Updated on 2024/11/07

写真a

 
FURUKAWA Kazuhiro
 
Organization
Academic Assembly Institute of Science and Technology Fundamental Sciences Professor
Graduate School of Science and Technology Fundamental Sciences Professor
Faculty of Science Department of Science Professor
Title
Professor
External link

Degree

  • 医学博士 ( 1990.3   京都大学 )

Research History

  • Niigata University   Faculty of Science Department of Science   Professor

    2017.4

  • Niigata University   Graduate School of Science and Technology Fundamental Sciences   Professor

    2013.4

  • Niigata University   Graduate School of Science and Technology Fundamental Sciences   Professor

    2013.4

  • Niigata University   Faculty of Science Department of Chemistry   Professor

    2013.4 - 2017.3

  • Niigata University   Faculty of Science Department of Chemistry   Associate Professor

    2004.4 - 2013.3

 

Papers

  • Non-farnesylated B-type lamin can tether chromatin inside the nucleus and its chromatin interaction requires the Ig-fold region Reviewed

    Ryo Uchino, Shin Sugiyama, Motoi Katagiri, Yoshiro Chuman, Kazuhiro Furukawa

    CHROMOSOMA   126 ( 1 )   125 - 144   2017.2

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

    Lamins are thought to direct heterochromatin to the nuclear lamina (NL); however, this function of lamin has not been clearly demonstrated in vivo. To address this, we analyzed (p)olytene chromosome morphology when artificial lamin variants were expressed in Drosophila endoreplicating cells. We found that the CaaX-motif-deleted B-type lamin Dm(0), but not A-type lamin C, was able to form a nuclear envelope-independent layer that was closely associated with chromatin. Other nuclear envelope proteins were not detected in this "ectopic lamina," and the associated chromatin showed a repressive histone modification maker but not a permissive histone modification marker nor RNA polymerase II proteins. Furthermore, deletion of the C-terminal lamin-Ig-fold domain prevents chromatin association with this ectopic lamina. Thus, non-farnesylated B-type lamin Dm(0) can form an ectopic lamina and induce changes to chromatin structure and status inside the interphase nucleus.

    DOI: 10.1007/s00412-016-0581-x

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  • Loss of Drosophila A-type lamin C initially causes tendon abnormality including disintegration of cytoskeleton and nuclear lamina in muscular defects Reviewed

    Ryo Uchino, Yu-ki Nonaka, Tuneyoshi Horigome, Shin Sugiyama, Kazuhiro Furukawa

    DEVELOPMENTAL BIOLOGY   373 ( 1 )   216 - 227   2013.1

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ACADEMIC PRESS INC ELSEVIER SCIENCE  

    Lamins are the major components of nuclear envelope architecture, being required for both the structural and informational roles of the nuclei. Mutations of lamins cause a spectrum of diseases in humans, including muscular dystrophy. We report here that the loss of the A-type lamin gene, lamin C in Drosophila resulted in pupal metamorphic lethality caused by tendon defects, matching the characteristics of human A-type lamin revealed by Emery-Dreifuss muscular dystrophy (EDMD). In tendon cells lacking lamin C activity, overall cell morphology was affected and organization of the spectraplakin family cytoskeletal protein Shortstop which is prominently expressed in tendon cells gradually disintegrated, notably around the nucleus and in a manner correlating well with the degradation of musculature. Furthermore, lamin C null mutants were efficiently rescued by restoring lam in C expression to shortstop-expressing cells, which include tendon cells but exclude skeletal muscle cells. Thus the critical function of A-type lamin C proteins in Drosophila musculature is to maintain proper function and morphology of tendon cells. (C) 2012 Elsevier Inc. All rights reserved.

