The characterization of a mammalian DNA structure-specific endonuclease
about
Werner syndrome protein interacts with human flap endonuclease 1 and stimulates its cleavage activityMolecular interactions of human Exo1 with DNAFAN1 activity on asymmetric repair intermediates is mediated by an atypical monomeric virus-type replication-repair nuclease domainMapping of interaction domains between human repair proteins ERCC1 and XPFHuman DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediatesHex1: a new human Rad2 nuclease family member with homology to yeast exonuclease 1Biochemical analyses indicate that binding and cleavage specificities define the ordered processing of human Okazaki fragments by Dna2 and FEN1Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1).Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigenIdling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replicationReconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 proteinComponents of the secondary pathway stimulate the primary pathway of eukaryotic Okazaki fragment processingAn alternative pathway for Okazaki fragment processing: resolution of fold-back flaps by Pif1 helicaseComparative genomics and molecular dynamics of DNA repeats in eukaryotesLong patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complexThe 3'-flap pocket of human flap endonuclease 1 is critical for substrate binding and catalysisA network of multi-tasking proteins at the DNA replication fork preserves genome stabilityAssociation between FEN1 Polymorphisms -69G>A and 4150G>T with Susceptibility in Human Disease: A Meta-AnalysisUnpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleasesCrystal Structure of CRN-4: Implications for Domain Function in Apoptotic DNA DegradationStructure of flap endonuclease 1 from the hyperthermophilic archaeonDesulfurococcus amylolyticusThe structure of Escherichia coli ExoIX--implications for DNA binding and catalysis in flap endonucleasesMutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease suggests separate mechanisms of endo-and exonucleolytic cleavageSaccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nucleaseThe MPH1 gene of Saccharomyces cerevisiae functions in Okazaki fragment processing.The product of the DNA damage-inducible gene of Saccharomyces cerevisiae, DIN7, specifically functions in mitochondriaAccumulation of single-stranded DNA and destabilization of telomeric repeats in yeast mutant strains carrying a deletion of RAD27.A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential functionMeiotic recombination involving heterozygous large insertions in Saccharomyces cerevisiae: formation and repair of large, unpaired DNA loopsExpression and biochemical characterization of the Plasmodium falciparum DNA repair enzyme, flap endonuclease-1 (PfFEN-1)Overexpression and hypomethylation of flap endonuclease 1 gene in breast and other cancersThe Caenorhabditis elegans homolog of Gen1/Yen1 resolvases links DNA damage signaling to DNA double-strand break repairAn evolutionarily conserved synthetic lethal interaction network identifies FEN1 as a broad-spectrum target for anticancer therapeutic developmentProliferation failure and gamma radiation sensitivity of Fen1 null mutant mice at the blastocyst stageWuho Is a New Member in Maintaining Genome Stability through its Interaction with Flap Endonuclease 1Saccharomyces cerevisiae Rrm3p DNA helicase promotes genome integrity by preventing replication fork stalling: viability of rrm3 cells requires the intra-S-phase checkpoint and fork restart activitiesA general approach to break the concentration barrier in single-molecule imaging.Pif1 helicase directs eukaryotic Okazaki fragments toward the two-nuclease cleavage pathway for primer removal.Pif1 helicase lengthens some Okazaki fragment flaps necessitating Dna2 nuclease/helicase action in the two-nuclease processing pathway.Dna2 is a structure-specific nuclease, with affinity for 5'-flap intermediates.
