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William M. Bonner
Researcher at National Institutes of Health
Publications - 166
Citations - 32106
William M. Bonner is an academic researcher from National Institutes of Health. The author has contributed to research in topics: DNA damage & Histone. The author has an hindex of 66, co-authored 165 publications receiving 30182 citations. Previous affiliations of William M. Bonner include Georgetown University Medical Center.
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Journal ArticleDOI
DNA Double-stranded Breaks Induce Histone H2AX Phosphorylation on Serine 139
TL;DR: In this paper, a histone H2AX species that has been phosphorylated specifically at serine 139 was found to be a major component of DNA double-stranded break.
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Megabase chromatin domains involved in DNA double-strand breaks in vivo.
TL;DR: The results offer direct visual confirmation that γ-H2AX forms en masse at chromosomal sites of DNA double-strand breaks and suggest the possible existence of units of higher order chromatin structure involved in monitoring DNA integrity.
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A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage.
Tanya T. Paull,Emmy P. Rogakou,Vikky Yamazaki,Cordula U. Kirchgessner,Martin Gellert,William M. Bonner +5 more
TL;DR: The evidence presented strongly supports a role for the gamma-H2AX and the PI-3 protein kinase family in focus formation at sites of double-strand breaks and suggests the possibility of a change in chromatin structure accompanying double-Strand break repair.
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Genomic instability in mice lacking histone H2AX.
Arkady Celeste,Simone Petersen,Peter J. Romanienko,Oscar Fernandez-Capetillo,Hua Tang Chen,Olga A. Sedelnikova,Bernardo Reina-San-Martin,Vincenzo Coppola,Eric Meffre,Michael J. Difilippantonio,Christophe E. Redon,Duane R. Pilch,Alexandru Olaru,Michael Eckhaus,R. Daniel Camerini-Otero,Lino Tessarollo,Ferenc Livak,Katia Manova,William M. Bonner,Michel C. Nussenzweig,André Nussenzweig +20 more
TL;DR: Higher order chromatin structure presents a barrier to the recognition and repair of DNA damage, and H2AX is critical for facilitating the assembly of specific DNA-repair complexes on damaged DNA.
Journal ArticleDOI
γH2AX and cancer
William M. Bonner,Christophe E. Redon,Jennifer S. Dickey,Asako J. Nakamura,Olga A. Sedelnikova,Stéphanie Solier,Yves Pommier +6 more
TL;DR: In this paper, the authors used histone H2AX phosphorylation on a serine four residues from the carboxyl terminus (producing gammaH2AX) as a sensitive marker for DNA double-strand breaks (DSBs).