    DOI: 10.1016/j.ydbio.2012.08.001

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  • A-type and B-type lamins initiate layer assembly at distinct areas of the nuclear envelope in living cells Reviewed

    Kazuhiro Furukawa, Kazuya Ishida, Taka-aki Tsunoyama, Suguru Toda, Shinichi Osoda, Tsuneyoshi Horigome, Paul A. Fisher, Shin Sugiyama

    EXPERIMENTAL CELL RESEARCH   315 ( 7 )   1181 - 1189   2009.4

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ELSEVIER INC  

    To investigate nuclear lamina re-assembly in vivo, Drosophila A-type and B-type lamins were artificially expressed in Drosophila lamin Dm(0) null mutant brain cells. Both exogenous lamin C (A-type) and Dm(0) (B-type) formed sub-layers at the nuclear periphery, and efficiently reverted the abnormal Clustering of the NPC. Lamin C initially appeared where NPCs were clustered, and subsequently extended along the nuclear periphery accompanied by the recovery of the regular distribution of NPCs. In contrast, lamin Dm(0) did not show association with the clustered NPCs during lamina formation and NPC spacing recovered only after completion of a closed lamin Dm(0) layer. Further, when lamin Dm(0) and C were both expressed, they did not co-polymerize, initiating layer formation in separate regions. Thus, A and B-type lamins reveal differing properties during lamina assembly, with A-type having the primary role in organizing NPC distribution. This previously unknown complexity in the assembly of the nuclear lamina could be the basis for intricate nuclear envelope functions. (C) 2008 Published by Elsevier Inc.

    DOI: 10.1016/j.yexcr.2008.12.024

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  • BAF as a caspase-dependent mediator of nuclear apoptosis in Drosophila Reviewed

    Kazuhiro Furukawa, Tomoko Aida, Yuki Nonaka, Shinichi Osoda, Candido Juarez, Tsuneyoshi Horigome, Shin Sugiyama

    JOURNAL OF STRUCTURAL BIOLOGY   160 ( 2 )   125 - 134   2007.11

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    BAF is a double-stranded DNA binding protein required for proper nuclear morphology and function in Drosophila development. Imaginal discs of Drosophila baf-null mutants were found to exist only in younger larvae as small degenerative tissues. Immunohistochemical analyses showed diffuse lamin distribution, DNA fragmentation, and activation of caspase drICE in these tissues, suggesting that apoptotic events can be induced by the loss of baf. We therefore investigated the fate of BAF after induction of the pro-apoptotic hid transgene, and found that the loss of DNA binding forms of BAF preceded that of non-DNA binding forms of BAF. Furthermore, the DNA binding forms of BAF disappeared from nuclei before DNA fragmentation and NPC clustering were detected, showing that the loss of BAF occurs at the initial stages of nuclear apoptosis. This BAF loss was not detected before drICE activation and was inhibited by Ac-DEVD-CHO caspase inhibitors. In summary, BAF disappears at an early stage due to caspase activity when apoptosis is induced by hid, and its depletion in mutants is sufficient in itself to induce cell death, suggesting it is an apoptotic mediator. (C) 2007 Elsevier Inc. All rights reserved.

    DOI: 10.1016/j.jsb.2007.07.010

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  • Nuclear envelope precursor vesicle targeting to chromatin is stimulated by protein phosphatase 1 in Xenopus egg extracts Reviewed

    Hiromi Ito, Yuhei Koyama, Makoto Takano, Kohei Ishii, Mitsugu Maeno, Kazuhiro Furukawa, Tsuneyoshi Horigome

