Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading - Wikidata - awgldk - TriplyDB

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

http://www.wikidata.org/entity/Q34251375

about

Biochemical analyses indicate that binding and cleavage specificities define the ordered processing of human Okazaki fragments by Dna2 and FEN1 Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases Differential interaction kinetics of a bipolar structure-specific endonuclease with DNA flaps revealed by single-molecule imaging Human Flap Endonuclease Structures, DNA Double-Base Flipping, and a Unified Understanding of the FEN1 Superfamily Structures of Human Exonuclease 1 DNA Complexes Suggest a Unified Mechanism for Nuclease Family Direct observation of DNA threading in flap endonuclease complexes Phosphate steering by Flap Endonuclease 1 promotes 5'-flap specificity and incision to prevent genome instability.Complementary non-radioactive assays for investigation of human flap endonuclease 1 activity.Eukaryotic lagging strand DNA replication employs a multi-pathway mechanism that protects genome integrity A cryptic targeting signal creates a mitochondrial FEN1 isoform with tailed R-Loop binding properties.Rate-determining Step of Flap Endonuclease 1 (FEN1) Reflects a Kinetic Bias against Long Flaps and Trinucleotide Repeat Sequences.Flap endonucleases pass 5'-flaps through a flexible arch using a disorder-thread-order mechanism to confer specificity for free 5'-ends.Human exonuclease 1 (EXO1) activity characterization and its function on flap structures.Msh2-Msh3 interferes with Okazaki fragment processing to promote trinucleotide repeat expansions.Okazaki fragment metabolism.Flap endonuclease 1.The wonders of flap endonucleases: structure, function, mechanism and regulation.Flap endonuclease activity of gene 6 exonuclease of bacteriophage T7.Single-molecule FRET unveils induced-fit mechanism for substrate selectivity in flap endonuclease 1.DNA and Protein Requirements for Substrate Conformational Changes Necessary for Human Flap Endonuclease-1-catalyzed Reaction.Single-molecule characterization of Fen1 and Fen1/PCNA complexes acting on flap substrates Flap endonuclease of bacteriophage T7: Possible roles in RNA primer removal, recombination and host DNA breakdown.Proline scanning mutagenesis reveals a role for the flap endonuclease-1 helical cap in substrate unpairing.

P2860

Q24319140-4F97A555-9383-4AED-BD61-B74BFD272EEE Q27005670-D4BB2F40-36BD-4DF7-A38E-280CBD96FAB2 Q27323947-56C41F5D-5A6A-4874-AE97-C6860C5C06E8 Q27667524-FEFB7B37-2505-44FA-8E92-5DF7C74DE4A9 Q27667527-40CF6AFA-80CA-4897-9378-EB0186B59CE7 Q30783276-7CB3DCC1-CD7A-4AFD-8FDE-0E4EC19BCE96 Q33851243-C3936437-490F-4FA7-B5DF-DB3CCD2DD201 Q34513868-10BB3115-373A-46EC-9045-6C55F175C04F Q34606035-D913DA52-A696-48F0-B16C-BA0C4B3C2E39 Q34722618-87BF6D27-65AD-4DD5-87B7-55B28B172A64 Q35978312-984E4A72-6D63-46FD-BD91-008AF8BC631F Q36044859-154B760B-755A-469E-8DC4-E29A39D82A3C Q36185175-506A06B4-045C-4443-9964-F7A4A3E72412 Q36283765-656A0BC0-EA9D-497F-ABCF-0CE5BDDECFC9 Q36555193-5E7B8AF7-8875-4226-9A32-CE555D5CBA37 Q36920133-AFADBCE3-03C7-4C89-9E38-CEE9EA3089F9 Q37058058-83794D96-76C6-464E-AA3C-FEC596E7ABC8 Q37608497-13CE6308-5D22-4962-8C66-17EB18EE66B3 Q37712232-7F294C7F-ACE1-406B-B033-0326C9F9C642 Q39971733-324E1418-7312-435A-83C2-C23B8BE5C9B3 Q41941402-80EC1C4B-41FE-4AA5-9597-2BD7BD599326 Q42016749-3BC84A8C-62DC-4FE0-B7E1-7119FBC134D6 Q42873076-C60FAB62-3E53-40CF-8561-A24655074161

