 林 宏典

    日本小児科学会雑誌　127　(2)　231-231　2023/02

    Publisher: (公社)日本小児科学会

    ISSN： 0001-6543

  14. 新型コロナウイルスへの創薬に応用できるタンパク質間相互作用

    鈴木 聡志, 黒田 実央, 河治 久実, 村山 和隆, 林 宏典, 大石 真也, 児玉 栄一

    日本小児科学会雑誌　127　(2)　235-235　2023/02

    Publisher: (公社)日本小児科学会

    ISSN： 0001-6543

  15. Helix-based screening with structure prediction using artificial intelligence has potential for the rapid development of peptide inhibitors targeting class I viral fusion

    Satoshi Suzuki, Mio Kuroda, Keisuke Aoki, Kumi Kawaji, Yoshiki Hiramatsu, Mina Sasano, Akie Nishiyama, Kazutaka Murayama, Eiichi N. Kodama, Shinya Oishi, Hironori Hayashi

    RSC Chemical Biology　2023

    Publisher: Royal Society of Chemistry (RSC)

    DOI： 10.1039/d3cb00166k 　

    eISSN： 2633-0679

    More details Close

    Peptide inhibitors against the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are designed using a screening system for peptide-based inhibitors containing an α-helix region (SPICA) and structures predicted by AlphaFold2.

  16. Structural basis for the substrate specificity switching of lysoplasmalogen-specific phospholipase D from Thermocrispum sp. RD004668

    Hiroaki Hamana, Yoshiaki Yasutake, Miyuki Kato-Murayama, Toshiaki Hosaka, Mikako Shirouzu, Shin-ichi Sakasegawa, Daisuke Sugimori, Kazutaka Murayama

    Bioscience, Biotechnology, and Biochemistry　87　(1)　74-81　2022/12/21

    Publisher: Oxford University Press (OUP)

    DOI： 10.1093/bbb/zbac169 　

    eISSN： 1347-6947

    More details Close

    ABSTRACT Lysoplasmalogen-specific phospholipase D (LyPls-PLD) hydrolyzes choline lysoplasmalogen to choline and 1-(1-alkenyl)-sn-glycero-3-phosphate. Mutation of F211 to leucine altered its substrate specificity from lysoplasmalogen to 1-O-hexadecyl-2-hydroxy-sn-glycero-3-phosphocholine (lysoPAF). Enzymes specific to lysoPAF have good potential for clinical application, and understanding the mechanism of their activity is important. The crystal structure of LyPls-PLD exhibited a TIM barrel fold assigned to glycerophosphocholine phosphodiesterase, a member of glycerophosphodiester phosphodiesterase. LyPls-PLD possesses a hydrophobic cleft for the binding of the aliphatic chain of the substrate. In the structure of the F211L mutant, Met232 and Tyr258 form a “small lid” structure that stabilizes the binding of the aliphatic chain of the substrate. In contrast, F211 may inhibit small lid formation in the wild-type structure. LysoPAF possesses a flexible aliphatic chain; therefore, a small lid is effective for stabilizing the substrate during catalytic reactions.

  17. Little involvement of recycled-amino acids from proteasomal proteolysis in de novo protein synthesis

    Shion Osana, Yasuo Kitajima, Suzuki Naoki, Hiroaki Takada, Kazutaka Murayama, Yutaka Kano, Ryoichi Nagatomi

    Biochemical and Biophysical Research Communications　2022/10

    Publisher: Elsevier BV

    DOI： 10.1016/j.bbrc.2022.09.113 　

    ISSN： 0006-291X

  18. Autocitrullination and Changes in the Activity of Peptidylarginine Deiminase 3 Induced by High Ca2+ Concentrations

    Mizuki Sawata, Hiroki Shima, Kazutaka Murayama, Toshitaka Matsui, Kazuhiko Igarashi, Kazumasa Funabashi, Kenji Ite, Kenji Kizawa, Hidenari Takahara, Masaki Unno

    ACS Omega　2022/08/16

    DOI： 10.1021/acsomega.2c02972 　

  19. Serine hydroxymethyltransferase as a potential target of antibacterial agents acting synergistically with one-carbon metabolism-related inhibitors. International-journal

    Yuko Makino, Chihiro Oe, Kazuya Iwama, Satoshi Suzuki, Akie Nishiyama, Kazuya Hasegawa, Haruka Okuda, Kazushige Hirata, Mariko Ueno, Kumi Kawaji, Mina Sasano, Emiko Usui, Toshiaki Hosaka, Yukako Yabuki, Mikako Shirouzu, Makoto Katsumi, Kazutaka Murayama, Hironori Hayashi, Eiichi N Kodama

    Communications biology　5　(1)　619-619　2022/06/23

    DOI： 10.1038/s42003-022-03555-x 　

    More details Close

    Serine hydroxymethyltransferase (SHMT) produces 5,10-methylenetetrahydrofolate (CH2-THF) from tetrahydrofolate with serine to glycine conversion. SHMT is a potential drug target in parasites, viruses and cancer. (+)-SHIN-1 was developed as a human SHMT inhibitor for cancer therapy. However, the potential of SHMT as an antibacterial target is unknown. Here, we show that (+)-SHIN-1 bacteriostatically inhibits the growth of Enterococcus faecium at a 50% effective concentration of 10-11 M and synergistically enhances the antibacterial activities of several nucleoside analogues. Our results, including crystal structure analysis, indicate that (+)-SHIN-1 binds tightly to E. faecium SHMT (efmSHMT). Two variable loops in SHMT are crucial for inhibitor binding, and serine binding to efmSHMT enhances the affinity of (+)-SHIN-1 by stabilising the loop structure of efmSHMT. The findings highlight the potency of SHMT as an antibacterial target and the possibility of developing SHMT inhibitors for treating bacterial, viral and parasitic infections and cancer.

  20. The Cys‐Pro motifs in the intrinsically disordered regions of the transcription factor BACH1 mediate distinct and overlapping functions upon heme binding

    Kei Segawa, Kazuhiko Igarashi, Kazutaka Murayama

    FEBS Letters　2022/06

    Publisher: Wiley

    DOI： 10.1002/1873-3468.14338 　

  21. Lewis fucose is a key moiety for the recognition of histo‐blood group antigens by GI.9 norovirus, as revealed by structural analysis

    Tomomi Kimura‐Someya, Miyuki Kato‐Murayama, Kazushige Katsura, Naoki Sakai, Kazutaka Murayama, Kazuharu Hanada, Mikako Shirouzu, Yuichi Someya

    FEBS Open Bio　12　(3)　560-570　2022/03

    Publisher: Wiley

    DOI： 10.1002/2211-5463.13370 　

    ISSN： 2211-5463

    eISSN： 2211-5463

  22. Conformational alterations in unidirectional ion transport of a light-driven chloride pump revealed using X-ray free electron lasers. International-journal

    Toshiaki Hosaka, Takashi Nomura, Minoru Kubo, Takanori Nakane, Luo Fangjia, Shun-Ichi Sekine, Takuhiro Ito, Kazutaka Murayama, Kentaro Ihara, Haruhiko Ehara, Kazuhiro Kashiwagi, Kazushige Katsura, Ryogo Akasaka, Tamao Hisano, Tomoyuki Tanaka, Rie Tanaka, Toshi Arima, Ayumi Yamashita, Michihiro Sugahara, Hisashi Naitow, Yoshinori Matsuura, Susumu Yoshizawa, Kensuke Tono, Shigeki Owada, Osamu Nureki, Tomomi Kimura-Someya, So Iwata, Eriko Nango, Mikako Shirouzu

    Proceedings of the National Academy of Sciences of the United States of America　119　(9)　2022/03/01

    DOI： 10.1073/pnas.2117433119 　

    More details Close

    Light-driven chloride-pumping rhodopsins actively transport anions, including various halide ions, across cell membranes. Recent studies using time-resolved serial femtosecond crystallography (TR-SFX) have uncovered the structural changes and ion transfer mechanisms in light-driven cation-pumping rhodopsins. However, the mechanism by which the conformational changes pump an anion to achieve unidirectional ion transport, from the extracellular side to the cytoplasmic side, in anion-pumping rhodopsins remains enigmatic. We have collected TR-SFX data of Nonlabens marinus rhodopsin-3 (NM-R3), derived from a marine flavobacterium, at 10-µs and 1-ms time points after photoexcitation. Our structural analysis reveals the conformational alterations during ion transfer and after ion release. Movements of the retinal chromophore initially displace a conserved tryptophan to the cytoplasmic side of NM-R3, accompanied by a slight shift of the halide ion bound to the retinal. After ion release, the inward movements of helix C and helix G and the lateral displacements of the retinal block access to the extracellular side of NM-R3. Anomalous signal data have also been obtained from NM-R3 crystals containing iodide ions. The anomalous density maps provide insight into the halide binding site for ion transfer in NM-R3.

  23. Puromycin-sensitive aminopeptidase is required for C2C12 myoblast proliferation and differentiation. International-journal

    Shion Osana, Yasuo Kitajima, Naoki Suzuki, Aki Nunomiya, Hiroaki Takada, Takahiro Kubota, Kazutaka Murayama, Ryoichi Nagatomi

    Journal of cellular physiology　236　(7)　5293-5305　2021/07

    DOI： 10.1002/jcp.30237 　

    More details Close

    The ubiquitin-proteasome system is a major protein degradation pathway in the cell. Proteasomes produce several peptides that are rapidly degraded to free amino acids by intracellular aminopeptidases. Our previous studies reported that proteolysis via proteasomes and aminopeptidases is required for myoblast proliferation and differentiation. However, the role of intracellular aminopeptidases in myoblast proliferation and differentiation had not been clarified. In this study, we investigated the effects of puromycin-sensitive aminopeptidase (PSA) on C2C12 myoblast proliferation and differentiation by knocking down PSA. Aminopeptidase enzymatic activity was reduced in PSA-knockdown myoblasts. Knockdown of PSA induced impaired cell cycle progression in C2C12 myoblasts and accumulation of cells at the G2/M phase. Additionally, after the induction of myogenic differentiation in PSA-knockdown myoblasts, multinucleated circular-shaped myotubes with impaired cell polarity were frequently identified. Cell division cycle 42 (CDC42) knockdown in myoblasts resulted in a loss of cell polarity and the formation of multinucleated circular-shaped myotubes, which were similar to PSA-knockdown myoblasts. These data suggest that PSA is required for the proliferation of myoblasts in the growth phase and for the determination of cell polarity and elongation of myotubes in the differentiation phase.

  24. Anthocyanin 5,3'-aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin. International-journal

    Kazutaka Murayama, Miyuki Kato-Murayama, Tomohiro Sato, Toshiaki Hosaka, Kanako Ishiguro, Takayuki Mizuno, Kazunori Kitao, Teruki Honma, Shigeyuki Yokoyama, Yoshikazu Tanaka, Mikako Shirouzu

    Phytochemistry　186　112727-112727　2021/06

    DOI： 10.1016/j.phytochem.2021.112727 　

    More details Close

    The acylation of anthocyanins contributes to their structural diversity. Aromatic acylation is responsible for the blue color of anthocyanins and certain flowers. Aromatic acyltransferase from Gentiana triflora Pall. (Gentianaceae) (Gt5,3'AT) catalyzes the acylation of glucosyl moieties at the 5 and 3' positions of anthocyanins. Anthocyanin acyltransferase transfers an acyl group to a single position, such that Gt5,3'AT possesses a unique enzymatic activity. Structural investigation of this aromatic acyl group transfer is fundamental to understand the molecular mechanism of the acylation of double positions. In this study, structural analyses of Gt5,3'AT were conducted to identify the underlying mechanism. The crystal structure indicated that Gt5,3'AT shares structural similarities with other BAHD family enzymes, consisting of N and C terminal lobes. Structural comparison revealed that acyl group preference (aromatic or aliphatic) for the enzymes was determined by four amino acid positions, which are well conserved in aromatic and aliphatic CoA-binding acyltransferases. Although a complex structure with anthocyanins was not obtained, the binding of delphinidin 3,5,3'-triglucoside to Gt5,3'AT was investigated by evaluating the molecular dynamics. The simulation indicated that acyl transfer by Gt5,3'AT preferentially occurs at the 5-position rather than at the 3'-position, with interacting amino acids that are mainly located in the C-terminal lobe. Subsequent assays of chimeric enzymes (exchange of the N-terminal lobe and the C-terminal lobe between Gt5,3'AT and lisianthus anthocyanin 5AT) demonstrated that acyl transfer selectivity may be caused by the C-terminal lobe.

  25. Switching the substrate specificity of lysoplasmalogen-specific phospholipase D. International-journal

    Takayuki Oyama, Kazutaka Murayama, Daisuke Sugimori

    FEBS open bio　11　(4)　1132-1143　2021/04

    DOI： 10.1002/2211-5463.13123 　

    More details Close

    Lysoplasmalogen-specific phospholipase D (LyPls-PLD) catalyzes reactions in a manner similar to those catalyzed by glycerophosphodiester phosphodiesterase (GDPD) and other well-known PLDs. Although these enzymes hydrolyze the glycerophosphodiester bond, their substrate specificities are completely different. Previously, we reported that LyPls-PLD from Thermocrispum sp. RD004668 shows only 53% activity with 1-hexadecyl-2-hydroxy-sn-glycero-3-phosphocholine (LysoPAF) relative to the 100% activity it shows with choline lysoplasmalogen (LyPlsCho). Lipoprotein-associated phospholipase A2 (Lp-PLA2 ) activity can be used to evaluate for cardiovascular disease. Hence, development of a point-of-care testing kit requires a LysoPAF-specific PLD (LysoPAF-PLD) to measure Lp-PLA2 activity. Rational site-directed mutagenesis and kinetic analysis were applied to generate LysoPAF-PLD from LyPls-PLD and to clarify the mechanisms underlying the substrate-recognition ability of LyPls-PLD. Our results suggest that LyPls-PLD variants A47, M71, N173, F211, and W282 are possibly involved in substrate recognition and that F211L may substantially alter substrate preference. Moreover, the specific activity ratio LysoPAF/LyPlsCho corresponding to F211L was up to 25-fold higher than that corresponding to the wild-type enzyme. Thus, we succeeded in switching from LyPlsCho- to LysoPAF-PLD. These results suggest that the F211L variant may be utilized to measure Lp-PLA2 activity. Kinetic analyses demonstrated that product release was the rate-limiting step of the reaction, with flexibility of the sn-1 ether-linked vinyl/alkyl chain of the substrate being essential for substrate binding and product release. Our findings may lead to a better understanding of the differences between homologous enzymes (such as PLD, sphingomyelinase D, and GDPD of the phosphatidylinositol-phosphodiesterase superfamily) in relation to substrate recognition. ENZYME: EC 3.1.4.2 (currently assigned).