    EXPERIMENTAL CELL RESEARCH   313 ( 9 )   1897 - 1910   2007.5

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    The mechanism underlying targeting of the nuclear membrane to chromatin at the end of mitosis was studied using an in vitro cell-free system comprising Xenopus egg membrane and cytosol fractions, and sperm chromatin. The mitotic phase membrane, which was separated from a mitotic phase extract of Xenopus eggs and could not bind to chromatin, became able to bind to chromatin on pretreatment with a synthetic phase cytosol fraction of Xenopus eggs. When the cytosol fraction was depleted of protein phosphatase 1 (PP1) with anti-Xenopus PP1-gamma 1 antibodies, this ability was lost. The addition of recombinant xPP1 gamma 1 to the PP1-depleted cytosol fraction restored the ability. These and other results suggested that dephosphorylation of mitotic phosphorylation sites on membranes by PP1 in the synthetic phase cytosol fraction promoted targeting of the membranes to chromatin. On the other hand, a fragment containing the chromatin-binding domain of lamin B receptor (LBR) but not emerin inhibited targeting of membrane vesicles. It was also shown that PP1 dephosphorylates a phosphate group(s) responsible for regulation of the binding of LBR to chromatin. A possible mechanism involving PP1 and LBR for the regulation of nuclear membrane targeting to chromatin was discussed. (c) 2007 Elsevier Inc. All rights reserved.

    DOI: 10.1016/j.yexcr.2007.03.015

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  • [Nuclear envelopathies]. Reviewed

    Furukawa K, Nonaka Y, Osouda S, Horigome T

    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   51 ( 14 Suppl )   2263 - 2268   2006.11

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  • [Nuclear membrane and nuclear lamina]. Reviewed

    Furukawa K, Osouda S, Horigome T

    Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   51 ( 14 Suppl )   1931 - 1936   2006.11

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  • Null mutants of Drosophila B-type lamin Dm(0) show aberrant tissue differentiation rather than obvious nuclear shape distortion or specific defects during cell proliferation Reviewed

    S Osouda, Y Nakamura, B de Saint Phalle, M McConnell, T Horigome, S Sugiyama, PA Fisher, K Furukawa

    DEVELOPMENTAL BIOLOGY   284 ( 1 )   219 - 232   2005.8

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ACADEMIC PRESS INC ELSEVIER SCIENCE  

    To elucidate the function of metazoan B-type lamins during development, new null mutations of the Drosophila B-type lamin gene, lamDm(0), were analyzed in parallel with the misg(sz18) mutation, a lamDm(0) allele reported previously. Although in all these mutants, lamin Dm(0) protein was undetectable in neuroblasts and imaginal disc cells from the second instar larval stage onward, cells continued to proliferate. In contrast to the embryonic lethality of another Drosophila lamDm(0) allele, lam(PM15), reported previously, lethality did not occur until late pupal stages. Chromosomal structure and the overall nuclear shape remained normal even at these late pupal stages, although obviously abnormal nuclear pore complex distribution was observed concomitant with the loss of lamin Dm(0) protein. Compensating expression of lamin C was not induced in the absence of lamin Dm(0). Thus, no lamin-containing nuclear structures were found in proliferating larval neuroblasts. We did find that developmental abnormalities appeared in specific organs during the late pupal stage, preceding lethality. Surprisingly, coordinated size increase (hypertrophy) of the ventriculus was observed accompanied by cell division and muscle layer formation. Hypertrophy of the ventriculus correlated with a decrease in ecdysteroid hormone receptor B 1 (EcRB1) protein, and furthermore could be suppressed by a heat-inducible EcRB1 transgene. In contrast, both gonadal and CNS tissues exhibited underdevelopment. (c) 2005 Elsevier Inc. All rights reserved.

    DOI: 10.1016/j.ydbio.2005.05.022

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  • LAP2 alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly Reviewed

    T Dechat, A Gajewski, B Korbei, D Gerlich, N Daigle, T Haraguchi, K Furukawa, J Ellenberg, R Foisner

