{"id":174,"date":"2025-03-05T11:09:42","date_gmt":"2025-03-05T02:09:42","guid":{"rendered":"https:\/\/bsw3.naist.jp\/LabsW\/kimata\/?page_id=174"},"modified":"2025-08-14T12:48:43","modified_gmt":"2025-08-14T03:48:43","slug":"e_pub","status":"publish","type":"page","link":"https:\/\/bsw3.naist.jp\/kimata\/en\/e_pub\/","title":{"rendered":"PUBLICATIONS"},"content":{"rendered":"\n
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PUBLICATIONS<\/h1>\n<\/div><\/div>\n<\/div><\/div>\n\n\n\n
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Original Research Articles<\/h2>\n\n\n\n
    \n
  1. Ishiwata-Kimata Y, Nguyen PTM, Sugimoto M, Kimata Y
    “Potential of a constitutive-UPR and histone deacetylase A-deficient Saccharomyces cerevisiae strain for biomolecule production”
    Appl. Environ. Microbiol.<\/em> Vol.91, e0064425 (2025)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/40772766\/<\/a><\/li>\n\n\n\n
  2. Takano Y, Ishiwata-Kimata Y, Ushioda R, Kimata Y, Nakatsukasa K.
    “Hydroxyurea modulates thiol-disulfide homeostasis in the yeast endoplasmic reticulum”
    Life Sci. Alliance<\/em> Vol.8, e202503225 (2025)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/40541417\/<\/a><\/li>\n\n\n\n
  3. Ishiwata-Kimata Y, Monguchi M, Geronimo RAC, Sugimoto M, Kimata Y
    “Artificial induction of the UPR by Tet-off system-dependent expression of Hac1 and its application in Saccharomyces cerevisiae cells”
    Biosci. Biotechnol. Biochem.<\/em> Vol.89, 562-572 (2025)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/39953902\/<\/a><\/li>\n\n\n\n
  4. Nguyen SLT, Nguyen THT, Do TT, Nguyen TT, Le TH, Nguyen TAT, Kimata Y
    “Induction of endoplasmic reticulum stress by prodigiosin in yeast Saccharomyces cerevisiae”
    Curr. Issues Mol. Biol.<\/em> Vol.46, 1768-1776 (2024)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/38534732\/<\/a><\/li>\n\n\n\n
  5. Sogawa A, Komori R, Yanagitani K, Ohfurudono M, Tsuru A, Kadoi K, Kimata Y, Yoshida H, Kohno K
    “Signal sequence-triage is activated by translocon obstruction sensed by an ER stress sensor IRE1\u03b1”
    Cell Struct. Funct.<\/em> Vol.48, 211-221 (2023)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/37766570\/<\/a><\/li>\n\n\n\n
  6. Fauzee YNBM, Yoshida Y, Kimata Y
    “Endoplasmic stress sensor Ire1 is involved in cytosolic\/nuclear protein quality control in Pichia pastoris cells independent of HAC1”
    Front. Microbiol.<\/em> Vol.14, 1157146 (2023)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/37415818\/<\/a><\/li>\n\n\n\n
  7. Phuong HT, Ishiwata-Kimata Y, Kimata Y
    “An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response”
    Biochem. Biophys. Res. Commun.<\/em> Vol. 667, 58-63 (2023)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/37209563\/<\/a><\/li>\n\n\n\n
  8. Nguyen PTM, Ishiwata-Kimata Y, Kimata Y
    “Fast-growing Saccharomyces cerevisiae cells with a constitutive unfolded protein response and their potential for lipidic molecule production”
    Appl. Environ. Microbiol.<\/em> Vol.88, e0108322 (2022)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/36255243\/<\/a><\/li>\n\n\n\n
  9. Hata T, Ishiwata-Kimata Y, Kimata Y
    “Self-association status-dependent inactivation of the endoplasmic reticulum stress sensor Ire1 by C-terminal tagging with artificial peptides”
    Biosci. Biotechnol. Biochem.<\/em> Vol.86, 739-746 (2022)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/35285870\/<\/a><\/li>\n\n\n\n
  10. Hata T, Ishiwata-Kimata Y, Kimata Y
    “Induction of the unfolded protein response at high temperature in Saccharomyces cerevisiae”
    Int. J. Mol. Sci.<\/em> Vol.23, 1669 (2022)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/35163590\/<\/a><\/li>\n\n\n\n
  11. Ishiwata-Kimata Y, Le QG, Kimata Y
    “Induction and aggravation of the endoplasmic-reticulum stress by membrane-lipid metabolic intermediate phosphatidyl-N-monomethylethanolamine”
    Front. Cell Dev. Biol.<\/em> Vol.9, 743018 (2022)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/35071223\/<\/a><\/li>\n\n\n\n
  12. Phuong TH, Ishiwata-Kimata Y, Nishi Y, Oguchi N, Takagi H, Kimata Y
    “Aeration mitigates endoplasmic reticulum stress in Saccharomyces cerevisiae even without mitochondrial respiration.”
