Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Xavier V, Gomes"'
Autor:
Marcel, Margulies, Michael, Egholm, William E, Altman, Said, Attiya, Joel S, Bader, Lisa A, Bemben, Jan, Berka, Michael S, Braverman, Yi-Ju, Chen, Zhoutao, Chen, Scott B, Dewell, Lei, Du, Joseph M, Fierro, Xavier V, Gomes, Brian C, Godwin, Wen, He, Scott, Helgesen, Chun Heen, Ho, Chun He, Ho, Gerard P, Irzyk, Szilveszter C, Jando, Maria L I, Alenquer, Thomas P, Jarvie, Kshama B, Jirage, Jong-Bum, Kim, James R, Knight, Janna R, Lanza, John H, Leamon, Steven M, Lefkowitz, Ming, Lei, Jing, Li, Kenton L, Lohman, Hong, Lu, Vinod B, Makhijani, Keith E, McDade, Michael P, McKenna, Eugene W, Myers, Elizabeth, Nickerson, John R, Nobile, Ramona, Plant, Bernard P, Puc, Michael T, Ronan, George T, Roth, Gary J, Sarkis, Jan Fredrik, Simons, John W, Simpson, Maithreyan, Srinivasan, Karrie R, Tartaro, Alexander, Tomasz, Kari A, Vogt, Greg A, Volkmer, Shally H, Wang, Yong, Wang, Michael P, Weiner, Pengguang, Yu, Richard F, Begley, Jonathan M, Rothberg
Publikováno v:
Nature. 437:376-380
The proliferation of large-scale DNA-sequencing projects in recent years has driven a search for alternative methods to reduce time and cost. Here we describe a scalable, highly parallel sequencing system with raw throughput significantly greater tha
Publikováno v:
Journal of Biological Chemistry. 278:1618-1625
In the presence of proliferating cell nuclear antigen, yeast DNA polymerase δ (Pol δ) replicated DNA at a rate of 40–60 nt/s. When downstream double-stranded DNA was encountered, Pol δ paused, but most replication complexes proceeded to carry ou
Autor:
Xavier V. Gomes, Peter M. J. Burgers
Publikováno v:
Journal of Biological Chemistry. 276:34768-34775
Eukaryotic replication factor C is the heteropentameric complex that loads the replication clamp proliferating cell nuclear antigen (PCNA) onto primed DNA. In this study we used a derivative, designated RFC, with a N-terminal truncation of the Rfc1 s
Publikováno v:
Journal of Biological Chemistry. 276:34792-34800
Replication factor C is required to load proliferating cell nuclear antigen onto primer-template junctions, using the energy of ATP hydrolysis. Four of the five RFCgenes have consensus ATP-binding motifs. To determine the relative importance of these
Autor:
Xavier V. Gomes, Peter M. J. Burgers
Publikováno v:
The EMBO Journal. 19:3811-3821
The FEN1 nuclease functions during Okazaki fragment maturation in the eukaryotic cell. Like many other proliferating cell nuclear antigen (PCNA)-binding proteins, FEN1 interacts with the interdomain connector loop (IDCL) of PCNA, and PCNA greatly sti
Publikováno v:
Journal of Biological Chemistry. 275:14541-14549
Eukaryotic replication factor C (RF-C) is a heteropentameric complex that is required to load the replication clamp proliferating cell nuclear antigen onto primed DNA. Saccharomyces cerevisiae RF-C is encoded by the genes RFC1-RFC5. The RFC1 gene was
Publikováno v:
Biochemistry. 38:3963-3973
Human replication protein A (RPA) is a multiple subunit single-stranded DNA-binding protein that is required for multiple processes in cellular DNA metabolism. This complex, composed of subunits of 70, 32, and 14 kDa, binds to single-stranded DNA (ss
Autor:
Marc S. Wold, Andrew S. Lipton, Nancy G. Isern, Xavier V. Gomes, Doris M. Jacobs, Gary W. Daughdrill, David F. Lowry
Publikováno v:
Journal of Biomolecular NMR. 14:321-331
Human Replication Protein A (hsRPA) is required for multiple cellular processes in DNA metabolism including DNA repair, replication and recombination. It binds single-stranded DNA with high affinity and interacts specifically with multiple proteins.
Autor:
Marc S. Wold, Xavier V. Gomes
Publikováno v:
Biochemistry. 35:10558-10568
Human replication protein A (RPA) is a single-stranded DNA-binding protein that is composed of subunits of 70, 32, and 14 kDa. This heterotrimeric complex is required for multiple processes in DNA metabolism including DNA replication, DNA repair, and
Publikováno v:
Biochemistry. 35:5586-5595
Replication protein A (RPA) is multisubunit single-stranded DNA-binding protein required for multiple processes in DNA metabolism including DNA replication, DNA repair, and recombination. Human RPA is a stable complex of three subunits of 70, 32, and