Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
about
Multiple ATR-Chk1 pathway proteins preferentially associate with checkpoint-inducing DNA substratesHuman single-stranded DNA binding proteins are essential for maintaining genomic stabilityHuman Tim/Timeless-interacting protein, Tipin, is required for efficient progression of S phase and DNA replication checkpointCharacterization of functional domains in human ClaspinThe mitochondrial transcription termination factor mTERF modulates replication pausing in human mitochondrial DNATipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint functionThe human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacementMus81 functions in the quality control of replication forks at the rDNA and is involved in the maintenance of rDNA repeat number in Saccharomyces cerevisiaeTimeless links replication termination to mitotic kinase activationMcm2 phosphorylation and the response to replicative stressGenetic analysis of Saccharomyces cerevisiae H2A serine 129 mutant suggests a functional relationship between H2A and the sister-chromatid cohesion partners Csm3-Tof1 for the repair of topoisomerase I-induced DNA damage.Establishment of cohesion at the pericentromere by the Ctf19 kinetochore subcomplex and the replication fork-associated factor, Csm3The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control replication termination of Saccharomyces cerevisiaeHuman Timeless and Tipin stabilize replication forks and facilitate sister-chromatid cohesionRoles of ChlR1 DNA helicase in replication recovery from DNA damageMammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factorsTimeless preserves telomere length by promoting efficient DNA replication through human telomeresReplication foci dynamics: replication patterns are modulated by S-phase checkpoint kinases in fission yeast.Specific biomarkers for stochastic division patterns and starvation-induced quiescence under limited glucose levels in fission yeast.Replication fork stability is essential for the maintenance of centromere integrity in the absence of heterochromatinThe subunits of the S-phase checkpoint complex Mrc1/Tof1/Csm3: dynamics and interdependence.Protection of telomeres by a conserved Stn1-Ten1 complex.The role of the Fanconi anemia network in the response to DNA replication stress.Mcm4 C-terminal domain of MCM helicase prevents excessive formation of single-stranded DNA at stalled replication forksFission yeast Tel1(ATM) and Rad3(ATR) promote telomere protection and telomerase recruitment.Single Holliday junctions are intermediates of meiotic recombination.Critical functions of Rpa3/Ssb3 in S-phase DNA damage responses in fission yeast.Schizosaccharomyces pombe Swi1, Swi3, and Hsk1 are components of a novel S-phase response pathway to alkylation damage.Checkpoint-dependent and -independent roles of Swi3 in replication fork recovery and sister chromatid cohesion in fission yeast.Protection and replication of telomeres in fission yeast.Linking chromosome duplication and segregation via sister chromatid cohesionIdentification of a novel type of spacer element required for imprinting in fission yeastFission yeast Hsk1 (Cdc7) kinase is required after replication initiation for induced mutagenesis and proper response to DNA alkylation damage.Rad3 decorates critical chromosomal domains with gammaH2A to protect genome integrity during S-Phase in fission yeast.A genetic screen for replication initiation defective (rid) mutants in Schizosaccharomyces pombeSwi1 associates with chromatin through the DDT domain and recruits Swi3 to preserve genomic integrity.DNA polymerase α (swi7) and the flap endonuclease Fen1 (rad2) act together in the S-phase alkylation damage response in S. pombe.Timeless protection of telomeres.Coordinated degradation of replisome components ensures genome stability upon replication stress in the absence of the replication fork protection complexMinichromosome maintenance proteins interact with checkpoint and recombination proteins to promote s-phase genome stability.
P2860
Q21076125-7D20C0BD-F73F-4E39-A1BF-573FF61CD538Q21263027-504B15D8-6FEF-4064-B627-C8927D0671C6Q24315071-E2AD7497-B3E0-4A65-A302-84FF6CE9897AQ24601538-BF17207B-0EB8-4657-BB60-D0DD940EFE4FQ24669735-E20AA91E-670D-4850-A7E4-835D2FFF3897Q24682108-E93520DE-7F4B-4A2F-A1C3-09AE88DDCEDDQ24683336-ECE92BD3-F9CD-4CA2-A941-3A750C7691ACQ24684096-41B7D8E7-BBE8-4F2A-BA87-F8E2A027226CQ27342850-B82960FC-D1AA-464C-8D3B-7339CA932A0DQ27931022-FA3252A1-B986-487E-BCD6-C856BBC35382Q27936447-6CE4C621-96C9-4EFB-9C9C-CAFBDBD2E0ACQ27938489-477F3444-CA04-406E-BACD-7F8809A08368Q27940201-4634051F-ED19-4632-BCC7-38CF6866F5E8Q28118451-E43907AE-2AEE-431D-AF86-6DC99E8F5B0AQ28119141-4073C7A1-9E99-47A5-8953-31FF8D010369Q28587270-10F89DE9-D748-475C-B9B6-142B8A01C756Q29041627-DD4055FB-418F-49A8-B685-3123C68B9D5AQ30479065-9541F05B-A95B-4A88-97D9-B7569476BCA1Q30501631-B2ACEF60-6707-4BF8-9F4E-5307409B62D4Q30539756-14F1376B-AF4D-4E9F-A1B1-34CDC63A3028Q30596955-166C30B9-4C70-4EF5-BC14-A74D25DB6600Q33294968-335CBE5F-8561-4099-819C-3A3B71FA6D1FQ33347783-69D1DC9B-3F06-4417-BF5F-FD41A4DBE581Q33364389-144C07B6-9746-4956-8145-30A882AD9F2DQ33497909-9BACA077-AB2D-4BF3-BD68-0D0430A214BEQ33576921-4C56916F-958C-457F-BAA3-8582AFA8B172Q33707399-3C9C2E09-D389-4100-A536-9DBA29A6D80CQ33707715-1F0346E1-DE2C-417A-9F8E-C7F5E5F60885Q33725551-B62CF973-2A18-4588-8EB5-593489B8EFAEQ33789158-D53E5ABB-D20C-4F19-B528-36636A11B1A4Q33841394-3D732C79-4DC4-4CEF-AB3E-0D702C44E2D9Q33851567-AAEEC176-3475-43A3-91F5-69D648DAE361Q33853216-48647B16-C409-455F-9225-13199719201CQ34014307-FEAC9C48-EF4F-4B61-8E05-02037E9840CBQ34134053-62063357-DB42-40BA-8152-ACB6189F411DQ34406008-CA299844-67D6-4BA1-AC7B-4EC7FBCC010AQ34447883-2976295B-0733-490C-A370-4A2840486F35Q34521770-56EC51FA-FEBB-4423-84F1-212DC1FF8A87Q34561912-DEE24F2E-985B-4386-A241-607E288258ABQ34733887-C1414917-B9F5-4E58-936B-08281DC6C151
P2860
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
@en
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
@nl
type
label
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
@en
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
@nl
prefLabel
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
@en
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.
@nl
P2093
P2860
P1476
Swi1 and Swi3 are components of a replication fork protection complex in fission yeast
@en
P2093
Chiaki Noguchi
Eishi Noguchi
John R Yates
Paul Russell
P2860
P304
P356
10.1128/MCB.24.19.8342-8355.2004
P407
P577
2004-10-01T00:00:00Z