Updated on 2024/10/02

Information

 

写真a

 
INABA KENJI
 
Organization
Medical Institute of Bioregulation Department of Molecular and Structural Biology Professor
Graduate School of Systems Life Sciences Department of Systems Life Sciences(Joint Appointment)
Graduate School of Medical Sciences Department of Medical Sciences(Joint Appointment)
Title
Professor
Contact information
メールアドレス
Tel
0926426968

Degree

  • Ph.D

Research History

  • 1998.4-2001.11 日本学術振興会特別研究員PD 2001.12-2005.3 科学技術振興機構さきがけ21専任研究員 2005.4-2006.10 科学技術振興機構CREST研究員

    1998.4-2001.11 日本学術振興会特別研究員PD 2001.12-2005.3 科学技術振興機構さきがけ21専任研究員 2005.4-2006.10 科学技術振興機構CREST研究員

  • 東北大学多元物質科学研究所(2013年4月〜2024年3月)

Research Interests・Research Keywords

  • Research theme:Molecular and structural basis of protein quality control systems in cell

    Keyword:protein quality control, cryo-EM, cell imaging, zinc, calcium, redox

    Research period: 2000.6 - 2034.1

Awards

  • 日本学術振興会賞

    2011.1   日本学術振興会  

  • 日本分子生物学会三菱化学奨励賞

    2009.12  

  • 文部科学大臣表彰若手科学者賞

    2009.4  

Papers

  • Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport Reviewed International journal

    Watanabe S, Kise, Y., Yonezawa, K., Inoue, M., Shimizu, N., Nureki, O. and Inaba, K

    Nature Communications   15   2404   2024.3

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1038/s41467-024-46747-1

    Other Link: https://www.nature.com/articles/s41467-024-46747-1

  • Ca<sup>2+</sup>-driven PDIA6 phase separation to ensure proinsulin quality control

    Young-Ho Lee, Tomohide Saio, Mai Watabe, Motonori Matsusaki, Shingo Kanemura, Yuxi Lin, Taro Mannen, Tsubura Kuramochi, Katsuya Iuchi, Michiko Tajiri, Kotono Suzuki, Yan Li, Yunseok Heo, Yuka Kamada, Kenta Arai, Mayuko Hashimoto, Satoshi Ninagawa, Yoshikazu Hattori, Hiroyuki Kumeta, Airu Takeuchi, Hiroya Abe, Eiichiro Mori, Takahiro Muraoka, Tsukasa Okiyoneda, Satoko Akashi, Michele Vendruscolo, Kenji Inaba, Masaki Okumura

    2024.7

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    Publisher:Cold Spring Harbor Laboratory  

    Abstract

    The endoplasmic reticulum (ER) plays key roles in protein quality control<sup>1,2</sup>and dynamic Ca<sup>2+</sup>storage<sup>3,4</sup>in eukaryotic cells. However, the protein homeostasis (proteostasis) system that regulates these ER functions is still incompletely characterised. Previous study revealed the importance of oligomerization in the function PDIA1, an ER-resident disulfide isomerase and molecular chaperone, regulates oligomeric states in accordance with client folding<sup>5</sup>. This result suggests that at least some of the 20 members of other PDI family may undergo regulated self-assembly in order to optimally function. Here, we show that Ca<sup>2+</sup>triggers the phase separation of PDIA6 into liquid-like condensates. In contrast to the condensation mechanism observed for proteins containing low-complexity domains, our results indicate that transient but specific electrostatic interactions occur between the first and the third folded thioredoxin-like domains of PDIA6. We further show that the Ca<sup>2+</sup>-driven condensation of PDIA6 recruits PDIA3 and proinsulin, thus increasing their local concentrations. This process results in the 30-fold enhancement of proinsulin folding and in the inhibition of proinsulin aggregation. Our findings shed light on a condensation-driven Ca<sup>2+</sup>-mediated proteostasis cascade in the ER by revealing how the efficiency of the protein folding process can be enhanced within quality control granules.

    DOI: 10.1101/2024.07.30.605722

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  • Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms Invited Reviewed International journal

    Bui, H.B. and Inaba, K.

    International Journal of Molecular Sciences   2024.3

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.3390/ijms25053045

    Other Link: https://www.mdpi.com/1422-0067/25/5/3045

  • Diselenide-bond replacement of the external disulfide bond of insulin increases its oligomerization leading to sustained activity Invited Reviewed International journal

    Arai, K., Okumura, M., Lee, Y.-H., Katayama, H., Mizutani, K., Lin, Y., Prak, S.-Y., Sawada, K., Toyoda, M., Hojo, H., Inaba, K., Iwaoka, M.

    Communications Chemistry   6   258   2023.11

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1038/s42004-023-01056-4

  • Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus Reviewed International journal

    Han, Ba Bui, Watanabe, S, Nomura, N, Liu, K, Uemura, T, Inoue, M, Tsutsumi, A, Fujita, H, Kinoshita, K. Kato, Y, Iwata, S, Kikkawa, M, Inaba, K

    Nature Communications   14 ( 1 )   4770 - 4770   2023.8

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    Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn2+ uptake into the Golgi apparatus
    Zinc ions (Zn2+) are vital to most cells, with the intracellular concentrations of Zn2+ being tightly regulated by multiple zinc transporters located at the plasma and organelle membranes. We herein present the 2.2-3.1 Å-resolution cryo-EM structures of a Golgi-localized human Zn2+/H+ antiporter ZnT7 (hZnT7) in Zn2+-bound and unbound forms. Cryo-EM analyses show that hZnT7 exists as a dimer via tight interactions in both the cytosolic and transmembrane (TM) domains of two protomers, each of which contains a single Zn2+-binding site in its TM domain. hZnT7 undergoes a TM-helix rearrangement to create a negatively charged cytosolic cavity for Zn2+ entry in the inward-facing conformation and widens the luminal cavity for Zn2+ release in the outward-facing conformation. An exceptionally long cytosolic histidine-rich loop characteristic of hZnT7 binds two Zn2+ ions, seemingly facilitating Zn2+ recruitment to the TM metal transport pathway. These structures permit mechanisms of hZnT7-mediated Zn2+ uptake into the Golgi to be proposed.

    DOI: 10.1038/s41467-023-40521-5

  • Supersulphides provide airway protection in viral and chronic lung diseases Reviewed

    Nature Communications   14 ( 1 )   4476   2023.7

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    Supersulphides provide airway protection in viral and chronic lung diseases
    Abstract

    Supersulphides are inorganic and organic sulphides with sulphur catenation with diverse physiological functions. Their synthesis is mainly mediated by mitochondrial cysteinyl-tRNA synthetase (CARS2) that functions as a principal cysteine persulphide synthase (CPERS). Here, we identify protective functions of supersulphides in viral airway infections (influenza and COVID-19), in aged lungs and in chronic lung diseases, including chronic obstructive pulmonary disease (COPD), idiopathic pulmonary fibrosis (IPF). We develop a method for breath supersulphur-omics and demonstrate that levels of exhaled supersulphides increase in people with COVID-19 infection and in a hamster model of SARS-CoV-2 infection. Lung damage and subsequent lethality that result from oxidative stress and inflammation in mouse models of COPD, IPF, and ageing were mitigated by endogenous supersulphides production by CARS2/CPERS or exogenous administration of the supersulphide donor glutathione trisulphide. We revealed a protective role of supersulphides in airways with various viral or chronic insults and demonstrated the potential of targeting supersulphides in lung disease.

    DOI: 10.1038/s41467-023-40182-4

  • The oxidative folding of nascent polypeptides provides electrons for reductive reactions in the ER Reviewed

    Kaiku Uegaki, Yuji Tokunaga, Michio Inoue, Seiji Takashima, Kenji Inaba, Koh Takeuchi, Ryo Ushioda, Kazuhiro Nagata

    Cell Reports   42 ( 7 )   112742 - 112742   2023.7

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    The oxidative folding of nascent polypeptides provides electrons for reductive reactions in the ER

    DOI: 10.1016/j.celrep.2023.112742

  • Zinc homeostasis governed by Golgi-resident ZnT family members regulates ERp44-mediated proteostasis at the ER-Golgi interface. Reviewed International journal

    Yuta Amagai, Momo Yamada, Toshiyuki Kowada, Tomomi Watanabe, Yuyin Du, Rong Liu, Satoshi Naramoto, Satoshi Watanabe, Junko Kyozuka, Tiziana Anelli, Tiziana Tempio, Roberto Sitia, Shin Mizukami, Kenji Inaba

    Nature communications   14 ( 1 )   2683 - 2683   2023.5

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    DOI: 10.1038/s41467-023-38397-6

  • Cryo-EM structures of human SPCA1a reveal the mechanism of Ca 2+ /Mn 2+ transport into the Golgi apparatus Reviewed

    Zhenghao Chen, Satoshi Watanabe, Hironori Hashida, Michio Inoue, Yasukazu Daigaku, Masahide Kikkawa, Kenji Inaba

    Science Advances   9 ( 9 )   eadd9742   2023.3

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    Cryo-EM structures of human SPCA1a reveal the mechanism of Ca 2+ /Mn 2+ transport into the Golgi apparatus
    Secretory pathway Ca 2+ /Mn 2+ ATPase 1 (SPCA1) actively transports cytosolic Ca 2+ and Mn 2+ into the Golgi lumen, playing a crucial role in cellular calcium and manganese homeostasis. Detrimental mutations of the ATP2C1 gene encoding SPCA1 cause Hailey-Hailey disease. Here, using nanobody/megabody technologies, we determined cryo–electron microscopy structures of human SPCA1a in the ATP and Ca 2+ /Mn 2+ -bound (E1-ATP) state and the metal-free phosphorylated (E2P) state at 3.1- to 3.3-Å resolutions. The structures revealed that Ca 2+ and Mn 2+ share the same metal ion–binding pocket with similar but notably different coordination geometries in the transmembrane domain, corresponding to the second Ca 2+ -binding site in sarco/endoplasmic reticulum Ca 2+ -ATPase (SERCA). In the E1-ATP to E2P transition, SPCA1a undergoes similar domain rearrangements to those of SERCA. Meanwhile, SPCA1a shows larger conformational and positional flexibility of the second and sixth transmembrane helices, possibly explaining its wider metal ion specificity. These structural findings illuminate the unique mechanisms of SPCA1a-mediated Ca 2+ /Mn 2+ transport.

    DOI: 10.1126/sciadv.add9742

  • Multiple sub-state structures of SERCA2b reveal conformational overlap at transitio steps during the catalytic cycle Reviewed International journal

    Zhang Y, Kobayashi C, Cai X, Watanabe S, Tsutsumi A, Kikkawa M, Sugita Y, Inaba K

    Cell Reports   41 ( 10 )   111760 - 111760   2022.12

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    Multiple sub-state structures of SERCA2b reveal conformational overlap at transitio steps during the catalytic cycle
    Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) pumps Ca2+ into the endoplasmic reticulum (ER). Herein, we present cryo-electron microscopy (EM) structures of three intermediates of SERCA2b: Ca2+-bound phosphorylated (E1P·2Ca2+) and Ca2+-unbound dephosphorylated (E2·Pi) intermediates and another between the E2P and E2·Pi states. Our cryo-EM analysis demonstrates that the E1P·2Ca2+ state exists in low abundance and preferentially transitions to an E2P-like structure by releasing Ca2+ and that the Ca2+ release gate subsequently undergoes stepwise closure during the dephosphorylation processes. Importantly, each intermediate adopts multiple sub-state structures including those like the next one in the catalytic series, indicating conformational overlap at transition steps, as further substantiated by atomistic molecular dynamic simulations of SERCA2b in a lipid bilayer. The present findings provide insight into how enzymes accelerate catalytic cycles.