    JOURNAL OF CELL SCIENCE   117 ( 25 )   6117 - 6128   2004.12

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:COMPANY OF BIOLOGISTS LTD  

    Lamina-associated polypeptide (LAP) 2alpha is a LEM (lamina-associated polypeptide emerin MAN1) family protein associated with nucleoplasmic A-type lamins and chromatin. Using live cell imaging and fluorescence microscopy we demonstrate that LAP2alpha was mostly cytoplasmic in metaphase and associated with telomeres in anaphase. Telomeric LAP2alpha clusters grew in size, formed 'core' structures on chromatin adjacent to the spindle in telophase, and translocated to the nucleoplasm in G1 phase. A subfraction of lamin C and emerin followed LAP2alpha to the core region early on, whereas LAP2beta, lamin B receptor and lamin B initially bound to more peripheral regions of chromatin, before they spread to core structures with different kinetics. Furthermore, the DNA-crosslinking protein barrier-to-autointegration factor (BAF) bound to LAP2alpha in vitro and in mitotic extracts, and subfractions of BAF relocalized to core structures with LAP2alpha. We propose that LAP2alpha and a subfraction of BAF form defined complexes in chromatin core regions and may be involved in chromatin reorganization during early stages of nuclear assembly.

    DOI: 10.1242/jcs.01529

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  • Regulation of binding of lamin B receptor to chromatin by SR protein kinase and cdc2 kinase in Xenopus egg extracts Reviewed

    M Takano, Y Koyama, H Ito, S Hoshino, H Onogi, M Hagiwara, K Furukawa, T Horigome

    JOURNAL OF BIOLOGICAL CHEMISTRY   279 ( 13 )   13265 - 13271   2004.3

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

    Participation of multiple kinases in regulation of the binding of lamin B receptor (LBR) to chromatin was suggested previously (Takano, M., Takeuchi, M., Ito, H., Furukawa, K., Sugimoto, K., Omata, S., and Horigome, T. (2002) Eur. J. Biochem. 269, 943 - 953). To identify these kinases, regulation of the binding of the nucleoplasmic region (NK, amino acid residues 1 - 211) of LBR to sperm chromatin was studied using a cell cycle-dependent Xenopus egg extract in vitro. The binding was stimulated on specific phosphorylation of the NK fragment by an S-phase egg extract. Protein depletion with beads bearing SF2/ASF, which binds SR protein kinases, abolished this stimulation, suggesting that an SR protein kinase(s) is responsible for the activation of LBR. This was confirmed by direct phosphorylation and activation with recombinant SR protein-specific kinase 1. The binding of the NK fragment to chromatin pretreated with an S-phase extract was suppressed by incubation with an M-phase extract. Enzyme inhibitor experiments revealed that multiple kinases participate in the suppression. One of these kinases was shown to be cdc2 kinase using a specific inhibitor, roscovitine, and protein depletion with beads bearing p13, which specifically binds cdc2 kinase. Experiments involving a mutant NK fragment showed that the phosphorylation of serine 71 by cdc2 kinase is responsible for the suppression.

    DOI: 10.1074/jbc.M308854200

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Books

  • 核および染色体構造形成におけるBAFの機能解析

    古川 和広

    [古川和広]  2006 

MISC

  • Phosphoproteome analysis of schizophrenia model mouse brain

    Hashimoto Yoshiya, Akashi Kaori, Sakimura Kenji, Furukawa Kazuhiro, Horigome Tsuneyoshi

    Abstracts for Annual Meeting of Japanese Proteomics Society   2012 ( 0 )   184 - 184   2012

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    Language:Japanese   Publisher:日本プロテオーム学会(日本ヒトプロテオーム機構)  

    DOI: 10.14889/jhupo.2012.0.184.0

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  • Proteome analysis of a HeLa cell nuclear matrix fraction

    Ishii Kohei, Hirano Yasuhiro, Kumeta Masahiro, Takeyasu Kunio, Furukawa Kazuhiro, Horigome Tsuneyoshi

    Abstracts for Annual Meeting of Japanese Proteomics Society   2007 ( 0 )   75 - 75   2007

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    Language:Japanese   Publisher:日本プロテオーム学会(日本ヒトプロテオーム機構)  