    Microb. Cell<\/em> Vol.8, 77-86 (2021)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/33816593\/<\/a><\/li>\n\n\n\n
  13.  Le QG, Ishiwata-Kimata Y, Phuong TH, Fukunaka S, Kohno K, Kimata Y
    “The ADP-binding kinase region of Ire1 directly contributes to its responsiveness to endoplasmic reticulum stress.”
    Sci. Rep.<\/em> Vol.11, 4506 (2021)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/33627709\/<\/a><\/li>\n\n\n\n
  14.  Fauzee YNBM, Taniguchi N, Ishiwata-Kimata Y, Takagi H, Kimata Y
    “The unfolded protein response in Pichia pastoris without external stressing stimuli.”
    FEMS Yeast Res.<\/em> Vol.20, foaa053, (2020)
    https:\/\/pubmed.ncbi.nlm.nih.gov\/33775971\/<\/a><\/li>\n\n\n\n
  15. Tran DM, Ishiwata-Kimata Y, Mai TC, Kubo M, Kimata Y.
    \u201cThe unfolded protein response alongside the diauxic shift of yeast cells and its involvement in mitochondria enlargement.\u201d
    Sci. Rep.<\/em> Vol. 9 12780 (2019)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31484935<\/a><\/li>\n\n\n\n
  16. Mai TC, Ishiwata-Kimata Y, Le QG, Kido H, Kimata Y.
    \u201cDispersion of endoplasmic reticulum-associated compartments by 4-phenyl butyric acid in yeast cells.\u201d
    Cell. Struct. Funct.<\/em> Vol. 44, 173-182 (2019)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31619600<\/a><\/li>\n\n\n\n
  17. Nguyen PTM, Ishiwata-Kimata Y, Kimata Y.
    \u201cMonitoring ADP\/ATP ratio in yeast cells using the fluorescent-protein reporter PercevalHR.\u201d
    Biosci. Biotechnol. Biochem.<\/em> Vol. 83, 824-828 (2019)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30704350<\/a><\/li>\n\n\n\n
  18. Tran DM, Takagi H, Kimata Y.
    \u201cCategorization of endoplasmic reticulum stress as accumulation of unfolded proteins or membrane lipid aberrancy using yeast Ire1 mutants.\u201d
    Biosci. Biotechnol. Biochem.<\/em> Vol. 83, 326-329 (2019)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30319071<\/a><\/li>\n\n\n\n
  19. Mai TC, Munakata T, Tran DM, Takagi H, Kimata Y.
    \u201cA chimeric mutant analysis in yeast cells suggests BiP independent regulation of the mammalian endoplasmic reticulum-stress sensor IRE1\u03b1.\u201d
    Biosci. Biotechnol. Biochem.<\/em> Vol. 82, 1527-1530 (2018)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29806786<\/a><\/li>\n\n\n\n
