Author

A. A. Sysoev

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:proteomics· 1

Frequent Co-Authors

A. A. Antson· 2 shared J. L. R. Smith· 2 shared K. V. Tugaeva· 2 shared N. N. Sluchanko· 2 shared A. A. Kapitonova· 1 shared D. E. D. P. Hawkins· 1 shared D.-S. Ker· 1 shared O. I. Klychnikov· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiochemistry

A. A. Antson

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2 papers

Recent·Most cited

Human 14-3-3 proteins site-selectively bind the mutational hotspot region of SARS-CoV-2 nucleoprotein modulating its phosphoregulation

K. V. Tugaeva, A. A. Sysoev, A. A. Kapitonova, J. L. R. Smith, P. Zhu, R. B. Cooley, A. A. Antson, N. N. Sluchanko

This study shows that 14-3-3 proteins bind specific phosphorylation sites in SARS-CoV-2 nucleoprotein, affecting its phosphoregulation and potentially influencing viral replication.

bioRxiv · Dec 23, 2021Biochemistry

The mechanism of SARS-CoV-2 nucleocapsid protein recognition by the human 14-3-3 proteins

K. V. Tugaeva, D. E. D. P. Hawkins, J. L. R. Smith, O. W. Bayfield, D.-S. Ker, A. A. Sysoev, O. I. Klychnikov, A. A. Antson, N. N. Sluchanko

This paper identifies the molecular mechanism by which phosphorylated SARS-CoV-2 nucleocapsid protein binds to human 14-3-3 proteins, showing that Ser197 phosphorylation is critical for this interaction.

bioRxiv · Dec 26, 2020Biochemistry