    DOI: 10.1016/j.celrep.2022.111760

  • Structural basis of the conformational and functional regulation of human SERCA2b, the ubiquitous endoplasmic reticulum calcium pump Invited Reviewed

    Yuxia Zhang, Kenji Inaba

    BioEssays   e2200052   2022.5

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    Structural basis of the conformational and functional regulation of human SERCA2b, the ubiquitous endoplasmic reticulum calcium pump

  • Active Expression of Genes for Protein Modification Enzymes in Habu Venom Glands Reviewed

    Akiko Isomoto, Eiichi Shoguchi, Kanako Hisata, Jun Inoue, Yinrui Sun, Kenji Inaba, Noriyuki Satoh, Tomohisa Ogawa, Hiroki Shibata

    Toxins   14 ( 5 )   300   2022.4

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    Active Expression of Genes for Protein Modification Enzymes in Habu Venom Glands

  • Organelle-Level Labile Zn2+ Mapping Based on Targetable Fluorescent Sensors Reviewed

    Rong Liu, Toshiyuki Kowada, Yuyin Du, Yuta Amagai, Toshitaka Matsui, Kenji Inaba, Shin Mizukami

    ACS Sensors   7 ( 3 )   748 - 757   2022.3

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    Language:English   Publishing type:Research paper (scientific journal)  

    DOI: 10.1021/acssensors.1c02153

  • A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization. Reviewed International journal

    Masaki Okumura, Shingo Kanemura, Motonori Matsusaki, Misaki Kinoshita, Tomohide Saio, Dai Ito, Chihiro Hirayama, Hiroyuki Kumeta, Mai Watabe, Yuta Amagai, Young-Ho Lee, Shuji Akiyama, Kenji Inaba

    Structure (London, England : 1993)   29 ( 12 )   1357 - 1370   2021.12

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    A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization.
    P5, also known as PDIA6, is a PDI family member involved in the ER quality control. Here, we revealed that P5 dimerizes via a unique adhesive motif contained in the N-terminal thioredoxin-like domain. Unlike conventional leucine zipper motifs with leucine residues every two helical turns on ∼30-residue parallel α helices, this adhesive motif includes periodic repeats of leucine/valine residues at the third or fourth position spanning five helical turns on 15-residue anti-parallel α helices. The P5 dimerization interface is further stabilized by several reciprocal salt bridges and C-capping interactions between protomers. A monomeric P5 mutant with the impaired adhesive motif showed structural instability and local unfolding, and behaved as aberrant proteins that induce the ER stress response. Disassembly of P5 to monomers compromised its ability to inactivate IRE1α via intermolecular disulfide bond reduction and its Ca2+-dependent regulation of chaperone function in vitro. Thus, the leucine-valine adhesive motif supports structure and function of P5.

    DOI: 10.1016/j.str.2021.03.016

  • Cryo‐EM analysis provides new mechanistic insight into ATP binding to Ca2+‐ATPase SERCA2b Reviewed International journal

    40 ( 19 )   e108482   2021.10

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    DOI: 10.15252/embj.2021108482

  • Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding Invited Reviewed

    Motonori Matsusaki, Rina Okada, Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Mai Watabe, Hiroshi Yamaguchi, Tomohide Saio, Young-Ho Lee, Kenji Inaba, Masaki Okumura

    Biology   10 ( 11 )   1112 - 1112   2021.10

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    Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
    P5 is one of protein disulfide isomerase family proteins (PDIs) involved in endoplasmic reticulum (ER) protein quality control that assists oxidative folding, inhibits protein aggregation, and regulates the unfolded protein response. P5 reportedly interacts with other PDIs via intermolecular disulfide bonds in cultured cells, but it remains unclear whether complex formation between P5 and other PDIs is involved in regulating enzymatic and chaperone functions. Herein, we established the far-western blot method to detect non-covalent interactions between P5 and other PDIs and found that PDI and ERp72 are partner proteins of P5. The enzymatic activity of P5-mediated oxidative folding is up-regulated by PDI, while the chaperone activity of P5 is stimulated by ERp72. These findings shed light on the mechanism by which the complex formations among PDIs drive to synergistically accelerate protein folding and prevents aggregation. This knowledge has implications for understanding misfolding-related pathology.

    DOI: 10.3390/biology10111112

  • Ca2+ Regulates ERp57-Calnexin Complex Formation Invited Reviewed International journal

    Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Motonori Matsusaki, Kimiko Kuroki, Hiroshi Yamaguchi, Katsumi Maenaka, Young-Ho Lee, Kenji Inaba, Masaki Okumura

    Molecules   26 ( 10 )   2853 - 2853   2021.5

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    DOI: 10.3390/molecules26102853

  • Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation Reviewed

    Chihiro Hirayama, Kodai Machida, Kentaro Noi, Tadayoshi Murakawa, Masaki Okumura, Teru Ogura, Hiroaki Imataka, Kenji Inaba

    iScience   24 ( 4 )   102296 - 102296   2021.4

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    DOI: 10.1016/j.isci.2021.102296

  • Visualization of structural dynamics of protein disulfide isomerase enzymes in catalysis of oxidative folding and reductive unfolding. Invited Reviewed International journal

    Masaki Okumura, Kentaro Noi, Kenji Inaba

    Current opinion in structural biology   66   49 - 57   2021.2

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    DOI: 10.1016/j.sbi.2020.10.004

  • PDI family members as guides for client folding and assembly Invited Reviewed

    Shingo Kanemura, Motonori Matsusaki, Kenji Inaba, Masaki Okumura

    International Journal of Molecular Science   21 ( 24 )   9351   2020.12

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    PDI family members as guides for client folding and assembly

  • Antipsychotic olanzapine-induced misfolding of proinsulin in the endoplasmic reticulum accounts for atypical development of diabetes. Reviewed International journal

    Satoshi Ninagawa, Seiichiro Tada, Masaki Okumura, Kenta Inoguchi, Misaki Kinoshita, Shingo Kanemura, Koshi Imami, Hajime Umezawa, Tokiro Ishikawa, Robert B Mackin, Seiji Torii, Yasushi Ishihama, Kenji Inaba, Takayuki Anazawa, Takahiko Nagamine, Kazutoshi Mori

    eLife   9   2020.11

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    DOI: 10.7554/eLife.60970

  • Quantitative Imaging of Labile Zn2+ in the Golgi Apparatus Using a Localizable Small-Molecule Fluorescent Probe. Reviewed International journal

    Toshiyuki Kowada, Tomomi Watanabe, Yuta Amagai, Rong Liu, Momo Yamada, Hiroto Takahashi, Toshitaka Matsui, Kenji Inaba, Shin Mizukami

    Cell chemical biology   27 ( 12 )   1521 - 1531   2020.9

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    DOI: 10.1016/j.chembiol.2020.09.003

  • Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail. Reviewed International journal

    Yuxia Zhang, Michio Inoue, Akihisa Tsutsumi, Satoshi Watanabe, Tomohiro Nishizawa, Kazuhiro Nagata, Masahide Kikkawa, Kenji Inaba

    Science advances   6 ( 33 )   eabb0147   2020.8

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    DOI: 10.1126/sciadv.abb0147

  • Characterization of the ER-resident peroxidases GPx7 and GPx8 shows the higher oxidative activity of GPx7 and its linkage to oxidative protein folding Reviewed

    Shingo Kanemura, Elza Firdiani Sofia, Naoya Hirai, Masaki Okumura, Hiroshi Kadokura, Kenji Inaba

    Journal of Biological Chemistry   jbc.RA120.013607 - jbc.RA120.013607   2020.7

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    DOI: 10.1074/jbc.ra120.013607

  • Observing the nonvectorial yet cotranslational folding of a multidomain protein, LDL receptor, in the ER of mammalian cells. Reviewed International journal

    Hiroshi Kadokura, Yui Dazai, Yo Fukuda, Naoya Hirai, Orie Nakamura, Kenji Inaba

    Proceedings of the National Academy of Sciences of the United States of America   2020.6

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    DOI: 10.1073/pnas.2004606117

  • The protein disulfide isomerase family: from proteostasis to pathogenesis Reviewed

    Matsusaki, M, Kanemura, S, Kinoshita, M, Lee, Y.H, Inaba, K, Okumura, M

    Biochem. Biophys. Acta. General Subject   2020.1

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    The protein disulfide isomerase family: from proteostasis to pathogenesis

  • High-resolution crystal structure of Arabidopsis FLOWERING LOCUS T illuminates its phospholipid-binding site in flowering Reviewed

    Nakamura, Y, Lin, Y.-C, Watanabe, S, Liu, Y.C, Katsuyama, K, Kanehara, K, Inaba, K

    iScience   21   577 - 586   2019.10

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    High-resolution crystal structure of Arabidopsis FLOWERING LOCUS T illuminates its phospholipid-binding site in flowering

  • Structural basis of sarco/endoplasmic reticulum Ca2+-ATPase 2b regulation via transmembrane helix interplay Reviewed

    Inoue, M, Sakuta, N, Watanabe, S, Zhang, Y, Yoshikaie, K, Tanaka, Y, Ushioda, R, Kato, Y, Takagi, J, Tsukazaki, T, Nagata, K, Inaba, K

    Cell Reports   27 ( 4 )   1221 - 1230   2019.4

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    Structural basis of sarco/endoplasmic reticulum Ca2+-ATPase 2b regulation via transmembrane helix interplay

    DOI: 10.1016/j.celrep.2019.03.106

  • Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding Reviewed

    Okumura, M, Noi, K, Kanemura, S, Kinoshita, M, Saio, T, Inoue, Y, Hikima, T, Akiyama, S, Ogura, T, Inaba, K

    Nature Chemical Biology   15   499 - 509   2019.3

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    Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding

  • Zinc regulates ERp44-dependent protein quality control in the early secretory pathway Reviewed

    Watanabe S, Amagai Y, Sannino S, Tempio T, Anelli T, Harayama M, Masui S, Sorrentino I, Yamada M, Sitia R, Inaba K

    Nature Communications   10 ( 1 )   603   2019.2

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    Zinc regulates ERp44-dependent protein quality control in the early secretory pathway

  • Coupling effects of thiol and urea-type groups for promotion of oxidative protein folding Reviewed

    Okada, S, Matsusaki, M, Arai, K, Hidaka, Y, Inaba, K, Okumura, M, Muraoka, T

    Chem. Commun.   55 ( 6 )   759 - 762   2019.1

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    Coupling effects of thiol and urea-type groups for promotion of oxidative protein folding
    Coupling of thiol and urea-type-NHC(═X)NH2 (X = O or NH) groups is effective in promoting oxidative protein folding. In particular, a thiol compound coupled with a guanidyl (X = NH) group significantly accelerates the rates of folding processes and enhances the yields of native proteins.