  26. A small molecule compound with an indole moiety inhibits the main protease of SARS-CoV-2 and blocks virus replication. International-journal

    Shin-Ichiro Hattori, Nobuyo Higashi-Kuwata, Hironori Hayashi, Srinivasa Rao Allu, Jakka Raghavaiah, Haydar Bulut, Debananda Das, Brandon J Anson, Emma K Lendy, Yuki Takamatsu, Nobutoki Takamune, Naoki Kishimoto, Kazutaka Murayama, Kazuya Hasegawa, Mi Li, David A Davis, Eiichi N Kodama, Robert Yarchoan, Alexander Wlodawer, Shogo Misumi, Andrew D Mesecar, Arun K Ghosh, Hiroaki Mitsuya

    Nature communications　12　(1)　668-668　2021/01/28

    DOI： 10.1038/s41467-021-20900-6 　

    More details Close

    Except remdesivir, no specific antivirals for SARS-CoV-2 infection are currently available. Here, we characterize two small-molecule-compounds, named GRL-1720 and 5h, containing an indoline and indole moiety, respectively, which target the SARS-CoV-2 main protease (Mpro). We use VeroE6 cell-based assays with RNA-qPCR, cytopathic assays, and immunocytochemistry and show both compounds to block the infectivity of SARS-CoV-2 with EC50 values of 15 ± 4 and 4.2 ± 0.7 μM for GRL-1720 and 5h, respectively. Remdesivir permitted viral breakthrough at high concentrations; however, compound 5h completely blocks SARS-CoV-2 infection in vitro without viral breakthrough or detectable cytotoxicity. Combination of 5h and remdesivir exhibits synergism against SARS-CoV-2. Additional X-ray structural analysis show that 5h forms a covalent bond with Mpro and makes polar interactions with multiple active site amino acid residues. The present data suggest that 5h might serve as a lead Mpro inhibitor for the development of therapeutics for SARS-CoV-2 infection.

  27. Structural basis for the high thermal stability and optimum pH of sphingomyelinase C from Streptomyces griseocarneus.

    Ikuhide Fujisawa, Hiroaki Hamana, Yu Tomita, Yusaku Matsumoto, Kazutaka Murayama, Daisuke Sugimori

    Journal of bioscience and bioengineering　131　(1)　8-12　2021/01

    DOI： 10.1016/j.jbiosc.2020.09.005 　

    More details Close

    Sphingomyelinase C (SMC) hydrolyzes sphingomyelin to ceramide and phosphocholine. Prokaryotic SMCs share sequence homology with mammalian SMCs that have enzymatic pH optima at neutral pH. SMC from the nonpathogenic prokaryote Streptomyces griseocarneus shows notable enzymatic features such as higher optimum pH and thermostability than other prokaryotic SMCs. Determination of the three-dimensional structure of S. griseocarneus-SMC (Sg-SMC) and comparison with other SMC structures represents a promising strategy to elucidate the unique enzymatic features of Sg-SMC on a structural basis. Therefore, we determined the crystal structure of Sg-SMC at 2.0 Å resolution by X-ray crystallography. Comparison of the Sg-SMC structure with three other structurally known SMCs from Listeria ivanovii, Bacillus cereus, and Staphylococcus aureus indicated that Sg-SMC is more diverse in sequence and that structural differences in the main chain between these SMCs are primarily located on the molecular surface distant from the active site. Comparison of the surface area of the four SMCs revealed that Sg-SMC has the most compact structure, which may contribute to the enhanced thermostability of Sg-SMC. Regarding the hydrogen bond network in the active site of Sg-SMC, a basic amino acid, Arg278, is involved, whereas the corresponding residue in other SMCs (Ser or Asn) does not form hydrogen bonds with metal-coordinating water molecules. Hydrogen bond formation between Arg278 and a Mg2+ ion-coordinating water molecule may be responsible for the higher optimal pH of Sg-SMC compared to that of other SMCs.

  28. siRNA knockdown of alanine aminopeptidase impairs myoblast proliferation and differentiation. International-journal

    Shion Osana, Yasuo Kitajima, Naoki Suzuki, Yidan Xu, Kazutaka Murayama, Ryoichi Nagatomi

    Experimental cell research　397　(1)　112337-112337　2020/12/01

    DOI： 10.1016/j.yexcr.2020.112337 　

    More details Close

    A large number of intracellular proteins are degraded by the ubiquitin-proteasome system, one of the major protein degradation pathways. It produces peptides of several different sizes through protein degradation, and these peptides are rapidly degraded into free amino acids by various intracellular aminopeptidases. Previously, we reported that the activity of proteasomes and aminopeptidases in the proteolysis pathway are necessary for myoblast proliferation and differentiation. However, the detailed function of intracellular aminopeptidases in myoblast proliferation and differentiation has not yet been elucidated. In this study, we focused on alanine aminopeptidase (APN) and investigated the function of APN in C2C12 myoblast proliferation and differentiation. In myoblasts and myotubes, APN was mainly localized in the cell membrane as well as expressed at low levels in the cytoplasm and nucleus. The reduction of the APN enzymatic activity impaired the cell cycle progression in C2C12 myoblasts. In addition, apoptosis was induced after APN-knockdown. Finally, myogenic differentiation was also delayed in the APN-suppressed myoblasts. These findings indicate that APN is required for myoblast proliferation and differentiation.

  29. Structural basis for inhibitory effects of Smad7 on TGF-β family signaling. International-journal

    Kazutaka Murayama, Miyuki Kato-Murayama, Yuka Itoh, Kohei Miyazono, Keiji Miyazawa, Mikako Shirouzu

    Journal of structural biology　212　(3)　107661-107661　2020/12/01

    DOI： 10.1016/j.jsb.2020.107661 　

    More details Close

    Smad6 and Smad7 are classified as inhibitory Smads (I-Smads). They are crucial in the fine-tuning of signals by cytokines of the transforming growth factor-β (TGF-β) family. They are negative feedback regulators and principally target the activated type I receptors as well as the activated Smad complexes, but with distinct specificities. Smad7 inhibits Smad signaling from all seven type I receptors of the TGF-β family, whereas Smad6 preferentially inhibits Smad signaling from the bone morphogenetic protein (BMP) type I receptors, BMPR1A and BMPR1B. The target specificities are attributed to the C-terminal MH2 domain. Notably, Smad7 utilizes two alternative molecular surfaces for its inhibitory function against type I receptors. One is a basic groove composed of the first α-helix and the L3 loop, a structure that is shared with Smad6 and receptor-regulated Smads (R-Smads). The other is a three-finger-like structure (consisting of residues 331-361, 379-387, and the L3 loop) that is unique to Smad7. The underlying structural basis remains to be elucidated in detail. Here, we report the crystal structure of the MH2 domain of mouse Smad7 at 1.9 Å resolution. The three-finger-like structure is stabilized by a network of hydrogen bonds between residues 331-361 and 379-387, thus forming a molecular surface unique to Smad7. Furthermore, we discuss how Smad7 antagonizes the activated Smad complexes composed of R-Smad and Smad4, a common partner Smad.

  30. ヘムシグナルによる転写因子BACH2のリン酸化と相互作用因子の制御

    松井 美紀, 角屋 駿, 島 弘季, 武藤 哲彦, 松本 光代, 白水 美香子, 村山 和隆, 五十嵐 和彦

    日本生化学会大会プログラム・講演要旨集　92回　[3T15m-03]　2019/09

    Publisher: (公社)日本生化学会

  31. 膵島移植の現況と今後の方向性 膵島移植と再生医療の融合を促進する細胞デバイスの開発

    後藤 昌史, 稲垣 明子, 猪村 武弘, Ibrahim Fathi, 水井 崇浩, 金井 哲史, 宮城 重人, 村山 和隆

    移植　54　(総会臨時)　172-172　2019/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  32. ヘムシグナルによる転写因子BACH2のリン酸化と相互作用因子の制御

    松井 美紀, 角屋 駿, 島 弘季, 武藤 哲彦, 松本 光代, 白水 美香子, 村山 和隆, 五十嵐 和彦

    日本生化学会大会プログラム・講演要旨集　92回　[3T15m-03]　2019/09

    Publisher: (公社)日本生化学会

  33. Biophysical characterization of heme binding to the intrinsically disordered region of Bach1. International-journal Peer-reviewed

    Kei Segawa, Miki Watanabe-Matsui, Kengo Tsuda, Toshitaka Matsui, Mikako Shirouzu, Kazuhiko Igarashi, Kazutaka Murayama

    European biophysics journal : EBJ　48　(4)　361-369　2019/05

    DOI： 10.1007/s00249-019-01364-5 　

    ISSN： 0175-7571

    More details Close

    Transcriptional repressor Bach1 plays an important role in antioxidant response. Bach1 function is regulated by heme binding to the four cysteine-proline (CP) motifs in Bach1, which leads to inhibition of its activity. Three of these CP motifs are located N-terminal to the bZip (basic leucine zipper) domain that is responsible for DNA binding. Based on sequence analysis, the region surrounding these CP motifs was expected to be intrinsically disordered. Bach1 is one of few known intrinsically disordered proteins that accept multiple heme molecules for functional regulation, but the molecular mechanisms of heme binding and functional regulation remain unclear. Uncovering these mechanisms is important for understanding Bach1-mediated antioxidant response. Biophysical characterization revealed that 5-coordinated heme binding was unique to the CP motifs within the heme-binding region of Bach1, whereas 6-coordinated binding occurred nonspecifically. Comparison of the wild-type protein and a CP motif mutant indicated that the level of 6-coordinated heme binding was reduced in the absence of 5-coordinated heme binding. Analytical ultracentrifugation showed that the CP motif mutant protein had a more elongated conformation than the wild-type protein, suggesting that cysteines within the CP motifs contribute to intramolecular interactions in Bach1. Thus, heme binding at the CP motifs induces a global conformational change in the Bach1 heme-binding region, and this conformational change, in turn, regulates the biological activity of Bach1.

  34. Functional Heme Binding to the Intrinsically Disordered C-Terminal Region of Bach1, a Transcriptional Repressor. Peer-reviewed

    Kei Segawa, Miki Watanabe-Matsui, Toshitaka Matsui, Kazuhiko Igarashi, Kazutaka Murayama

    The Tohoku journal of experimental medicine　247　(3)　153-159　2019/03

    DOI： 10.1620/tjem.247.153 　

    More details Close

    Heme is one of the key factors involved in the oxidative stress response of cells. The transcriptional repressor Bach1 plays an important role in this response through its heme-binding activity. Heme inhibits the transcriptional-repressor activity of Bach1, and can occur in two binding modes: 5- and 6-coordinated binding. The Cys-Pro (CP) motif has been determined to be the heme-binding motif of Bach family proteins. The sequence of Bach1 includes six CP motifs, and four CP motifs are functional. With the aim of elucidating the molecular mechanism of heme-Bach1 regulation, we conducted biophysical analyses focusing on the C-terminal region of mouse Bach1 (residues 631-739) which is located after the bZip domain and includes one functional CP motif. UV-Vis spectroscopy indicated that the CP motif binds heme via 5-coordinated bond. A mutant, which included a cysteine to alanine substitution at the CP motif, did not show 5-coordination, suggesting that this binding mode is specific to the CP motif. Surface plasmon resonance revealed that the binding affinity and stoichiometry of heme with the Bach1 C-terminal region were KD = 1.37 × 10-5 M and 2.3, respectively. The circular dichroism spectrum in the near-UV region exhibited peaks for heme binding to the CP motif. No significant spectral shifts were observed in the far-UV region when samples with and without heme were compared. Therefore, disordered-ordered transition such as "coupled folding and binding" is not involved in the Bach1-heme system. Consequently, the heme response of this C-terminal region is accomplished by disorder-disorder conformational alteration.

  35. Strategy towards tailored donor tissue-specific pancreatic islet isolation. International-journal Peer-reviewed

    Yuki Miyazaki, Kazutaka Murayama, Ibrahim Fathi, Takehiro Imura, Youhei Yamagata, Kimiko Watanabe, Hiroshi Maeda, Akiko Inagaki, Yasuhiro Igarashi, Shigehito Miyagi, Hiroki Shima, Kazuhiko Igarashi, Takashi Kamei, Michiaki Unno, Masafumi Goto

    PloS one　14　(5)　e0216136　2019

    DOI： 10.1371/journal.pone.0216136 　

    ISSN： 1932-6203

  36. ドナー膵の細胞外マトリックス組成に対応する膵島分離の実現に向けた試み

    宮崎 勇希, 猪村 武弘, 村山 和隆, 稲垣 明子, 宮城 重人, 島 弘季, 五十嵐 和彦, 海野 倫明, 亀井 尚, 後藤 昌史

    Organ Biology　25　(3)　94-94　2018/10

    Publisher: (一社)日本臓器保存生物医学会

    ISSN： 1340-5152

    eISSN： 2188-0204

  37. 本邦の膵島移植の今後の展開 東北大学が目指す膵島移植の次の展開

    後藤 昌史, 稲垣 明子, 山形 洋平, 村山 和隆, 渡邉 君子, 前田 浩, 猪村 武弘, 五十嵐 康宏, 植松 智海, 宮崎 勇希, 水井 崇浩, Fathi Ibrahim, 戸子台 和哲, 宮城 重人, 藤盛 啓成, 亀井 尚, 海野 倫明

    移植　53　(総会臨時)　275-275　2018/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  38. ドナー膵組織の細胞外マトリックス組成に対応する膵島分離酵素の至適化に向けた試み

    宮崎 勇希, 猪村 武弘, 村山 和隆, Fathi Ibrahim, 山形 洋平, 前田 浩, 渡邉 君子, 稲垣 明子, 宮城 重人, 島 弘季, 五十嵐 和彦, 海野 倫明, 亀井 尚, 後藤 昌史

    移植　53　(総会臨時)　523-523　2018/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  39. 生体金属のMagical Powerとその研究最前線 形質細胞分化におけるヘムシグナルと天然変性タンパク質Bach2

    松井 美紀, 角屋 駿, 島 弘季, 武藤 哲彦, 松本 光代, 白水 美香子, 村山 和隆, 五十嵐 和彦

    日本生化学会大会プログラム・講演要旨集　91回　[3S09m-03]　2018/09

    Publisher: (公社)日本生化学会

  40. Structural Basis for the Inhibition of Cyclin G-Associated Kinase by Gefitinib. International-journal Peer-reviewed

    Naomi Ohbayashi, Kazutaka Murayama, Miyuki Kato-Murayama, Mutsuko Kukimoto-Niino, Tamami Uejima, Takayoshi Matsuda, Noboru Ohsawa, Shigeyuki Yokoyoma, Hiroshi Nojima, Mikako Shirouzu

    ChemistryOpen　7　(9)　721-727　2018/09

    DOI： 10.1002/open.201800177 　

    More details Close

    Gefitinib is the molecular target drug for advanced non-small-cell lung cancer. The primary target of gefitinib is the positive mutation of epidermal growth factor receptor, but it also inhibits cyclin G-associated kinase (GAK). To reveal the molecular bases of GAK and gefitinib binding, structure analyses were conducted and determined two forms of the gefitinib-bound nanobody⋅GAK kinase domain complex structures. The first form, GAK_1, has one gefitinib at the ATP binding pocket, whereas the second form, GAK_2, binds one each in the ATP binding site and a novel binding site adjacent to the activation segment C-terminal helix, a unique element of the Numb-associated kinase family. In the novel binding site, gefitinib binds in the hydrophobic groove around the activation segment, disrupting the conserved hydrogen bonds for the catalytic activity. These structures suggest possibilities for the development of selective GAK inhibitors for viral infections, such as the hepatitis C virus.

