Author

K. V. Tugaeva

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

Biology Disciplines

Click to filter author papers

Biochemistry· 5

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 5 Organism:human· 4 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:protein structure· 1

Frequent Co-Authors

N. N. Sluchanko· 5 shared A. A. Antson· 4 shared A. A. Sysoev· 2 shared J. L. R. Smith· 2 shared A. A. Kapitonova· 1 shared C. Kostmann· 1 shared D. E. D. P. Hawkins· 1 shared D. V. Sotnikov· 1 shared

Activity by Year

2017-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

5 shared papersBiochemistry

N. N. Sluchanko

Mutual co-authors in cluster

Author profile →

5 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

Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms

G. Gogl, K. V. Tugaeva, P. Eberling, C. Kostmann, G. Trave, N. N. Sluchanko

The paper investigates the binding preferences of seven human 14-3-3 isoforms to phospho-motifs in E6 oncoproteins and RSK1, revealing a conserved binding hierarchy across targets.

bioRxiv · Jul 24, 2020Biochemistry

Molecular basis for the recognition of steroidogenic acute regulatory protein by the 14-3-3 protein family

K. V. Tugaeva, J. Titterington, D. V. Sotnikov, E. G. Maksimov, A. A. Antson, N. N. Sluchanko

The paper investigates how phosphorylation of STARD1 at specific sites enables interaction with 14-3-3 proteins, modulating its activity and mitochondrial import.

bioRxiv · Apr 14, 2020Biochemistry

Chimeric 14-3-3 Proteins For Unravelling Interactions With Intrinsically Disordered Partners

N. N. Sluchanko, K. V. Tugaeva, A. A. Antson

This paper introduces chimeric 14-3-3 proteins to study interactions with intrinsically disordered partners, showing they enable structural analysis of phosphopeptide binding.

bioRxiv · Apr 24, 2017Biochemistry