    DOI: 10.1039/c8cc08657e

  • Methods to identify the substrates of thiol-disulfide oxidoreductases Reviewed

    Fujimoto, T, Inaba, K, Kadokura, H

    Protein Science   28 ( 1 )   30 - 40   2019.1

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    Methods to identify the substrates of thiol-disulfide oxidoreductases

  • Identification of the physiological substrates of PDIp, a pancreas-specific protein disulfide isomerase family member protein, from a mouse tissue Reviewed International journal

    Fujimoto, T, Nakamura, O, Saito, M, Tsuru, A, Matsumoto, M, Kohno, K, Inaba, K, Kdokura, H

    J. Biol. Chem.   293 ( 48 )   18421 - 18433   2018.11

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    Identification of the physiological substrates of PDIp, a pancreas-specific protein disulfide isomerase family member protein, from a mouse tissue
    About 20 members of the protein-disulfide isomerase (PDI) family are present in the endoplasmic reticulum of mammalian cells. They are thought to catalyze thiol-disulfide exchange reactions within secretory or membrane proteins to assist in their folding or to regulate their functions. PDIp is a PDI family member highly expressed in the pancreas and known to bind estrogen in vivo and in vitro However, the physiological functions of PDIp remained unclear. In this study, we set out to identify its physiological substrates. By combining acid quenching and thiol alkylation, we stabilized and purified the complexes formed between endogenous PDIp and its target proteins from the mouse pancreas. MS analysis of these complexes helped identify the disulfide-linked PDIp targets in vivo, revealing that PDIp interacts directly with a number of pancreatic digestive enzymes. Interestingly, when pancreatic elastase, one of the identified proteins, was expressed alone in cultured cells, its proenzyme formed disulfide-linked aggregates within cells. However, when pancreatic elastase was co-expressed with PDIp, the latter prevented the formation of these aggregates and enhanced the production and secretion of proelastase in a form that could be converted to an active enzyme upon trypsin treatment. These findings indicate that the main targets of PDIp are digestive enzymes and that PDIp plays an important role in the biosynthesis of a digestive enzyme by assisting with the proper folding of the proenzyme within cells.

    DOI: 10.1074/jbc.RA118.003694

  • Ero1-mediated reoxidation of PDI accelerates the folding of cone snail Reviewed

    O'Brien, H, Kanemura, S, Okumura, M, Baskin, P, Bandyopadhyay, P, Ellgaard, L, Inaba, K, Safavi-Hemami, H

    Int. J. Mol. Sci.   19 ( 11 )   E3418   2018.10

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    Ero1-mediated reoxidation of PDI accelerates the folding of cone snail

  • Characterization and optimization of two-chain folding pathways of insulin via native chain assembly Reviewed

    Arai, K, Takei, T, Shinozaki, R, Noguchi, M, Fujisawa, S, Katayama, H, Moroder, M, Ando, S, Okumura, M, Inaba, K, Hojo, H, Iwaoka, M

    Cummunications Chemistry   26   1 - 15   2018.5

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    Characterization and optimization of two-chain folding pathways of insulin via native chain assembly
    Until recently the total synthesis of insulin, with its characteristic heterodimeric structure crosslinked by two interchain and one intrachain disulfide (SS) bridge, remained largely an unsolved challenge. By optimizing the synthesis and directed disulfide crosslinking of the two chains, and by applying biomimetic monocomponent proinsulin approaches, efficient insulin syntheses have been realized. Here we report the optimization and characterisation of an alternative strategy, oxidative native chain assembly. In this method unprotected A- and B-chains assemble oxidatively under thermodynamic control to afford bovine pancreatic insulin in 39% yield. Folding is found to proceed predominantly via structured 1SS(star) and 2SS(star) intermediates with a common interchain Cys(A20)-Cys(B19) disulfide. These results suggest that native chain assembly, long considered inefficient, may represent a reasonable strategy to access insulin variants. This is supported by the synthesis of human insulin and human type-II relaxin in yields of up to 49 and 47%, respectively, although the application to human insulin Val(A16) variant is unsuccessful.

    DOI: 10.1038/s42004-018-0024-0

  • Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. Reviewed International journal

    Nature communications   8 ( 1 )   1177 - 1177   2017.10

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    DOI: 10.1038/s41467-017-01311-y

  • The Highly Dynamic Nature of ERdj5 Is Key to Efficient Elimination of Aberrant Protein Oligomers through ER-Associated Degradation Reviewed

    Ken-ichi Maegawa, Satoshi Watanabe, Kentaro Noi, Masaki Okumura, Yuta Amagai, Michio Inoue, Ryo Ushioda, Kazuhiro Nagata, Teru Ogura, Kenji Inaba

    STRUCTURE   25 ( 6 )   846 - +   2017.6

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    DOI: 10.1016/j.str.2017.04.001

  • Preparation of Selenoinsulin as a Long‐Lasting Insulin Analogue

    129 ( 20 )   5614 - 5618   2017.5

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    DOI: 10.1002/ange.201701654

  • Preparation of Selenoinsulin as a Long-Lasting Insulin Analogue Reviewed

    Kenta Arai, Toshiki Takei, Masaki Okumura, Satoshi Watanabe, Yuta Amagai, Yuya Asahina, Luis Moroder, Hironobu Hojo, Kenji Inaba, Michio Iwaoka

    ANGEWANDTE CHEMIE-INTERNATIONAL EDITION   56 ( 20 )   5522 - 5526   2017.5

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    DOI: 10.1002/anie.201701654

  • Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface Reviewed

    Satoshi Watanabe, Manami Harayama, Shingo Kanemura, Roberto Sitia, Kenji Inaba

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA   114 ( 16 )   E3224 - E3232   2017.4

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    DOI: 10.1073/pnas.1621426114

  • Human ER Oxidoreductin-1 alpha (Ero1 alpha) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase Reviewed

    Shingo Kanemura, Masaki Okumura, Katsuhide Yutani, Thomas Ramming, Takaaki Hikima, Christian Appenzeller-Herzog, Shuji Akiyama, Kenji Inaba

    JOURNAL OF BIOLOGICAL CHEMISTRY   291 ( 46 )   23952 - 23964   2016.11

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    DOI: 10.1074/jbc.M116.735662

  • Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5 Reviewed

    Ryo Ushioda, Akitoshi Miyamoto, Michio Inoue, Satoshi Watanabe, Masaki Okumura, Ken-ichi Maegawa, Kaiku Uegaki, Shohei Fujii, Yasuko Fukuda, Masataka Umitsu, Junichi Takagi, Kenji Inaba, Katsuhiko Mikoshiba, Kazuhiro Nagata

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA   113 ( 41 )   E6055 - E6063   2016.10

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    DOI: 10.1073/pnas.1605818113

  • Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover. Reviewed

    7   14 - 20   2016.4

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    8638

    DOI: 10.1016/j.redox.2015.11.004

  • The membrane topology of vitamin K epoxide reductase is conserved between human isoforms and the bacterial enzyme Reviewed

    Zhenbo Cao, Marcel van Lith, Lorna J. Mitchell, Marie Anne Pringle, Kenji Inaba, Neil J. Bulleid

    BIOCHEMICAL JOURNAL   473 ( 7 )   851 - 858   2016.4

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    DOI: 10.1042/BJ20151223

  • One-Dimensional Sliding of p53 Along DNA Is Accelerated in the Presence of Ca2+ or Mg2+ at Millimolar Concentrations Reviewed

    Agato Murata, Yuji Ito, Risa Kashima, Saori Kanbayashi, Kei Nanatani, Chihiro Igarashi, Masaki Okumura, Kenji Inaba, Takashi Tokino, Satoshi Takahashi, Kiyoto Kamagata

    JOURNAL OF MOLECULAR BIOLOGY   427 ( 16 )   2663 - 2678   2015.8

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    DOI: 10.1016/j.jmb.2015.06.016

  • A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1 Reviewed

    Thomas Ramming, Masaki Okumura, Shingo Kanemura, Sefer Baday, Julia Birk, Suzette Moes, Martin Spiess, Paul Jenoe, Simon Berneche, Kenji Inaba, Christian Appenzeller-Herzog

    FREE RADICAL BIOLOGY AND MEDICINE   83   361 - 372   2015.6

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    DOI: 10.1016/j.freeradbiomed.2015.02.011

  • Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum Invited Reviewed

    Masaki Okumura, Hiroshi Kadokura, Kenji Inaba

    FREE RADICAL BIOLOGY AND MEDICINE   83   314 - 322   2015.6

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    DOI: 10.1016/j.freeradbiomed.2015.02.010

  • Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer Reviewed

    Satoshi Watanabe, Takumi Kawashima, Yuichi Nishitani, Tamotsu Kanai, Takehiko Wada, Kenji Inaba, Haruyuki Atomi, Tadayuki Imanaka, Kunio Miki

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA   112 ( 25 )   7701 - 7706   2015.6

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    DOI: 10.1073/pnas.1503102112

  • Progressive quality control of secretory proteins in the early secretory compartment by ERp44 Reviewed

    Sara Sannino, Tiziana Anelli, Margherita Cortini, Shoji Masui, Massimo Degano, Claudio Fagioli, Kenji Inaba, Roberto Sitia

    JOURNAL OF CELL SCIENCE   127 ( 19 )   4260 - 4269   2014.10

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    DOI: 10.1242/jcs.153239

  • Inhibition of the Functional Interplay between Endoplasmic Reticulum (ER) Oxidoreduclin-1 alpha (Ero1 alpha) and Protein-disulfide Isomerase (PDI) by the Endocrine Disruptor Bisphenol A Reviewed

    Masaki Okumura, Hiroshi Kadokura, Shoko Hashimoto, Katsuhide Yutani, Shingo Kanemura, Takaaki Hikima, Yuji Hidaka, Len Ito, Kohei Shiba, Shoji Masui, Daiki Imai, Susumu Imaoka, Hiroshi Yamaguchi, Kenji Inaba

    JOURNAL OF BIOLOGICAL CHEMISTRY   289 ( 39 )   27004 - 27018   2014.9

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    DOI: 10.1074/jbc.M114.564104

  • Radically Different Thioredoxin Domain Arrangement of ERp46, an Efficient Disulfide Bond Introducer of the Mammalian PDI Family Reviewed

    Rieko Kojima, Masaki Okumura, Shoji Masui, Shingo Kanemura, Michio Inoue, Masatoshi Saiki, Hiroshi Yamaguchi, Takaaki Hikima, Mamoru Suzuki, Shuji Akiyama, Kenji Inaba

    STRUCTURE   22 ( 3 )   431 - 443   2014.3

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    DOI: 10.1016/j.str.2013.12.013

  • The α-proteobacteria Wolbachia pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria. Reviewed

    8 ( 11 )   e81440   2013.11

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    7800

    DOI: 10.1371/journal.pone.0081440

  • Identification of the redox partners of ERdj5/JPDI, a PDI family member, from an animal tissue Reviewed

    Hiroshi Kadokura, Michiko Saito, Akio Tsuru, Akira Hosoda, Takao Iwawaki, Kenji Inaba, Kenji Kohno

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   440 ( 2 )   245 - 250   2013.10

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    DOI: 10.1016/j.bbrc.2013.09.063

  • Structural basis of disulfide bond formation in the bacterial periplasm and ER. Invited Reviewed

    Kojima, R, Okumura, M, Inaba, K

    Encyclopedia of Life Science   10 ( 1002 )   2013.9

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    Structural basis of disulfide bond formation in the bacterial periplasm and ER.

