Zobrazeno 1 - 10
of 90
pro vyhledávání: '"Joseph J Loparo"'
Autor:
Sean M Carney, Andrew T Moreno, Sadie C Piatt, Metztli Cisneros-Aguirre, Felicia Wednesday Lopezcolorado, Jeremy M Stark, Joseph J Loparo
Publikováno v:
eLife, Vol 9 (2020)
Non-homologous end joining (NHEJ) is the predominant pathway that repairs DNA double-strand breaks in vertebrates. During NHEJ DNA ends are held together by a multi-protein synaptic complex until they are ligated. Here, we use Xenopus laevis egg extr
Externí odkaz:
https://doaj.org/article/a69dfe15dfac41d0bcf7b6e555d1a2a5
Autor:
Michelle K Scotland, Justin M H Heltzel, James E Kath, Jung-Suk Choi, Anthony J Berdis, Joseph J Loparo, Mark D Sutton
Publikováno v:
PLoS Genetics, Vol 11, Iss 9, p e1005507 (2015)
Translesion DNA synthesis (TLS) by specialized DNA polymerases (Pols) is a conserved mechanism for tolerating replication blocking DNA lesions. The actions of TLS Pols are managed in part by ring-shaped sliding clamp proteins. In addition to catalyzi
Externí odkaz:
https://doaj.org/article/a93f1e5911504317a3253dcdaa0248cf
Autor:
Madeleine Bossaert, Andrew T. Moreno, Antonio Peixoto, Marie-Jeanne Pillaire, Pauline Chanut, Philippe Frit, Patrick Calsou, Joseph J. Loparo, Sébastien Britton
Publikováno v:
Cell Reports, Vol 43, Iss 8, Pp 114538- (2024)
Summary: Repair of DNA double-strand breaks by the non-homologous end-joining pathway is initiated by the binding of Ku to DNA ends. Multiple Ku proteins load onto linear DNAs in vitro. However, in cells, Ku loading is limited to ∼1–2 molecules p
Externí odkaz:
https://doaj.org/article/a6f4ae965ac4434cb1366a88f8f04bc3
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Nonhomologous end joining (NHEJ), the primary pathway of vertebrate DNA double-strand-break (DSB) repair, directly re-ligates broken DNA ends. Damaged DSB ends that cannot be immediately re-ligated are modified by NHEJ processing enzymes, in
Externí odkaz:
https://doaj.org/article/7f144421046948c4965c6d45b0ca0c4a
Autor:
Irina Shlosman, Elayne M. Fivenson, Morgan S. A. Gilman, Tyler A. Sisley, Suzanne Walker, Thomas G. Bernhardt, Andrew C. Kruse, Joseph J. Loparo
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract The peptidoglycan (PG) cell wall protects bacteria against osmotic lysis and determines cell shape, making this structure a key antibiotic target. Peptidoglycan is a polymer of glycan chains connected by peptide crosslinks, and its synthesis
Externí odkaz:
https://doaj.org/article/46f4aabe611d4823be2a46c4d4c0f829
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
The multi-subunit SWR1C remodeler deposits histone variant H2A.Z at nucleosomes flanking protein-coding genes. Here the authors use single-molecule and ensemble methodologies to identify three ATP-dependent phases in the H2A.Z deposition reaction.
Externí odkaz:
https://doaj.org/article/4f912a6a1e004577aac46127ebee3290
Publikováno v:
mBio, Vol 12, Iss 1 (2021)
The initial transfer of genomic material from a virus into a host cell is a key step in any viral infection. Consequently, understanding how viruses deliver their genomes into cells could reveal attractive therapeutic targets.
Externí odkaz:
https://doaj.org/article/d51b1a60549c4cc3b03c4aacdf68bbc1
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
Translesion synthesis (TLS) enables cells to tolerate damaged DNA encountered during replication. Here the authors use super-resolution photoactivation localization microscopy to reveal a lesion type dependent mechanism of recruitment of the TLS poly
Externí odkaz:
https://doaj.org/article/d3bdcb38b59846ff94dc46e555e13faf
Autor:
Seungwoo Chang, Elizabeth S. Thrall, Luisa Laureti, Sadie C. Piatt, Vincent Pagès, Joseph J. Loparo
Publikováno v:
Nature Structural & Molecular Biology
Nature Structural & Molecular Biology, 2022, 29 (9), pp.932+. ⟨10.1038/s41594-022-00827-2⟩
Nat Struct Mol Biol
Nature Structural & Molecular Biology, 2022, 29 (9), pp.932+. ⟨10.1038/s41594-022-00827-2⟩
Nat Struct Mol Biol
Processivity clamps tether DNA polymerases to DNA, allowing their access to the primer-template junction. In addition to DNA replication, DNA polymerases also participate in various genome maintenance activities, including translesion synthesis (TLS)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a976ee7bf300c9759acd8812d70dfd9a
https://doi.org/10.1038/s41594-022-00827-2
https://doi.org/10.1038/s41594-022-00827-2
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-7 (2016)
Single-molecule imaging of protein-DNA association requires fluorescently labelled protein, which limits the protein concentration that can be used. Here the authors exploit protein induced fluorescent enhancement of DNA sparsely labelled with Cy3 to
Externí odkaz:
https://doaj.org/article/e1e0b846b15649ecbc5a25f8158812ab