Zobrazeno 1 - 10
of 150
pro vyhledávání: '"Thomas A. Kirby"'
Autor:
Thomas W. Kirby, Scott A. Gabel, Eugene F. DeRose, Lalith Perera, Juno M. Krahn, Lars C. Pedersen, Robert E. London
Publikováno v:
Biomolecules, Vol 13, Iss 11, p 1603 (2023)
Formation of active HIV-1 reverse transcriptase (RT) proceeds via a structural maturation process that involves subdomain rearrangements and formation of an asymmetric p66/p66′ homodimer. These studies were undertaken to evaluate whether the inform
Externí odkaz:
https://doaj.org/article/376b12fa42bb4eceacdfd0459bcc8b10
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Abstract Human Nbs1, a component of the MRN complex involved in DNA double strand break repair, contains a concatenated N-terminal FHA-BRCT1/2 sequence that supports interaction with multiple phosphopeptide binding partners. MDC1 binding localizes Nb
Externí odkaz:
https://doaj.org/article/84fb1171b31f475c9785c36d1516f766
Publikováno v:
Traffic. 19:723-735
Despite the essential roles of pol X family enzymes in DNA repair, information about the structural basis of their nuclear import is limited. Recent studies revealed the unexpected presence of a functional nuclear localization signal (NLS) in DNA pol
Publikováno v:
Nucleic Acids Research
Aprataxin and PNKP-like factor (APLF) is a DNA repair factor containing a forkhead-associated (FHA) domain that supports binding to the phosphorylated FHA domain binding motifs (FBMs) in XRCC1 and XRCC4. We have characterized the interaction of the A
Autor:
Thomas A. Kirby
Publikováno v:
Chaucer and Middle English Studies ISBN: 9780429341786
Chaucer and Middle English Studies
Chaucer and Middle English Studies
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ef8e101be085ddebecf2a098d485b8c
https://doi.org/10.4324/9780429341786-33
https://doi.org/10.4324/9780429341786-33
Autor:
Jungki Min, Kyungmin Kim, Robert E. London, Lars C. Pedersen, Thomas W. Kirby, Scott A. Gabel
Publikováno v:
DNA Repair (Amst)
The N-terminal von Willebrand domain of Ku80 supports interactions with a Ku binding motif (KBM) that has been identified in at least three other DNA repair proteins: the non-homologous end joining (NHEJ) scaffold APLF, the modulator of retrovirus in
Autor:
Samuel H. Wilson, Robert E. London, Geoffrey A. Mueller, Thomas W. Kirby, William A. Beard, Eugene F. DeRose
Publikováno v:
Nucleic Acids Research
DNA polymerase β (pol β) plays a central role in the DNA base excision repair pathway and also serves as an important model polymerase. Dynamic characterization of pol β from methyl-TROSY 13C-1H multiple quantum CPMG relaxation dispersion experime
Autor:
Matthew J. Cuneo, Geoffrey A. Mueller, Scott A. Gabel, Robert E. London, Thomas W. Kirby, Juno M. Krahn, Cassandra E. Smith, Eugene F. DeRose
Publikováno v:
Structure. 22:1754-1763
Summary XRCC1, a scaffold protein involved in DNA repair, contains an N-terminal domain (X1NTD) that interacts specifically with DNA polymerase β. It was recently discovered that X1NTD contains a disulfide switch that allows it to adopt either of tw
Autor:
Eugene F. DeRose, Samuel H. Wilson, William A. Beard, Thomas W. Kirby, David D. Shock, Robert E. London
Publikováno v:
Biochemistry
DNA polymerase (pol) β is a multidomain enzyme with two enzymatic activities that plays a central role in the overlapping base excision repair and single-strand break repair pathways. The high frequency of pol β variants identified in tumor-derived
Autor:
Ming-Lang Zhao, Robert E. London, Julie K. Horton, Samuel H. Wilson, Natalie R. Gassman, Cassandra E. Smith, Thomas W. Kirby
Publikováno v:
Nucleic Acids Research
DNA polymerase β (pol β) requires nuclear localization to fulfil its DNA repair function. Although its small size has been interpreted to imply the absence of a need for active nuclear import, sequence and structural analysis suggests that a monopa