    細胞核は、"構造"と"機能"が密接に関わり合ったダイナミックな構造体である。その内部には、核小体や核スペックルなどの核内構造体が存在し、プロテオーム解析によってそれらの構成因子が解析されてきたが、これまでの研究では核構造全体に真に重要な難溶性タンパク質の同定が見逃されているという問題がある。そこで、細胞核機能をより理解するために、細胞核構造内の難溶性である核マトリックス画分をプロテオーム解析することによって細胞核構造基盤分子の検索を行った。<BR> 具体的には、HeLa細胞を塩、界面活性剤、DNaseで処理したときに難溶性画分として得られた核マトリックス画分を、(1)難溶性画分タンパク質分離クロマト系とSDS-PAGEを組み合わせた分離・精製を用いたpeptide mass fingerprint (PMF)法、(2)SDS-PAGEとnanoLC-MS/MSを用いたpeptide sequence tag (PST)法、という2つの方法で核マトリックス画分のプロテオーム解析を行った。最初に、HeLa細胞から調製した核マトリックス画分タンパク質を一次元目に60% ギ酸中で逆相HPLCにより、二次元目に濃度勾配ゲルを用いたSDS-PAGEで分離した。それをCBB染色した結果、138種類のタンパク質バンドが検出され、それらすべてをトリプシンでゲル内消化後、PMF法により、85種類のタンパク質を同定した。この中には、細胞内局在が未知である新規タンパク質が6種類、機能未知のタンパク質が8種類含まれていた。また、さらに網羅的に解析を行うために、核マトリックス画分をSDS-PAGEで分離・CBB染色後、ゲルを29断片にスライスし、トリプシン消化後、ペプチドをnanoLC-MS/MSで分析した。その結果、PST法により、334種類のタンパク質を同定し、この中には、細胞内局在が未知である新規タンパク質が40種類、機能未知のタンパク質が76種類含まれていた。今回の解析で、難溶性画分として得られた核マトリックス画分内に、核機能に関与するタンパク質が多く含まれていることが明らかになったことから、細胞核の機能を理解するために有用な情報を得ることができた。<BR> 新規タンパク質群に関しては、現在GFP融合タンパク質発現ベクターを構築し、細胞核内での詳細な局在の動態を明らかにする解析を進めている。

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  • 核脂質膜と核ラミナ (細胞核の世界--ダイナミクスから病態まで) -- (細胞核の構造とダイナミクス)

    古川 和広, 襲田 真一, 堀米 恒好

    蛋白質核酸酵素   51 ( 14 )   1931 - 1936   2006.11

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  • 核膜病 (細胞核の世界--ダイナミクスから病態まで) -- (細胞核と高次生命機能・疾患)

    古川 和広, 野中 由喜, 襲田 真一

    蛋白質核酸酵素   51 ( 14 )   2263 - 2268   2006.11

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  • 細胞核のプロテオーム解析 (細胞核の世界--ダイナミクスから病態まで) -- (細胞核の解析技術)

    堀米 恒好, 石井 宏平, 古川 和広

    蛋白質核酸酵素   51 ( 14 )   2013 - 2019   2006.11

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  • 真核細胞の核基盤構造である核ラミナによるクロマチンおよび細胞機能の制御

    古川 和広, 堀米 恒好, 小俣 三郎

    蛋白質核酸酵素   46 ( 14 )   2052 - 2059   2001.11

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  • 核ラミナの構築と核機能 (細胞核研究の最先端--核の機能構造とダイナミックス) -- (核膜,核ラミナと核構造の動態)

    古川 和広

    蛋白質核酸酵素   44 ( 12 )   1927 - 1934   1999.9

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  • 核膜崩壊・再形成におけるLamina-Associated Peptide(LAP)2の機能

    古川 和広

    日産科学振興財団研究報告書   ( 20 )   229 - 232   1997

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    Language:Japanese   Publisher:日産科学振興財団  

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  • Structure and function of lamin - associated - proteins