  41. ヘムシグナルによる天然変性タンパク質Bach2の制御機構と生理学的意義の解明

    松井 美紀, 島 弘季, 武藤 哲彦, 松本 光代, 村山 和隆, 五十嵐 和彦

    生命科学系学会合同年次大会　2017年度　[4P2T15-0632)]　2017/12

    Publisher: 生命科学系学会合同年次大会運営事務局

  42. Increase in proapoptotic activity of inhibitory PAS domain protein via phosphorylation by MK2 Peer-reviewed

    Shuya Kasai, Mary J. E. Richardson, Satoru Torii, Ken-ichi Yasumoto, Hiroki Shima, Kazuhiko Igarashi, Ken Itoh, Kazuhiro Sogawa, Kazutaka Murayama

    FEBS JOURNAL　284　(23)　4115-4127　2017/12

    DOI： 10.1111/febs.14300 　

    ISSN： 1742-464X

    eISSN： 1742-4658

  43. Solid state structures of lead complexes with relevance for biological systems Peer-reviewed

    Katsuyuki Aoki, Kazutaka Murayama, Ning-Hai Hu

    Lead: Its Effects on Environment and Health　17　123-199　2017/04/10

    Publisher: Walter de Gruyter GmbH

    DOI： 10.1515/9783110434330-007 　

    ISSN： 1559-0836

  44. Structural basis of cucumisin protease activity regulation by its propeptide Peer-reviewed

    Ami Sotokawauchi, Miyuki Kato-Murayama, Kazutaka Murayama, Toshiaki Hosaka, Lori Maeda, Michio Onjo, Noboru Ohsawa, Dai-Ichiro Kato, Kazunari Arima, Mikako Shirouzur

    JOURNAL OF BIOCHEMISTRY　161　(1)　45-53　2017/01

    DOI： 10.1093/jb/mvw053 　

    ISSN： 0021-924X

    eISSN： 1756-2651

  45. Charge-state-distribution analysis of Bach2 intrinsically disordered heme binding region Peer-reviewed

    Tomoji Suenaga, Miki Watanabe-Matsui, Tamami Uejima, Hiroki Shima, Toshitaka Matsui, Masao Ikeda-Saito, Mikako Shirouzu, Kazuhiko Igarashi, Kazutaka Murayama

    JOURNAL OF BIOCHEMISTRY　160　(5)　291-298　2016/11

    DOI： 10.1093/jb/mvw035 　

    ISSN： 0021-924X

    eISSN： 1756-2651

  46. Molecular cloning, heterologous expression, and enzymatic characterization of lysoplasmalogen-specific phospholipase D from Thermocrispum sp. Peer-reviewed

    Yusaku Matsumoto, Nana Kashiwabara, Takayuki Oyama, Kazutaka Murayama, Hideyuki Matsumoto, Shin-ich Sakasegawa, Daisuke Sugimori

    FEBS OPEN BIO　6　(11)　1113-1130　2016/11

    DOI： 10.1002/2211-5463.12131 　

    ISSN： 2211-5463

  47. 膵消化酵素が膵島分離工程で膵島に与える影響

    宮崎 勇希, 猪村 武弘, 山形 洋平, 前田 浩, 村山 和隆, 渡邉 君子, 稲垣 明子, 五十嵐 康宏, 大内 憲明, 里見 進, 後藤 昌史

    Organ Biology　23　(3)　82-82　2016/10

    Publisher: (一社)日本臓器保存生物医学会

    ISSN： 1340-5152

    eISSN： 2188-0204

  48. 実用化へ向けた膵島分離用新規中性プロテアーゼカクテルの構築

    後藤 昌史, 山形 洋平, 村山 和隆, 渡邉 君子, 前田 浩, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 里見 進

    移植　51　(総会臨時)　322-322　2016/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  49. 膵島分離における消化酵素剤の膵島障害性に関する検討

    宮崎 勇希, 猪村 武弘, 山形 洋平, 前田 浩, 村山 和隆, 渡邉 君子, 稲垣 明子, 五十嵐 康宏, 大内 憲明, 里見 進, 後藤 昌史

    移植　51　(総会臨時)　322-322　2016/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  50. ヘムによる転写因子Bach2天然変性領域の制御機構の解明

    松井 美紀[渡部], 島 弘季, 上島 珠美, 白水 美香子, 村山 和隆, 五十嵐 和彦

    日本生化学会大会プログラム・講演要旨集　89回　[2T15-274)]　2016/09

    Publisher: (公社)日本生化学会

  51. 膵島移植の長期生着のための課題と克服 膵島分離成否の鍵を握る中性プロテアーゼ使用法に関する戦略

    後藤 昌史, 山形 洋平, 村山 和隆, 渡邉 君子, 前田 浩, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 佐藤 真実, 宮崎 勇希, 植松 智海, 宮城 重人, 藤盛 啓成, 大内 憲明, 里見 進

    移植　51　(2-3)　274-274　2016/08

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  52. 高濃度コラゲナーゼが膵島分離へ及ぼす影響に関する検討

    猪村 武弘, 山形 洋平, 村山 和隆, 渡邉 君子, 稲垣 明子, 五十嵐 康宏, 里見 進, 後藤 昌史

    移植　51　(2-3)　288-288　2016/08

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  53. テーラーメイド膵島分離実現へ向けたコラゲナーゼサブタイプGの対象基質の検証

    吉田 諭, 山形 洋平, 中川 香奈子, 前田 憲寿, 村山 和隆, 渡邊 君子, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 宮城 重人, 大橋 一夫, 大内 憲明, 里見 進, 後藤 昌史

    移植　51　(2-3)　288-288　2016/08

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  54. 膵島分離工程において消化酵素剤が分離膵島へ及ぼす影響

    宮崎 勇希, 猪村 武弘, 山形 洋平, 前田 浩, 村山 和隆, 渡邉 君子, 稲垣 明子, 五十嵐 康宏, 大内 憲明, 里見 進, 後藤 昌史

    移植　51　(2-3)　289-289　2016/08

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  55. Syncephalastrum racemosum amine oxidase with high catalytic efficiency toward ethanolamine and its application in ethanolamine determination Peer-reviewed

    Yoshitaka Hirano, Keisuke Chonan, Kazutaka Murayama, Shin-ich Sakasegawa, Hideyuki Matsumoto, Daisuke Sugimori

    APPLIED MICROBIOLOGY AND BIOTECHNOLOGY　100　(9)　3999-4013　2016/05

    DOI： 10.1007/s00253-015-7198-5 　

    ISSN： 0175-7598

    eISSN： 1432-0614

  56. 次世代の外科治療における早期探索的医療研究の役割 新規リコンビナント型コラゲナーゼの膵島移植への臨床応用

    後藤 昌史, 山形 洋平, 村山 和隆, 渡邉 君子, 前田 浩, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 宮城 重人, Korsgren Olle, 大内 憲明, 里見 進

    日本外科学会定期学術集会抄録集　116回　WS-3　2016/04

    Publisher: (一社)日本外科学会

  57. Crystal structure of [{Cu(tren)}2(cytosinato)].(ClO4)3.0.5H2O (tren = tris(2-aminoethyl)amine) and an overview on intra-molecular interligand interactions affecting metal binding sites of cytosine Peer-reviewed

    Md. Shahidur Rahman, Md. Abdus Salam, Ning-Hai Hu, Kazutaka Murayama, Katsuyuki Aoki

    Inorg. Chim. Acta　452　238-243　2016

    DOI： 10.1016/j.ica.2016.01.020 　

  58. Hydrolysis of plasmalogen by phospholipase A(1) from Streptomyces albidoflavus for early detection of dementia and arteriosclerosis Peer-reviewed

    Shin-ich Sakasegawa, Ryota Maeba, Kazutaka Murayama, Hideyuki Matsumoto, Daisuke Sugimori

    BIOTECHNOLOGY LETTERS　38　(1)　109-116　2016/01

    DOI： 10.1007/s10529-015-1955-5 　

    ISSN： 0141-5492

    eISSN： 1573-6776

  59. Solid State Structures of Alkali Metal Ion Complexes Formed by Low-Molecular-Weight Ligands of Biological Relevance Peer-reviewed

    Katsuyuki Aoki, Kazutaka Murayama, Ning-Hai Hu

    Metal Ions in Life Sciences　16　27-101　2016

    Publisher: Walter de Gruyter GmbH

    DOI： 10.1007/978-3-319-21756-7-3 　

    ISSN： 2041-9821 1559-0836

  60. Collagen V Is a Potential Substrate for Clostridial Collagenase G in Pancreatic Islet Isolation Peer-reviewed

    Hiroki Shima, Akiko Inagaki, Takehiro Imura, Youhei Yamagata, Kimiko Watanabe, Kazuhiko Igarashi, Masafumi Goto, Kazutaka Murayama

    JOURNAL OF DIABETES RESEARCH　2016　4396756　2016

    DOI： 10.1155/2016/4396756 　

    ISSN： 2314-6745

    eISSN： 2314-6753

  61. 生体金属の最前線 ヘムによる新たなタンパク質制御機構とその生理学的意義

    松井 美紀[渡部], 島 弘季, 村山 和隆, 五十嵐 和彦

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集　88回・38回　[4W8-5]　2015/12

    Publisher: (公社)日本生化学会

  62. Cloning a neutral protease of Clostridium histolyticum, determining its substrate specificity, and designing a specific substrate Peer-reviewed

    Hiroshi Maeda, Kanako Nakagawa, Kazutaka Murayama, Masafumi Goto, Kimiko Watanabe, Michio Takeuchi, Youhei Yamagata

    APPLIED MICROBIOLOGY AND BIOTECHNOLOGY　99　(24)　10489-10499　2015/12

    DOI： 10.1007/s00253-015-6923-4 　

    ISSN： 0175-7598

    eISSN： 1432-0614

  63. 再生医療新時代の膵・膵島移植の課題と対応 安全で高性能な新規膵島分離用酵素剤のヒト膵臓におけるPOC樹立および今後の戦略

    後藤 昌史, 山形 洋平, 村山 和隆, 渡邉 君子, 前田 浩, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 宮城 重人, 佐藤 真実, 藤盛 啓成, Korsgren Olle, 大内 憲明, 里見 進

    移植　50　(総会臨時)　259-259　2015/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  64. 肝細胞分離における中性プロテアーゼとクロストリパインの併用の有効性に関する検証

    吉田 諭, 山形 洋平, 村山 和隆, 渡邉 君子, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 宮城 重人, 大橋 一夫, 大内 憲明, 里見 進, 後藤 昌史

    移植　50　(総会臨時)　392-392　2015/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  65. 肝細胞分離における細胞分離酵素成分の役割解明と至適化

    吉田 諭, 山形 洋平, 中川 香奈子, 村山 和隆, 渡邉 君子, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 宮城 重人, 大橋 一夫, 大内 憲明, 里見 進, 後藤 昌史

    移植　50　(総会臨時)　392-392　2015/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  66. 膵島分離酵素剤が膵島へ及ぼす影響 高濃度の酵素剤は膵島障害を引き起こすのか?

