Zobrazeno 1 - 10
of 42
pro vyhledávání: '"R, Chapados"'
Autor:
Samantha G Zeitlin, Brian R Chapados, Norman M Baker, Caroline Tai, Geir Slupphaug, Jean Y J Wang
Publikováno v:
PLoS ONE, Vol 6, Iss 3, p e17151 (2011)
Uracil is removed from DNA by the conserved enzyme uracil DNA N-glycosylase (UNG). Previously, we observed that inhibiting UNG in Xenopus egg extracts blocked assembly of CENP-A, a histone H3 variant. CENP-A is an essential protein in all species, si
Externí odkaz:
https://doaj.org/article/daa6d77585eb4b38b51f181627e19706
Autor:
Susan E. Tsutakawa, Peter Thompson, Altaf H. Sarker, Christopher G. Tomlinson, L. David Finger, Scott Classen, Andrew S. Arvai, Jane A. Grasby, Brian R. Chapados, John A. Tainer, Priscilla K. Cooper, Binghui Shen, Grant Guenther
Publikováno v:
Cell. 145:198-211
SummaryFlap endonuclease (FEN1), essential for DNA replication and repair, removes RNA and DNA 5′ flaps. FEN1 5′ nuclease superfamily members acting in nucleotide excision repair (XPG), mismatch repair (EXO1), and homologous recombination (GEN1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e44a19136cf7040e517e67f6b295d36
https://doi.org/10.1016/j.cell.2011.03.004
https://doi.org/10.1016/j.cell.2011.03.004
Publikováno v:
Biochemical Society Transactions. 38:433-437
FENs (flap endonucleases) and related FEN-like enzymes [EXO-1 (exonuclease-1), GEN-1 (gap endonuclease 1) and XPG (xeroderma pigmentosum complementation group G)] are a family of bivalent-metal-ion-dependent nucleases that catalyse structure-specific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34a5884d03a7e282561e53a6704e39f
https://doi.org/10.1042/bst0380433
https://doi.org/10.1042/bst0380433
Autor:
Brian R. Chapados, Samantha G. Zeitlin, Evi Soutoglou, Michael W. Berns, Norman M. Baker, Don W. Cleveland, Jean Y. J. Wang
Publikováno v:
Zeitlin, SG; Baker, NM; Chapados, BR; Soutoglou, E; Wang, JYJ; Berns, MW; et al.(2009). Double-strand DNA breaks recruit the centromeric histone CENP-A. Proceedings of the National Academy of Sciences of the United States of America, 106(37), 15762-15767. doi: 10.1073/pnas.0908233106. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3z3776mp
The histone H3 variant CENP-A is required for epigenetic specification of centromere identity through a loading mechanism independent of DNA sequence. Using multiphoton absorption and DNA cleavage at unique sites by I- Sce I endonuclease, we demonstr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cd87a4709da1776293190d0949d7992
https://doi.org/10.1073/pnas.0908233106
https://doi.org/10.1073/pnas.0908233106
Autor:
Jane A. Grasby, John A. Tainer, Karl Syson, Nicholas H. Williams, Christopher G. Tomlinson, Brian R. Chapados, Jon R. Sayers
Publikováno v:
Journal of Biological Chemistry. 283:28741-28746
Protein nucleases and RNA enzymes depend on divalent metal ions to catalyze the rapid hydrolysis of phosphate diester linkages of nucleic acids during DNA replication, DNA repair, RNA processing, and RNA degradation. These enzymes are widely proposed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::877115d405a3c77d89b69f021af74f95
https://doi.org/10.1074/jbc.m801264200
https://doi.org/10.1074/jbc.m801264200
Autor:
John A. Tainer, Brian R. Chapados, Sangeetha Vijayakumar, Kristina H. Schmidt, Alan E. Tomkinson, Richard D. Kolodner
Publikováno v:
Nucleic Acids Research
There is compelling evidence that proliferating cell nuclear antigen (PCNA), a DNA sliding clamp, co-ordinates the processing and joining of Okazaki fragments during eukaryotic DNA replication. However, a detailed mechanistic understanding of functio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4a0ba0528dcc8fcaf12c8bd6a419186
https://doi.org/10.1093/nar/gkm006
https://doi.org/10.1093/nar/gkm006
Publikováno v:
Nucleic Acids Research
Proliferating cell nuclear antigen (PCNA) acts as a biologically essential processivity factor that encircles DNA and provides binding sites for polymerase, flap endonuclease-1 (FEN-1) and ligase during DNA replication and repair. We have computation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ced32e0bcc027a17119ba2ff9df402d
https://doi.org/10.1093/nar/gkl744
https://doi.org/10.1093/nar/gkl744
Autor:
Brian R. Chapados, June Hyung Lee, Erik W. Debler, James R. Williamson, Anette Schneemann, Jeffrey A. Chao
Publikováno v:
Nature Structural & Molecular Biology. 12:952-957
As a counter-defense against antiviral RNA silencing during infection, the insect Flock House virus (FHV) expresses the silencing suppressor protein B2. Biochemical experiments show that B2 binds to double-stranded RNA (dsRNA) without regard to lengt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f753f9051d75a2f2503990a59c5e2b67
https://doi.org/10.1038/nsmb1005
https://doi.org/10.1038/nsmb1005
Autor:
John A. Tainer, David J. Hosfield, Biana Yelent, Binghui Shen, Seungil Han, Junzhuan Qiu, Brian R. Chapados
Publikováno v:
Cell. 116(1):39-50
Flap EndoNuclease-1 (FEN-1) and the processivity factor proliferating cell nuclear antigen (PCNA) are central to DNA replication and repair. To clarify the molecular basis of FEN-1 specificity and PCNA activation, we report here structures of FEN-1:D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93d388b9d70efacc766d3ad41c5c3c88
Publikováno v:
Biochemical and Biophysical Research Communications. 286:1073-1081
RNA primer removal during DNA replication is dependent on ribonucleotide- and structure-specific RNase H and FEN-1 nuclease activities. A specific RNase H involved in this reaction has long been sought. RNase HII is the only open reading frame in Arc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b47f41b025c38ec5b7874b9e4975469
https://doi.org/10.1006/bbrc.2001.5523
https://doi.org/10.1006/bbrc.2001.5523