Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
about
Proliferating cell nuclear antigen (PCNA) may function as a double homotrimer complex in the mammalian cellBiochemical analyses indicate that binding and cleavage specificities define the ordered processing of human Okazaki fragments by Dna2 and FEN1Structural and biochemical studies of human proliferating cell nuclear antigen complexes provide a rationale for cyclin association and inhibitor designXPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutationsOkazaki fragment maturation: nucleases take centre stageTwo fundamentally distinct PCNA interaction peptides contribute to chromatin assembly factor 1 functionThe 3'-flap pocket of human flap endonuclease 1 is critical for substrate binding and catalysisDNA replication in the archaeaPCNA-binding proteins in the archaea: novel functionality beyond the conserved coreDouble strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamilyUnpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleasesThe C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligaseCrystal structure of bacteriophage T4 5' nuclease in complex with a branched DNA reveals how flap endonuclease-1 family nucleases bind their substratesStructure of a Sliding Clamp on DNADNA apurinic-apyrimidinic site binding and excision by endonuclease IVStructures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and openingMre11 Dimers Coordinate DNA End Bridging and Nuclease Processing in Double-Strand-Break RepairSuperoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosisp38α MAP Kinase C-Terminal Domain Binding Pocket Characterized by Crystallographic and Computational AnalysesFlipping of alkylated DNA damage bridges base and nucleotide excision repairStructure and function of a novel endonuclease acting on branched DNA substratesThe crystal structure of Haloferax volcanii proliferating cell nuclear antigen reveals unique surface charge characteristics due to halophilic adaptation.Structural insights into the adaptation of proliferating cell nuclear antigen (PCNA) fromHaloferax volcaniito a high-salt environmentCrystal Structure of Epstein-Barr Virus DNA Polymerase Processivity Factor BMRF1Nbs1 Flexibly Tethers Ctp1 and Mre11-Rad50 to Coordinate DNA Double-Strand Break Processing and RepairPCNA directs type 2 RNase H activity on DNA replication and repair substratesCrystal structures of two active proliferating cell nuclear antigens (PCNAs) encoded by Thermococcus kodakaraensisStructure of flap endonuclease 1 from the hyperthermophilic archaeonDesulfurococcus amylolyticusCrystal structure of a KSHV-SOX-DNA complex: insights into the molecular mechanisms underlying DNase activity and host shutoffHuman Flap Endonuclease Structures, DNA Double-Base Flipping, and a Unified Understanding of the FEN1 SuperfamilyStructures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease FamilyThe structure of Escherichia coli ExoIX--implications for DNA binding and catalysis in flap endonucleasesA small protein inhibits proliferating cell nuclear antigen by breaking the DNA clampInteractions among DNA ligase I, the flap endonuclease and proliferating cell nuclear antigen in the expansion and contraction of CAG repeat tracts in yeastProcessing and joining of DNA ends coordinated by interactions among Dnl4/Lif1, Pol4, and FEN-1.Expression