    猪村 武弘, 山形 洋平, 村山 和隆, 渡邉 君子, 前田 浩, 稲垣 明子, 五十嵐 康宏, 後藤 昌史

    移植　50　(総会臨時)　443-443　2015/09

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  67. Secondary Publication 膵島分離におけるコラゲナーゼHの作用機序に関する研究

    藤尾 淳, 村山 和隆, 山形 洋平, 渡邉 君子, 猪村 武弘, 稲垣 明子, 大林 尚美, 島 弘季, 関口 悟, 藤盛 啓成, 五十嵐 和彦, 大内 憲明, 里見 進, 後藤 昌史

    移植　50　(2-3)　216-228　2015/08

    Publisher: (一社)日本移植学会

    ISSN： 0578-7947

    eISSN： 2188-0034

  68. 肝細胞分離用酵素剤の至適化

    吉田 諭, 山形 洋平, 中川 香奈子, 村山 和隆, 渡邉 君子, 猪村 武弘, 稲垣 明子, 五十嵐 康宏, 宮城 重人, 大橋 一夫, 大内 憲明, 里見 進, 後藤 昌史

    日本組織移植学会雑誌　14　(1)　40-40　2015/08

    Publisher: 日本組織移植学会

    ISSN： 1347-6491

  69. Synergistic Effect of Neutral Protease and Clostripain on Rat Pancreatic Islet Isolation Peer-reviewed

    Mami Dendo, Hiroshi Maeda, Youhei Yamagata, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Akiko Inagaki, Yasuhiro Igarashi, Yasutake Katoh, Masayuki Ebina, Keisei Fujimori, Kazuhiko Igarashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    TRANSPLANTATION　99　(7)　1349-1355　2015/07

    DOI： 10.1097/TP.0000000000000662 　

    ISSN： 0041-1337

    eISSN： 1534-6080

  70. Protein stabilization utilizing a redefined codon Peer-reviewed

    Kazumasa Ohtake, Atsushi Yamaguchi, Takahito Mukai, Hiroki Kashimura, Nobutaka Hirano, Mitsuru Haruki, Sosuke Kohashi, Kenji Yamagishi, Kazutaka Murayama, Yuri Tomabechi, Takashi Itagaki, Ryogo Akasaka, Masahito Kawazoe, Chie Takemoto, Mikako Shirouzu, Shigeyuki Yokoyama, Kensaku Sakamoto

    SCIENTIFIC REPORTS　5　9762　2015/05

    DOI： 10.1038/srep09762 　

    ISSN： 2045-2322

  71. Characterization of glycerophosphoethanolamine ethanolaminephosphodiesterase from Streptomyces sanglieri Peer-reviewed

    Shingo Mineta, Kazutaka Murayama, Daisuke Sugimori

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING　119　(2)　123-130　2015/02

    DOI： 10.1016/j.jbiosc.2014.07.005 　

    ISSN： 1389-1723

    eISSN： 1347-4421

  72. Heme binds to an intrinsically disordered region of Bach2 and alters its conformation Peer-reviewed

    Miki Watanabe-Matsui, Takashi Matsumoto, Toshitaka Matsui, Masao Ikeda-Saito, Akihiko Muto, Kazutaka Murayama, Kazuhiko Igarashi

    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS　565　25-31　2015/01

    DOI： 10.1016/j.abb.2014.11.005 　

    ISSN： 0003-9861

    eISSN： 1096-0384

  73. ヘムによる天然変性タンパク質Bach2の制御

    渡部 美紀, 村山 和隆, 松井 敏高, 齋藤 正男, 五十嵐 和彦

    日本生化学会大会プログラム・講演要旨集　87回　[3P-341]　2014/10

    Publisher: (公社)日本生化学会

  74. The Influence of Collagen III Expression on the Efficiency of Cell Isolation With the Use of Collagenase H. Peer-reviewed

    Yoshida S, Yamagata Y, Murayama K, Watanabe K, Imura T, Igarashi Y, Inagaki A, Fujimori K, Ohashi K, Ohuchi N, Satomi S, Goto M

    Transplant Proc　46　(6)　1942-1944　2014/08

    DOI： 10.1016/j.transproceed.2014.06.007 　

  75. Synergistic Effect of Neutral Protease and Clostripain On Pancreatic Islet Isolation. Peer-reviewed

    Dendo M, Yamagata Y, Murayama K, Watanabe K, Maeda H, Imura T, Inagaki A, Igarashi Y, Fujimori K, Ohuchi N, Satomi S, Goto M

    American Journal of Transplantation　14　358-359　2014/07

  76. Purification, characterization, molecular cloning, and extracellular production of a novel bacterial glycerophosphocholine cholinephosphodiesterase from Streptomyces sanglieri Peer-reviewed

    Daisuke Sugimori, Junki Ogasawara, Koki Okuda, Kazutaka Murayama

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING　117　(4)　422-430　2014/04

    DOI： 10.1016/j.jbiosc.2013.10.004 　

    ISSN： 1389-1723

    eISSN： 1347-4421

  77. Crystal structures of resorcin[4]arene and pyrogallol[4]arene complexes with DL-pipecolinic acid. Model compounds for the recognition of the pipecolinyl ring, a key fragment of FK506, through C-H center dot center dot center dot pi interaction Peer-reviewed

    Ikuhide Fujisawa, Yuji Kitamura, Ryo Kato, Kazutaka Murayama, Katsuyuki Aoki

    JOURNAL OF MOLECULAR STRUCTURE　1056　292-298　2014/01

    DOI： 10.1016/j.molstruc.2013.10.026 　

    ISSN： 0022-2860

    eISSN： 1872-8014

  78. 1P088 Multiple site-selective integrations of bulky halogenated tyrosines enhance protein stability(01F. Protein : Engineering,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

    Ohtake Kazumasa, Yamaguchi Atsushi, Haruki Mitsuru, Yamagishi Kenji, Murayama Kazutaka, Shirouzu Mikako, Yokoyama Shigeyuki, Sakamoto Kensaku

    Seibutsu Butsuri　54　(1)　S155　2014

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI： 10.2142/biophys.54.S155_4 　

  79. Collagenase H Is Crucial for Isolation of Rat Pancreatic Islets Peer-reviewed

    Atsushi Fujio, Kazutaka Murayama, Youhei Yamagata, Kimiko Watanabe, Takehiro Imura, Akiko Inagaki, Naomi Ohbayashi, Hiroki Shima, Satoshi Sekiguchi, Keisei Fujimori, Kazuhiko Igarashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    CELL TRANSPLANTATION　23　(10)　1187-1198　2014

    DOI： 10.3727/096368913X668654 　

    ISSN： 0963-6897

    eISSN： 1555-3892

  80. Collagenase H is Crucial for Isolation of Rat Pancreatic Islets Peer-reviewed

    Fujio Atsushi, Murayama Kazutaka, Yamagata Youhei, Watanabe Kimiko, Imura Takehiro, Inagaki Akiko, Ohbayashi Naomi, Shima Hiroki, Sekiguchi Satoshi, Fujimori Keisei, Igarashi Kazuhiko, Ohuchi Noriaki, Satomi Susumu, Goto Masafumi

    TRANSPLANTATION　96　(6)　S141-S142　2013/09/27

    ISSN： 0041-1337

  81. novel phospholipase B from Streptomyces sp NA684-purification, characterization, gene cloning, extracellular production and prediction of the catalytic residues Peer-reviewed

    Yusaku Matsumoto, Shingo Mineta, Kazutaka Murayama, Daisuke Sugimori

    FEBS JOURNAL　280　(16)　3780-3796　2013/08

    DOI： 10.1111/febs.12366 　

    ISSN： 1742-464X

    eISSN： 1742-4658

  82. [Structure and conformational change of collagenase as multi-domain protein]. Peer-reviewed

    Ohbayashi N, Murayama K

    Seikagaku. The Journal of Japanese Biochemical Society　85　(8)　692-699　2013/08

    Publisher:

    ISSN： 0037-1017

  83. Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297 Peer-reviewed

    Kazutaka Murayama, Kota Kano, Yusaku Matsumoto, Daisuke Sugimori

    Journal of Structural Biology　182　(2)　192-196　2013/05

    DOI： 10.1016/j.jsb.2013.02.003 　

    ISSN： 1047-8477 1095-8657

  84. Crystal structure of pyrogallol[4]arene complex with phosphocholine: A molecular recognition model for phosphocholine through cation-π interaction Peer-reviewed

    Ikuhide Fujisawa, Yuji Kitamura, Rumi Okamoto, Kazutaka Murayama, Ryo Kato, Katsuyuki Aoki

    Journal of Molecular Structure　1038　188-193　2013/04/24

    DOI： 10.1016/j.molstruc.2013.01.030 　

    ISSN： 0022-2860

  85. Solution Structure of Clostridial Collagenase H and Its Calcium-Dependent Global Conformation Change Peer-reviewed

    Naomi Ohbayashi, Takashi Matsumoto, Hiroki Shima, Masafumi Goto, Kimiko Watanabe, Akihito Yamano, Yasutake Katoh, Kazuhiko Igarashi, Youhei Yamagata, Kazutaka Murayama

    BIOPHYSICAL JOURNAL　104　(7)　1538-1545　2013/04

    DOI： 10.1016/j.bpj.2013.02.022 　

    ISSN： 0006-3495

    eISSN： 1542-0086

  86. 2P093 Heme binding region of Bach2 as intrinsically disordered protein(02. Heme proteins,Poster)

    Murayama Kazutaka, Matsui Miki, Igarashi Kazuhiko

    Seibutsu Butsuri　53　(1)　S174　2013

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI： 10.2142/biophys.53.S174_3 　

  87. Stereospecific intra-molecular interligand interactions affecting base-specific metal bonding to purine nucleobases in the solid state Invited

    Katsuyuki Aoki, Ikuhide Fujisawa, Kazutaka Murayama, Ning-Hai Hu

    Coordination Chemistry Reviews　2013

    DOI： 10.1016/j.ccr.2013.02.008 　

  88. 生体遷移金属のパラダイムシフト 生体内シグナル分子としての機能 ヘムによる天然変性タンパク質の制御

    渡部 美紀, 村山 和隆, 松井 敏高, 齋藤 正男, 五十嵐 和彦

    日本生化学会大会プログラム・講演要旨集　85回　2S13-8　2012/12

    Publisher: (公社)日本生化学会

  89. Structure of the Rho-specific guanine nucleotide-exchange factor Xpln Peer-reviewed

    Kazutaka Murayama, Miyuki Kato-Murayama, Ryogo Akasaka, Takaho Terada, Shigeyuki Yokoyama, Mikako Shirouzu

    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS　68　(Pt 12)　1455-1459　2012/12

    DOI： 10.1107/S1744309112045265 　

    ISSN： 1744-3091

  90. Crystal Structure of Cucumisin, a Subtilisin-Like Endoprotease from Cucumis melo L. Peer-reviewed

    Kazutaka Murayama, Miyuki Kato-Murayama, Toshiaki Hosaka, Ami Sotokawauchi, Shigeyuki Yokoyama, Kazunari Arima, Mikako Shirouzu

    JOURNAL OF MOLECULAR BIOLOGY　423　(3)　386-396　2012/10

    DOI： 10.1016/j.jmb.2012.07.013 　

    ISSN： 0022-2836

  91. Proline Recognition through C–H···π Interaction within Crystal Structures of DL-Proline–Calix[4]pyrogallolarene Molecular Complexes

    Ikuhide Fujisawa, Noriko Harima, Kenji Takagi, Shuichi Hiraoka, Mitsuhiko Shionoya, Kazutaka Murayama, Shinichi Itsuno, Ryo Kato, Katsuyuki Aoki

    Bulletin of the Chemical Society of Japan　85　(9)　1037-1039　2012/09/15

    Publisher: The Chemical Society of Japan

    DOI： 10.1246/bcsj.20120025 　

    ISSN： 0009-2673

    eISSN： 1348-0634

  92. Crystallographic study of the interaction of the anti-HIV lectin actinohivin with the alpha(1-2)mannobiose moiety of gp120 HMTG Peer-reviewed

    Kaoru Suzuki, Naomi Ohbayashi, Jiandong Jiang, Xiaoxue Zhang, M. Mominul Hoque, Masaru Tsunoda, Kazutaka Murayama, Haruo Tanaka, Akio Takenaka

    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS　68　(Pt 9)　1060-1063　2012/09

    DOI： 10.1107/S1744309112031077 　

    ISSN： 1744-3091

  93. Enhancement of the Structural Stability of Full-Length Clostridial Collagenase by Calcium Ions Peer-reviewed

    Naomi Ohbayashi, Noriko Yamagata, Masafumi Goto, Kimiko Watanabe, Youhei Yamagata, Kazutaka Murayama

    APPLIED AND ENVIRONMENTAL MICROBIOLOGY　78　(16)　5839-5844　2012/08

    DOI： 10.1128/AEM.00808-12 　

    ISSN： 0099-2240

  94. Kinetic characterization and Mg2+ enhancement of Streptomyces griseocarneus sphingomyelinase C produced by recombinant Streptomyces lividans Peer-reviewed

    Daisuke Sugimori, Yusaku Matsumoto, Yu Tomita, Kazutaka Murayama, Chiaki Ogino

    PROTEIN EXPRESSION AND PURIFICATION　81　(2)　151-156　2012/02

    DOI： 10.1016/j.pep.2011.10.004 　

    ISSN： 1046-5928

  95. Nucleic acid-metal ion interactions in the solid state Peer-reviewed

    Katsuyuki Aoki, Kazutaka Murayama

    Metal Ions in Life Sciences　10　43-102　2012

    Publisher: Taylor and Francis Ltd.

