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Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases. / Alemasova, Elizaveta E.; Naumenko, Konstantin N.; Sukhanova, Maria V. et al.

In: Biochemistry (Moscow), Vol. 87, No. Suppl 1, 01.2022, p. S32-S47.

Research output: Contribution to journal › Review article › peer-review

Harvard

Alemasova, EE, Naumenko, KN, Sukhanova, MV & Lavrik, OI 2022, 'Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases', Biochemistry (Moscow), vol. 87, no. Suppl 1, pp. S32-S47. https://doi.org/10.1134/S0006297922140048

APA

Alemasova, E. E., Naumenko, K. N., Sukhanova, M. V., & Lavrik, O. I. (2022). Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases. Biochemistry (Moscow), 87(Suppl 1), S32-S47. https://doi.org/10.1134/S0006297922140048

Vancouver

Alemasova EE, Naumenko KN, Sukhanova MV, Lavrik OI. Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases. Biochemistry (Moscow). 2022 Jan;87(Suppl 1):S32-S47. doi: 10.1134/S0006297922140048

Author

Alemasova, Elizaveta E. ; Naumenko, Konstantin N. ; Sukhanova, Maria V. et al. / Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases. In: Biochemistry (Moscow). 2022 ; Vol. 87, No. Suppl 1. pp. S32-S47.

BibTeX

@article{3eb0b861e3374cae850d3b513077818b,
title = "Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases",
abstract = "Poly(ADP-ribosyl)ation is a post-translational modification of proteins that performs an essential regulatory function in the cellular response to DNA damage. The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. The mechanisms of PARP1 activity stimulation by YB-1 protein can possibly be extended to other RNA-binding proteins involved in the maintenance of the genome stability.",
keywords = "poly(ADP-ribose) (PAR), poly(ADP-ribose) polymerase 1 (PARP1), poly(ADP-ribosyl)ation (PARylation), RNA-binding protein (RBP), Y-box-binding protein 1 (YB-1), Poly ADP Ribosylation, Proteins/metabolism, Poly(ADP-ribose) Polymerases/metabolism, Catalysis, DNA Damage, Poly Adenosine Diphosphate Ribose",
author = "Alemasova, {Elizaveta E.} and Naumenko, {Konstantin N.} and Sukhanova, {Maria V.} and Lavrik, {Olga I.}",
note = "Funding Information: The work was supported by the Russian Science Foundation (projects no. 19-14-00107 and no. 20-14-00086). Publisher Copyright: {\textcopyright} 2022, Pleiades Publishing, Ltd.",
year = "2022",
month = jan,
doi = "10.1134/S0006297922140048",
language = "English",
volume = "87",
pages = "S32--S47",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "Suppl 1",

}

RIS

TY - JOUR

T1 - Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases

AU - Alemasova, Elizaveta E.

AU - Naumenko, Konstantin N.

AU - Sukhanova, Maria V.

AU - Lavrik, Olga I.

N1 - Funding Information: The work was supported by the Russian Science Foundation (projects no. 19-14-00107 and no. 20-14-00086). Publisher Copyright: © 2022, Pleiades Publishing, Ltd.

PY - 2022/1

Y1 - 2022/1

N2 - Poly(ADP-ribosyl)ation is a post-translational modification of proteins that performs an essential regulatory function in the cellular response to DNA damage. The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. The mechanisms of PARP1 activity stimulation by YB-1 protein can possibly be extended to other RNA-binding proteins involved in the maintenance of the genome stability.

AB - Poly(ADP-ribosyl)ation is a post-translational modification of proteins that performs an essential regulatory function in the cellular response to DNA damage. The key enzyme synthesizing poly(ADP-ribose) (PAR) in the cells is poly(ADP-ribose) polymerase 1 (PARP1). Understanding the mechanisms of the PARP1 activity regulation within the cells is necessary for development of the PARP1-targeted antitumor therapy. This review is devoted to the studies of the role of the RNA-binding protein YB-1 in the PARP1-catalyzed PARylation. The mechanisms of PARP1 activity stimulation by YB-1 protein can possibly be extended to other RNA-binding proteins involved in the maintenance of the genome stability.

KW - poly(ADP-ribose) (PAR)

KW - poly(ADP-ribose) polymerase 1 (PARP1)

KW - poly(ADP-ribosyl)ation (PARylation)

KW - RNA-binding protein (RBP)

KW - Y-box-binding protein 1 (YB-1)

KW - Poly ADP Ribosylation

KW - Proteins/metabolism

KW - Poly(ADP-ribose) Polymerases/metabolism

KW - Catalysis

KW - DNA Damage

KW - Poly Adenosine Diphosphate Ribose

UR - http://www.scopus.com/inward/record.url?scp=85124032535&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/97f9a842-2210-3c8e-9baf-9d4dd94717e8/

U2 - 10.1134/S0006297922140048

DO - 10.1134/S0006297922140048

M3 - Review article

C2 - 35501985

AN - SCOPUS:85124032535

VL - 87

SP - S32-S47

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - Suppl 1

ER -

ID: 35430035