  • A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly Reviewed

    Stefano Vavassori, Margherita Cortini, Shoji Masui, Sara Sannino, Tiziana Anelli, Imma R. Caserta, Claudio Fagioli, Maria F. Mossuto, Arianna Fornili, Eelco vanAnken, Massimo Degano, Kenji Inaba, Roberto Sitia

    Molecular Cell   50 ( 6 )   783 - 792   2013.6

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    DOI: 10.1016/j.molcel.2013.04.016

  • Bisphenol A induces a conformational change in protein disulfide isomerase. Reviewed

    Okumura, M, Hashimoto, S, Nawata, M, Yutani, K, Hikima, T, Hamada, D, Hidaka, Y, Ito, L, Shiba, K, Hosokawa, K, Inoue, T, Maekawa, S, Imaoka, S, Inaba, K, Yamaguchi, H

    Peptide Science   331 - 332   2013.6

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    Bisphenol A induces a conformational change in protein disulfide isomerase.
    7804

  • Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals Invited Reviewed

    Yoshimi Sato, Kenji Inaba

    FEBS JOURNAL   279 ( 13 )   2262 - 2271   2012.7

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    DOI: 10.1111/j.1742-4658.2012.08593.x

  • Structure, Mechanism, and Evolution of Ero1 Family Enzymes Invited Reviewed

    Kazutaka Araki, Kenji Inaba

    ANTIOXIDANTS & REDOX SIGNALING   16 ( 8 )   790 - 799   2012.4

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    DOI: 10.1089/ars.2011.4418

  • Molecular bases of cyclic and specific disulfide interchange between human Ero1 protein and protein-disulfide isomerase (PDI) Reviewed

    286 ( 18 )   16262 - 16271   2011.5

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    DOI: 10.1074/jbc.M111.231357

  • Structural Basis of an ERAD Pathway Mediated by the ER-Resident Protein Disulfide Reductase ERdj5 Reviewed

    Masatoshi Hagiwara, Ken-ichi Maegawa, Mamoru Suzuki, Ryo Ushioda, Kazutaka Araki, Yushi Matsumoto, Jun Hoseki, Kazuhiro Nagata, Kenji Inaba

    MOLECULAR CELL   41 ( 4 )   432 - 444   2011.2

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    DOI: 10.1016/j.molcel.2011.01.021

  • Homodimerization of Nemo-like kinase is essential for activation and nuclear localization Reviewed

    Shizuka Ishitani, Kenji Inaba, Kunihiro Matsumoto, Tohru Ishitani

    MOLECULAR BIOLOGY OF THE CELL   22 ( 2 )   266 - 277   2011.1

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    DOI: 10.1091/mbc.E10-07-0605

  • Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. Reviewed

    29 ( 19 )   3330 - 3343   2010.10

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    DOI: 10.1038/emboj.2010.222

  • Structural basis of protein disulfide bond generation in the cell Invited Reviewed

    Kenji Inaba

    GENES TO CELLS   15 ( 9 )   935 - 943   2010.9

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    DOI: 10.1111/j.1365-2443.2010.01434.x

  • Redox-Dependent Domain Rearrangement of Protein Disulfide Isomerase Coupled with Exposure of Its Substrate-Binding Hydrophobic Surface Reviewed

    Olivier Serve, Yukiko Kamiya, Aya Maeno, Michiko Nakano, Chiho Murakami, Hiroaki Sasakawa, Yoshiki Yamaguchi, Takushi Harada, Eiji Kurimoto, Maho Yagi-Utsumi, Takeshi Iguchi, Kenji Inaba, Jun Kikuchi, Osamu Asami, Tsutomu Kajino, Toshihiko Oka, Masayoshi Nakasako, Koichi Kato

    JOURNAL OF MOLECULAR BIOLOGY   396 ( 2 )   361 - 374   2010.2

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    DOI: 10.1016/j.jmb.2009.11.049

  • Disulfide Bond Formation System in Escherichia coli Invited Reviewed

    Kenji Inaba

    JOURNAL OF BIOCHEMISTRY   146 ( 5 )   591 - 597   2009.11

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    DOI: 10.1093/jb/mvp102

  • タンパク質品質管理とレドックス制御 小胞体内在性ジスルフィド還元酵素ERdj5が促進するERAD経路の構造的基盤(Structural Basis of an ERAD pathway mediated by an ER-resident protein disuifide reductase, ERdj5)

    稲葉 謙次, 萩原 誠智, 前川 憲一, 鈴木 守, 潮田 亮, 寳関 淳, 永田 和宏

    日本生化学会大会プログラム・講演要旨集   82回   2S1a - 5   2009.9

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  • Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB Reviewed

    Kenji Inaba, Satoshi Murakami, Atsushi Nakagawa, Hiroka Iida, Mai Kinjo, Koreaki Ito, Mamoru Suzuki

    EMBO JOURNAL   28 ( 6 )   779 - 791   2009.3

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    DOI: 10.1038/emboj.2009.21

  • A Pair of Circularly Permutated PDZ Domains Control RseP, the S2P Family Intramembrane Protease of Escherichia coli Reviewed

    Kenji Inaba, Mamoru Suzuki, Ken-ichi Maegawa, Shuji Akiyama, Koreaki Ito, Yoshinori Akiyama

    JOURNAL OF BIOLOGICAL CHEMISTRY   283 ( 50 )   35042 - 35052   2008.12

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    DOI: 10.1074/jbc.M806603200

  • The disulfide bond formation (Dsb) system Reviewed

    Koreaki Ito, Kenji Inaba

    CURRENT OPINION IN STRUCTURAL BIOLOGY   18 ( 4 )   450 - 458   2008.8

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    DOI: 10.1016/j.sbi.2008.02.002

  • Protein disulfide bond generation in Escherichia coli DsbB-DsbA Invited Reviewed

    Kenji Inaba

    JOURNAL OF SYNCHROTRON RADIATION   15 ( Pt 3 )   199 - 201   2008.5

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    DOI: 10.1107/S090904950706061X

  • Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine. Invited Reviewed

    Inaba K, Ito K

    Biochimica et biophysica acta   1783 ( 4 )   520 - 529   2008.4

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    Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine.
    All organisms possess specific cellular machinery that introduces disulfide bonds into proteins newly synthesized and transported out of the cytosol. In E. coli, the membrane-integrated DsbB protein cooperates with ubiquinone to generate a disulfide bond, which is transferred to DsbA, a periplasmic dithiol oxido-reductase that serves as the direct disulfide bond donor to proteins folding oxidatively in this compartment. Despite the extensive accumulation of knowledge on this oxidation system, molecular details of the DsbB reaction mechanisms had been controversial due partly to the lack of structural information until our recent determination of the crystal structure of a DsbA-DsbB-ubiquinone complex. In this review we discuss the structural and chemical nature of reaction intermediates in the DsbB catalysis and the illuminated molecular mechanisms that account for the de novo formation of a disulfide bond and its donation to DsbA. It is suggested that DsbB gains the ability to oxidize its specific substrate, DsbA, having very high redox potential, by undergoing a DsbA-induced rearrangement of cysteine residues. One of the DsbB cysteines that are now reduced then interacts with ubiquinone to form a charge transfer complex, leading to the regeneration of a disulfide at the DsbB active site, and the cycle can begin anew. (C) 2007 Elsevier B.V. All rights reserved.

    DOI: 10.1016/j.bbamcr.2007.11.006

  • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation Reviewed

    Kenji Inaba, Satoshi Murakami, Mamoru Suzuki, Atsushi Nakagawa, Eiki Yamashita, Kengo Okada, Koreaki Ito

    CELL   127 ( 4 )   789 - 801   2006.11

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    DOI: 10.1016/j.cell.2006.10.034

  • Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex Reviewed

    Yoh-Hei Takahashi, Kenji Inaba, Koreaki Ito

    ANTIOXIDANTS & REDOX SIGNALING   8 ( 5-6 )   743 - 752   2006.5

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    DOI: 10.1089/ars.2006.8.743

  • Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB Reviewed

    K Inaba, Y Takahashi, K Ito, S Hayashi

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA   103 ( 2 )   287 - 292   2006.1

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    DOI: 10.1073/pnas.0507570103

  • Reactivities of quinone-free DsbB from Escherichia coli Reviewed

    K Inaba, YH Takahashi, K Ito

    JOURNAL OF BIOLOGICAL CHEMISTRY   280 ( 38 )   33035 - 33044   2005.9

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    DOI: 10.1074/jbc.M506189200

  • Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli Reviewed

    YH Takahashi, K Inaba, K Ito

    JOURNAL OF BIOLOGICAL CHEMISTRY   279 ( 45 )   47057 - 47065   2004.11

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    DOI: 10.1074/jbc.M407153200

  • DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation Reviewed

    K Inaba, YH Takahashi, K Ito

    JOURNAL OF BIOLOGICAL CHEMISTRY   279 ( 8 )   6761 - 6768   2004.2

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    DOI: 10.1074/jbc.M310765200

  • Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade Reviewed

    K Inaba, K Ito

    EMBO JOURNAL   21 ( 11 )   2646 - 2654   2002.6

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    DOI: 10.1093/emboj/21.11.2646

  • Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons Reviewed

    K Inaba, N Kobayashi, AR Fersht

    JOURNAL OF MOLECULAR BIOLOGY   302 ( 1 )   219 - 233   2000.9

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    DOI: 10.1006/jmbi.2000.4024

  • Substitution of the heme binding module in hemoglobin alpha- and beta-subunits - Implication for different regulation mechanisms of the heme proximal structure between hemoglobin and myoglobin Reviewed

    K Inaba, K Ishimori, K Imai, Morishima, I

    JOURNAL OF BIOLOGICAL CHEMISTRY   275 ( 17 )   12438 - 12445   2000.4

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    DOI: 10.1074/jbc.275.17.12438

  • Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 angstrom resolution Reviewed

    T Shirai, M Fujikake, T Yamane, K Inaba, K Ishimori, Morishima, I

    JOURNAL OF MOLECULAR BIOLOGY   287 ( 2 )   369 - 382   1999.3

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    DOI: 10.1006/jmbi.1999.2603

  • Structural and functional roles of heme binding module in globin proteins: Identification of the segment regulating the heme binding structure Reviewed

    K Inaba, K Ishimori, Morishima, I

    JOURNAL OF MOLECULAR BIOLOGY   283 ( 1 )   311 - 327   1998.10

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    DOI: 10.1006/jmbi.1998.2073

  • Design, construction, crystallization, and preliminary X-ray studies of a fine-tuning mutant (F133V) of module-substituted chimera hemoglobin Reviewed

    T Shirai, M Fujikake, T Yamane, K Inaba, K Ishimori, Morishima, I

    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS   32 ( 3 )   263 - 267   1998.8

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    DOI: 10.1002/(SICI)1097-0134(19980815)32:3<263::AID-PROT1>3.0.CO;2-J

  • Structural and functional effects of pseudo-module substitution in hemoglobin subunits - New structural and functional units in globin structure Reviewed

