Acetylation regulates WRN catalytic activities and affects base excision DNA repair

Research output: Contribution to journalJournal articleResearchpeer-review

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Acetylation regulates WRN catalytic activities and affects base excision DNA repair. / Muftuoglu, Meltem; Kusumoto, Rika; Speina, Elzbieta; Beck, Gad; Cheng, Wen-Hsing; Bohr, Vilhelm A.

In: P L o S One, Vol. 3, No. 4, 01.2008, p. e1918.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Muftuoglu, M, Kusumoto, R, Speina, E, Beck, G, Cheng, W-H & Bohr, VA 2008, 'Acetylation regulates WRN catalytic activities and affects base excision DNA repair', P L o S One, vol. 3, no. 4, pp. e1918. https://doi.org/10.1371/journal.pone.0001918

APA

Muftuoglu, M., Kusumoto, R., Speina, E., Beck, G., Cheng, W-H., & Bohr, V. A. (2008). Acetylation regulates WRN catalytic activities and affects base excision DNA repair. P L o S One, 3(4), e1918. https://doi.org/10.1371/journal.pone.0001918

Vancouver

Muftuoglu M, Kusumoto R, Speina E, Beck G, Cheng W-H, Bohr VA. Acetylation regulates WRN catalytic activities and affects base excision DNA repair. P L o S One. 2008 Jan;3(4):e1918. https://doi.org/10.1371/journal.pone.0001918

Author

Muftuoglu, Meltem ; Kusumoto, Rika ; Speina, Elzbieta ; Beck, Gad ; Cheng, Wen-Hsing ; Bohr, Vilhelm A. / Acetylation regulates WRN catalytic activities and affects base excision DNA repair. In: P L o S One. 2008 ; Vol. 3, No. 4. pp. e1918.

Bibtex

@article{967e659b3c66423197b279eaae5fe4c9,
title = "Acetylation regulates WRN catalytic activities and affects base excision DNA repair",
abstract = "The Werner protein (WRN), defective in the premature aging disorder Werner syndrome, participates in a number of DNA metabolic processes, and we have been interested in the possible regulation of its function in DNA repair by post-translational modifications. Acetylation mediated by histone acetyltransferases is of key interest because of its potential importance in aging, DNA repair and transcription.",
keywords = "Aging, Catalysis, Cell Line, DNA, DNA Damage, DNA Repair, Exodeoxyribonucleases, Exonucleases, Hela Cells, Histone Acetyltransferases, Humans, Protein Processing, Post-Translational, Protein Structure, Tertiary, RecQ Helicases, Recombinant Proteins, Transcription, Genetic",
author = "Meltem Muftuoglu and Rika Kusumoto and Elzbieta Speina and Gad Beck and Wen-Hsing Cheng and Bohr, {Vilhelm A}",
year = "2008",
month = "1",
doi = "10.1371/journal.pone.0001918",
language = "English",
volume = "3",
pages = "e1918",
journal = "P L o S One",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "4",

}

RIS

TY - JOUR

T1 - Acetylation regulates WRN catalytic activities and affects base excision DNA repair

AU - Muftuoglu, Meltem

AU - Kusumoto, Rika

AU - Speina, Elzbieta

AU - Beck, Gad

AU - Cheng, Wen-Hsing

AU - Bohr, Vilhelm A

PY - 2008/1

Y1 - 2008/1

N2 - The Werner protein (WRN), defective in the premature aging disorder Werner syndrome, participates in a number of DNA metabolic processes, and we have been interested in the possible regulation of its function in DNA repair by post-translational modifications. Acetylation mediated by histone acetyltransferases is of key interest because of its potential importance in aging, DNA repair and transcription.

AB - The Werner protein (WRN), defective in the premature aging disorder Werner syndrome, participates in a number of DNA metabolic processes, and we have been interested in the possible regulation of its function in DNA repair by post-translational modifications. Acetylation mediated by histone acetyltransferases is of key interest because of its potential importance in aging, DNA repair and transcription.

KW - Aging

KW - Catalysis

KW - Cell Line

KW - DNA

KW - DNA Damage

KW - DNA Repair

KW - Exodeoxyribonucleases

KW - Exonucleases

KW - Hela Cells

KW - Histone Acetyltransferases

KW - Humans

KW - Protein Processing, Post-Translational

KW - Protein Structure, Tertiary

KW - RecQ Helicases

KW - Recombinant Proteins

KW - Transcription, Genetic

U2 - 10.1371/journal.pone.0001918

DO - 10.1371/journal.pone.0001918

M3 - Journal article

VL - 3

SP - e1918

JO - P L o S One

JF - P L o S One

SN - 1932-6203

IS - 4

ER -

ID: 32949176