  20. Mai CT, Le QG, Ishiwata-Kimata Y, Takagi H, Kohno K, Kimata Y.
    \u201c4-Phenylbutyrate suppresses the unfolded protein response without restoring protein folding in Saccharomyces cerevisiae.\u201d
    FEMS Yeast Res.<\/em> Vol. 18, foy016 (2018)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29452364<\/a><\/li>\n\n\n\n
  21. Itooka K, Takahashi K, Kimata Y, Izawa S.
    \u201cCold atmospheric pressure plasma causes protein denaturation and endoplasmic reticulum stress in Saccharomyces cerevisiae.\u201d
    Appl. Microbiol. Biotechnol.<\/em> Vol. 102, 2279-2288 (2018)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29356871<\/a><\/li>\n\n\n\n
  22. Kawazoe N, Kimata Y, Izawa S.
    \u201cAcetic acid causes endoplasmic reticulum stress and induces the unfolded protein response in Saccharomyces cerevisiae.\u201d
    Front. Microbiol.<\/em> Vol. 8, 1192 (2017)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28702017<\/a><\/li>\n\n\n\n
  23. Le QG, Ishiwata-Kimata Y, Kohno K, Kimata Y.
    \u201cCadmium impairs protein folding in the endoplasmic reticulum and induces the unfolded protein response.\u201d
    FEMS Yeast Res.<\/em> Vol.16, fow049 (2016)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27298227<\/a><\/li>\n\n\n\n
  24. Mathuranyanon R, Tsukamoto T, Takeuchi A, Ishiwata-Kimata Y, Tsuchiya Y, Kohno K, Kimata Y.
    \u201cTight regulation of the unfolded protein sensor Ire1 by its intramolecularly antagonizing subdomain.\u201d
    J. Cell Sci.<\/em> Vol.128, 1762-172 (2015)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25770101<\/a><\/li>\n\n\n\n
  25. Mochizuki T, Kimata Y, Uemura S, Abe F.
    \u201cRetention of chimeric Tat2-Gap1 permease in the endoplasmic reticulum induces unfolded protein response in Saccharomyces cerevisiae.\u201d
    FEMS Yeast Res.<\/em> Vol.15, fov044 (2015)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/26071436<\/a><\/li>\n\n\n\n
  26. Miyagawa D, Ishiwata-Kimata Y, Kohno K, Kimata Y
    \u201cEthanol stress impairs protein folding in the endoplasmic reticulum and activates Ire1 in Saccharomyces cerevisiae.\u201d
    Biosci. Biotechnol. Biochem.<\/em> Vol.78,1389-1391 (2014)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25130742<\/a><\/li>\n\n\n\n
  27. Ishiwata-Kimata Y, Yamamoto YH, Takizawa K, Kohno K, Kimata Y
    \u201cF-actin and a type-II myosin are required for efficient clustering of the ER stress sensor Ire1.\u201d
    Cell Struct. Funct.<\/em> Vol.38, 135-143 (2013)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23666407<\/a><\/li>\n\n\n\n
  28.  Ishiwata-Kimata Y, Promlek T, Kohno K, Kimata Y
    \u201cBiP-bound and nonclustered mode of Ire1 evokes a weak but sustained unfolded protein response.\u201d
    Genes Cells<\/em> Vol.18, 288-301, 2013
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23387983<\/a><\/li>\n\n\n\n
  29. Nguyen TSL, Kohno K, Kimata Y
    \u201cZinc depletion activates the endoplasmic reticulum-stress sensor Ire1 via pleiotropic mechanisms.\u201d
    Biosci. Biotechnol. Biochem.<\/em> Vol. 77, 1337-1339 (2013)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23748779<\/a><\/li>\n\n\n\n
  30. Promlek T, Ishiwata-Kimata Y, Shido M, Sakuramoto M, Kohno K, Kimata Y
    \u201cMembrane aberrancy and unfolded aroteins activate the endoplasmic reticulum-stress sensor Ire1 by different manners.\u201d
    Mol. Biol. Cell <\/em>Vol.22, 3520-3532 (2011)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21775630<\/a><\/li>\n\n\n\n
  31. Yanagitani K, Kimata Y, Kadokura H, Kohno K
    \u201cTranslational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA.\u201d