    K Inaba, K Ishimori, K Imai, Morishima, I

    JOURNAL OF BIOLOGICAL CHEMISTRY   273 ( 14 )   8080 - 8087   1998.4

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    DOI: 10.1074/jbc.273.14.8080

  • Structural and functional roles of modules in hemoglobin - substitution of module M4 in hemoglobin subunits Reviewed

    K Inaba, K Wakasugi, K Ishimori, T Konno, M Kataoka, Morishima, I

    JOURNAL OF BIOLOGICAL CHEMISTRY   272 ( 48 )   30054 - 30060   1997.11

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    DOI: 10.1074/jbc.272.48.30054

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Books

  • クライオ電子顕微鏡ハンドブック「SERCA2bの構造解析:結晶構造解析からクライオ電顕単粒子解析までの変遷」

    渡部 聡, 稲葉 謙次( Role: Joint author)

    2023.1 

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  • Structural insights into disulfide bond formation and protein quality control in the mammalian endoplasmic reticulum

    Masaki Okumura, Satoshi Watanabe, Kenji Inaba( Role: Joint author)

    Royal Society of Chemistry  2018.10 

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    Language:English   Book type:Scholarly book

Presentations

  • Mechanisms of calcium homeostasis in the ER and Golgi apparatus revealed by cross-scale microscopic measurements Invited

    The 3rd cross-scale biology international meeting  2023.9 

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    Event date: 2023.9

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    Mechanisms of calcium homeostasis in the ER and Golgi apparatus revealed by cross-scale microscopic measurements

  • “Molecular basis of redox- and zinc-dependent protein quality control at the ER-Golgi interface” Oct 31, 2022(招待講演) Invited

    2022.10 

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    Event date: 2022.10

    Language:Others  

    Country:Other  

  • 細胞内で翻訳合成途上のLDL受容体にジスルフィド結合が形成される仕組み

    門倉 広, 平井直也, 福田 洋, 太宰 結, 稲葉謙次

    第94回日本生化学大会, 横浜(オンライン開催) 

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    Event date: 2021.11

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  • .“Molecular basis of redox-, pH-, and metal ion-dependent protein quality control at the ER-Golgi interface”

    2020.6 

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    Event date: 2020.6

    Language:Others  

    Country:Other  

  • Molecular basis for the zinc-dependent protein quality control at the ER-Golgi interface

    Inaba, K

    The 6th Meeting of International Society for Zinc Biology  2019.9 

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    Event date: 2019.9

    Language:English  

    Country:Other  

  • Structural basis of zinc-dependent protein quality control in the early secretory pathway

    Watanabe, S., Amagai, Y., Sannino, S., Yamada, M., Sitia, R. and Inaba, K.

    Cell Biology of Metals, Gordon Research Conference  2019.7 

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    Event date: 2019.7

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  • Molecular basis for the pH- and zinc-dependent protein quality control at the ER-Golgi interface

    Inaba, K

    Structural Biology Seminar at Weissman Institute of Science  2019.5 

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    Event date: 2019.5

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  • Molecular basis for the cooperation of ERp44 and zinc for protein quality control at the ER-Golgi interface

    Inaba, K

    The 14th ER & Redox Club Meeting  2019.5 

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  • Molecular basis of the ERp44-Zn2+ cooperation for protein quality control in the early secretory pathway.

    Inaba,K.

    The 91st annual meeting of the Japan Biochemical Society  2018.9 

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    Event date: 2018.9

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  • Structural basis of pH- and zinc-dependent multiple client recognition by ERp44

    Watanabe S., Amagai Y. Sitia R. Inaba K

    2018.9 

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    Event date: 2018.9

    Language:Others  

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    Structural basis of pH- and zinc-dependent multiple client recognition by ERp44

  • 筋小胞体カルシウムATPアーゼSERCA2bの膜貫通ヘリックス相互作用による制御機構の構造基盤

    井上 道雄、作田 菜奈美、渡部 聡、田中 良樹、潮田 亮、加藤 幸成、高木 淳一、塚崎 智也、永田 和宏、稲葉 謙次

    第56回日本生物物理学会年会  2018.9 

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    Event date: 2018.9

    Language:Japanese  

    Country:Other  

  • Structural basis of zinc-dependent ERp44 regulation for protein quality control in the early secretory pathway

    Satoshi Watanabe, Yuta Amagai, Sara Sannino, Manami Harayama, Shoji Masui, Momo Yamada, Roberto Sitia, and Kenji Inaba

    2018.8 

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    Event date: 2018.8

    Language:English  

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  • Cooperation of pH and zinc ions in ERp44-mediated protein quality control at the ER-Golgi interface

    Inaba, K.

    Neoprotein biology- from synthesis to trafficking  2018.8 

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    Cooperation of pH and zinc ions in ERp44-mediated protein quality control at the ER-Golgi interface

  • Crystal Structure of DsbB-DsbA Complex Revealing a Cysteine Relocation Mechanism International conference

    Inaba K. and Ito K.  2006.7 

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    Crystal Structure of DsbB-DsbA Complex Revealing a Cysteine Relocation Mechanism

  • Crystal structure of the DsbB-DsbA complex revealing a cysteine relocation process for disulfide bond generation Invited International conference

    Switzerland-Japan Symposium on Structural Biology 2006  2006.9 

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    Crystal structure of the DsbB-DsbA complex revealing a cysteine relocation process for disulfide bond generation

  • Crystal Structure of DsbB-DsbA Complex Revealing a Cysteine Relocation Mechanism Invited International conference

    Joint Conference of the Asian Crystallographic association and the Crystallographic Society of Japan  2006.11 

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    Crystal Structure of DsbB-DsbA Complex Revealing a Cysteine Relocation Mechanism

  • How are protein disulfide bonds generated in the cell? Invited International conference

    International Symposium on Milestone of Life of Proteins, Kyoto  2007.3 

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    How are protein disulfide bonds generated in the cell?

  • Structural basis of the DsbA-DsbB-UQ oxidative system in E. coli. Invited International conference

    Boden Conference on disulfide bonds and their role in protein folding and function  2007.7 

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    Structural basis of the DsbA-DsbB-UQ oxidative system in E. coli.

  • Crystal structure of the DsbB-DsbA complex reveals a mechanism of protein disulfide bond generation in E. coli. Invited International conference

    2nd International Symposium on Diffraction structural Biology  2007.9 

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    Crystal structure of the DsbB-DsbA complex reveals a mechanism of protein disulfide bond generation in E. coli.

  • Structural basis for protein disulfide generation in the cell Invited International conference

    Gordon Research Conference on thiol-based redox regulation & signaling  2008.5 

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    Structural basis for protein disulfide generation in the cell

  • Structure and mechanism of the DsbB-DsbA protein disulfide generation system in E. coli Invited International conference

    XXI Congress and General Assembly of the International union of Crystallography  2008.8 

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    Structure and mechanism of the DsbB-DsbA protein disulfide generation system in E. coli

  • Crystal structures of mammalian human Ero1 and ERdj5, the enzymes involved in ER quality control Invited International conference

    稲葉 謙次

    2010.5 

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  • Structural basis of regulated protein disulfide bond formation in human cells Invited International conference

    The 3rd international symposium on protein community  2010.9 

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    Structural basis of regulated protein disulfide bond formation in human cells

  • Structure and mechanism of protein disulfide bond formation systems in human cells International conference

    ESF research conference; Glutathione and related thiols in living cells  2011.9 

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    Structure and mechanism of protein disulfide bond formation systems in human cells

  • Structural and mechanistic basis of regulated and specific protein disulfide bond formation in human cells International conference

    Quality control; folding and degradation of proteins in the endoplasmic reticulum  2011.9 

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    Structural and mechanistic basis of regulated and specific protein disulfide bond formation in human cells

  • Structural and mechanistic basis of protein disulfide bond formation network in mammalian cells Invited International conference

    17th Biennial Meeting of Society for Free Radical Research International  2014.3 

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    Structural and mechanistic basis of protein disulfide bond formation network in mammalian cells

  • Structural and mechanistic basis of the protein disulfide bond formation system in mammalian cells Invited International conference

    The 7th Korea-Japan Seminars on Biomolecular Sciences  2014.11 

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    Structural and mechanistic basis of the protein disulfide bond formation system in mammalian cells

  • Structural and mechanistic basis of the protein disulfide bond formation system in mammalian cells Invited International conference

    The 15th RIES-Hokudai International Symposium  2014.12 

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    Structural and mechanistic basis of the protein disulfide bond formation system in mammalian cells

  • The protein disulfide bond formation system in mammalian cells Invited International conference

    Kyushu-U and Stanford-U Joint Research and Education Program  2015.3 

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    The protein disulfide bond formation system in mammalian cells

  • Dual conformations of ERdj5 play a significant role in acceleration of the ER associated degradation. International conference

    ER & Redox club meeting  2015.4 

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    Dual conformations of ERdj5 play a significant role in acceleration of the ER associated degradation.

  • Dynamic natures of PDI family members in catalysis of oxidative protein folding and ER associated degradation Invited

    Case Western Reserve University-Tohoku University joint symposium  2015.7 

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    Dynamic natures of PDI family members in catalysis of oxidative protein folding and ER associated degradation

  • Dynamic natures of PDI family members in catalysis of oxidative protein folding and ER associated degradation Invited

    EMBO meeting  2015.9 

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    Dynamic natures of PDI family members in catalysis of oxidative protein folding and ER associated degradation

  • How do PDI family member proteins act on unfolded/misfolded proteins to ensure protein quality control in the ER? Invited International conference

    Nascent Chain Biology meeting  2016.8 

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    How do PDI family member proteins act on unfolded/misfolded proteins to ensure protein quality control in the ER?

  • The highly dynamic nature of ERdj5 plays a key role in efficient ER-associated degradation of aberrant protein oligomers Invited International conference

    Inaba, K.