    DOI： 10.1007/978-94-007-2172-2-2 　

    ISSN： 2041-9821 1559-0836

  96. Crystal Structures of the Armadillo Repeat Domain of Adenomatous Polyposis Coli and Its Complex with the Tyrosine-Rich Domain of Sam68 Peer-reviewed

    Ella Czarina Morishita, Kazutaka Murayama, Miyuki Kato-Murayama, Yoshiko Ishizuka-Katsura, Yuri Tomabechi, Tomoatsu Hayashi, Takaho Terada, Noriko Handa, Mikako Shirouzu, Tetsu Akiyama, Shigeyuki Yokoyama

    STRUCTURE　19　(10)　1496-1508　2011/10

    DOI： 10.1016/j.str.2011.07.013 　

    ISSN： 0969-2126

  97. 転写抑制因子Bach2におけるヘム制御ドメインの解析

    松井 美紀, 村山 和隆, 松井 敏高, 齋藤 正男, 武藤 哲彦, 五十嵐 和彦

    日本生化学会大会プログラム・講演要旨集　84回　3P-0443　2011/09

    Publisher: (公社)日本生化学会

  98. Heme regulates B-cell differentiation, antibody class switch, and heme oxygenase-1 expression in B cells as a ligand of Bach2 Peer-reviewed

    Miki Watanabe-Matsui, Akihiko Muto, Toshitaka Matsui, Ari Itoh-Nakadai, Osamu Nakajima, Kazutaka Murayama, Masayuki Yamamoto, Masao Ikeda-Saito, Kazuhiko Igarashi

    BLOOD　117　(20)　5438-5448　2011/05

    DOI： 10.1182/blood-2010-07-296483 　

    ISSN： 0006-4971

  99. Tetrameric Ring Formation of Epstein-Barr Virus Polymerase Processivity Factor Is Crucial for Viral Replication Peer-reviewed

    Sanae Nakayama, Takayuki Murata, Yoshihiro Yasui, Kazutaka Murayama, Hiroki Isomura, Teru Kanda, Tatsuya Tsurumi

    JOURNAL OF VIROLOGY　84　(24)　12589-12598　2010/12

    DOI： 10.1128/JVI.01394-10 　

    ISSN： 0022-538X

  100. 3P108 Spectoroscopic analyses of heme-acceptor region of Bach2 protein(Heme proteins,The 48th Annual Meeting of the Biophysical Society of Japan)

    Murayama Kazutaka, Watamabe-Matsui Miki, Matsui Toshitaka, Ikeda-Saito Masao, Igarashi Kazuhiko

    Seibutsu Butsuri　50　(2)　S163　2010

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI： 10.2142/biophys.50.S163_5 　

  101. NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes Peer-reviewed

    Alexander K. Goroncy, Kazutaka Murayama, Mikako Shirouzu, Seiki Kuramitsu, Takanori Kigawa, Shigeyuki Yokoyama

    Journal of Structural and Functional Genomics　11　(4)　247-256　2010

    DOI： 10.1007/s10969-010-9096-5 　

    ISSN： 1345-711X

  102. Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme from Thermus thermophilus HB8 Peer-reviewed

    Ryoichi Arai, Kazutaka Murayama, Tomomi Uchikubo-Kamo, Madoka Nishimoto, Mitsutoshi Toyama, Seiki Kuramitsu, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama

    JOURNAL OF STRUCTURAL BIOLOGY　168　(3)　575-581　2009/12

    DOI： 10.1016/j.jsb.2009.07.007 　

    ISSN： 1047-8477

    eISSN： 1095-8657

  103. Crystal Structure of Epstein-Barr Virus DNA Polymerase Processivity Factor BMRF1 Peer-reviewed

    Kazutaka Murayama, Sanae Nakayama, Miyuki Kato-Murayama, Ryogo Akasaka, Naomi Ohbayashi, Yuki Kamewari-Hayami, Takaho Terada, Mikako Shirouzu, Tatsuya Tsurumi, Shigeyuki Yokoyama

    JOURNAL OF BIOLOGICAL CHEMISTRY　284　(51)　35896-35905　2009/12

    DOI： 10.1074/jbc.M109.051581 　

    ISSN： 0021-9258

  104. Epstein-Barr Virus Polymerase Processivity Factor Enhances BALF2 Promoter Transcription as a Coactivator for the BZLF1 Immediate-Early Protein Peer-reviewed

    Sanae Nakayama, Takayuki Murata, Kazutaka Murayama, Yoshihiro Yasui, Yoshitaka Sato, Ayumi Kudoh, Satoko Iwahori, Hiroki Isomura, Teru Kanda, Tatsuya Tsurumi

    JOURNAL OF BIOLOGICAL CHEMISTRY　284　(32)　21557-21568　2009/08

    DOI： 10.1074/jbc.M109.015685 　

    ISSN： 0021-9258

  105. Structure of the putative thioesterase protein TTHA1846 from Thermus thermophilus HB8 complexed with coenzyme A and a zinc ion Peer-reviewed

    Toshiaki Hosaka, Kazutaka Murayama, Miyuki Kato-Murayama, Akiko Urushibata, Ryogo Akasaka, Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, Shigeyuki Yokoyama

    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY　65　(8)　767-776　2009/08

    DOI： 10.1107/S0907444909015601 　

    ISSN： 0907-4449

  106. Novel dimerization mode of the human Bcl-2 family protein Bak, a mitochondrial apoptosis regulator Peer-reviewed

    Hongfei Wang, Chie Takemoto, Ryogo Akasaka, Tomomi Uchikubo-Kamo, Seiichiro Kishishita, Kazutaka Murayama, Takaho Terada, Lirong Chen, Zhi-Jie Liu, Bi-Cheng Wang, Sumio Sugano, Akiko Tanaka, Makoto Inoue, Takanori Kigawa, Mikako Shirouzu, Shigeyuki Yokoyama

    JOURNAL OF STRUCTURAL BIOLOGY　166　(1)　32-37　2009/04

    DOI： 10.1016/j.jsb.2008.12.003 　

    ISSN： 1047-8477

  107. Genetic Encoding of 3-lodo-L-Tyrosine in Escherichia coli for Single-Wavelength Anomalous Dispersion Phasing in Protein Crystallography Peer-reviewed

    Kensaku Sakamoto, Kazutaka Murayama, Kenji Oki, Fumie Lraha, Miyuki Kato-Murayama, Masahiro Takahashi, Kazumasa Ohtake, Takatsugu Kobayashi, Seiki Kuramitsu, Mikako Shirouzu, Shigeyuki Yokoyama

    STRUCTURE　17　(3)　335-344　2009/03

    DOI： 10.1016/j.str.2009.01.008 　

    ISSN： 0969-2126

  108. Crystal structure of the Bach1 BTB domain and its regulation of homodimerization Peer-reviewed

    Nobutoshi Ito, Miki Watanabe-Matsui, Kazuhiko Igarashi, Kazutaka Murayama

    GENES TO CELLS　14　(2)　167-178　2009/02

    DOI： 10.1111/j.1365-2443.2008.01259.x 　

    ISSN： 1356-9597

  109. Crystal structure of the Bruton's tyrosine kinase PH domain with phosphatidylinositol Peer-reviewed

    Kazutaka Murayama, Miyuki Kato-Murayama, Chiemi Mishima, Ryogo Akasaka, Mikako Shirouzu, Yasuhisa Fakui, Shigeyuki Yokoyama

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS　377　(1)　23-28　2008/12

    DOI： 10.1016/j.bbrc.2008.09.055 　

    ISSN： 0006-291X

  110. Structures of two archaeal diphthine synthases: insights into the post-translational modification of elongation factor 2 Peer-reviewed

    Seiichiro Kishishita, Katsumi Shimizu, Kazutaka Murayama, Takaho Terada, Mikako Shirouzu, Shigeyuki Yokoyama, Naoki Kunishima

    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY　64　(4)　397-406　2008/04

    DOI： 10.1107/S0907444908000723 　

    ISSN： 0907-4449

  111. Crystal structure of the interleukin-15 center dot interleukin-15 receptor alpha complex - Insights into trans and cis presentation Peer-reviewed

    Shaun K. Olsen, Naruhisa Ota, Seiichiro Kishishita, Mutsuko Kukimoto-Niino, Kazutaka Murayama, Hidemi Uchiyama, Mitsutoshi Toyama, Takaho Terada, Mikako Shirouzu, Osami Kanagawa, Shigeyuki Yokoyama

    JOURNAL OF BIOLOGICAL CHEMISTRY　282　(51)　37191-37204　2007/12

    DOI： 10.1074/jbc.M706150200 　

    ISSN： 0021-9258

  112. Structure of the minimized alpha/beta-hydrolase fold protein from Thermus thermophilus HB8 Peer-reviewed

    Yong Xie, Chie Takemoto, Seiichiro Kishishita, Tomomi Uchikubo-Kamo, Kazutaka Murayama, Lirong Chen, Zhi-Jie Liu, Bi-Cheng Wang, Miho Manzoku, Akio Ebihara, Seiki Kuramitsu, Mikako Shirouzu, Shigeyuki Yokoyama

    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS　63　(12)　993-997　2007/12

    DOI： 10.1107/S1744309107061106 　

    ISSN： 1744-3091

  113. Structural basis for functional mimicry of long-variable-arm tRNA by transfer-messenger RNA Peer-reviewed

    Yoshitaka Bessho, Rie Shibata, Shun-ichi Sekine, Kazutaka Murayama, Kyoko Higashijima, Chie Hori-Takemoto, Mikako Shirouzu, Seiki Kuramitsu, Shigeyuki Yokoyama

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA　104　(20)　8293-8298　2007/05

    DOI： 10.1073/pnas.0700402104 　

    ISSN： 0027-8424

  114. Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors Peer-reviewed

    Sean R. Connell, Chie Takemoto, Daniel N. Wilson, Hongfei Wang, Kazutaka Murayama, Takaho Terada, Mikako Shirouzu, Maximilian Rost, Martin Schueler, Jan Giesebrecht, Marylena Dabrowski, Thorsten Mielke, Paola Fucini, Shigeyuki Yokoyama, Christian M. T. Spahn

    MOLECULAR CELL　25　(5)　751-764　2007/03

    DOI： 10.1016/j.molcel.2007.01.027 　

    ISSN： 1097-2765

    eISSN： 1097-4164

  115. Crystal structure of the Rac activator, Asef, reveals its autoinhibitory mechanism Peer-reviewed

    Kazutaka Murayama, Mikako Shirouzu, Yoshihiro Kawasaki, Miyuki Kato-Murayama, Kyoko Hanawa-Suetsugu, Ayako Sakamoto, Yasuhiro Katsura, Atsushi Suenaga, Mitsutoshi Toyama, Takaho Terada, Makoto Taiji, Tetsu Akiyama, Shigeyuki Yokoyama

    JOURNAL OF BIOLOGICAL CHEMISTRY　282　(7)　4238-4242　2007/02

    DOI： 10.1074/jbc.C600234200 　

    ISSN： 0021-9258

  116. 3P355 Crystallization Experiment Support System : Development of Database and Imaging System(Others,Poster Presentations)

    Takemoto Chie, Akasaka Ryogo, Uchikubo Tomomi, Nishino Aya, Murayama Kazutaka, Shirouzu Mikako, Yokoyama Shigeyuki

    Seibutsu Butsuri　47　S291　2007

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI： 10.2142/biophys.47.S291_4 　

  117. 1P065 X-ray structure analyses for iodo-tyrosine incorporated proteins(Proteins-methodology,Poster Presentations)

    Murayama Kazutaka, Akasaka Ryogo, Kato-Murayama Miyuki, Terada Takaho, Sakamoto Kensaku, Shirouzu Mikako, Yokoyama Shigeyuki

    Seibutsu Butsuri　47　S39　2007

    Publisher: The Biophysical Society of Japan General Incorporated Association

    DOI： 10.2142/biophys.47.S39_4 　

  118. Structure of the UNC5H2 death domain Peer-reviewed

    Noriko Handa, Mutsuko Kukimoto-Niino, Ryogo Akasaka, Kazutaka Murayama, Takaho Terada, Makoto Inoue, Takashi Yabuki, Masaaki Aoki, Eiko Seki, Takayoshi Matsuda, Emi Nunokawa, Akiko Tanaka, Yoshihide Hayashizaki, Takanori Kigawa, Mikako Shirouzu, Shigeyuki Yokoyama

    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY　62　1502-1509　2006/12

    DOI： 10.1107/S0907444906039369 　

    ISSN： 0907-4449

  119. The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation Peer-reviewed

    Shiro Suetsugu, Kazutaka Murayama, Ayako Sakamoto, Kyoko Hanawa-Suetsugu, Azusa Seto, Tsukasa Oikawa, Chiemi Mishima, Mikako Shirouzu, Tadaomi Takenawa, Shigeyuki Yokoyama

    JOURNAL OF BIOLOGICAL CHEMISTRY　281　(46)　35347-35358　2006/11

    DOI： 10.1074/jbc.M606814200 　

    ISSN： 0021-9258

  120. The crystal structure of mouse Nup35 reveals atypical RNP motifs and novel homodimerization of the RRM domain Peer-reviewed

    Noriko Handa, Mutsuko Kukimoto-Niino, Ryogo Akasaka, Sefichiro Kishishita, Kazutaka Murayama, Takaho Terada, Makoto Inoue, Takanori Kigawa, Shingo Kose, Naoko Imamoto, Akiko Tanaka, Yoshihide Hayashizaki, Mikako Shirouzu, Shigeyuki Yokoyama

    JOURNAL OF MOLECULAR BIOLOGY　363　(1)　114-124　2006/10

    DOI： 10.1016/j.jmb.2006.07.089 　

    ISSN： 0022-2836

  121. Crystal structure of the RUN domain of the RAP2-interacting protein x Peer-reviewed

    Mutsuko Kukimoto-Niino, Tetsuo Takagi, Ryogo Akasaka, Kazutaka Murayama, Tomomi Uchikubo-Kamo, Takaho Terada, Makoto Inoue, Satoru Watanabe, Akiko Tanaka, Yoshihide Hayashizaki, Takanori Kigawa, Mikako Shirouzu, Shigeyuki Yokoyama

    JOURNAL OF BIOLOGICAL CHEMISTRY　281　(42)　31843-31853　2006/10

    DOI： 10.1074/jbc.M604960200 　

    ISSN： 0021-9258

    eISSN： 1083-351X

  122. Crystal structure of the single-domain rhodanese homologue TTHA0613 from Thermus thermophilus HB8 Peer-reviewed

    M Hattori, E Mizohata, A Tatsuguchi, R Shibata, S Kishishita, K Murayama, T Terada, S Kuramitsu, M Shirouzu, S Yokoyama

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS　64　(1)　284-287　2006/07

    DOI： 10.1002/prot.20937 　

    ISSN： 0887-3585

  123. Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7) Peer-reviewed

    R Arai, S Yoshikawa, K Murayama, Y Imai, R Takahashi, M Shirouzu, S Yokoyama

    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS　62　(Pt 4)　330-334　2006/04

    DOI： 10.1107/S1744309106009006 　

    ISSN： 1744-3091

  124. Crystal structures of tyrosyl-tRNA synthetases from Archaea Peer-reviewed

    M Kuratani, H Sakai, M Takahashi, T Yanagisawa, T Kobayashi, K Murayama, LR Chen, ZJ Liu, BC Wang, C Kuroishi, S Kuramitsu, T Terada, Y Bessho, M Shirouzu, S Sekine, S Yokoyama

    JOURNAL OF MOLECULAR BIOLOGY　355　(3)　395-408　2006/01

    DOI： 10.1016/j.jmb.2005.10.073 　

    ISSN： 0022-2836

  125. Crystal structure of the hypothetical protein TTHA1013 from Thermus thermophilus HB8 Peer-reviewed

    M Hattori, E Mizohata, M Manzoku, Y Bessho, K Murayama, T Terada, S Kuramitsu, M Shirouzu, S Yokoyama

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS　61　(4)　1117-1120　2005/12

    DOI： 10.1002/prot.20692 　

    ISSN： 0887-3585

  126. Crystal structure of an archaeal peroxiredoxin from the aerobic hyperthermophilic crenarchaeon Aeropyrum pernix K1 Peer-reviewed