    Science<\/em> Vol.331, 586-589 (2011)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21233347<\/a><\/li>\n\n\n\n
  32. Yamamoto YH, Kimura T, Momohara S, Takeuchi M, Tani T, Kimata Y, Kadokura H, Kohno K
    \u201cA novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR.\u201d
    Cell Struct. Funct.<\/em> Vol.35, 107-116 (2010)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21150129<\/a><\/li>\n\n\n\n
  33. Yanagitani K, Imagawa Y, Iwawaki T, Hosoda A, Saito M, Kimata Y, Kohno K
    \u201cCotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA.\u201d
    Mol. Cell<\/em> Vol.34, 191-200 (2009)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/19394296<\/a><\/li>\n\n\n\n
  34. Oikawa D, Kimata Y, Kohno K, Iwawaki T
    \u201cActivation of mammalian IRE1alpha upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins.\u201d
    Exp. Cell Res.<\/em> Vol. 315, 2496-2504 (2009)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/19538957<\/a><\/li>\n\n\n\n
  35. Takeuchi M, Kimata Y, Kohno K
    \u201cSaccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum.\u201d
    Mol. Biol. Cell<\/em> Vol.19, 3514-3525 (2008)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/18508919<\/a><\/li>\n\n\n\n
  36. Kimata Y, Ishiwata-Kimata Y, Ito T, Hirata A, Suzuki T, Oikawa D, Takeuchi M, Kohno K
    \u201cTwo regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.\u201d
    J. Cell Biol.<\/em> Vol.179, 75-86 (2007)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/17923530<\/a><\/li>\n\n\n\n
  37. Kimura Y, Saito M, Kimata Y, Kohno K
    \u201cTransgenic mice expressing a fully nontoxic diphtheria toxin mutant, not CRM197 mutant, acquire immune tolerance against diphtheria toxin.\u201d
    J. Biochem. <\/em>Vol.142, 105-112 (2007)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/17522091<\/a><\/li>\n\n\n\n
  38. Oikawa D, Kimata Y, Kohno K
    \u201cSelf-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1.\u201d
    J. Cell Sci.<\/em> Vol.120, 1681-1688 (2007)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/17452628<\/a><\/li>\n\n\n\n
  39. Takeuchi M, Kimata Y, Hirata A, Oka M, Kohno K
    \u201cSaccharomyces cerevisiae Rot1p Is an ER-Localized Membrane Protein That May Function with BiP\/Kar2p in Protein Folding.\u201d
    J. Biochem.<\/em> Vol.139, 597-605 (2006)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/16567426<\/a><\/li>\n\n\n\n
  40. Kimata Y, Ishiwata-Kimata Y, Yamada S, Kohno K
    \u201cYeast unfolded protein response pathway regulates expression of genes for anti-oxidative stress and for cell surface proteins.\u201d
    Genes Cells<\/em> Vol.11, 59-69 (2006)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/16371132<\/a><\/li>\n\n\n\n
  41. Oikawa D, Kimata Y, Takeuchi M, Kohno K
    \u201cAn essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1.\u201d
    Biochem J.<\/em> Vol.391, 135-142 (2005)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15954865<\/a><\/li>\n\n\n\n
  42. Kimata Y, Oikawa D, Shimizu Y, Ishiwata-Kimata Y, Kohno, K
    \u201cA role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1.\u201d
    J. Cell Biol.<\/em> Vol.167, 445-456 (2004)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15520230<\/a><\/li>\n\n\n\n
  43. Kimata Y, Kimata YI, Shimizu Y, Abe H, Farcasanu IC, Takeuchi M, Rose MD, Kohno K
    \u201cGenetic evidence for a role of BiP\/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.\u201d
    Mol. Biol. Cell<\/em> Vol.14, 2559-2569 (2003)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/12808051<\/a><\/li>\n\n\n\n
  44. Ohdate H, Lim CR, Kokubo T, Matsubara K, Kimata Y, Kohno K