    International Forum "Redpx Biology"  2018.3 

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    The highly dynamic nature of ERdj5 plays a key role in efficient ER-associated degradation of aberrant protein oligomers

  • Zinc ions regulate ERp44-mediated protein quality control in the early secretory pathway Invited International conference

    2018.8 

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    Zinc ions regulate ERp44-mediated protein quality control in the early secretory pathway

  • Zinc ions have a new physiological role in protein quality control in the early secretory pathway Invited International conference

    CWRU-Tohoku joint symposium  2018.8 

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    Zinc ions have a new physiological role in protein quality control in the early secretory pathway

  • ERp44の機能制御に関わる亜鉛トランスポーターの同定

    山田 桃、天貝佑太、渡部 聡、Roberto Sitia、稲葉 謙次

    第41回分子日本分子生物学会  2018.12 

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  • Molecular basis for the pH- and zinc-dependent protein quality control at the ER-Golgi interface

    Inaba, K

    Structural Biology Seminar at Technical University of Munich  2019.5 

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  • 亜鉛イオンとシャペロンタンパク質ERp44による新たなタンパク質品質管理機構

    渡部 聡, 天貝佑太, 山田桃, Roberto Sitia, 稲葉謙次

    第19回日本蛋白質科学会年会  2019.6 

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  • 構造生物学が明らかにする細胞のタンパク質品質管理機構

    稲葉 謙次

    第1回バイオ単分子研究会  2019.9 

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  • Novel protein quality control system cooperated by zinc ions and ERp44 in the early secretory pathway

    2019.12 

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    Novel protein quality control system cooperated by zinc ions and ERp44 in the early secretory pathway

  • “Protein Disulfide Isomerase family; their molecular actions and functions” Invited

    2020.10 

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  • X線結晶構造解析とクライオ電子顕微鏡単粒子解析がもたらす知見の対比:小胞体カルシウムポンプSERCA2bを例に Invited

    稲葉 謙次

    第一回生命金属科学地方巡業、仙台(オンライン開催)  2021.1 

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  • 哺乳動物細胞分泌経路における亜鉛調節とタンパク質品質管理

    天貝佑太, 山田桃, 渡邊朝美, 小和田俊行, 楢本悟史, 渡部聡, 経塚淳子, Roberto Sitia, 水上進, 稲葉謙次

    第62回 日本植物生理学会年会、島根(オンライン開催)  2021.3 

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  • ミスフォールドタンパク質およびジスルフィド結合依存的なIRE1の会合状態制御

    松崎元紀, 金村進吾, 田尻道子, 明石知子, 稲葉謙次, 奥村正樹

    日本農芸化学会2021年度大会、仙台  2021.3 

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  • 初期分泌経路における亜鉛濃度制御が小胞体―ゴルジ体シャペロンERp44の機能をコントロールする

    天貝佑太, 山田桃, 渡邊朝美, 小和田俊行, 楢本悟史, 渡部聡, 経塚淳子, Roberto Sitia, 水上進, 稲葉謙次

    第21回 日本蛋白質科学会年会、富山(オンライン開催)  2021.6 

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  • 入力予定

    岡田莉奈, 金村進吾, 黒井邦巧, 松崎元紀, 山口宏, 中林孝和, 稲葉謙次, 奥村正樹

    2021.6 

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  • 入力予定

    関凪沙, 金村進吾, 荒井堅太, 山口宏, Lee Young-Ho, 稲葉謙次, 奥村正樹

    第21回 日本蛋白質科学会年会、富山(オンライン開催)  2021.6 

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  • 入力予定

    谷川雄哉, 金村進吾, 伊藤大, Lin Yuxi, 松崎元紀, 山口宏, 黒木喜美子, 前仲勝実, Lee Young-Ho, 稲葉謙次, 奥村正樹

    第21回 日本蛋白質科学会年会、富山(オンライン開催)  2021.6 

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  • 亜鉛に依存したERp44-クライアント複合体の解離機構の解明

    渡部 聡, 三宅杏美子, 天貝佑太, 稲葉謙次

    第21回蛋白質科学会年会、富山(オンライン開催)  2021.6 

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  • Observing the cotranslational disulfide rearrangement in a cell surface multidomain protein, LDL receptor, in the ER of mammalian cells Invited

    Kadokura, H, Dazai, Y, Fukuda, Y, Hirai, N, Nakamura, O, Inaba, K

    2021.6 

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  • Mechanisms of ER-associated degradation pathway mediated by the cooperation of ERdj5 and BiP

    Cai, X, Ito, S, Noi, K, Inoue, M, Ushioda, R, Nagata, K, Inaba, K

    The 21st Annual Meeting of the Protein Science Society of Japan  2021.6 

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  • Elucidating the in vivo oxidative folding mechanism

    Kanemura,S, Okumura,M, Inaba,K

    The 21st Annual Meeting of the Protein Science Society of Japan  2021.6 

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  • 初期分泌経路における亜鉛イオンに依存したタンパク質品質管理機構の分子構造基盤 Invited

    稲葉 謙次

    第58回日本生化学会北海道支部会、札幌(オンライン開催)  2021.7 

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  • Structural and mechanistic basis of protein quality control systems in the endoplasmic reticulum and Golgi apparatus of human cells Invited

    Kenji Inaba

    UST Global mentoring program meeting, Korea Web  2021.9 

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  • 酸化還元制御によるヒトガレクチン1の構造機能調節の理解

    岡田莉奈, 金村進吾, 黒井邦巧, 松崎元紀, 齋尾智英, 山口宏, 伊藤大, 李映昊, 中林孝和, 稲葉謙次, 奥村正樹

    第44回 日本分子生物学会年会、横浜  2021.12 

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  • 全長カーゴ受容体ERGIC-53と補助因子MCFD2との複合体のクライオ電顕構造

    渡部 聡, 木瀬孔明, 米澤健人, 清水伸隆, 濡木理, 稲葉謙次

    第44回日本分子生物学会年会、横浜、  2021.12 

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  • 亜鉛輸送体によって制御されるERp44の小胞体―ゴルジ体輸送

    天貝佑太, 稲葉謙次

    第44回 日本分子生物学会年会、横浜  2021.12 

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  • 亜鉛結合性シャペロンERp44-基質複合体の形成・解離機構の解明とクライオ電顕構造

    木谷美思, 渡部聡, 天貝佑太, 稲葉謙次

    第44回日本分子生物学会年会、横浜  2021.12 

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  • プロインスリンのフォールディング中間体の理解(Characterization of proinsulin folding intermediates along its folding pathway)

    関凪沙, 金村進吾, 荒井堅太, 山口宏, 稲葉謙次, 奥村正樹

    第44回 日本分子生物学会年会、横浜  2021.12 

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  • ヒト細胞小胞体関連機能の変化を検出するための鋭敏で簡便なレポーターの開発と機能評価

    原田楠子, 八巻 聡, 平井直也, 中村大祐, 河野憲二, 稲葉謙次, 門倉 広

    第44回 日本分子生物学会年会、横浜  2021.12 

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  • PDIファミリー酵素による前駆体タンパク質の酸化的フォールディング触媒機構の解明

    新納翔悟, 金村進吾, 山口宏, 日高雄二, 稲葉謙次, 奥村正樹

    第44回 日本分子生物学会年会、横浜  2021.12 

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  • PDIファミリータンパク質PDIRの構造機能解析

    東晃太, 松崎元紀, 渡部聡, 稲葉謙次

    第44回 日本分子生物学会年会、横浜  2021.12 

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  • Ca2+によるERp57-CNX複合体の構造機能調節メカニズムの解明

    金村進吾, 谷川雄哉, 伊藤大, 林雨曦, 松崎元紀, 黒木喜美子, 山口宏, 前仲勝実, 李映昊, 稲葉謙次, 奥村正樹

    第44回 日本分子生物学会年会、横浜  2021.12 

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  • 小胞体における亜鉛とレドックスのクロストークの新規メカニズムの発見 Invited

    天貝 佑太, 新井 千尋, 稲葉 謙次

    第2回 レドックスR&D戦略委員会春のシンポジウム  2022.3 

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  • レドックスと金属イオンが織りなす新たなタンパク質品質管理機構 Invited

    稲葉 謙次

    学術変革領域A「硫黄生物学」第一回領域会議  2022.3 

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  • 「小胞体ストレスセンサーの会合状態分布を介した応答制御機構の研究」

    松崎 元紀, 横山 武司, 次田 篤史, 金村 進吾, 田尻 道子, 明石 知子, 齋尾 智英, 稲葉 謙次, 奥村 正樹

    日本農芸化学会2022年度大会  2022.3 

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  • 「レドックスと金属イオンが織りなす新たなタンパク質品質管理機構」

    稲葉 謙次

    学術変革領域A「硫黄生物学」第一回領域会議、仙台  2022.3 

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  • クライオ電子顕微鏡で明らかになったカーゴ受容体ERGIC-53の柔らかな全長構造 Invited

    渡部 聡, 木瀬, 孔明, 米澤, 健人, 清水, 伸隆, 濡木, 理, 稲葉 謙次

    第22回蛋白質科学会年会  2022.6 

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  • 「酸化型ガレクチン1の分子構造基盤」

    金村 進吾, 黒井 邦巧, 岡田 莉奈, 松崎 元紀, 山口 宏, 伊藤 大, 李 映昊, 稲葉 謙次, 齋尾 智英, 中林 孝和, 奥村 正樹

    回日本蛋白質科学会  2022.6 

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  • Molecular basis of redox-, pH-, and metal ion-dependent protein quality control at the ER-Golgi interface Invited

    Kenji Inaba

    KPPS symposium 2022  2022.6 

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    Molecular basis of redox-, pH-, and metal ion-dependent protein quality control at the ER-Golgi interface

  • IRE1の会合状態変化によるストレスレベル感知機構の研究

    松崎 元紀, 横山 武司, 次田 篤史, 金村 進吾, 田尻 道子, 明石 知子, 齋尾 智英, 稲葉 謙次, 奥村 正樹

    第22回日本蛋白質科学会年会  2022.6 

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  • ERp44を介した亜鉛とレドックスホメオスタシスのクロストーク Invited

    天貝 佑太, 新井 千尋, 稲葉 謙次

    第22回 日本蛋白質科学会年会、つくば  2022.6 

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  • 「IRE1による定量的小胞体ストレスセンシングの分子機構」

    松崎 元紀, 横山 武司, 次田 篤史, 金村 進吾, 田尻 道子, 明石 知子, 野井 健太郎, 齋尾智英, 稲葉 謙次, 奥村 正樹

    第15回小胞体ストレス研究会  2022.7 

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  • “Close linkage between redox and zinc homeostasis in the endoplasmic reticulum” October 30, 2022(招待講演) Invited

    2022.10 

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  • Protein Disulfide Isomerase family; their molecular actions and functions Invited

    Okumura, M, Inaba, K

    Redox week in Sendai  2022.10 

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    Protein Disulfide Isomerase family; their molecular actions and functions

  • Molecular basis of redox- and zinc-dependent protein quality control at the ER-Golgi interface Invited

    Kenji Inaba

    Redox week in Sendai  2022.10 

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    Molecular basis of redox- and zinc-dependent protein quality control at the ER-Golgi interface

  • Close linkage between redox and zinc homeostasis in the endoplasmic reticulum Invited

    Amagai, Y, Arai, C, Inaba, K

    Redox Week in Sendai  2022.10 

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    Close linkage between redox and zinc homeostasis in the endoplasmic reticulum

  • 「亜鉛輸送体の機能不全により影響を受ける分泌・膜タンパク質の解析」

    大山 莉央, 天貝 佑太, 幡野 敦, 松本 雅記, 稲葉 謙次

    第45回 日本分子生物学会年会  2022.11 

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  • 小胞体とゴルジ体間のコミュニケーションによる新たなタンパク質品質管理機構 Invited

    稲葉 謙次

    第95回日本生化学会  2022.11 

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  • 亜鉛輸送体の機能不全により影響を受ける分泌・膜タンパク質の解析

    大山 莉央, 天貝 佑太, 幡野 敦, 松本 雅記, 稲葉 謙次

    第45回 日本分子生物学会年会  2022.11 

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  • 「小胞体局在酵素の酸化還元依存的相分離制御の理解」

    鈴木 琴乃, 金村 進吾, 松﨑 元紀, 渡部 マイ, 齋尾 智英, 李 映昊, 中林 孝和, 稲葉 謙次, 奥村 正樹

    第45回 日本分子生物学会  2022.11 

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  • 「小胞体とゴルジ体間のコミュニケーションによる新たなタンパク質品質管理機構」 Invited