and biochemical characterization of the Plasmodium falciparum DNA repair enzyme, flap endonuclease-1 (PfFEN-1)Subtle alterations in PCNA-partner interactions severely impair DNA replication and repairReduced stability and increased dynamics in the human proliferating cell nuclear antigen (PCNA) relative to the yeast homologDynamics of Dnmt1 interaction with the replication machinery and its role in postreplicative maintenance of DNA methylationX-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution
P2860
Q24299392-A0F0F4F9-8C72-40FB-A5FC-84E028351908Q24319140-2074C585-75C8-44F7-BE99-4C128E7438E5Q24556671-008E8908-6288-4CF7-84F9-33E15BE5D9E8Q24603061-D6CE50E0-D79F-4FD3-B73D-8A0F87FD9BB9Q24632622-3E9E18A7-C4A5-4765-B790-F2D2BBBDE0CAQ24647319-D83443B2-47F5-4801-BCD8-96DA6F75A04BQ24658277-96874435-723E-4C35-A38F-FC5BCD1592C5Q24672512-1C4EBE8B-4E5C-4FE5-8688-7B1B0E45FB9AQ26765162-B80CFA27-313E-4A40-9A2F-2150C8A59D23Q26850039-5C0FCF3B-7525-440D-B473-C0367C133307Q27005670-1CBB054C-6B01-4482-A029-FCD79E4CD065Q27643859-EC35E52F-C5C2-480E-9765-94D1FB0A7443Q27647139-D98D35A4-4BE1-4B74-AC89-046A809C994EQ27649528-B8D3626F-D196-4D02-BBE8-4C42CAE9DD9FQ27650316-2ADC9478-7467-4032-8F2D-04FEE17E6D28Q27651596-C393A2D5-91C6-42C9-8C29-0D64E6457B78Q27652502-D249196E-F7D1-43D7-A900-D647C535551DQ27653085-65C04E63-7E5E-43D1-97A1-AB421801FE6DQ27655779-60A10537-EFB7-4F6C-BF0C-36324D1F3177Q27655873-A6A0DB8E-4255-4283-B074-BBEFC2367A3CQ27656505-F7D973F4-439C-41A7-B9B0-DD08FCA5BAABQ27657124-DBC902B9-B0F1-4423-B1EF-D6214073EC49Q27657512-2A88EBE1-0714-4220-8541-22A12503E965Q27657653-A0AE1B5E-A8B1-47D5-A6B9-121184656564Q27657670-5E6B474A-DD77-477E-882E-6253F5BD968DQ27666608-2BFA99AE-F372-479D-9EC3-311CC5E993ECQ27666749-2A71FFB1-0CD8-4660-8A6F-59E0B50789F6Q27666897-926F5147-AB25-40C7-8C73-DEB69F654A2FQ27667301-4D2FB24D-0DB3-4879-8D1A-8F0531E70D20Q27667524-616E0C5E-F82D-4416-98A5-D7AC542F3338Q27667527-FE1F81E6-9F7F-42AB-B9BD-72DD6D760831Q27678894-23DEAB8B-C0C1-4DFB-ACAD-1B9DED14FF43Q27704812-7B5326B9-93DF-4075-AB32-F45404DF6787Q27939439-97E2D6D7-5EBF-4D42-98D8-8211C67AE30FQ27939628-A2481B0D-59B5-4265-8296-6250F9E3B671Q27972548-0ABB8926-D9AF-4C18-98DD-398D06A7D05BQ28475748-397B9E32-8016-4E25-94DB-93754E54DB37Q28477198-A6B20CE4-558D-4802-A9B4-40792F6C88BBQ28592823-AB1F53BC-3E3E-4518-9ECD-434E416E657BQ29619405-E1AD5AF8-8703-46E4-A223-45CCA463C540
P2860
Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Structural basis for FEN-1 sub ...... in DNA replication and repair
@ast
Structural basis for FEN-1 sub ...... in DNA replication and repair
@en
Structural basis for FEN-1 sub ...... in DNA replication and repair
@nl
type
label
Structural basis for FEN-1 sub ...... in DNA replication and repair
@ast
Structural basis for FEN-1 sub ...... in DNA replication and repair
@en
Structural basis for FEN-1 sub ...... in DNA replication and repair
@nl
prefLabel
Structural basis for FEN-1 sub ...... in DNA replication and repair
@ast
Structural basis for FEN-1 sub ...... in DNA replication and repair
@en
Structural basis for FEN-1 sub ...... in DNA replication and repair
@nl
P2093
P3181
P1433
P1476
Structural basis for FEN-1 sub ...... in DNA replication and repair
@en
P2093
Biana Yelent
Binghui Shen
Brian R Chapados
David J Hosfield
John A Tainer
Junzhuan Qiu
Seungil Han
P3181
P356
10.1016/S0092-8674(03)01036-5
P407
P577
2004-01-09T00:00:00Z