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Noncatalytic Domains in DNA Glycosylases. / Torgasheva, Natalia A.; Diatlova, Evgeniia A.; Grin, Inga R. и др.

в: International Journal of Molecular Sciences, Том 23, № 13, 7286, 01.07.2022.

Результаты исследований: Научные публикации в периодических изданиях › обзорная статья › Рецензирование

Harvard

Torgasheva, NA, Diatlova, EA, Grin, IR, Endutkin, AV, Mechetin, GV, Vokhtantsev, IP, Yudkina, AV & Zharkov, DO 2022, 'Noncatalytic Domains in DNA Glycosylases', International Journal of Molecular Sciences, Том. 23, № 13, 7286. https://doi.org/10.3390/ijms23137286

APA

Torgasheva, N. A., Diatlova, E. A., Grin, I. R., Endutkin, A. V., Mechetin, G. V., Vokhtantsev, I. P., Yudkina, A. V., & Zharkov, D. O. (2022). Noncatalytic Domains in DNA Glycosylases. International Journal of Molecular Sciences, 23(13), [7286]. https://doi.org/10.3390/ijms23137286

Vancouver

Torgasheva NA, Diatlova EA, Grin IR, Endutkin AV, Mechetin GV, Vokhtantsev IP и др. Noncatalytic Domains in DNA Glycosylases. International Journal of Molecular Sciences. 2022 июль 1;23(13):7286. doi: 10.3390/ijms23137286

Author

Torgasheva, Natalia A. ; Diatlova, Evgeniia A. ; Grin, Inga R. и др. / Noncatalytic Domains in DNA Glycosylases. в: International Journal of Molecular Sciences. 2022 ; Том 23, № 13.

BibTeX

@article{55772200f47f4bffb50925e533172390,
title = "Noncatalytic Domains in DNA Glycosylases",
abstract = "Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.",
keywords = "base excision repair, DNA binding, DNA glycosylases, DNA repair, intrinsically disordered protein regions, lesion search in DNA, noncatalytic protein domains, post-translational modifications, protein–protein interactions, Humans, DNA/chemistry, DNA Repair, DNA Glycosylases/metabolism, DNA Damage",
author = "Torgasheva, {Natalia A.} and Diatlova, {Evgeniia A.} and Grin, {Inga R.} and Endutkin, {Anton V.} and Mechetin, {Grigory V.} and Vokhtantsev, {Ivan P.} and Yudkina, {Anna V.} and Zharkov, {Dmitry O.}",
note = "Funding Information: Funding: The study was supported by the Russian Science Foundation (Grant No. 21-64-00017). I.R.G., A.V.E., I.P.V., and D.O.Z. acknowledge partial salary support from the Russian Ministry of Science and Education (Grant No. 121031300056-8). Publisher Copyright: {\textcopyright} 2022 by the authors. Licensee MDPI, Basel, Switzerland.",
year = "2022",
month = jul,
day = "1",
doi = "10.3390/ijms23137286",
language = "English",
volume = "23",
journal = "International Journal of Molecular Sciences",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "13",

}

RIS

TY - JOUR

T1 - Noncatalytic Domains in DNA Glycosylases

AU - Torgasheva, Natalia A.

AU - Diatlova, Evgeniia A.

AU - Grin, Inga R.

AU - Endutkin, Anton V.

AU - Mechetin, Grigory V.

AU - Vokhtantsev, Ivan P.

AU - Yudkina, Anna V.

AU - Zharkov, Dmitry O.

N1 - Funding Information: Funding: The study was supported by the Russian Science Foundation (Grant No. 21-64-00017). I.R.G., A.V.E., I.P.V., and D.O.Z. acknowledge partial salary support from the Russian Ministry of Science and Education (Grant No. 121031300056-8). Publisher Copyright: © 2022 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2022/7/1

Y1 - 2022/7/1

N2 - Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.

AB - Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.

KW - base excision repair

KW - DNA binding

KW - DNA glycosylases

KW - DNA repair

KW - intrinsically disordered protein regions

KW - lesion search in DNA

KW - noncatalytic protein domains

KW - post-translational modifications

KW - protein–protein interactions

KW - Humans

KW - DNA/chemistry

KW - DNA Repair

KW - DNA Glycosylases/metabolism

KW - DNA Damage

UR - http://www.scopus.com/inward/record.url?scp=85133136227&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/e3ba57c3-68ec-3483-aa87-0b8886405abc/

U2 - 10.3390/ijms23137286

DO - 10.3390/ijms23137286

M3 - Review article

C2 - 35806289

AN - SCOPUS:85133136227

VL - 23

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 13

M1 - 7286

ER -

ID: 36541420