Updated on 2021/12/04

写真a

 
ANISIMOV SERGEI
 
Organization
Academic Assembly Institute of Medicine and Dentistry Specially Appointed Assistant Professor
Graduate School of Medical and Dental Sciences Specially Appointed Assistant Professor
Title
Specially Appointed Assistant Professor
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Degree

  • Ph.D. ( 2019 )

  • Medical Doctor ( 2014 )

Research Interests

  • autophagy

  • neurodegeneration

  • virology

  • protein aggregations

Research Areas

  • Life Science / Pathophysiologic neuroscience  / Parkinsons disease

  • Life Science / Cell biology  / Autophagy

Research History (researchmap)

  • Niigata University Graduate School of Medical and Dental Sciences   Virology Division   Postdoctoral researcher

    2019

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Research History

  • Niigata University   Graduate School of Medical and Dental Sciences   Specially Appointed Assistant Professor

    2020.7

  • Niigata University   Institute of Medicine and Dentistry, Academic Assembly   Specially Appointed Assistant Professor

    2020.7

  • Niigata University   Graduate School of Medical and Dental Sciences   Specially Appointed Assistant

    2019.10 - 2020.6

Education

  • Niigata University   Graduate School of Medical and Dental Sciences, Virology Division   Ph.D. course

    2015.10 - 2019.9

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  • Krasnoyarsk State Medical University   Faculty of General Medicine   General Medicine

    2009.9 - 2015.6

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Professional Memberships

 

Papers

  • G3BP1 inhibits ubiquitinated protein aggregations induced by p62 and USP10 Reviewed International journal

    Anisimov S, Takahashi M, Kakihana T, Katsuragi Y, Kitaura H, Zhang L, Kakita A, Fujii M

    Scientific Reports   9 (1) ( 12896 )   12896 - 12896   2019.9

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

    The aberrant accumulation of ubiquitinated protein aggregates in cells plays a critical role in the pathogenesis of several degenerative diseases, including Parkinson disease (PD) and cystic fibrosis (CF). In this study, we found that Ras GTPase-activating protein-binding protein 1 (G3BP1) inhibits ubiquitinated protein aggregations induced by p62 and USP10 in cultured cells. p62 is a ubiquitin receptor, and p62 and its binding partner USP10 have been shown to augment ubiquitinated protein aggregation. G3BP1 interacted with p62 and USP10 and inhibited p62/USP10-induced protein aggregation. The G3BP1 inhibition of protein aggregations targeted two aggregation-prone proteins, α-synuclein and CFTR-ΔF508, which are causative factors of PD and CF, respectively. G3BP1 depletion increased the amounts of ubiquitinated α-synuclein and CFTR-ΔF508 protein. A proteasome reporter indicated that G3BP1 depletion inhibits the proteasome activity. We herein present evidence that G3BP1, p62 and USP10 together control ubiquitinated protein toxicity by controlling both ubiquitination and aggregation. Taken together, these results suggest that G3BP1, p62 and USP10 could be therapeutic targets for ubiquitinated protein aggregation disorders, including PD and CF.

    DOI: 10.1038/s41598-019-46237-1

    PubMed

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  • USP10 inhibits apoptosis induced by ubiquitinated protein oligomers by inducing protein aggregates and aggresomes

    Takahashi M, Piatnitskaia Svetlana, Anisimov S, Masahiro Fujii

    Niigata Medical Journal   133 ( 4 )   2019.4

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    Language:Japanese  

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