Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Remy, Le Meur"'
Autor:
Michal Hammel, Norie Sugitani, Daniel J. Rosenberg, Kateryna V Le Meur, Agnieszka M. Topolska-Woś, Orlando D. Schärer, Remy Le Meur, Hyunsuk Kim, Jung-Eun Yeo, Walter J. Chazin, John J Cordoba
Publikováno v:
Nucleic acids research, vol 48, iss 4
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2020, 48 (4), pp.2173-2188. ⟨10.1093/nar/gkz1231⟩
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2020, 48 (4), pp.2173-2188. ⟨10.1093/nar/gkz1231⟩
The XPA protein functions together with the single-stranded DNA (ssDNA) binding protein RPA as the central scaffold to ensure proper positioning of repair factors in multi-protein nucleotide excision repair (NER) machinery. We previously determined t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28e16d90031468ce11a44073363fb9b9
https://escholarship.org/uc/item/80p224cp
https://escholarship.org/uc/item/80p224cp
Autor:
Raj K. Pandita, Rajesh Kumar, Tej K. Pandita, Walter J. Chazin, Katharina Schlacher, Albino Bacolla, Shashank Hambarde, Vijay Charaka, Paul Russell, Anirban Maitra, Susan E. Tsutakawa, Chi Lin Tsai, Remy Le Meur, Oliver Limbo, Clayton R. Hunt, John A. Tainer
Publikováno v:
Molecular cell, vol 81, iss 14
Mol Cell
Mol Cell
Stalled DNA replication fork restart after stress as orchestrated by ATR kinase, BLM helicase, and structure-specific nucleases enables replication, cell survival, and genome stability. Here we unveil human exonuclease V (EXO5) as an ATR-regulated DN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbf9292008a0846df20b886b28749772
https://doi.org/10.1016/j.molcel.2021.05.027
https://doi.org/10.1016/j.molcel.2021.05.027
Autor:
Christopher N, Johnson, Rekha, Pattanayek, Franck, Potet, Robyn T, Rebbeck, Daniel J, Blackwell, Roman, Nikolaienko, Vasco, Sequeira, Remy, Le Meur, Przemysław B, Radwański, Jonathan P, Davis, Aleksey V, Zima, Razvan L, Cornea, Steven M, Damo, Sandor, Györke, Alfred L, George, Björn C, Knollmann
Publikováno v:
Cell Calcium
Here we report the structure of the widely utilized calmodulin (CaM)-dependent protein kinase II (CaMKII) inhibitor KN93 bound to the Ca(2+)-sensing protein CaM. KN93 is widely believed to inhibit CaMKII by binding to the kinase. The CaM-KN93 interac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2d311458be0ae13ccb17a5c29535b117
https://pubmed.ncbi.nlm.nih.gov/31401388
https://pubmed.ncbi.nlm.nih.gov/31401388
Autor:
Sarah R. Wessel, Aditya A. Sathe, David Cortez, Runxiang Zhao, Shyam K. Sharan, Huzefa Dungrawala, Xia Ding, Remy Le Meur, Kamakoti P. Bhat, Walter J. Chazin
Publikováno v:
Molecular Cell
Molecular Cell, Elsevier, 2017, 67 (3), pp.374-386.e5. ⟨10.1016/j.molcel.2017.06.023⟩
Molecular Cell, Elsevier, 2017, 67 (3), pp.374-386.e5. ⟨10.1016/j.molcel.2017.06.023⟩
RAD51 promotes homology-directed repair (HDR), replication fork reversal, and stalled fork protection. Defects in these functions cause genomic instability and tumorigenesis but also generate hypersensitivity to cancer therapeutics. Here we describe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::502b2c27130f4dc296fc35e86bfd21a8
https://europepmc.org/articles/PMC5548441/
https://europepmc.org/articles/PMC5548441/