    E Mizohata, H Sakai, E Fusatomi, T Terada, KK Murayama, M Shirouzu, S Yokoyama

    JOURNAL OF MOLECULAR BIOLOGY　354　(2)　317-329　2005/11

    DOI： 10.1016/j.jmb.2005.09.006 　

    ISSN： 0022-2836

  127. Structures of a putative RNA 5-methyluridine methyltransferase, Thermus thermophilus TTHA1280, and its complex with S-adenosyl-L-homocysteine Peer-reviewed

    AA Pioszak, K Murayama, N Nakagawa, A Ebihara, S Kuramitsu, M Shirouzu, S Yokoyama

    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS　61　(Pt 10)　867-874　2005/10

    DOI： 10.1107/S1744309105029842 　

    ISSN： 1744-3091

  128. Crystal structure of a predicted phosphoribosyltransferase (TT1426) from Thermus thermophilus HB8 at 2.01 angstrom resolution Peer-reviewed

    M Kukimoto-Niino, R Shibata, K Murayama, H Hamana, M Nishimoto, Y Bessho, T Terada, M Shirouzu, S Kuramitsu, S Yokoyama

    PROTEIN SCIENCE　14　(3)　823-827　2005/03

    DOI： 10.1110/ps.041229405 　

    ISSN： 0961-8368

  129. Crystal structure of TT1662 from Thermus thermophilus HB8: A member of the alpha/beta hydrolase fold enzymes Peer-reviewed

    K Murayama, M Shirouzu, T Terada, S Kuramitsu, S Yokoyama

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS　58　(4)　982-984　2005/03

    DOI： 10.1002/prot.20361 　

    ISSN： 0887-3585

  130. ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8 Peer-reviewed

    A Seto, K Murayama, M Toyama, A Ebihara, N Nakagawa, S Kuramitsu, M Shirouzu, S Yokoyama

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS　58　(1)　235-242　2005/01

    DOI： 10.1002/prot.20276 　

    ISSN： 0887-3585

    eISSN： 1097-0134

  131. Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 angstrom resolution Peer-reviewed

    K Murayama, M Kato-Murayama, K Katsura, T Uchikubo-Kamo, M Yamaguchi-Hirafuji, M Kawazoe, R Akasaka, K Hanawa-Suetsugu, C Hori-Takemoto, T Terada, M Shirouzu, S Yokoyama

    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS　61　(Pt 1)　26-29　2005/01

    DOI： 10.1107/S1744309104032555 　

    ISSN： 1744-3091

  132. Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 angstrom resolution Peer-reviewed

    K Murayama, M Kato-Murayama, K Katsura, T Uchikubo-Kamo, M Yamaguchi-Hirafuji, M Kawazoe, R Akasaka, K Hanawa-Suetsugu, C Hori-Takemoto, T Terada, M Shirouzu, S Yokoyama

    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS　61　(1)　26-29　2005/01

    DOI： 10.1107/S1744309104032555 　

    ISSN： 1744-3091

  133. Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8 Peer-reviewed

    M Kukimoto-Niino, K Murayama, M Kato-Murayama, M Idaka, A Tatsuguchi, R Ushikoshi-Nakayama, T Terada, S Kuramitsu, M Shirouzu, S Yokoyama

    PROTEIN SCIENCE　13　(11)　3038-3042　2004/11

    DOI： 10.1110/ps.041012404 　

    ISSN： 0961-8368

  134. Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8 Peer-reviewed

    HF Wang, CH Takemoto, K Murayama, H Sakai, A Tatsuguchi, T Terada, M Shirouzu, S Kuramitsu, S Yokoyama

    PROTEIN SCIENCE　13　(10)　2806-2810　2004/10

    DOI： 10.1110/ps.04864904 　

    ISSN： 0961-8368

  135. Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8 Peer-reviewed

    M Kukimoto-Niino, K Murayama, M Inoue, T Terada, JRH Tame, S Kuramitsu, M Shirouzu, S Yokoyama

    JOURNAL OF MOLECULAR BIOLOGY　337　(3)　761-770　2004/03

    DOI： 10.1016/j.jmb.2004.01.047 　

    ISSN： 0022-2836

  136. Crystal structure of a hypothetical protein, TT1725, from Thermus thermophilus HB8 at 1.7 A resolution Peer-reviewed

    A Seto, M Shirouzu, T Terada, K Murayama, S Kuramitsu, S Yokoyama

    PROTEINS-STRUCTURE FUNCTION AND GENETICS　53　(3)　768-771　2003/11

    DOI： 10.1002/prot.10412 　

    ISSN： 0887-3585

  137. Crystal structure of the 2 '-5 ' RNA ligase from Thermus thermophilus HB8 Peer-reviewed

    M Kato, M Shirouzu, T Terada, H Yamaguchi, K Murayama, H Sakai, S Kuramitsu, S Yokoyama

    JOURNAL OF MOLECULAR BIOLOGY　329　(5)　903-911　2003/06

    DOI： 10.1016/S0022-2836(03)00448-0 　

    ISSN： 0022-2836

  138. Thickness-shear-mode acoustic wave sensor for acetone vapour coated with C-ethylcalix[4]resorcinarene and C-H center dot center dot center dot pi interactions as a molecular recognition mechanism Peer-reviewed

    Z Cao, K Murayama, K Aoki

    ANALYTICA CHIMICA ACTA　448　(1-2)　47-59　2001/12

    DOI： 10.1016/S0003-2670(01)01325-3 　

    ISSN： 0003-2670

  139. Crystal structure of omega transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 A resolution Peer-reviewed

    K Murayama, P Orth, AB de la Hoz, JC Alonso, W Saenger

    JOURNAL OF MOLECULAR BIOLOGY　314　(4)　789-796　2001/12

    DOI： 10.1006/jmbi.2001.5157 　

    ISSN： 0022-2836

  140. Stability and DNA-binding properties of the omega regulator protein from the broad-host range Streptococcus pyogenes plasmid pSM19035 Peer-reviewed

    R Misselwitz, AB de la Hoz, S Ayora, K Welfle, J Behlke, K Murayama, W Saenger, JC Alonso, H Welfle

    FEBS LETTERS　505　(3)　436-440　2001/09

    DOI： 10.1016/S0014-5793(01)02865-4 　

    ISSN： 0014-5793

  141. Crystallization and preliminary X-ray diffraction studies of Streptococcus pyogenes plasmid pSM19035-encoded omega transcriptional repressor Peer-reviewed

    K Murayama, AB de la Hoz, C Alings, G Lopez, P Orth, JC Alonso, W Saenger

    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY　55　2041-2042　1999/12

    DOI： 10.1107/S0907444999012275 　

    ISSN： 0907-4449

  142. Cation-pi interactions between potassium ions and aromatic rings. Crystal structures of three potassium complexes of calix[6]arene Peer-reviewed

    K Murayama, K Aoki

    INORGANICA CHIMICA ACTA　281　(1)　36-42　1998/10

    DOI： 10.1016/S0020-1693(98)00139-X 　

    ISSN： 0020-1693

  143. Resorcin[4]arene dimer linked by eight water molecules and incorporating a tetraethylammonium ion: guest-driven capsule formation via cation-pi interactions Peer-reviewed

    K Murayama, K Aoki

    CHEMICAL COMMUNICATIONS　(5)　607-608　1998/03

    DOI： 10.1039/a800340h 　

    ISSN： 1359-7345

  144. Multiple cation-pi interactions between the trimethylammonium moiety and the aromatic rings within a molecular complex formed between 3-phenylpropionic acid choline ester and resorcin[4]arene Peer-reviewed

    K Murayama, K Aoki

    CHEMISTRY LETTERS　(4)　301-302　1998

    DOI： 10.1246/cl.1998.301 　

    ISSN： 0366-7022

    eISSN： 1348-0715

  145. Molecular recognition involving multiple cation-pi interactions: The inclusion of the acetylcholine trimethylammonium moiety in resorcin[4]arene Peer-reviewed

    K Murayama, K Aoki

    CHEMICAL COMMUNICATIONS　(1)　119-120　1997/01

    DOI： 10.1039/a607131g 　

    ISSN： 1359-7345

  146. カチオン-π相互作用による超分子カプセル状分子複合体の形成: レゾルシノール環状4量体―テトラエチルアンモニウム2: 1錯体の構造

    村山 和隆, 青木 克之

    日本結晶学会誌　38　168-168　1996

    Publisher: The Crystallographic Society of Japan

    DOI： 10.5940/jcrsj.38.Supplement_168 　

    ISSN： 0369-4585

  147. CATION-PI INTERACTION BETWEEN THE TRIMETHYLAMMONIUM MOIETY AND THE AROMATIC RING WITH INDOLE-3-ACETIC-ACID CHOLINE ESTER, A MODEL-COMPOUND FOR MOLECULAR RECOGNITION BETWEEN ACETYLCHOLINE AND ITS ESTERASE - AN X-RAY STUDY Peer-reviewed

    K AOKI, K MURAYAMA, H NISHIYAMA

    JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS　(21)　2221-2222　1995/11

    DOI： 10.1039/c39950002221 　

    ISSN： 0022-4936

  148. インドール酢酸コリンエステルの結晶構造: カチオン-π相互作用

    村山 和隆, 青木 克之, 西山 久雄

    日本結晶学会誌　35　22-22　1993

    Publisher: The Crystallographic Society of Japan

    DOI： 10.5940/jcrsj.35.Supplement_22 　

    ISSN： 0369-4585

Show all ︎Show first 5

Misc. 63

  1. アミノペプチダーゼによる筋分化制御メカニズムの解明

    長名 シオン, 北嶋 康雄, 鈴木 直輝, 高田 拓明, 村山 和隆, 永富 良一

    日本筋学会学術集会プログラム・抄録集　8回　144-144　2022/08

    Publisher: (一社)日本筋学会

    ISSN： 2433-975X

  2. Structural insights into the small GTPase specificity of the DOCK guanine nucleotide exchange factors

    Mutsuko Kukimoto-Niino, Kentaro Ihara, Kazutaka Murayama, Mikako Shirouzu

    Current Opinion in Structural Biology　71　249-258　2021/12/01

    Publisher: Elsevier Ltd

    DOI： 10.1016/j.sbi.2021.08.001 　

    ISSN： 1879-033X 0959-440X

  3. The impact of intracellular aminopeptidase on C2C12 myoblast proliferation and differentiation. International-journal

    Shion Osana, Kazutaka Murayama, Ryoichi Nagatomi

    Biochemical and biophysical research communications　524　(3)　608-613　2020/04/09

    DOI： 10.1016/j.bbrc.2020.01.115 　

    More details Close

    The ubiquitin-proteasome pathway is essential for skeletal muscle growth and development. Proteasomes generate oligopeptides in the cytoplasm, and these peptides are considered to be rapidly degraded to amino acids by several intracellular aminopeptidases. However, the role of intracellular aminopeptidases in muscle growth remains unknown. In this study, therefore, we investigated the role of intracellular aminopeptidases in C2C12 myoblast proliferation and differentiation. Inhibition of intracellular aminopeptidases by Bestatin methyl ester (Bes-ME) decreased leucine and alanine aminopeptidase activity, and impaired proliferation and differentiation of C2C12 myoblasts. Furthermore, we observed that the inhibition of intracellular aminopeptidases reduced intracellular levels of amino acid and ATP level, and suppressed the phosphorylation of the mTOR pathway. These results suggested that intracellular aminopeptidases affect C2C12 myoblast proliferation and differentiation via mTOR pathway; however, further studies are required to clarify the role of aminopeptidase in skeletal muscle.

  4. Inhibition of leucine aminopeptidase affects myocyte proliferation and differentiation

    Shion Osana, Kazutaka Murayama, Naoki Suzuki, Hiroaki Takada, Takahiro Kubota, Ryoichi Nagatomi

    FASEB JOURNAL　34　2020/04

    DOI： 10.1096/fasebj.2020.34.s1.02075 　

    ISSN： 0892-6638

    eISSN： 1530-6860

  5. コリン型リゾプラズマローゲン特異的ホスホリパーゼDの基質認識におけるPhe211およびTyr258の役割

    河原光希, 小山貴之, 酒瀬川信一, 村山和隆, 杉森大助, 杉森大助

    日本生物工学会大会講演要旨集　70th　200-200　2018/08/07

    Publisher: (公社)日本生物工学会

  6. 高純度組換え体ラット膵臓カルボキシペプチダーゼ製剤の作出

    前田浩, 村山和隆, 渡邉君子, 後藤昌史, 山形洋平

    日本農芸化学会大会講演要旨集(Web)　2018　2018

    ISSN： 2186-7976

  7. 工業グレードへスケールアップした新規中性プロテアーゼの膵島分離における安全性及び有効性に関する検証

    猪村武弘, 前田浩, 山形洋平, 村山和隆, 渡邉君子, 稲垣明子, 里見進, 後藤昌史, 後藤昌史

    日本膵・膵島移植研究会プログラム・抄録集　45th　2018

  8. 膵島分離に用いる新規中性プロテアーゼ2種の品質評価に有用な特異的基質の同定

    前田浩, 猪村武弘, 村山和隆, 渡邉君子, 後藤昌史, 後藤昌史, 山形洋平

    日本膵・膵島移植研究会プログラム・抄録集　45th　2018

  9. ドナー膵組織のマトリックス組成に対応するテーラーメイド型膵島分離法の確立へ向けた試み

    宮崎勇希, 猪村武弘, 村山和隆, 山形洋平, 前田浩, 渡邉君子, 稲垣明子, 宮城重人, 内藤剛, 海野倫明, 亀井尚, 里見進, 後藤昌史, 後藤昌史

    日本膵・膵島移植研究会プログラム・抄録集　45th　2018

  10. 細胞分離酵素剤が分離膵島へ及ぼす影響に関する検証

    宮崎勇希, 猪村武弘, 山形洋平, 山形洋平, 前田浩, 前田浩, 村山和隆, 渡邉君子, 稲垣明子, 五十嵐康宏, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    再生医療　16　2017

    ISSN： 1347-7919

  11. 膵島分離に用いるClostridium histolyticum由来の臨床用組換え活性型clostripainの調製

    前田浩, 村山和隆, 渡邉君子, 後藤昌史, 山形洋平

    日本農芸化学会大会講演要旨集(Web)　2017　2017

    ISSN： 2186-7976

  12. 膵島分離工程における膵島障害因子の検討

    宮崎勇希, 猪村武弘, 山形洋平, 前田浩, 村山和隆, 渡邉君子, 稲垣明子, 五十嵐康宏, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    日本膵・膵島移植研究会プログラム・抄録集　44th　2017

  13. 東北大学における次世代膵島移植確立へ向けた技術革新

    後藤昌史, 後藤昌史, 稲垣明子, 山形洋平, 村山和隆, 渡邉君子, 前田浩, 猪村武弘, 五十嵐康宏, 植松智海, 宮崎勇希, 水井崇浩, 戸子台和哲, 宮城重人, 角昭一郎, 藤盛啓成, 大内憲明, 里見進

    日本膵・膵島移植研究会プログラム・抄録集　44th　2017

  14. The influence of dissociation enzymes on isolated islets during pancreatic islet isolation procedures

    Yuki Miyazaki, Takehiro Imura, Youhei Yamagata, Hiroshi Maeda, Kazutaka Murayama, Kimiko Watanabe, Akiko Inagaki, Yasuhiro Igarashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    TRANSPLANTATION　100　(7)　S59-S59　2016/07

    ISSN： 0041-1337

    eISSN： 1534-6080

  15. The investigation on target matrix of collagenase G for achieving tailor-made islet isolation

    Satoru Yoshida, Youhei Yamagata, Kanako Nakagawa, Kazuhisa Maeda, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Akiko Inagaki, Yasuhiro Igarashi, Shigehito Miyagi, Kazuo Ohashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    TRANSPLANTATION　100　(7)　S849-S849　2016/07

    ISSN： 0041-1337

    eISSN： 1534-6080

  16. PROOF OF CONCEPT FOR THE CLINICAL APPLICATION OF ANIMAL COMPONENT FREE RECOMBINANT COLLAGENASE FOR ISOLATING PANCREATIC ISLETS.

