The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer
about
Clamp loader ATPases and the evolution of DNA replication machinery.DNA replication in the archaeaThe RFC clamp loader: structure and functionThe Mechanism of ATP-Dependent Primer-Template Recognition by a Clamp Loader ComplexThe Escherichia coli Clamp Loader Can Actively Pry Open the -Sliding ClampHow a DNA Polymerase Clamp Loader Opens a Sliding ClampMechanism of proliferating cell nuclear antigen clamp opening by replication factor CRecognition of the ring-opened state of proliferating cell nuclear antigen by replication factor C promotes eukaryotic clamp-loading.Probing DNA clamps with single-molecule force spectroscopy.A slow ATP-induced conformational change limits the rate of DNA binding but not the rate of beta clamp binding by the escherichia coli gamma complex clamp loader.Replisome dynamics and use of DNA trombone loops to bypass replication blocks.Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesisThe mechanical properties of PCNA: implications for the loading and function of a DNA sliding clamp.Stepwise loading of yeast clamp revealed by ensemble and single-molecule studies.Impact of individual proliferating cell nuclear antigen-DNA contacts on clamp loading and function on DNA.Replication factor C is a more effective proliferating cell nuclear antigen (PCNA) opener than the checkpoint clamp loader, Rad24-RFC.A central swivel point in the RFC clamp loader controls PCNA opening and loading on DNAATP binding and hydrolysis-driven rate-determining events in the RFC-catalyzed PCNA clamp loading reactionHow a holoenzyme for DNA replication is formed.Regulation of polymerase exchange between Poleta and Poldelta by monoubiquitination of PCNA and the movement of DNA polymerase holoenzymeStepwise assembly of the human replicative polymerase holoenzyme.The bacterial DnaC helicase loader is a DnaB ring breaker.Replication clamps and clamp loaders.Loading clamps for DNA replication and repairMechanism of ATP-driven PCNA clamp loading by S. cerevisiae RFC.A tale of two tails: activation of DNA damage checkpoint kinase Mec1/ATR by the 9-1-1 clamp and by Dpb11/TopBP1.Molecular analyses of a three-subunit euryarchaeal clamp loader complex from Methanosarcina acetivoransThe ATP sites of AAA+ clamp loaders work together as a switch to assemble clamps on DNAMonitoring the Retention of Human Proliferating Cell Nuclear Antigen at Primer/Template Junctions by Proteins That Bind Single-Stranded DNA.Review: The lord of the rings: Structure and mechanism of the sliding clamp loader.A novel function for the conserved glutamate residue in the walker B motif of replication factor C.Communication between subunits within an archaeal clamp-loader complex.Kinetic analysis of PCNA clamp binding and release in the clamp loading reaction catalyzed by Saccharomyces cerevisiae replication factor C.Mechanism of opening a sliding clamp.Linchpin DNA-binding residues serve as go/no-go controls in the replication factor C-catalyzed clamp-loading mechanism.Investigation of sliding DNA clamp dynamics by single-molecule fluorescence, mass spectrometry and structure-based modeling.On the mechanism of loading the PCNA sliding clamp by RFC
P2860
Q21245381-2D7A405A-190B-4037-9CCE-E5649276F206Q24672512-8F91FC66-DC1E-408B-B5AC-BDF12065323BQ26825605-D9AF0525-214D-4408-86E7-6407D251C257Q27655502-CCB118CC-6653-4594-882B-3A56B830CA83Q27674727-AC0520AC-2127-40BB-829E-E8674ED4FD28Q27676381-9EBF4EE7-B085-4DCA-832E-C8C6DD8DB160Q28306688-A3C8B917-5A35-40FE-82A3-850C77FF891DQ30494687-243ABC74-DEB8-4679-9F4E-35515BB152A6Q30544116-9F392B16-9C0F-4E30-8BB9-70CFDC3A3ECAQ33553879-D91AD427-9552-4780-B7E0-83DCDA26B277Q33571008-BF2F9AFA-B6DA-4375-B1F2-49D7EDA445DEQ33756104-C6DC6399-D972-4DF3-9067-71A56C772808Q33908367-B6872AB8-4BC9-43A8-9D00-B3579B4B657EQ34358765-6E8A0309-4ECC-4AF9-BCEF-5CE391626EFEQ34383645-8A1504C7-2BA9-4CCB-BE32-8B267F9065C5Q35694079-617C4908-D87F-45FD-8EEA-A0AAE47B06CDQ35718144-10900275-A9C8-4811-B663-DAC478053AF9Q36218801-2B63A022-31DB-4B27-A815-7BE9AEE4FE24Q36512078-B2FEA721-4BFF-4E08-A3C3-D36563C32B3EQ36535537-DDD246F6-05F2-43A7-8567-4E08958FFA34Q36733760-4EFB6FE3-DA0B-4B63-B0B8-D0F259A9A5B1Q36895278-DC0AA31C-C8E8-4CDB-A3FD-2192503B44B9Q36932854-20D8CC0C-2013-4A3A-8479-9E0D3F17390FQ37215085-C3EAA68C-568A-415E-8D61-4499D828FE2EQ37236750-5AAB2657-309F-4D67-AD05-D6DB197FD472Q37301087-BBED784A-DF76-4E5C-ADF1-F90BDE3A9D10Q37481416-25286785-3D9E-4CC1-A6A7-4518E93D4DB3Q37608441-1B820CCA-37CA-40F5-90AA-853AAE94B7EFQ38287987-2F325F05-FAB4-4E82-9722-A64060E1541FQ38751208-3B81F6E4-82F1-4DFE-B5A1-F45A57FF9A73Q42261115-540B5643-0AFA-4AD7-BFF6-70A50D90A663Q42532936-857E6D81-B630-4941-BC1D-7A2B1E3AD8B9Q42566375-1028812A-4BC5-4BC9-94EB-48479888D352Q47706604-21E21C6C-BC4F-4860-B4EA-53F521C4E679Q47953015-C18CE5F3-C575-4DA1-8717-38972DCC5D07Q52359081-E165515C-E192-4F8B-8985-957C55AB9B7DQ57979743-90BF65AA-F4F9-4206-AA8A-8B0728C9F04E
P2860
The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The structure of a ring-opened ...... y fluorescence energy transfer
@ast
The structure of a ring-opened ...... y fluorescence energy transfer
@en
The structure of a ring-opened ...... y fluorescence energy transfer
@nl
type
label
The structure of a ring-opened ...... y fluorescence energy transfer
@ast
The structure of a ring-opened ...... y fluorescence energy transfer
@en
The structure of a ring-opened ...... y fluorescence energy transfer
@nl
prefLabel
The structure of a ring-opened ...... y fluorescence energy transfer
@ast
The structure of a ring-opened ...... y fluorescence energy transfer
@en
The structure of a ring-opened ...... y fluorescence energy transfer
@nl
P2093
P2860
P356
P1476
The structure of a ring-opened ...... y fluorescence energy transfer
@en
P2093
Bonita L Yoder
Peter M J Burgers
Stephen J Benkovic
P2860
P304
P356
10.1073/PNAS.0511263103
P407
P577
2006-02-13T00:00:00Z