    \u201cImpairment of the DNA binding activity of the TATA-binding protein renders the transcriptional function of Rvb2p\/Tih2p, the yeast RuvB-like protein, essential for cell growth.\u201d
    J. Biol. Chem.<\/em> Vol.278, 14647-14656 (2003)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/12576485<\/a><\/li>\n\n\n\n
  45. Hosoda A, Kimata Y, Tsuru A, Kohno K
    \u201cJPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs.\u201d
    J. Biol. Chem.<\/em> Vol.278, 2669-2676 (2003)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/12446677<\/a><\/li>\n\n\n\n
  46. Fujioka Y, Kimata Y, Nomaguchi K, Watanabe K, Kohno K
    \u201cIdentification of a novel non-structural maintenance of chromosomes (SMC) component of the SMC5\/SMC6 complex involved in DNA repair.\u201d
    J. Biol. Chem. <\/em>Vol.277, 21585-21591 (2002)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11927594<\/a><\/li>\n\n\n\n
  47. Okushima Y, Koizumi N, Yamaguchi Y, Kimata Y, Kohno K, Sano H
    \u201cIsolation and characterization of a putative transducer of endoplasmic reticulum stress in Oryza sativa.\u201d
    Plant Cell Physiol.<\/em> Vol.43, 532-539, 2002
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/12040100<\/a><\/li>\n\n\n\n
  48. Koizumi N, Martinez I, Kimata Y, Kohno K, Sano H, Chrispeels MJ
    \u201cMolecular characterization of two Arabidopsis Ire1 homologs, endoplasmic reticulum located transmembrane protein kinases.\u201d
    Plant Physiol.<\/em> Vol.127, 949-962, 2001
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11706177<\/a><\/li>\n\n\n\n
  49. Saito M, Iwawaki T, Taya C, Yonekawa H, Noda M, Inui Y, Mekada E, Kimata Y, Tsuru A, Kohno K
    \u201cDiphtheria toxin receptor-mediated conditional and targeted cell ablation in transgenic mice.\u201d
    Nature Biotechnol.<\/em> Vol.19, 746-750 (2001)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11479567<\/a><\/li>\n\n\n\n
  50.  Iwawaki T, Hosoda A, Okuda T, Kamigori Y, Nomura-Furuwatari C, Kimata Y, Tsuru A, Kohno K
    \u201cTranslation control by ER transmembrane kinase\/ribonuclease IRE1 under ER stress.\u201d
    Nature Cell Biol.<\/em> Vol.3, 158-164 (2001)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11175748<\/a><\/li>\n\n\n\n
  51. Kimata Y, Ooboki K, Nomura-Furuwatari C, Hosoda A, Tsuru A, Kohno K
    \u201cIdentification of a novel mammalian endoplasmic reticulum-resident KDEL protein using an EST database motif search.\u201d
    Gene<\/em> Vol.261, 321-327 (2000)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11167020<\/a><\/li>\n\n\n\n
  52. Yoshizawa F, Miura Y, Tsurumaru K, Kimata Y, Yagasaki K, Funabiki R
    \u201cElongation factor 2 in the liver and skeletal muscle of mice is decreased by starvation.\u201d
    Biosci. Biotechnol. Biochem.<\/u><\/em> Vol.64, 2482-2485 (2000)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11193422<\/a><\/li>\n\n\n\n
  53. Okamura K, Kimata Y, Higashio H, Tsuru A, Kohno K
    \u201cDissociation of Kar2p\/BiP from an endoplasmic reticulum sensory molecule, Ire1p, triggers unfolded protein response in yeast.\u201d
    Biochem. Biophys. Res. Commun.<\/em> Vol.279, 445-450 (2000)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/11118306<\/a><\/li>\n\n\n\n
  54.  Lim CR, Kimata Y, Ohdate H, Kokubo T, Kikuchi N, Horigome T, Kohno K
    \u201cThe Saccharomyces cerevisiae RuvB-like protein, Tih2p is required for cell cycle progression.\u201d
    J. Biol. Chem.<\/em> Vol.275, 22409-22417 (2000)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10787406<\/a><\/li>\n\n\n\n
  55. Higashio H, Kimata Y, Kiriyama T, Hirata A, Kohno K
