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Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair. / Kosova, A. A.; Khodyreva, S. N.; Lavrik, O. I.

In: Biochemistry (Moscow), Vol. 82, No. 6, 01.06.2017, p. 643-654.

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

Harvard

Kosova, AA, Khodyreva, SN & Lavrik, OI 2017, 'Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair', Biochemistry (Moscow), vol. 82, no. 6, pp. 643-654. https://doi.org/10.1134/S0006297917060013

APA

Kosova, A. A., Khodyreva, S. N., & Lavrik, O. I. (2017). Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair. Biochemistry (Moscow), 82(6), 643-654. https://doi.org/10.1134/S0006297917060013

Vancouver

Kosova AA, Khodyreva SN, Lavrik OI. Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair. Biochemistry (Moscow). 2017 Jun 1;82(6):643-654. doi: 10.1134/S0006297917060013

Author

Kosova, A. A. ; Khodyreva, S. N. ; Lavrik, O. I. / Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair. In: Biochemistry (Moscow). 2017 ; Vol. 82, No. 6. pp. 643-654.

BibTeX

@article{2b1dbb6981af4ea696c93793fd57360c,
title = "Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair",
abstract = "Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is widely known as a glycolytic enzyme. Nevertheless, various functions of GAPDH have been found that are unrelated to glycolysis. Some of these functions presume interaction of GAPDH with DNA, but the mechanism of its translocation to the nucleus is not fully understood. When in the nucleus, GAPDH participates in the initiation of apoptosis and transcription of genes involved in antiapoptotic pathways and cell proliferation and plays a role in the regulation of telomere length. Several authors have shown that GAPDH displays the uracil-DNA glycosylase activity and interacts with some types of DNA damages, such as apurinic/apyrimidinic sites, nucleotide analogs, and covalent DNA adducts with alkylating agents. Moreover, GAPDH can interact with proteins participating in DNA repair, such as APE1, PARP1, HMGB1, and HMGB2. In this review, the functions of GAPDH associated with DNA repair are discussed in detail.",
keywords = "AP site, DNA repair, GAPDH, glyceraldehyde-3-phosphate dehydrogenase, protein–DNA interactions",
author = "Kosova, {A. A.} and Khodyreva, {S. N.} and Lavrik, {O. I.}",
year = "2017",
month = jun,
day = "1",
doi = "10.1134/S0006297917060013",
language = "English",
volume = "82",
pages = "643--654",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "6",

}

RIS

TY - JOUR

T1 - Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair

AU - Kosova, A. A.

AU - Khodyreva, S. N.

AU - Lavrik, O. I.

PY - 2017/6/1

Y1 - 2017/6/1

N2 - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is widely known as a glycolytic enzyme. Nevertheless, various functions of GAPDH have been found that are unrelated to glycolysis. Some of these functions presume interaction of GAPDH with DNA, but the mechanism of its translocation to the nucleus is not fully understood. When in the nucleus, GAPDH participates in the initiation of apoptosis and transcription of genes involved in antiapoptotic pathways and cell proliferation and plays a role in the regulation of telomere length. Several authors have shown that GAPDH displays the uracil-DNA glycosylase activity and interacts with some types of DNA damages, such as apurinic/apyrimidinic sites, nucleotide analogs, and covalent DNA adducts with alkylating agents. Moreover, GAPDH can interact with proteins participating in DNA repair, such as APE1, PARP1, HMGB1, and HMGB2. In this review, the functions of GAPDH associated with DNA repair are discussed in detail.

AB - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is widely known as a glycolytic enzyme. Nevertheless, various functions of GAPDH have been found that are unrelated to glycolysis. Some of these functions presume interaction of GAPDH with DNA, but the mechanism of its translocation to the nucleus is not fully understood. When in the nucleus, GAPDH participates in the initiation of apoptosis and transcription of genes involved in antiapoptotic pathways and cell proliferation and plays a role in the regulation of telomere length. Several authors have shown that GAPDH displays the uracil-DNA glycosylase activity and interacts with some types of DNA damages, such as apurinic/apyrimidinic sites, nucleotide analogs, and covalent DNA adducts with alkylating agents. Moreover, GAPDH can interact with proteins participating in DNA repair, such as APE1, PARP1, HMGB1, and HMGB2. In this review, the functions of GAPDH associated with DNA repair are discussed in detail.

KW - AP site

KW - DNA repair

KW - GAPDH

KW - glyceraldehyde-3-phosphate dehydrogenase

KW - protein–DNA interactions

UR - http://www.scopus.com/inward/record.url?scp=85020699564&partnerID=8YFLogxK

U2 - 10.1134/S0006297917060013

DO - 10.1134/S0006297917060013

M3 - Review article

C2 - 28601074

AN - SCOPUS:85020699564

VL - 82

SP - 643

EP - 654

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 6

ER -

ID: 8680969