    Masafumi Goto, Andrew Friberg, Magnus Stahle, Takehiro Imura, Youhei Yamagata, Kimiko Watanabe, Kazutaka Murayama, Akiko Inagaki, Yasuhiro Igarashi, Susumu Satomi, Olle Korsgren

    TRANSPLANTATION　99　(11)　S80-S80　2015/11

    ISSN： 0041-1337

    eISSN： 1534-6080

  17. CHARACTERIZATION AND OPTIMIZATION OF ENZYME COMPONENTS FOR HEPATOCYTE ISOLATION

    Satoru Yoshida, Youhei Yamagata, Kanako Nakagawa, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Yasuhiro Igarashi, Akiko Inagaki, Shigehito Miyagi, Kazuo Ohashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    TRANSPLANTATION　99　(11)　S253-S253　2015/11

    ISSN： 0041-1337

    eISSN： 1534-6080

  18. Characterization and optimization of enzyme components for hepatocyte isolation

    Satoru Yoshida, Youhei Yamagata, Kanako Nakagawa, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Yasuhiro Igarashi, Akiko Inagaki, Shigehito Miyagi, Kazuo Ohashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    XENOTRANSPLANTATION　22　S154-S154　2015/11

    ISSN： 0908-665X

    eISSN： 1399-3089

  19. THE INFLUENCE OF THE SYNERGISTIC EFFECT OF NEUTRAL PROTEASE DERIVED FROM CLOSTRIDIUM HISTOLYTICUM AND CLOSTRIPAIN ON THE HEPATOCYTE ISOLATION.

    Satoru Yoshida, Youhei Yamagata, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Yasuhiro Igarashi, Akiko Inagaki, Shigehito Miyagi, Kazuo Ohashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    TRANSPLANTATION　99　(11)　S220-S220　2015/11

    ISSN： 0041-1337

    eISSN： 1534-6080

  20. The influence of the synergistic effect of neutral protease derived from clostridium histolyticum and clostripain on the hepatocyte isolation

    Satoru Yoshida, Youhei Yamagata, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Yasuhiro Igarashi, Akiko Inagaki, Shigehito Miyagi, Kazuo Ohashi, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    XENOTRANSPLANTATION　22　S132-S132　2015/11

    ISSN： 0908-665X

    eISSN： 1399-3089

  21. Proof of concept for the clinical application of animal component free recombinant collagenase for isolating pancreatic islets

    Masafumi Goto, Andrew Friberg, Magnus Stahle, Takehiro Imura, Youhei Yamagata, Kimiko Watanabe, Kazutaka Murayama, Akiko Inagaki, Yasuhiro Igarashi, Susumu Satomi, Olle Korsgren

    XENOTRANSPLANTATION　22　S50-S50　2015/11

    ISSN： 0908-665X

    eISSN： 1399-3089

  22. 2P-038 Heterologous expression and characterization of ethanolamine oxidase from Syncephalastrum racemosum

    Chonan Keisuke, Murayama Kazutaka, Sakasegawa Shin-ichi, Matsumoto Hideyuki, Sugimori Daisuke

    67　184-184　2015

    Publisher: 日本生物工学会

  23. (Secondary Publication) Collagenase H is crucial for isolation of rat pancreatic islets

    藤尾淳, 村山和隆, 山形洋平, 渡邉君子, 猪村武弘, 稲垣明子, 大林尚美, 大林尚美, 島弘季, 関口悟, 藤盛啓成, 五十嵐和彦, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    移植(Web)　50　(2-3)　2015

    ISSN： 2188-0034

  24. 膵島分離に用いるClostridium histolyticum由来の臨床用組換えneutral proteaseの調製と,新規特異的基質の設計

    前田浩, 前田浩, 村山和隆, 渡邉君子, 後藤昌史, 後藤昌史, 山形洋平, 山形洋平

    日本農芸化学会大会講演要旨集(Web)　2015　2015

    ISSN： 2186-7976

  25. 膵組織消化過程におけるコラゲナーゼの役割

    猪村武弘, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 前田浩, 前田浩, 稲垣明子, 五十嵐康宏, 五十嵐康宏, 後藤昌史, 後藤昌史

    日本膵・膵島移植研究会プログラム・抄録集　42nd　2015

  26. 新規膵島分離用酵素剤の臨床応用と今後の戦略

    後藤昌史, 後藤昌史, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 前田浩, 前田浩, 猪村武弘, 稲垣明子, 五十嵐康宏, 宮城重人, 戸子台和哲, 田頭真実, 藤盛啓成, KORSGREN Olle, 大内憲明, 里見進

    日本膵・膵島移植研究会プログラム・抄録集　42nd　2015

  27. Heme regulates unstructured region of transcription factor Bach2

    M. Matsui, K. Igarashi, K. Murayama, T. Matsui, M. Ikeda-Saito, T. Matsumoto

    JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY　19　S243-S243　2014/03

    ISSN： 0949-8257

    eISSN： 1432-1327

  28. 肝細胞分離用酵素剤の至適化に関する検討

    吉田諭, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 猪村武弘, 稲垣明子, 五十嵐康宏, 大橋一夫, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    Organ Biology　21　(3)　2014

    ISSN： 1340-5152

  29. 肝細胞分離におけるコラゲナーゼGの重要性

    吉田諭, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 猪村武弘, 稲垣明子, 五十嵐康宏, 大橋一夫, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    日本移植学会総会プログラム抄録集　50th　2014

  30. 新規膵島分離用酵素剤の開発

    田頭真実, 前田浩, 前田浩, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 猪村武弘, 稲垣明子, 五十嵐康宏, 藤盛啓成, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    日本移植学会総会プログラム抄録集　50th　2014

  31. 膵島移植を医療として確立するための技術革新

    後藤昌史, 後藤昌史, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 前田浩, 前田浩, 中川香奈子, 中川香奈子, 稲垣明子, 五十嵐康宏, 猪村武弘, 宮城重人, 武田郁央, 藤盛啓成, 大内憲明, 里見進

    日本膵・膵島移植研究会プログラム・抄録集　41st　2014

  32. 膵島分離におけるクロストリジウム由来中性プロテアーゼとクロストリパインの併用効果に関する検討

    田頭真実, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 前田浩, 前田浩, 猪村武弘, 稲垣明子, 五十嵐康宏, 藤盛啓成, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    日本膵・膵島移植研究会プログラム・抄録集　41st　2014

  33. タンパク質分解酵素ククミシン‐プロペプチド複合体の結晶構造

    外川内亜美, 村山和隆, 村山(加藤)美幸, 保坂俊彰, 伊東祐二, 横山茂之, 白水美香子, 有馬一成

    日本生化学会大会(Web)　87th　2P-118 (WEB ONLY)　2014

  34. The Influence of Collagen-III Expression on the Efficiency of Cell Isolation by Collagenase H

    Satoru Yoshida, Youhei Yamagata, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Yasuhiro Igarashi, Akiko Inagaki, Keisei Fujimori, Noriaki Ohuchi, Susumu Satomi, Masafumi Goto

    TRANSPLANTATION　96　(6)　S143-S143　2013/09

    ISSN： 0041-1337

    eISSN： 1534-6080

  35. Distinct Role of Collagenase Subtypes in the Isolation of Large Animal Pancreatic Islets

    Masafumi Goto, Youhei Yamagata, Kazutaka Murayama, Kimiko Watanabe, Takehiro Imura, Yasuhiro Igarashi, Akiko Inagaki, Hideyuki Yamaya, Keisei Fujimori, Susumu Satomi

    TRANSPLANTATION　96　(6)　S142-S142　2013/09

    ISSN： 0041-1337

    eISSN： 1534-6080

  36. 2P-055 Plasmalogen hydrolysis by Streptomyces albidoflavus phospholipase A_1 and estimation of mechanism of regioselective hydrolysis

    Sugimori Daisuke, Matsumoto Yusaku, Mineta Shingo, Murayama Kazutaka, Sakasegawa Shin-ich, Matsumoto Hideyuki

    65　117-117　2013

    Publisher: 日本生物工学会

  37. 肝細胞移植に必要な細胞分離用酵素成分の考察

    吉田諭, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 猪村武弘, 五十嵐康宏, 稲垣明子, 大橋一夫, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    日本組織移植学会雑誌　12　(1)　2013

    ISSN： 1347-6491

  38. 安全で高性能な膵島分離用酵素剤の開発

    後藤昌史, 山形洋平, 村山和隆, 渡邉君子, 前田浩, 稲垣明子, 五十嵐康宏, 藤森啓成, 中川香奈子, 猪村武弘, 里見進

    移植　48　2013

    ISSN： 0578-7947

  39. 細胞分離のCollagenase H至適化において対象組織が発現するコラーゲンIIIの意義

    吉田諭, 山形洋平, 山形洋平, 村山和隆, 渡邉君子, 猪村武弘, 稲垣明子, 五十嵐康宏, 藤盛啓成, 大橋一夫, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    移植　48　2013

    ISSN： 0578-7947

  40. 膵島分離におけるコラゲナーゼHの作用機序の解明および対象マトリックスの検討

    藤尾淳, 村山和隆, 山形洋平, 渡邉君子, 猪村武弘, 稲垣明子, 大林尚美, 大林尚美, 島弘季, 関口悟, 藤盛啓成, 五十嵐和彦, 大内憲明, 里見進, 後藤昌史, 後藤昌史

    日本膵・膵島移植研究会プログラム・抄録集　40th　2013

  41. ドナー膵臓に至適化するテーラーメード型膵島分離の実現へ向けて

    後藤昌史, 後藤昌史, 山形洋平, 村山和隆, 渡邉君子, 猪村武弘, 稲垣明子, 五十嵐康宏, 山谷英之, 関口悟, 藤盛啓成, 里見進

    日本膵・膵島移植研究会プログラム・抄録集　40th　2013

  42. メロン由来セリンプロテアーゼククミシンの結晶構造

    村山和隆, 村山和隆, 村山(加藤)美幸, 保坂俊彰, 外川内亜美, 横山茂之, 有馬一成, 白水美香子

    日本結晶学会年会講演要旨集　2012　2012

  43. C.histolyticum由来コラゲナーゼHの溶液構造の解析

    大林尚美, 大林尚美, 松本崇, 島弘季, 後藤昌史, 後藤昌史, 渡邉君子, 五十嵐和彦, 山形洋平, 村山和隆

    日本薬学会年会要旨集　132nd　(4)　2012

    ISSN： 0918-9823

  44. リコンビナントタイプ新規膵島分離用酵素剤による分離膵島に起因する炎症性メディエーターの制御

    後藤昌史, 山形洋平, 渡邉君子, 村山和隆, 猪村武弘, 稲垣明子, 山谷英之, 関口悟, 藤盛啓成, 黒川良望, 里見進

    日本外科学会雑誌　113　2012

    ISSN： 0301-4894

  45. Crystal Structures of the Armadillo Repeat Domain of Adenomatous Polyposis Coli and Its Complex with the Tyrosine-Rich Domain of Sam68 (vol 19, pg 1496, 2011)

    Ella Czarina Morishita, Kazutaka Murayama, Miyuki Kato-Murayama, Yoshiko Ishizuka-Katsura, Yuri Tomabechi, Tomoatsu Hayashi, Takaho Terada, Noriko Handa, Mikako Shirouzu, Tetsu Akiyama, Shigeyuki Yokoyama

    STRUCTURE　19　(12)　1896-1896　2011/12

    DOI： 10.1016/j.str.2011.11.010 　

    ISSN： 0969-2126

  46. Crystal Structures of Resorcin[4]arene and Tetramethylated Resorcin[4]arene Complexes Incorporating L-Carnitine through Cation-π Interaction

