Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Kendall L. Knight"'
Autor:
Dima M. Baitin, Michael M. Cox, Alexandra V. Dudkina, Vladislav A. Lanzov, Kendall L. Knight, Irina V. Bakhlanova
Publikováno v:
Molecular Microbiology. 78:1523-1538
The wild-type Escherichia coli RecA protein is a recombinase platform with unrealized recombination potential. We have explored the factors affecting recombination during conjugation with a quantitative assay. Regulatory proteins that affect RecA fun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5411ae40db51dd503ffc1ff2d0d0ce8
https://doi.org/10.1111/j.1365-2958.2010.07424.x
https://doi.org/10.1111/j.1365-2958.2010.07424.x
Publikováno v:
Journal of Biological Chemistry. 285:18984-18990
Homologous recombination (HR) plays a critical role in facilitating replication fork progression when the polymerase complex encounters a blocking DNA lesion, and it also serves as the primary mechanism for error-free repair of DNA double strand brea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2ca1a380802f8458e6e219d81f25c44b
https://doi.org/10.1074/jbc.m109.099846
https://doi.org/10.1074/jbc.m109.099846
Publikováno v:
Journal of Biological Chemistry. 284:31945-31952
Exposure of cells to DNA-damaging agents results in a rapid increase in the formation of subnuclear complexes containing Rad51. To date, it has not been determined to what extent DNA damage-induced cytoplasmic to nuclear transport of Rad51 may contri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e6a318fee3b20281741fcac7269a2cb
https://doi.org/10.1074/jbc.m109.024646
https://doi.org/10.1074/jbc.m109.024646
Publikováno v:
Proceedings of the National Academy of Sciences. 103:18137-18142
DNA double-strand breaks (DSBs) caused by cellular exposure to genotoxic agents or produced by inherent metabolic processes initiate a rapid and highly coordinated series of molecular events resulting in DNA damage signaling and repair. Phosphorylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6356187990c78fd66b033b110e493f96
https://doi.org/10.1073/pnas.0608709103
https://doi.org/10.1073/pnas.0608709103
Autor:
Kendall L. Knight, Melissa A. Calmann, Celia A. Schiffer, Dharia A. McGrew, Anthony L. Forget, Michelle M. Kudron
Publikováno v:
Biochemistry. 45:13537-13542
All RecA-like recombinase enzymes catalyze DNA strand exchange as elongated filaments on DNA. Despite numerous biochemical and structural studies of RecA and the related Rad51 and RadA proteins, the unit oligomer(s) responsible for nucleoprotein fila
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7838c72d3a61bf277d0a3f27908dac7
https://doi.org/10.1021/bi060938q
https://doi.org/10.1021/bi060938q
Publikováno v:
Journal of Molecular Biology. 345:239-249
Human Rad52 (HsRad52) is a DNA-binding protein (418 residues) that promotes the catalysis of DNA double strand break repair by the Rad51 recombinase. HsRad52 self-associates to form ring-shaped oligomers as well as higher order complexes of these rin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8507b7cd9e6283267dd257d82f118700
https://doi.org/10.1016/j.jmb.2004.10.065
https://doi.org/10.1016/j.jmb.2004.10.065
Publikováno v:
Journal of Cellular Biochemistry. 93:429-436
Rad51-mediated homologous recombination (HR) is essential for maintenance of genome integrity. The Xrcc3 protein functions in HR DNA repair, and studies suggest it has multiple roles at different stages in this pathway. Defects in vertebrate XRCC3 re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::851d414ca1d105e0f3a7c1b645ff67b7
https://doi.org/10.1002/jcb.20232
https://doi.org/10.1002/jcb.20232
Publikováno v:
Journal of Molecular Biology. 299:91-101
We have introduced targeted mutations in two areas that make up part of the RecA subunit interface. In the RecA crystal structure, cross-subunit interactions are observed between the Lys6 and Asp139 side-chains, and between the Arg28 and Asn113 side-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::97da93d6f4521bdb6788e2c3b67f61cb
https://doi.org/10.1006/jmbi.2000.3721
https://doi.org/10.1006/jmbi.2000.3721
Autor:
Kendall L. Knight, J. K. De Zutter
Publikováno v:
Journal of Molecular Biology. 293:769-780
The human Rad51 protein (hRad51), like its bacterial homologue RecA, catalyzes genetic recombination between homologous single and double-stranded DNA substrates. Using IAsys biosensor technology, we have examined the critical first step in this proc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bfca091fc17a3998c31bc92789cabf9
https://doi.org/10.1006/jmbi.1999.3200
https://doi.org/10.1006/jmbi.1999.3200
Publikováno v:
Biochemistry. 38:11933-11941
Mutational studies of regions that make up the oligomeric interface within the RecA protein filament structure have shown that F217 is an important determinant of RecA function and oligomer stability. All substitutions, other than Tyr and Cys, comple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f2496d442c78302078f2fb040ef28aa
https://doi.org/10.1021/bi991118z
https://doi.org/10.1021/bi991118z