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pro vyhledávání: '"Valerie L. O'Shea"'
Autor:
Neha Puri, Amy J Fernandez, Valerie L O'Shea Murray, Sarah McMillan, James L Keck, James M Berger
Publikováno v:
eLife, Vol 10 (2021)
In many bacteria and eukaryotes, replication fork establishment requires the controlled loading of hexameric, ring-shaped helicases around DNA by AAA+(ATPases Associated with various cellular Activities) ATPases. How loading factors use ATP to contro
Externí odkaz:
https://doaj.org/article/7dcf11f7533b4950a44e0b03c6c2212d
Autor:
James L. Keck, Neha Puri, Amy J. Fernandez, Sarah McMillan, Valerie L O'Shea Murray, James M. Berger
Publikováno v:
eLife
eLife, Vol 10 (2021)
eLife, Vol 10 (2021)
In many bacteria and eukaryotes, replication fork establishment requires the controlled loading of hexameric, ring-shaped helicases around DNA by AAA+(ATPases Associated with various cellular Activities) ATPases. How loading factors use ATP to contro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c3a63c09a57060161866d9191f840a5
https://doi.org/10.7554/elife.64232
https://doi.org/10.7554/elife.64232
Autor:
Neha Puri, Valerie L O'Shea Murray, Amy J. Fernandez, James L. Keck, Sarah McMillan, James M. Berger
In many bacteria and in eukaryotes, replication fork establishment requires the controlled loading of hexameric, ring-shaped helicases around DNA by AAA+ ATPases. How loading factors use ATP to control helicase deposition is poorly understood. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57601e5282bdc10023f1e7feb5d9a956
https://doi.org/10.1101/2020.10.21.345918
https://doi.org/10.1101/2020.10.21.345918
Akademický článek
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Autor:
Merve Demir, Sheila S. David, Sonia L. Sehgal, L. Peyton Russelburg, Martin P. Horvath, Sheng Cao, Valerie L. O’Shea Murray, Kyle R. Knutsen
Publikováno v:
ACS Chem Biol
ACS chemical biology, vol 15, iss 1
ACS chemical biology, vol 15, iss 1
The adenine glycosylase MutY selectively initiates repair of OG:A lesions and, by comparison, avoids G:A mispairs. The ability to distinguish these closely related substrates relies on the C-terminal domain of MutY which structurally resembles MutT.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cd960e782a14e5740280e269c299814
https://europepmc.org/articles/PMC7069122/
https://europepmc.org/articles/PMC7069122/
Akademický článek
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Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
81 p.- 7 fig.-1 tab.-7 fig. supl.-6 vid.
In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases onto DNA to initiate chromosomal replication. To better understand the mechanisms by which helicase loading can occur, we used cry
In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases onto DNA to initiate chromosomal replication. To better understand the mechanisms by which helicase loading can occur, we used cry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7844c8e3a0ee9261f0f7dfd57ea2367
https://europepmc.org/articles/PMC6450724/
https://europepmc.org/articles/PMC6450724/
Autor:
Valerie L. O'Shea, Ryan D. Woods, Sheng Cao, Sheila S. David, Aurea Chu, Martin P. Horvath, Jody L. Richards
Publikováno v:
Nucleic Acids Research
MutY adenine glycosylases prevent DNA mutations by excising adenine from promutagenic 8-oxo-7,8-dihydroguanine (OG):A mismatches. Here, we describe structural features of the MutY active site bound to an azaribose transition state analog which indica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ac3552d464c678c10b190d0d714fa4c
https://doi.org/10.1093/nar/gkv1469
https://doi.org/10.1093/nar/gkv1469
Autor:
Valerie L. O’Shea, Jacob S. Lewis, Allen T.Y. Lo, Nicholas E. Dixon, Antoine M. van Oijen, James M. Berger, Zhi-Qiang Xu, Enrico Monachino, Slobodan Jergic
Publikováno v:
Mol Cell
Molecular Cell, 79(1), 140-154.e7. CELL PRESS
Molecular Cell, 79(1), 140-154.e7. CELL PRESS
SUMMARYRecent studies of bacterial DNA replication have led to a picture of the replisome as an entity that freely exchanges DNA polymerases and displays intermittent coupling between the helicase and polymerase(s). Challenging the textbook model of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36423d9ef2d1528b5b69492642acaffc
https://doi.org/10.1016/j.molcel.2020.04.037
https://doi.org/10.1016/j.molcel.2020.04.037