    稲葉 謙次

    第95回日本生化学会、名古屋  2022.11 

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  • 「プロインスリンの酸化的フォールディングにおける過渡的フォールディング中間体の生化学的評価」

    関 凪沙, 金村 進吾, 荒井 堅太, 山口 宏, 稲葉 謙次, 奥村 正樹

    第95回 日本生化学会  2022.11 

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  • 「ヒトガレクチン1の酸化還元依存的な機能制御における分子構造基盤」

    金村 進吾, 黒井 邦巧, 岡田 莉奈, 松崎 元紀, 山口 宏, 伊藤 大, 李 映昊, 稲葉 謙次, 齋尾 智英, 中林 孝和, 奥村 正樹

    第95回 日本生化学会  2022.11 

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  • “Molecular basis of zinc-dependent protein quality control at the ER-Golgi interface” Invited

    2022.11 

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  • Molecular basis of zinc-dependent protein quality control at the ER-Golgi interface Invited

    Kenji Inaba

    10th Asian Biological Inorganic Chemistry Conference  2022.11 

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    Molecular basis of zinc-dependent protein quality control at the ER-Golgi interface

  • 「酸化還元依存的なヒトガレクチン1の構造機能制御機構の解明」2022年12月1日

    金村 進吾, 黒井 邦巧, 岡田 莉奈, 松崎 元紀, 山口 宏, 伊藤 大, 李 映昊, 稲葉 謙次, 齋尾 智英, 中林 孝和, 奥村 正樹

    第45回 日本分子生物学会  2022.12 

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  • 「ヒト小胞体膜タンパク質LMF1による膜を介した電子移動メカニズムの解析」

    佃 竜介, 原田 楠子, 平井 直也, 東 晃太, 小林 大樹, 松本 雅記, 稲葉 謙次, 門倉 広

    第45回 日本分子生物学会年会、千葉  2022.12 

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  • 「⼩胞体亜鉛輸送体ZIP7の構造解析」

    富岡 竜也, 陳 正豪, 天貝 佑太, 渡部 聡, 稲葉 謙次

    第45回 日本分子生物学会年会、千葉  2022.12 

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  • 「PDIファミリーによるプロインスリンの酸化的フォールディング中間体の触媒機序の理解」

    関 凪沙, 金村 進吾, 荒井 堅太, 山口 宏, 稲葉 謙次, 奥村 正樹

    第45回 日本分子生物学会  2022.12 

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  • 「PDIファミリータンパク質PDIRの構造機能解析」 2022年12月2日

    東 晃太, 松崎 元紀, 渡部 聡, 稲葉 謙次

    第45回 日本分子生物学会年会、千葉  2022.12 

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  • Cryo-EM Structures of Human Zinc Transporter ZnT7 Reveal the Mechanism of Zn2+ Uptake into the Golgi Apparatus Invited

    Han Ba Bui, Satoshi Watanabe, Kenji Inaba

    2023.5 

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    Cryo-EM Structures of Human Zinc Transporter ZnT7 Reveal the Mechanism of Zn2+ Uptake into the Golgi Apparatus

  • 活性酸素種および活性窒素種による小胞体局在酵素の相分離形成機序の理解

    渡部マイ, 金村進吾, 鈴木琴乃, 松﨑元紀, 稲葉謙次, 李映昊, 齋尾智英, 奥村正樹

    第23回日本蛋白質科学会年会  2023.7 

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  • 小胞体内プロインスリンの品質管理の理解

    倉持円来, 関凪沙, 荒井堅太, 山口宏, 稲葉謙次, 金村進吾, 奥村正樹

    第23回日本蛋白質科学会年会  2023.7 

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  • PDI familyによる前駆体タンパク質プロウログアニリンの酸化的フォールディング触媒機構の解明

    石井琴音, 金村進吾, 山口宏, 日高雄二, 稲葉謙次, 奥村正樹

    第23回日本蛋白質科学会年会  2023.7 

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  • Mechanisms of calcium homeostasis in the ER and Golgi apparatus revealed by cross-scale microscopic measurements. Invited

    2023.7 

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    Mechanisms of calcium homeostasis in the ER and Golgi apparatus revealed by cross-scale microscopic measurements.

  • 亜鉛が制御する分泌経路内タンパク質品質管理機構. Invited

    天貝 佑太, 稲葉 謙次

    第34回日本微量元素学会学術集会  2023.9 

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  • Structure analysis of a cargo receptor ERGIC-53 homolog, ERGL

    Ouyang Li, Satoshi Watanabe, Kenji Inaba

    The 3rd cross-scale biology international meeting  2023.9 

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    Structure analysis of a cargo receptor ERGIC-53 homolog, ERGL

  • Structural analysis of cargo transport by ERGIC-53

    Satoshi Watanabe, Yoshiaki Kise, Kento Yonezawa, Mariko Inoue, Nobutaka Shimizu, Osamu Nureki, Kenji Inaba

    The 3rd cross-scale biology international meeting  2023.9 

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    Structural analysis of cargo transport by ERGIC-53

  • Insulin quality control mechanism in the endoplasmic reticulum Invited

    Kuramochi, T, Seki, N, Arai, K, Yamaguchi, H, Inaba, K, Kanemura, S, Okumura, M

    International Cross-disciplinary Symposium  2023.10 

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    Insulin quality control mechanism in the endoplasmic reticulum

  • 小胞体局在酵素の相分離制御に対する活性酸素種および活性窒素種の影響

    渡部マイ, 金村進吾, 鈴木琴乃, 松﨑元紀, 稲葉謙次, 李映昊, 齋尾智英, 奥村正樹

    第96回日本生化学会大会  2023.11 

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  • 小胞体ストレスセンサーIRE1によるストレス感知と越膜シグナル変換の分子機構

    松崎元紀, 横山武司, 次田篤史, 金村進吾, 田尻道子, 明石知子, 齋尾智英, 稲葉謙次, 奥村正樹

    第96回日本生化学会大会  2023.11 

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  • Zinc homeostasis and proteostasis at the ER-Golgi interface Invited

    2023.11 

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    Zinc homeostasis and proteostasis at the ER-Golgi interface

  • PDIファミリーによるプロインスリンの品質管理の触媒機序の理解

    倉持円来, 関凪沙, 荒井堅太, 山口宏, 稲葉謙次, 金村進吾, 奥村正樹

    第96回日本生化学会大会  2023.11 

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  • 小胞体内の亜鉛恒常性維持はPDIファミリー酵素のレドックス制御に重要である

    天貝 佑太, 新井 千尋, 稲葉 謙次

    第45回 日本分子生物学会年会、千葉  2023.11 

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  • 小胞体局在酵素の酸化還元依存的相分離制御の理解

    鈴木琴乃, 渡部マイ, 松﨑元紀, 坂和範, 李映昊, 中林孝和, 齋尾智英, 稲葉謙次, 金村進吾, 奥村正樹

    第46回日本分子生物学会  2023.12 

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  • Yuta Amagai, Kenji Inaba Invited

    Zinc homeostasis in, he ER is crucial for, proteostasis of, he, early secretory pathway

    2023.12 

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    Yuta Amagai, Kenji Inaba

  • PDIファミリーによるフォールディング中間体触媒機構の解明

    石井琴音, 金村進吾, 山口宏, 日高雄二, 稲葉謙次, 奥村正樹

    第46回日本分子生物学会年会  2023.12 

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  • PDI familyによる小胞体内プロインスリンのフォールディング触媒機構の理解

    倉持円来, 関凪沙, 荒井堅太, 山口宏, 稲葉謙次, 金村進吾, 奥村正樹

    第46回日本分子生物学会  2023.12 

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  • ケミカルプロテオスタシス:亜鉛恒常性維持とタンパク質恒常性維持 Invited

    稲葉 謙次

    第2回タンパク質シンポジウム  2024.1 

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  • クライオ電子顕微鏡が明らかにした亜鉛輸送体SLC30A7の亜鉛輸送機構 Invited

    稲葉 謙次

    キャノンメディカルR&Dフォーラム2024  2024.3 

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MISC

  • 新たな顕微技術が明らかにする細胞内分子動態 Reviewed

    井澤 俊明, 稲葉 謙次, 斎藤知恵子, 山本 林, 関根 清薫, 倉永 英里奈, 野村 高志, 田中 元雅

    顕微鏡   2023.8

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  • クライオ電子顕微鏡が観たカルシウムポンプの分子描像 Reviewed

    稲葉 謙次

    高分子   2023.8

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  • Dose-response relationship for the resistance of human insulin to degradation by insulin-degrading enzyme

    Masaki Okumura, Tsubura Kuramochi, Yuxi Lin, Ran Furukawa, Kenji Mizutani, Takeshi Yokoyama, Mingeun Kim, Mi Hee Lim, Hyon-Seung Yi, Kenta Arai, Hiroshi Yamaguchi, Hironobu Hojo, Michio Iwaoka, Yoshikazu Tanaka, Sam-Yong Park, Kenji Inaba, Shingo Kanemura, Young-Ho Lee

    BioRxiv   2023.4

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    DOI: 10.1101/2023.04.08.536135

  • 小胞体ジスルフィド結合形成ネットワークを支える酵素群の構造基盤

    金村 進吾, 稲葉 謙次, 奥村 正樹

    日本結晶学会誌   2022.9

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  • クライオ電子顕微鏡がもたらす新しいタンパク質構造の知見 Reviewed

    稲葉 謙次, 張 玉霞

    実験医学   2022.8

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  • 研究分野を変える「勇気」~自身の研究ワールドを築こう~ Reviewed

    稲葉 謙次

    日本生物物理学会誌   2021.2

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  • 初期分泌経路における新たなタンパク質品質管理機構 ---亜鉛イオンとERp44の協奏

    天貝佑太, 渡部聡, 稲葉謙次

    実験医学   2020.3

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  • タンパク質の運命を制御する生体システムと疾病のフロンティア 小胞体ストレス応答性酸化還元調節酵素を標的とした創薬スクリーニング

    野村 尚生, 松丸 尊紀, 春山 知樹, 前田 直良, 奥村 正樹, 金村 進吾, 稲葉 謙次, 田村 保明, 前仲 勝実

    日本生化学会大会プログラム・講演要旨集   2019.9

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  • 次世代のアカデミア創薬を担う若手の力 抗がん剤を目指した若手研究者連携による創薬スクリーニング

    野村 尚生, 松丸 尊紀, 奥村 正樹, 稲葉 謙次, 田村 保明, 前仲 勝実

    日本薬学会年会要旨集   2017.3

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  • 膵臓で特異的に発現するPDIファミリータンパク質(PDIp)の生理的機能の解析

    藤本拓志, 斎藤美知子, 都留秋雄, 松本雅記, 河野憲二, 稲葉謙次, 門倉広

    日本蛋白質科学会年会プログラム・要旨集   2016.5

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  • 小胞体ストレスタンパク質を標的とした抗癌剤スクリーニング

    野村尚生, 鈴木華央, 松丸尊紀, 奥村正樹, 稲葉謙次, 田村保明, 前仲勝実

    日本薬学会年会要旨集(CD-ROM)   2016.3

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  • 膵特異的に発現するPDIファミリータンパク質(PDIp)の生理的機能の解析

