Kirill V Volkov
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Explore the profile of Kirill V Volkov including associated specialties, affiliations and a list of published articles.
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Articles
11
Citations
222
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Recent Articles
1.
Kosolapova A, Belousov M, Sulatsky M, Tsyganova A, Sulatskaya A, Bobylev A, et al.
Front Plant Sci
. 2022 Nov;
13:1014699.
PMID: 36388578
Amyloids represent protein aggregates with highly ordered fibrillar structure associated with the development of various disorders in humans and animals and involved in implementation of different vital functions in all...
2.
Kachkin D, Volkov K, Sopova J, Bobylev A, Fedotov S, Inge-Vechtomov S, et al.
Int J Mol Sci
. 2022 Oct;
23(19).
PMID: 36232958
RAD51 is a central protein of homologous recombination and DNA repair processes that maintains genome stability and ensures the accurate repair of double-stranded breaks (DSBs). In this work, we assessed...
3.
Radchenko E, Aksenova A, Volkov K, Shishkin A, Pavlov Y, Mirkin S
PNAS Nexus
. 2022 Jul;
1(3):pgac080.
PMID: 35832866
In humans, telomeric repeats (TTAGGG) are known to be present at internal chromosomal sites. These interstitial telomeric sequences (ITSs) are an important source of genomic instability, including repeat length polymorphism,...
4.
Antonets K, Belousov M, Sulatskaya A, Belousova M, Kosolapova A, Sulatsky M, et al.
PLoS Biol
. 2020 Jul;
18(7):e3000564.
PMID: 32701952
Amyloids are protein aggregates with a highly ordered spatial structure giving them unique physicochemical properties. Different amyloids not only participate in the development of numerous incurable diseases but control vital...
5.
Sopova J, Koshel E, Belashova T, Zadorsky S, Sergeeva A, Siniukova V, et al.
Sci Rep
. 2019 Dec;
9(1):18983.
PMID: 31831836
Amyloids are β-sheets-rich protein fibrils that cause neurodegenerative and other incurable human diseases affecting millions of people worldwide. However, a number of proteins is functional in the amyloid state in...
6.
Kosolapova A, Belousov M, Sulatskaya A, Belousova M, Sulatsky M, Antonets K, et al.
Biomolecules
. 2019 Nov;
9(11).
PMID: 31690032
Amyloids represent protein fibrils with a highly ordered spatial structure, which not only cause dozens of incurable human and animal diseases but also play vital biological roles in Archaea, Bacteria,...
7.
Ryzhova T, Sopova J, Zadorsky S, Siniukova V, Sergeeva A, Galkina S, et al.
Curr Genet
. 2017 Oct;
64(2):469-478.
PMID: 29027580
The search for novel pathological and functional amyloids represents one of the most important tasks of contemporary biomedicine. Formation of pathological amyloid fibrils in the aging brain causes incurable neurodegenerative...
8.
Nizhnikov A, Ryzhova T, Volkov K, Zadorsky S, Sopova J, Inge-Vechtomov S, et al.
PLoS Genet
. 2016 Dec;
12(12):e1006504.
PMID: 28027291
The concept of "protein-based inheritance" defines prions as epigenetic determinants that cause several heritable traits in eukaryotic microorganisms, such as Saccharomyces cerevisiae and Podospora anserina. Previously, we discovered a non-chromosomal...
9.
Aksenova A, Han G, Shishkin A, Volkov K, Mirkin S
Cell Rep
. 2015 Nov;
13(8):1545-51.
PMID: 26586439
Telomeric repeats located within chromosomes are called interstitial telomeric sequences (ITSs). They are polymorphic in length and are likely hotspots for initiation of chromosomal rearrangements that have been linked to...
10.
Zhang Y, Shishkin A, Nishida Y, Marcinkowski-Desmond D, Saini N, Volkov K, et al.
Mol Cell
. 2012 Sep;
48(2):254-65.
PMID: 22959270
Triplex structure-forming GAA/TTC repeats pose a dual threat to the eukaryotic genome integrity. Their potential to expand can lead to gene inactivation, the cause of Friedreich's ataxia disease in humans....