Author

R. Ziganshin

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 Biophysics· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 3 Approach:experimental assay· 3 Organism:non-human primate· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

A. A. Kotlobay· 1 shared A. Bannikov· 1 shared A. E. Fedosov· 1 shared A. Fomenkov· 1 shared A. Glushkevich· 1 shared A. Kniazev· 1 shared A. Mamaeva· 1 shared A. Nosov· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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1 shared paperBiochemistry

A. A. Kotlobay

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Author profile →

4 papers

Recent·Most cited

Vexitoxins: a novel class of conotoxin-like venom peptides from predatory gastropods of the genus Vexillum

K. G. Kuznetsova, S. S. Zvonareva, R. Ziganshin, E. S. Mekhova, P. Y. Dgebuadze, Y. T. H. Dinh, T. H. T. Nguyen, S. A. Moshkovskii, A. E. Fedosov

This study identifies vexitoxins, a novel class of venom peptides in Vexillum snails, similar to conotoxins in structure and function, and explores their evolutionary relationship.

bioRxiv · Jan 15, 2022 · PreprintBiochemistry

FAMOSS, a conserved 41-aa peptide involved in plant tip growth regulation

A. Mamaeva, A. Kniazev, I. Sedlov, N. Golub, D. Kharlampieva, V. Manuvera, V. Rakitin, A. Nosov, A. Fomenkov, M. Pavlyukov, S. Kovalchuk, R. Ziganshin, A. Glushkevich, V. Lazarev, I. Fesenko

The paper identifies and characterizes FAMOSS, a conserved 41-aa peptide from moss that regulates tip growth by interacting with Rab GTPases and modulating vesicular transport.

bioRxiv · Nov 24, 2021 · PreprintPlant Biology

Crystal Structure of the putative tail fiber protein gp53 from the Acinetobacter baumannii bacteriophage AP22

L. Sycheva, M. Shneider, A. Popova, R. Ziganshin, N. Volozhantsev, K. Miroshnikov, P. Leiman

The paper reports the crystal structure of gp53, a putative host cell-binding protein from bacteriophage AP22, showing it forms a trimeric fiber and binds small sugar-like molecules but does not inhibit infection.

bioRxiv · Jan 16, 2019 · PreprintBiophysics

Luciferase of the Japanese syllid polychaete Odontosyllis umdecimdonta

D. T. Schultz, A. A. Kotlobay, R. Ziganshin, A. Bannikov, N. M. Markina, T. V. Chepurnyh, E. S. Shakhova, K. Palkina, S. H. Haddock, I. V. Yampolsky, Y. Oba

This paper identifies and characterizes the luciferase protein from the Japanese syllid polychaete Odontosyllis undecimdonta, showing it is evolutionarily unique and does not require cofactors or exogenous luciferin.

bioRxiv · May 24, 2018Biochemistry