    FURUKAWA Kazuhiro

    生化学   68 ( 11 )   1721 - 1725   1996.11

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  • 減数分裂(Meiosis)の分子機構

    古川 和広, 堀田 康雄

    バイオサイエンスとインダストリ-   51 ( 5 )   p377 - 384   1993.5

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Teaching Experience

  • SDGsを支える化学

    2024
    Institution name:新潟大学

  • 統合化学入門

    2024
    Institution name:新潟大学

  • 化学コロキウム

    2022
    Institution name:新潟大学

  • 理学基礎演習

    2022
    Institution name:新潟大学

  • 数理物質科学の最前線

    2022
    Institution name:新潟大学

  • 安全教育

    2022
    Institution name:新潟大学

  • 課題研究

    2021
    Institution name:新潟大学

  • 日本事情自然系A

    2021
    Institution name:新潟大学

  • 細胞機能化学

    2021
    Institution name:新潟大学

  • 理学スタディ・スキルズ

    2021
    Institution name:新潟大学

  • 分子細胞化学

    2021
    Institution name:新潟大学

  • 課題研究 a

    2020
    Institution name:新潟大学

  • 課題研究 b

    2020
    Institution name:新潟大学

  • 先端科学技術総論

    2020
    Institution name:新潟大学

  • 理学スタディ・スキルズ

    2019
    -
    2021
    Institution name:新潟大学

  • 新素材の物性

    2018
    -
    2019
    Institution name:新潟大学

  • 生体分子化学Ⅲ

    2017
    Institution name:新潟大学

  • 専門力アクティブ・ラーニング

    2017
    -
    2021
    Institution name:新潟大学

  • 科学・技術と社会

    2017
    -
    2018
    Institution name:新潟大学

  • 化学入門

    2016
    Institution name:新潟大学

  • 数理物質科学特定研究Ⅲ(化学)

    2015
    Institution name:新潟大学

  • 論文演習

    2015
    Institution name:新潟大学

  • 研究発表演習・発表Ⅲ

    2015
    Institution name:新潟大学

  • 数理物質科学演習Ⅲ(化学)

    2015
    Institution name:新潟大学

  • 数理物質科学演習Ⅱ(化学)

    2014
    Institution name:新潟大学

  • 数理物質科学特定研究Ⅱ(化学)

    2014
    Institution name:新潟大学

  • 生体分子化学I

    2013
    Institution name:新潟大学

  • 生活の化学

    2013
    Institution name:新潟大学

  • 課題研究(化学科)

    2013
    -
    2016
    Institution name:新潟大学

  • 数理物質科学演習Ⅰ(化学)

    2013
    -
    2015
    Institution name:新潟大学

  • 数理物質科学特定研究ⅡA(化学)

    2013
    -
    2015
    Institution name:新潟大学

  • 数理物質科学特定研究ⅡB(化学)

    2013
    -
    2015
    Institution name:新潟大学

  • 数理物質科学特定研究Ⅰ(化学)

    2013
    -
    2015
    Institution name:新潟大学

  • 生化学特論

    2012
    Institution name:新潟大学

  • グリーンケミストリー概説

    2010
    Institution name:新潟大学

  • スタディ・スキルズ(化学学習法)

    2009
    -
    2016
    Institution name:新潟大学

  • 基礎化学Ⅱ

    2009
    Institution name:新潟大学

  • コミュニケーション演習

    2009
    Institution name:新潟大学

  • 科学技術英語

    2009
    Institution name:新潟大学

  • 化学英語

    2008
    -
    2020
    Institution name:新潟大学

  • 生体分子化学III

    2008
    -
    2016
    Institution name:新潟大学

  • 自然科学総論Ⅰ

    2008
    Institution name:新潟大学

  • 化学コロキュウム

    2008
    Institution name:新潟大学

  • 生化学演習

    2007
    Institution name:新潟大学

  • 分子細胞化学

    2007
    -
    2021
    Institution name:新潟大学

  • 細胞機能化学

    2007
    -
    2021
    Institution name:新潟大学

  • 課題研究

    2007
    -
    2019
    Institution name:新潟大学

  • 生化学実験

    2007
    -
    2013
    Institution name:新潟大学

  • 化学実験

    2007
    -
    2012
    Institution name:新潟大学

  • 生体機能化学

    2007
    -
    2011
    Institution name:新潟大学

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