The DNA-protein interaction modes of FEN-1 with gap substrates and their implication in preventing duplication mutations.
about
Human MUS81 complexes stimulate flap endonuclease 1The 3'-flap pocket of human flap endonuclease 1 is critical for substrate binding and catalysisNucleases in homologous recombination as targets for cancer therapyDouble strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamilyDirect observation of DNA threading in flap endonuclease complexesPartial reconstitution of DNA large loop repair with purified proteins from Saccharomyces cerevisiaeDna2 is a structure-specific nuclease, with affinity for 5'-flap intermediates.Comprehensive classification of the PIN domain-like superfamilyThe FEN1 E359K germline mutation disrupts the FEN1-WRN interaction and FEN1 GEN activity, causing aneuploidy-associated cancers.Functional regulation of FEN1 nuclease and its link to cancerDevelopment of a high-throughput fluorescence polarization DNA cleavage assay for the identification of FEN1 inhibitors.A cryptic targeting signal creates a mitochondrial FEN1 isoform with tailed R-Loop binding properties.Human Fanconi anemia complementation group a protein stimulates the 5' flap endonuclease activity of FEN1.Comparison of the catalytic parameters and reaction specificities of a phage and an archaeal flap endonucleaseMechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stabilityNucleolar localization and dynamic roles of flap endonuclease 1 in ribosomal DNA replication and damage repair.Removal of oxidative DNA damage via FEN1-dependent long-patch base excision repair in human cell mitochondria.Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1PCNA stimulates catalysis by structure-specific nucleases using two distinct mechanisms: substrate targeting and catalytic step.Comprehensive mapping of the C-terminus of flap endonuclease-1 reveals distinct interaction sites for five proteins that represent different DNA replication and repair pathwaysSaccharomyces cerevisiae Mus81-Mms4 is a catalytic, DNA structure-selective endonuclease.Identification of human flap endonuclease 1 (FEN1) inhibitors using a machine learning based consensus virtual screening.Human replication factor C stimulates flap endonuclease 1FEN1 ensures telomere stability by facilitating replication fork re-initiationDmGEN shows a flap endonuclease activity, cleaving the blocked-flap structure and model replication fork.
P2860
Q24318451-162A8671-6ED5-4BBF-87C5-668956051184Q24658277-61564783-4F2C-43A3-B919-DA01B4A0B2A1Q26822478-D10C1271-9684-46A8-9828-843FD507707DQ26850039-0B429502-4342-46E7-B482-686C65A67F9EQ30783276-234C6101-07D9-4E91-AD9F-FE9863BAFD10Q33351867-277D02A4-ABAB-4D4E-96EF-FBA921054DDAQ33633735-E317A638-A588-4723-9F1D-BA8DF1FC1E68Q33878209-8A74DBF5-39C1-44EF-AC34-EFFE070385E5Q34161115-8AD26D1F-45B1-4CCF-A61B-4AABB2472102Q34559690-0178EB04-A329-4D60-9CDD-D9DE0EFF90E5Q34593788-74DCDA83-9B4C-4131-A254-E97B78A8A756Q34722618-4ED3AF55-F3A9-47BB-AAD5-C8EF1CBAA566Q35070427-865DEDFE-0E1A-4F5F-BC0A-FE251E8372A3Q36011996-D4E33F34-47F6-42A6-B72A-1A33B10F861EQ36573932-2BF07C02-4301-473A-AFFC-91EED867143EQ36748151-0843CEB9-E5C6-4CC4-B21B-FCC3401126E0Q36845992-98DFBCAB-82F8-42FE-81E4-33993DC392CBQ36914462-C1FB8F60-2866-4650-BBD8-615087DA8BE7Q36986746-54E54CAF-B58E-4C09-9C43-BD86C007F3B2Q37188352-15BACEB4-513D-47E0-8D2C-9AAD16BA2D50Q38293464-C54FC284-5343-4C52-A874-E5D530FA7BEEQ38689827-EE914D9F-26ED-42F1-9108-38606FE18AC9Q41809029-2ADF8195-FB5C-4D4B-BC7B-25B234853BBBQ42043800-CDF42A52-0516-440D-8D58-B97E0A323875Q47070570-8D083856-DEC2-4AB6-B3C9-01131B301FB4
P2860
The DNA-protein interaction modes of FEN-1 with gap substrates and their implication in preventing duplication mutations.
description
2006 nî lūn-bûn
@nan
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին 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 DNA-protein interaction mo ...... venting duplication mutations.
@ast
The DNA-protein interaction mo ...... venting duplication mutations.
@en
The DNA-protein interaction mo ...... venting duplication mutations.
@nl
type
label
The DNA-protein interaction mo ...... venting duplication mutations.
@ast
The DNA-protein interaction mo ...... venting duplication mutations.
@en
The DNA-protein interaction mo ...... venting duplication mutations.
@nl
prefLabel
The DNA-protein interaction mo ...... venting duplication mutations.
@ast
The DNA-protein interaction mo ...... venting duplication mutations.
@en
The DNA-protein interaction mo ...... venting duplication mutations.
@nl
P2093
P2860
P356
P1476
The DNA-protein interaction mo ...... eventing duplication mutations
@en
P2093
Binghui Shen
Junzhuan Qiu
P2860
P304
P356
10.1093/NAR/GKL106
P407
P577
2006-03-31T00:00:00Z