    \u201cSfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum.\u201d
    J. Biol. Chem.<\/em> Vol.275, 17900-17908 (2000)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10749860<\/a><\/li>\n\n\n\n
  56. Kimata Y, Higashio H, Kohno K
    \u201cImpaired proteasome function rescues thermosensitivity of yeast cells lacking the coatomer subunit epsilon-COP.\u201d
    J. Biol. Chem.<\/em> Vol.275, 10655-10660 (2000)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10744762<\/a><\/li>\n\n\n\n
  57. Kimata Y, Lim CR, Kiriyama T, Nara A, Hirata A, Kohno K
    \u201cMutation of the yeast epsilon-COP gene ANU2 causes abnormal nuclear morphology and defects in intracellular vesicular transport.\u201d
    Cell Struct. Funct.<\/em> Vol.24, 197-208 (1999)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10532354<\/a><\/li>\n\n\n\n
  58. Oka M, Nakai M, Endo T, Lim CR, Kimata Y, Kohno K
    \u201cLoss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae.\u201d
    J. Biol. Chem.<\/em> Vol.273, 29727-29737 (1998)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/9792686<\/a><\/li>\n\n\n\n
  59.  Kimata Y, Iwaki M, Lim CR, Kohno K
    \u201cA novel mutation which enhances the fluorescence of green fluorescent protein at high temperatures.\u201d
    Biochem. Biophys. Res. Commun.<\/em> Vol.232, 69-73 (1997)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/9125154<\/a><\/li>\n\n\n\n
  60. Oka M, Kimata Y, Mori K, Kohno K
    \u201cSaccharomyces cerevisiae KAR2 (BiP) gene expression is induced by loss of cytosolic HSP70\/Ssa1p through a heat shock element-mediated pathway.\u201d
    J. Biochem.<\/em> Vol.121, 578-584 (1997)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/9133628<\/a><\/li>\n\n\n\n
  61.  Lim CR, Kimata Y, Oka M, Nomaguchi K, Kohno K
    \u201cThermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin NSP1.\u201d
    J. Biochem.<\/em> Vol.118, 13-17 (1995)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/8537302<\/a><\/li>\n\n\n\n
  62. Kimata Y, Kohno K
    \u201cElongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth.\u201d
    J. Biol. Chem.<\/em> Vol.269, 13497-134501 (1994)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/8175783<\/a><\/li>\n\n\n\n
  63. Kimata Y, Harashima S, Kohno K
    \u201cExpression of non-ADP-ribosylatable, diphtheria toxin-resistant elongation factor 2 in Saccharomyces cerevisiae.\u201d
    Biochem. Biophys. Res. Commun.<\/em> Vol.191, 1145-1151 (1993)
    https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/8466491<\/a><\/li>\n\n\n\n
  64. Masui M, Tsuchida K, Kimata Y, Ozaki S
    \u201cEpoxidation catalyzed by manganese(III) tetraphenylporphyrin chloride using dioxygen activated by a novel system containing N-hydroxyphthalimide and styrene.\u201d
    Chem. Pharm. Bull.<\/em> Vol.35, 3078-3081 (1987)
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    Reviews and Book Chapters in English Language<\/h2>\n\n\n\n
      \n
    1. Monguchi M, Kimata Y
      “Enforcement and enlargement of the Saccharomyces cerevisiae endoplasmic reticulum through artificial evocation of the unfolded protein response”
      IgMin Research<\/em> Vol.2 (2024)
      https:\/\/www.igminresearch.com\/articles\/html\/igmin142<\/a><\/li>\n\n\n\n
    2. Ishiwata-Kimata Y, Kimata Y
      “Fundamental and applicative aspects of the unfolded protein response in yeasts”
      J. Fungi (Basel)<\/em> Vol.9, 989 (2023)
      https:\/\/pubmed.ncbi.nlm.nih.gov\/37888245\/<\/a><\/li>\n\n\n\n
    3. Le QG, Kimata Y.
      “Multiple ways for stress sensing and regulation of the endoplasmic reticulum-stress sensors.”