    藤本拓志, 斎藤美知子, 都留秋雄, 河野憲二, 稲葉謙次, 門倉広

    日本細胞生物学会大会要旨集   2015.6

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  • [NiFe]ヒドロゲナーゼへNiを組み込むHypAB複合体の結晶構造解析

    河島拓未, 渡部聡, 西谷優一, 金井保, 和田健彦, 稲葉謙次, 跡見晴幸, 今中忠行, 三木邦夫

    日本蛋白質科学会年会プログラム・要旨集   2015.5

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  • 新規PDIファミリータンパク質ERp46の構造と機能

    奥村 正樹, 金村 進吾, 稲葉 謙次

    日本生物物理学会誌   2014.12

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    DOI: 10.2142/biophys.55.034

  • ERdj5(JPDI)基質候補タンパク質のマウス個体組織からの網羅的同定

    門倉広, 斉藤美知子, 都留秋雄, 稲葉謙次, 河野憲二

    日本細胞生物学会大会要旨集   2014.5

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  • 哺乳動物細胞の小胞体におけるジスルフィド結合形成ネットワークの構造基盤

    奥村 正樹, 稲葉 謙次

    実験医学   2014.4

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  • 哺乳動物細胞小胞体に局在するERdj5(JPDI)の生理的基質候補タンパク質の網羅的解析

    門倉広, 斉藤美知子, 都留秋雄, 稲葉謙次, 河野憲二

    日本農芸化学会大会講演要旨集(Web)   2014.3

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  • 分泌タンパク質の成熟化を監視するpHに依存的な新たなタンパク質品質管理機構の発見

    増井 翔史, Roberto Sitia, 稲葉 謙次

    ライフサイエンス新着論文レビュー   2013.5

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  • 1P009 NMRによるプロテインジスルフィドイソメラーゼのマルチドメイン構造と機能発現の連関の解析(蛋白質 B) 構造・機能相関)

    中野路子, 山口芳樹, 村上千穂, 原田拓志, 栗本英治, 浅見修, 梶野勉, 稲葉謙次, 加藤晃一

    生物物理   2004.11

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    DOI: 10.2142/biophys.44.S32_1

  • DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation (vol 279, pg 6761, 2004)

    K Inaba, YH Takahashi, N Fujieda, K Kano, H Miyoshi, K Ito

    JOURNAL OF BIOLOGICAL CHEMISTRY   2004.6

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  • Redox-dependent conformational alteration of protein disulfide isomerase

    Yoshiki Yamaguchi, Michiko Nakano, Chiho Murakami, Hiroaki Sasakawa, Takushi Harada, Eiji Kurimoto, Takeshi Iguchi, Osamu Asami, Tsutomu Kajino, Kenji Inaba, Koichi Kato

    CELL STRUCTURE AND FUNCTION   2004.5

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  • プロテインジスルフィドイソメラーゼの高次構造およびドメイン間相互作用のNMR解析

    中野路子, 山口芳樹, 村上千穂, 原田拓志, 栗本英治, 浅見修, 梶野勉, 稲葉謙次, 加藤晃一

    生物物理   2003.8

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    DOI: 10.2142/biophys.43.S45_4

  • 2R1600 プロテインジスルフィドイソメラーゼの活性部位のミクロ環境とドメイン間相互作用の解析(1.蛋白質(A)構造,一般演題,日本生物物理学会第40回年会)

    宮崎千穂, 原田拓志, 山口芳樹, 栗本英治, 浅見修, 梶野勉, 稲葉謙次, 西義則, 小林祐次, 加藤晃一

    生物物理   2002.10

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    DOI: 10.2142/biophys.42.S150_3

  • 蛍光消光を用いたミオグロビンの巻き戻り中間状態の構造解析

    谷岡 弘章, 秋山 修志, 稲葉 謙次, 高橋 聡, 石森 浩一郎, 森島 績

    生物物理   1998.9

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  • α1β1界面に位置する水素結合の切断によるHbの会合特性変化

    近藤 詩乃, 稲葉 謙次, 石森 浩一郎, 森島 績

    生物物理   1997.10

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  • モジュール置換キメラヘモグロビンの結晶構造解析

    白井 剛, 田中 道明, 藤掛 真広, 山根 隆, 稲葉 謙次, 石森 浩一郎, 森島 績

    生物物理   1997.10

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  • ヘム結合モジュールを置換した人工グロビン蛋白質の構造と機能

    稲葉 謙次, 石森 浩一郎, 森島 績

    生物物理   1997.10

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  • Preparation and characterization of novel hemoproteins by module substitution in hemoglobin subunits

    K Inaba, K Wakasugi, K Ishimori, Morishima, I

    PROTEIN ENGINEERING   1995.9

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Industrial property rights

Patent   Number of applications: 1   Number of registrations: 0
Utility model   Number of applications: 0   Number of registrations: 0
Design   Number of applications: 0   Number of registrations: 0
Trademark   Number of applications: 0   Number of registrations: 0

Professional Memberships

  • THE MOLECULAR BIOLOGY SOCIETY OF JAPAN

  • THE JAPANESE BIOCHEMICAL SOCIETY

  • THE BIOPHYSICAL SOCIETY OF JAPAN

  • JAPAN SOCIETY FOR CELL BIOLOGY

  • PROTEIN SCIENCE SOCIETY OF JAPAN

Committee Memberships

  • Executive   Domestic

    2022.7 - 2024.6   

  • 日本蛋白質科学会   庶務   Domestic

    2022.7 - 2024.6   

Academic Activities

  • Screening of academic papers

    Role(s): Peer review

    2023

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:5

    Number of peer-reviewed articles in Japanese journals:0

  • 日本学術振興会科学研究費補助金 学術変革領域A 公募班審査員

    Role(s): Review, evaluation

    日本学術振興会  2022.4 - 2024.12

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    Type:Scientific advice/Review 

  • JST CREST 「細胞内現象の時空間ダイナミクス」領域の領域アドバイザー

    Role(s): Review, evaluation

    2021.4 - 2028.3

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    Type:Scientific advice/Review 

  • 日本学術振興会科学研究費補助金 基盤A 審査員

    Role(s): Review, evaluation

    2021.4 - 2024.3

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    Type:Scientific advice/Review 

Other

  • 小胞体とゴルジ体における亜鉛イオンに依存した新たなタンパク質品質管理機構とその分子構造基盤に関する論文を、最終責任著者として Nature Communications (2023a, 2023b)、Nature Communications (2024)に発表した。またゴルジ体におけるカルシウムを取り込むカルシウムポンプSPCA1aのクライオ電顕構造を世界で初めて解き、論文をScience Advances (2023)に発表した。

    2023.5

Research Projects

  • 科学研究費補助金 基盤A 「ゴルジ体カルシウム恒常性維持の分子細胞基盤」

    2024.4 - 2027.3

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    Authorship:Principal investigator 

  • ゴルジ体カルシウム恒常性維持の分子細胞基盤

    Grant number:24H00561  2024 - 2027

    日本学術振興会  科学研究費助成事業  基盤研究(A)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • SLCトランスポーターに関する共同研究

    2023.4 - 2025.3

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    Authorship:Principal investigator 

  • AMED-CREST 「ケミカルプロテオスタシス:レドックス、pH、金属イオンが織りなすタンパク質品質管理機構の研究開発」

    2021.10 - 2027.3

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    Authorship:Principal investigator 

  • 科学研究費補助金 学術変革領域研究A 「クロススケール細胞内分子構造動態解析が解明する小胞体恒常性維持機構」

    2021.10 - 2026.3

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    Authorship:Principal investigator 

  • AMED-CREST 「ケミカルプロテオスタシス:レドックス、pH、金属イオンが織りなすタンパク質恒常性維持機構の研究開発」

    2021 - 2026

    厚生労働科学研究費補助金 (厚生労働省)

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    Authorship:Principal investigator  Grant type:Contract research

  • クロススケール細胞内分子構造動態解析が解明する小胞体恒常性維持機構

    Grant number:21H05253  2021 - 2025

    日本学術振興会・文部科学省  科学研究費助成事業  学術変革領域研究(A)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 総括班:クロススケール新生物学

    Grant number:21H05247  2021 - 2025

    日本学術振興会・文部科学省  科学研究費助成事業  学術変革領域研究(A)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • 初期分泌経路における亜鉛恒常性維持とタンパク質恒常性維持の相関と分子構造基盤

    Grant number:21H04758  2021 - 2023

    日本学術振興会  科学研究費助成事業  基盤研究(A)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 亜鉛イオンとERp44の連携による分泌経路の新たなタンパク質品質管理機構

    Grant number:18H03978  2018 - 2020

    日本学術振興会  科学研究費助成事業  基盤研究(A)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 小胞体とゴルジ体間のpH勾配に依存した新たなタンパク質品質管理機構の分子基盤

    Grant number:15H04335  2015 - 2017

    日本学術振興会  科学研究費助成事業  基盤研究(B)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 新生鎖の立体構造形成を支えるジスルフィド形成システムの解明

    Grant number:26116005  2014 - 2018

    日本学術振興会・文部科学省  科学研究費助成事業  新学術領域研究(研究領域提案型)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 総括班:新生鎖の生物学

    Grant number:26116001  2014 - 2018

    日本学術振興会・文部科学省  科学研究費助成事業  新学術領域研究(研究領域提案型)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • タンパク質品質管理に関わるジスルフィド結合形成・開裂因子の分子基盤

    2010 - 2013

    日本学術振興会  最先端・次世代研究開発支援プログラム

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    Authorship:Principal investigator  Grant type:Joint research

  • 小胞体におけるタンパク質品質管理機構

    Grant number:19058008  2007 - 2011

    科学研究費助成事業  特定領域研究(A)

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • タンパク質品質管理機構

    Grant number:19GS0314  2007 - 2011

    科学研究費助成事業  学術創成研究費

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    Authorship:Coinvestigator(s)  Grant type:Scientific research funding

  • 蛋白質ジスルフィド結合の創生に関わる細胞マシーナリの構造生物化学

    Grant number:19687005  2007 - 2010

    科学研究費助成事業  若手研究(A,B)

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    Authorship:Principal investigator  Grant type:Scientific research funding

  • 蛋白質の巻戻り機構における、モジュール構造の役割の解明

    2000 - 2001

    日本学術振興会  科学研究費助成事業  特別研究員奨励費

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    Authorship:Principal investigator  Grant type:Scientific research funding

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Class subject

  • 生命医科学I、生命医科学特論I

    2024.4 - 2024.9   First semester

Visiting, concurrent, or part-time lecturers at other universities, institutions, etc.

  • 2024  東北大学学際科学フロンティア研究所  Classification:Affiliate faculty  Domestic/International Classification:Japan 

Media Coverage

  • 東北大・九大・京大・東大、クライオ電子顕微鏡によりゴルジ体の亜鉛輸送体による亜鉛輸送機構の全容を解明 Newspaper, magazine

    日本経済新聞  2023.8

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    東北大・九大・京大・東大、クライオ電子顕微鏡によりゴルジ体の亜鉛輸送体による亜鉛輸送機構の全容を解明

  • 東北大と九大、ゴルジ体の亜鉛調節機構を解明 Newspaper, magazine

    日本経済新聞  2023.5

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    東北大と九大、ゴルジ体の亜鉛調節機構を解明