P2860
Q24291787-F95BA655-32CB-4BC4-AA20-BD8278B483E9Q24292290-10730569-36A5-420A-87CD-75E984D75379Q24300106-34D36D23-40CD-4BBA-B7B9-9E85314CB50AQ24309451-43C3637E-0231-46C4-BDAE-52D9C5A01480Q24312975-C1E6FD33-C5AC-43E0-8DE0-EA35545A2131Q24319085-138406D4-D69A-44D8-AD1F-FF1275DE476FQ24319140-09BC9782-D05F-4525-B34F-3ABEDBC5E182Q24532243-4EBD3B80-7CEE-456A-8138-3D9E02CDFDC8Q24533222-3B56B925-BFB3-4DD1-864A-F100968C8189Q24560006-F03BF77B-B089-4030-BE78-70858ABF9167Q24561768-6328477D-D314-44BA-91AA-8D77D4A73546Q24611034-A9944EDE-9DF2-4F1D-84EC-CD2F891B9B04Q24621929-AE3694FA-5625-47AC-A7B4-BA3561222950Q24650948-38D5B783-6534-4E17-88CE-E0DDEB307115Q24657219-0B869A93-4037-4529-9AA3-FFBD58F3C529Q24658277-D8E9707F-4CA0-4058-BBD9-DE93F5816E73Q24814638-C687422B-072E-4783-B01F-E13E3A26A186Q26774395-A134D543-FB89-4AD3-B800-28319A51C938Q27005670-7EF92C8D-12DC-4BE3-8C11-5E7367C05232Q27652750-18140EBE-DE02-4088-8C88-052839455881Q27666897-E18BB1A0-7934-463A-9C1F-C692C304E98FQ27678894-3AE18394-B913-4CF6-B78D-B77029B99552Q27766414-3B45349D-034B-4B38-BD63-CCC9DB6A0C66Q27930354-A49AEF45-E95E-4AB6-A768-1FE09FC50434Q27932411-CBB32039-6A54-403E-8857-A4541A7E1F78Q27933751-6161BE81-8E8D-4374-B490-A0915233F728Q27936665-4C0D8FF6-4C57-427D-BC33-88770C71B62CQ27937789-E25A15C8-8060-4656-941D-F7424786FCA9Q27939603-AFC43BD1-43DE-4194-8E75-AD42BE06DC3FQ27972548-FBAB8A82-73D3-4843-8A94-BDD3449AB3DFQ28300982-2AD5110E-64EF-42A9-8DA3-0FE658551D4BQ28474884-1875A51D-C460-45C6-91BD-C03136B81236Q28485395-82FF540A-4256-469D-9455-58BE25E5CC1FQ28509911-04FB3474-45D7-49DD-B98E-AF6ED8EA4FF0Q28552317-E504DDD8-72A3-44B4-9ABC-1EBC27C716B1Q28776095-D8B7377A-F678-4409-9564-43A73A44473DQ30538113-7127B4FC-1B69-44CD-AFFD-26F5E8B645F1Q33358808-BF4CD8DA-7984-4BB4-A4CF-3E0448D6FE83Q33482605-02E486A3-2E3C-44E7-90D5-3A5DF3A0154FQ33633735-5C46A15A-2945-440E-8439-E9D72C3FFC8B
P2860
The characterization of a mammalian DNA structure-specific endonuclease
description
1994 nî lūn-bûn
@nan
1994 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մարտին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The characterization of a mammalian DNA structure-specific endonuclease
@ast
The characterization of a mammalian DNA structure-specific endonuclease
@en
The characterization of a mammalian DNA structure-specific endonuclease
@en-gb
The characterization of a mammalian DNA structure-specific endonuclease
@nl
type
label
The characterization of a mammalian DNA structure-specific endonuclease
@ast
The characterization of a mammalian DNA structure-specific endonuclease
@en
The characterization of a mammalian DNA structure-specific endonuclease
@en-gb
The characterization of a mammalian DNA structure-specific endonuclease
@nl
prefLabel
The characterization of a mammalian DNA structure-specific endonuclease
@ast
The characterization of a mammalian DNA structure-specific endonuclease
@en
The characterization of a mammalian DNA structure-specific endonuclease
@en-gb
The characterization of a mammalian DNA structure-specific endonuclease
@nl
P2860
P3181
P1433
P1476
The characterization of a mammalian DNA structure-specific endonuclease
@en
P2093
J J Harrington
M R Lieber
P2860
P304
P3181
P356
10.1002/J.1460-2075.1994.TB06373.X
P407
P577
1994-03-01T00:00:00Z