      Cell Struct. Funct.<\/em> Vol.46, 37-49 (2021)
      https:\/\/pubmed.ncbi.nlm.nih.gov\/33775971\/<\/a><\/li>\n\n\n\n
    4. Ishiwata-Kimata Y, Le QG, Kimata Y.
      \u201cStress-sensing and regulatory mechanism of the endoplasmic-stress sensors Ire1 and PERK.\u201d
      Endoplasmic Reticulum Stress in Diseases<\/em> Vol.5, 1-10 (2018)
      https:\/\/www.degruyter.com\/view\/j\/ersc.2018.5.issue-1\/ersc-2018-0001\/ersc-2018-0001.xml<\/a><\/li>\n\n\n\n
    5. Tran DM, Kimata Y.
      \u201cThe unfolded protein response of yeast Saccharomyces cerevisiae and other organisms.\u201d
      Plant Morphology<\/em> Vol.30, 15-24 (2018)
      https:\/\/www.jstage.jst.go.jp\/article\/plmorphol\/30\/1\/30_15\/_article\/-char\/en<\/a><\/li>\n\n\n\n
    6. Kimata Y, Nguyen PTM, Kohno K
      \u201cResponse and cytoprotective mechanisms against proteotoxic stress in yeast and fungi.\u201d
      in Stress Response Mechanisms in Fungi -Theoretical and Practical Aspects<\/em>– (Book) pp. 161-188, Springer
      https:\/\/www.springer.com\/gp\/book\/9783030006822<\/a><\/li>\n\n\n\n
    7. Oikawa D, Kimata Y
      \u201cExperimental approaches for elucidation of stress-sensing mechanisms of the Ire1 family proteins.\u201d
      Methods Enzymol.<\/em> Vol.490, 195-216 (2011)<\/li>\n\n\n\n
    8.  Kimata Y, Kohno K
      \u201cEndoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells\u201d
      Curr. Opp. Cell. Biol.<\/em> Vol.23, 135-142 (2011)
      https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21093243<\/a><\/li>\n\n\n\n
    9. Takeuchi M, Kimata Y, Kohno K
      \u201cCausal links between protein folding in the ER and events along the secretory pathway.\u201d
      Autophagy<\/em> Vol.2, 323-324 (2006)
      https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/16874095<\/a><\/li>\n\n\n\n
    10. Kimata Y, Lim CR, Kohno K
      \u201cS147P green fluorescent protein: a less thermosensitive green fluorescent protein variant.\u201d
      Methods Enzymol.<\/em> Vol.302, 373-378 (1999)
      <\/li>\n<\/ol>\n\n\n\n
      <\/div>\n\n\n\n

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      Reviews and Book Chapters in English Language<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"neve_meta_sidebar":"","neve_meta_container":"","neve_meta_enable_content_width":"on","neve_meta_content_width":100,"neve_meta_title_alignment":"","neve_meta_author_avatar":"","neve_post_elements_order":"","neve_meta_disable_header":"","neve_meta_disable_footer":"","neve_meta_disable_title":"on","footnotes":""},"class_list":["post-174","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/bsw3.naist.jp\/kimata\/wp-json\/wp\/v2\/pages\/174","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/bsw3.naist.jp\/kimata\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/bsw3.naist.jp\/kimata\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/bsw3.naist.jp\/kimata\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/bsw3.naist.jp\/kimata\/wp-json\/wp\/v2\/comments?post=174"}],"version-history":[{"count":0,"href":"https:\/\/bsw3.naist.jp\/kimata\/wp-json\/wp\/v2\/pages\/174\/revisions"}],"wp:attachment":[{"href":"https:\/\/bsw3.naist.jp\/kimata\/wp-json\/wp\/v2\/media?parent=174"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}