P2860

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

http://www.wikidata.org/entity/Q34251375

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@ast

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@en

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@nl

type

label

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@ast

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@en

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@nl

prefLabel

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@ast

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@en

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@nl

P1433

Q34251375-3CAE3593-A0B0-4CA7-9ED2-0B5856135F5B

P1476

Q34251375-5307AE89-1B73-453A-9027-D5E5CAA6FDEC

P2093

Q34251375-9E42925B-569F-4130-966A-DEA84B9E0903

Q34251375-E44A2903-42DC-4494-ADEB-6BDFFB0F95F2

P2860

Q34251375-1560DBD2-68D8-48CD-8DDE-CA042057C8F7

Q34251375-1ABC111F-8DFC-42C1-9B8A-5938E4180374

Q34251375-214F7413-D436-42E8-BEDF-7CFC4E895E04

Q34251375-2769A388-C8DB-472F-A759-31CF1D000387

Q34251375-2901EC2C-5297-4606-B9FF-78D2F14DD8B0

Q34251375-31AA8459-616A-4F0F-9C0E-91A9CEB75278

Q34251375-41D40B64-176E-4821-9E82-0E53640C23FC

Q34251375-42235B02-4631-4CAF-86B6-9B3F308F8CC4

Q34251375-453017EF-5302-40CE-8664-24639AADEB16

Q34251375-488993A1-7648-4CAC-9A2D-1E7F1FFA35A4

P304

Q34251375-7960E85E-BCF7-46EA-9415-0348C6728168

P31

Q34251375-0E5442E6-27AF-4A7B-A3F4-BFFF1A8C1AED

P356

Q34251375-F617D4F7-F770-4FF6-8CA7-5514DE50A4D2

P407

Q34251375-2BC179B6-2C0D-41A8-AA78-2991BBED8F77

P433

Q34251375-6970D2A4-4F43-48C9-986E-E28E554627A5

P478

Q34251375-85A5AE1B-926A-4C16-9CE1-32CCF089CB19

P50

Q34251375-D71DE55A-61BD-4CC8-B3D3-5423425D5AF7

P577

Q34251375-737C4606-8874-4E00-ADAD-4F6466EC47B0

P698

Q34251375-C9935DFF-3DD4-4CA2-A0EB-89681E2BEEAB

P932

Q34251375-54664AF0-1C04-4FB2-9888-522DA7BFE03F

P356

JBC.M110.165902

P1433

Journal of Biological Chemistry

P1476

Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading

@en

P2093

Jason W Gloor

http://www.w3.org/2001/XMLSchema#string

Robert A Bambara

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity

The characterization of a mammalian DNA structure-specific endonuclease

Structural and functional homology between mammalian DNase IV and the 5'-nuclease domain of Escherichia coli DNA polymerase I

Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1).

Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex

The 3'-flap pocket of human flap endonuclease 1 is critical for substrate binding and catalysis

The interaction site of Flap Endonuclease-1 with WRN helicase suggests a coordination of WRN and PCNA

Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair

A helical arch allowing single-stranded DNA to thread through T5 5'-exonuclease

The crystal structure of flap endonuclease-1 from Methanococcus jannaschii

P304

34922-34931

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M110.165902

http://www.w3.org/2001/XMLSchema#string

P407

P433

45

http://www.w3.org/2001/XMLSchema#string

P478

285

http://www.w3.org/2001/XMLSchema#string

P50

Lata Balakrishnan

P577

2010-08-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

20739288

http://www.w3.org/2001/XMLSchema#string

P932

2966106

http://www.w3.org/2001/XMLSchema#string