    FUJISAWA Ikuhide, TAKEUCHI Daiki, KATO Ryo, MURAYAMA Kazutaka, AOKI Katsuyuki

    Bulletin of the Chemical Society of Japan　84　(10)　1133-1135　2011/10/15

    Publisher: Chemical Society of Japan

    ISSN： 0009-2673

  47. Clostridium由来コラゲナーゼの高次構造変化におけるカルシウムイオンの影響

    大林尚美, 大林尚美, 後藤昌史, 後藤昌史, 渡邉君子, 山形洋平, 村山和隆

    日本蛋白質科学会年会プログラム・要旨集　11th　2011

  48. C.histolyticum由来コラゲナーゼのCa2+による高次構造安定化の解析

    大林尚美, 大林尚美, 後藤昌史, 後藤昌史, 渡邉君子, 山形洋平, 村山和隆

    日本薬学会年会要旨集　131st　(4)　2011

    ISSN： 0918-9823

  49. 現状における臨床グレードの膵島分離用酵素剤の検証

    後藤昌史, 後藤昌史, 山形洋平, 渡邉君子, 村山和隆, 猪村武弘, 稲垣明子, 山谷英之, 小川則彦, 藤盛啓成, 黒川良望, 里見進

    移植　45　2010

    ISSN： 0578-7947

  50. 安全で高性能な新規膵島分離用酵素剤の開発

    後藤昌史, 後藤昌史, 山形洋平, 渡邉君子, 村山和隆, 猪村武弘, 稲垣明子, 山谷英之, 小川則彦, 藤盛啓成, 黒川良望, 里見進

    移植　45　2010

    ISSN： 0578-7947

  51. 膵島分離におけるTLA活性の意義に関する検討

    後藤昌史, 後藤昌史, 山形洋平, 渡邉君子, 村山和隆, 猪村武弘, 稲垣明子, 山谷英之, 黒川良望, 里見進

    Organ Biology　17　(2)　2010

    ISSN： 1340-5152

  52. 臨床再開へ向けた膵島分離用酵素剤の比較検討

    後藤昌史, 後藤昌史, 山形洋平, 渡邉君子, 村山和隆, 猪村武弘, 稲垣明子, 山谷英之, 小川則彦, 藤盛啓成, 黒川良望, 里見進

    日本膵・膵島移植研究会プログラム・抄録集　37th　2010

  53. 膵島分離用酵素剤の活性評価システムの構築

    後藤昌史, 後藤昌史, 山形洋平, 國定孝夫, 間塚風介, 矢内耕二, 永里敏秋, 渡邉君子, 村山和隆, 猪村武弘, 藤盛啓成, 黒川良望, 里見進

    日本膵・膵島移植研究会プログラム・抄録集　37th　2010

  54. 2Ep04 Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme from Thermus thermophilus HB8

    ARAI Ryoichi, MURAYAMA Kazutaka, UCHIKUBO-KAMO Tomomi, NISHIMOTO Madoka, TOYAMA Mitsutoshi, KURAMITSU Seiki, TERADA Takaho, SHIROUZU Mikako, YOKOYAMA Shigeyuki

    21　62-62　2009/08/25

    Publisher: 社団法人日本生物工学会

  55. ヨードチロシンの部位特異的導入と長波長X線を用いた単波長異常分散法による結晶構造解析

    村山和隆, 坂本健作

    日本結晶学会誌　51　(4)　251-257　2009/08

    DOI： 10.5940/jcrsj.51.251 　

  56. 高度好熱菌由来アセチルトランスフェラーゼTTHA1799の結晶構造

    村山和隆, 村山和隆, 村山(加藤)美幸, 寺田貴帆, 竹本千重, 白水美香子, 横山茂之, 横山茂之

    PFシンポジウム要旨集　25th　2008

  57. アポトーシス調節因子Bak-1の結晶構造解析

    WANG H, 竹本千重, 岸下誠一郎, 内窪友美, 村山和隆, 村山和隆, 寺田貴帆, 田仲昭子, 菅野純夫, CHEN Lirong, LIU Zhi-Jie, WANG Bi-Cheng, 白水美香子, 横山茂之, 横山茂之

    高度好熱菌丸ごと一匹プロジェクト 第6回連携研究会 理研シンポジウム 平成19年　2007

  58. リボソームと翻訳伸長因子の相互作用についての構造生物学的考察

    竹本千重, CONNELL S R, WILSON D N, WANG H., 村山和隆, 村山和隆, 寺田貴帆, 白水美香子, FUCINI P, SPAHN C M T, 横山茂之, 横山茂之

    高度好熱菌丸ごと一匹プロジェクト 第6回連携研究会 理研シンポジウム 平成19年　2007

  59. タンパク質結晶化支援データベースシステムの開発

    赤坂領吾, 竹本千重, 内窪友美, 西野綾, 村山和隆, 村山和隆, 寺田貴帆, 白水美香子, 横山茂之, 横山茂之

    生化学　2007

    ISSN： 0037-1017

  60. AdipoR1とAPPL1の相互作用解析

    田辺弘明, 樋野展正, 保坂俊彰, 村山和隆, 山内敏正, 門脇孝, 坂本健作, 寺田貴帆, 白水美香子, 横山茂之

    生化学　2P-0210　2007

    ISSN： 0037-1017

  61. 低分子量Ｇタンパク質を介したシグナル伝達に関わるタンパク質の構造と機能

    白水美香子, 村山和隆, 新野-柊元睦子, 嶋田睦, 横山茂之

    実験医学　24　(17)　2601-2605　2006/11

    Publisher: 羊土社

  62. 好熱菌tmRNA-tRNAドメインの結晶構造解析

    別所義隆, 柴田理恵, 村山和隆, 村山和隆, 関根俊一, 関根俊一, 東島今日子, 竹本千重, 白水美香子, 倉光成紀, 倉光成紀, 横山茂之, 横山茂之

    RNAミーティング　7th　2005

  63. 異常分散効果を用いたタンパク質の高速・大量解析

    村山和隆

    バイオインダストリー　21　(11)　58-62　2004/11

    Publisher: シーエムシー出版

    ISSN： 0910-6545

Show all ︎Show first 5

Books and Other Publications 2

  1. Metal Ions in Life Sciences vol.10

    Katsuyuki Aoki, Kazutaka Murayama

    Springer Science　2011

  2. 遺伝子工学集中マスター

    山本雅, 仙波憲太郎

    羊土社　2006/12

Research Projects 10

  1. Contribution of post-proteolytic pathways to skeletal muscle volume

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (A)

    Institution: Tohoku University

    2024/04/01 - 2027/03/31

  2. The role of post-proteolytic aminopeptidases in skeletal muscle homeostasis

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (A)

    Institution: Tohoku University

    2021/04/05 - 2024/03/31

  3. Development of a basis for establishing the ultimate transplantation medicine that does not require the administration of immunosuppressive drugs

    Goto Masafumi

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (A)

    Institution: Tohoku University

    2018/04/01 - 2022/03/31

    More details Close

    This study was conducted to establish the basis of transplantation medicine that does not require immunosuppressants by combining a new transplantation method to subcutaneous space, which is an ideal transplant site, with an immunoisolated cell device. As a result, it has been clarified that we could cure diabetes for more than 6 months without need of immunosuppressants even in a rat diabetic model, by implanting a gelatin hydrogel nonwoven fabric (GHNF) into the subcutaneous space as pre-treatment, then replacing it with pancreatic islets encapsulated in a novel immunoisolated cell device consisting of modified polyvinyl alcohol. It was also revealed that the dramatic effect of GHNF is due not only to the construction of new blood vessels but also to the compensation of various extracellular matrices and various growth factors derived from host cells (IGF-2, HGF, etc.).

  4. Contribution of protein recycling system for the maintenance of skeletal muscle mass

    Nagatomi Ryoichi

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (A)

    Institution: Tohoku University

    2018/04/01 - 2021/03/31

    More details Close

    Proteolysis has long been considered deleterious to skeletal muscle. Recent studies, however, have identified that impaired proteolytic function leads to loss instead of an increase in skeletal muscle mass. Dysfunction in the proteasome-dependent proteolytic pathway in skeletal muscle induced more significant loss or impaired development than dysfunction in the autophagy pathway. Although we failed to detect the recycling of degradation derived amino acids for de-novo protein synthesis, we found the induction of various aminopeptidases linked to the proteasome-dependent proteolytic pathway. Each aminopeptidase in cultured myoblasts demonstrated essential roles, such as the regulations of ATP concentration, cell cycle and initiation of differentiation, and determination of polarity and structure of myotubes. Although further studies are required to elucidate the underlying mechanisms, we could demonstrate the essential roles of post-proteolytic aminopeptidases in developing myoblasts.

  5. Establishment of next-generation diabetes treatment by construction of tailor-made cell isolation system

    Goto Masafumi

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (B)

    Institution: Tohoku University

    2015/04/01 - 2019/03/31

    More details Close

    This study was conducted to establish the basis of "tailor-made islet isolation method" that can correspond to the extracellular matrix component of donor pancreatic tissues. As a result, it has been clarified that the specific target substrates of collagenase G which have not been identified until now are collagens IV and V, and by combining it with the knowledge about the target substrates of collagenase H which has already been identified by our team, it has been reported that it is possible to establish a tailor-made islet isolation method for specific donor species by using animal models. Regarding the neutral proteases, we have revealed that laminin and fibronectin are the main target matrices, and we succeeded in identifying the cleavage epitopes of each of the two newly constructed neutral proteases (ChNP and Clostripain).

  6. Elucidation of regulatory mechanism of RhoGEF by multidomains cooperation

    Kukimoto Mutsuko

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Institute of Physical and Chemical Research

    2015/04/01 - 2018/03/31

    More details Close

    In this study, we aimed to elucidate the activation regulation mechanism of RhoGEF proteins by GEF domain and other functional domains by analyzing their structure in full length or multidomain state. By dynamic light scattering and ultracentrifugation analysis, we found that intersectin 2 has multiple SH3 domains and DH-PH domains connected by a flexible loop, and acquires the structural freedom as a whole molecule. We also found that DOCK5 forms a stable complex with the regulatory protein ELMO1, takes up an extended structure, and binds to Rac1 on the side of the molecule. Finally, X-ray crystal structure analysis revealed structural changes of the DOCK7 DHR-2 domain in G protein binding.

  7. Elucidation of substrate recognition of choline lysoplasmalogen-specific phospholipase D

    Sugimori Daisuke, MURAYAMA Kazutaka

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Fukushima University

    2015/04/01 - 2018/03/31

    More details Close

    Choline lysoplasmalogen-specific phospholipase D (LyPlsCho-PLD) is an enzyme that catalyzes the hydrolytic cleavage of the phosphoester bond of LyPls, releasing choline and lysoplasmenic acid. LyPlsCho-PLD exhibited weak activity toward LysoPAF. Our goal is to elucidate the substrate recognition mechanism of LyPlsCho-PLD. Based on the homology-modeled structure of LyPls-PLD and the docking model with substrate analog, amino acid residues predicted to interact with the head group and sn-1-alkenyl ether chain were substituted by site-directed mutagenesis. The princial conclusions of the study by mutation analysis and kinetics were as follows: 1) M71, N173 and F211 of LyPlsCho-PLD may be involved in the recognition of sn-1 alkenyl ether chain of LyPlsCho. F211 and W282 may take part in substrate binding and reaction products release (=k+2). 2) F211A, I, L, and C variants remarkably altered in the substrate preference (LysoPAF >> LyPlsCho) while maintaining the high activity.

  8. Regulation of Bach2 intrinsically disordered region by ligand

    MURAYAMA Kazutaka, MUTO Akihiko, MATSUI Miki

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (C)

    Institution: Tohoku University

    2012/04/01 - 2015/03/31

    More details Close

    Bach2 plays an important role in the transcriptional process. Bach2 includes long intrinsically disordered regions. We prepared the region of 331-520 to investigate its biophysical properties. Spectroscopic measurements revealed that Bach2(331-520) is intrinsically disordered region, in which heme binds. SAXS and dynamic light scattering mesurements indicated that heme binding form of Bach2(331-520) is unstabler than the non heme binding form and the structure will be more compact. Our results showed the first example of the heme binding protein which is (1) intrinsically disordered protein/region, (2) indicates structural change by heme binding.

  9. Biomedical engineering approach to establish a new evaluation system for osteoconductivity by focusing on the protein adsorption properties to biomaterials

    KANETAKA Hiroyasu, SASAKI Keiichi, SHIMIZU Yoshinaka, KUDO Tada-aki, KAWASHITA Masakazu, MURAYAMA Kazutaka

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Challenging Exploratory Research

    Institution: Tohoku University

    2012/04/01 - 2014/03/31

    More details Close

    The aim of this study was to establish a new evaluation system for osteoconductivity by focusing on the protein adsorption properties to biomaterials. First, we revealed the difference in the three-dimensional conformational status of the protein on the surface of such osteoconductive biomaterials as hydroxyapatite, as well as the amount of adsorption, concerning the adsorption behavior of serum proteins. Next, by revealing the correlation between the proliferative capacity of mouse pre-osteoblastic cell line MC3T3-E1 and protein adsorption properties on the material, the possibility of a new evaluation system for osteoconductivity was investigated.

  10. Regulation of immune cell responses by heme

    IGARASHI Kazuhiko, MOTOHASHI Hozumi, MUTO Akihiko, KATOH Yasutake, MURAYAMA Kazutaka

    Offer Organization: Japan Society for the Promotion of Science

    System: Grants-in-Aid for Scientific Research

    Category: Grant-in-Aid for Scientific Research (A)

    Institution: Tohoku University

    2009 - 2011

    More details Close

    The transcription factor Bach2 is required in B cells for the antibody class switch DNA recombination and somatic hypermutation. In this project, we have established that the prosthetic group heme binds directly to Bach2 to inhibits its DNA binding activity and to induce rapid turnover within cells. We also identified a domain-like structure within Bach2 that mediates the regulation by heme. Three cysteine residues within this domain were critical for the heme-Bach2 interaction. These results suggest that heme functions as a signaling molecule in B cells to regulate immune responses.

Show all Show first 5

Other 2

  1. 転写調節にかかわるタンパク質ゆらぎのヘムによる制御

    More details Close

    Bachタンパク質は酸化ストレス応答や液性免疫など医学的に重要な機能を有し、その生物学的側面からは研究が進んでいる。しかしながら、タンパク質の分子機構の解明に重要な物理化学的側面(特に構造)には手がつけられていない状況であることより、「やわらかいタンパク質」としてのBachタンパク質の性質とヘム結合との関連に注目した機能の解明を行なう。

  2. アカデミアのTR拠点が創出する膵島移植確立のための戦略的アプローチ

    More details Close

    本開発研究は、膵島移植をあらゆる細胞療法の雛形として、安全で高性能な細胞分離用酵素剤のProof of Concept (POC) を確立する事を第一義的な目標と定めている。そのため、現在開発中の新規酵素剤を臨床グレードに引き上げることを目的とし、GMP化・高性能化・テーラーメード化を可能とする諸技術の構築を目指していく。開発酵素剤のPOC取得に際しては、東北大学未来医工学治療開発センターを拠点に効率よく臨床試験を進めていき、世界をリードする日本発の細胞分離酵素剤を確立することを目指していく。