Role of double-stranded DNA translocase activity of human HLTF in replication of damaged DNA - Test2 - elhamkhani - TriplyDB

Role of double-stranded DNA translocase activity of human HLTF in replication of damaged DNA

Role of double-stranded DNA translocase activity of human HLTF in replication of damaged DNA

http://www.wikidata.org/entity/Q33614018

about

ZRANB3 is a structure-specific ATP-dependent endonuclease involved in replication stress response The Regulation of DNA Damage Tolerance by Ubiquitin and Ubiquitin-Like Modifiers Helicase-like transcription factor (Hltf) regulates G2/M transition, Wt1/Gata4/Hif-1a cardiac transcription networks, and collagen biogenesis A structure-specific nucleic acid-binding domain conserved among DNA repair proteins The DNA Damage Response: Making It Safe to Play with Knives Replication stress: getting back on track DNA damage-specific deubiquitination regulates Rad18 functions to suppress mutagenesis Characterization of human Spartan/C1orf124, an ubiquitin-PCNA interacting regulator of DNA damage tolerance SHPRH and HLTF act in a damage-specific manner to coordinate different forms of postreplication repair and prevent mutagenesis.Human HLTF mediates postreplication repair by its HIRAN domain-dependent replication fork remodelling.Structure of a Novel DNA-binding Domain of Helicase-like Transcription Factor (HLTF) and Its Functional Implication in DNA Damage Tolerance Helicase-like transcription factor: a new marker of well-differentiated thyroid cancers.Identification of a Substrate Recognition Domain in the Replication Stress Response Protein Zinc Finger Ran-binding Domain-containing Protein 3 (ZRANB3).Coordinated protein and DNA remodeling by human HLTF on stalled replication fork Human HEL308 localizes to damaged replication forks and unwinds lagging strand structures Two replication fork maintenance pathways fuse inverted repeats to rearrange chromosomes Identification of novel DNA-damage tolerance genes reveals regulation of translesion DNA synthesis by nucleophosmin.Cooperation of RAD51 and RAD54 in regression of a model replication fork.Role of helicase-like transcription factor (hltf) in the G2/m transition and apoptosis in brain.Branching out with DNA helicases.Rad51-mediated replication fork reversal is a global response to genotoxic treatments in human cells.Clearance of roadblocks in replication fork restart.A genome-wide association study identifies a region at chromosome 12 as a potential susceptibility locus for restenosis after percutaneous coronary intervention Functional analysis of DNA replication fork reversal catalyzed by Mycobacterium tuberculosis RuvAB proteins.HLTF's Ancient HIRAN Domain Binds 3' DNA Ends to Drive Replication Fork Reversal.Protein degradation pathways regulate the functions of helicases in the DNA damage response and maintenance of genomic stability DNA damage tolerance pathway involving DNA polymerase ι and the tumor suppressor p53 regulates DNA replication fork progression.A Novel Rrm3 Function in Restricting DNA Replication via an Orc5-Binding Domain Is Genetically Separable from Rrm3 Function as an ATPase/Helicase in Facilitating Fork Progression.SMARCAL1 maintains telomere integrity during DNA replication.Genomic assay reveals tolerance of DNA damage by both translesion DNA synthesis and homology-dependent repair in mammalian cells.The PCNA-associated protein PARI negatively regulates homologous recombination via the inhibition of DNA repair synthesis.HIV-1 Vpr degrades the HLTF DNA translocase in T cells and macrophages.Replicating damaged DNA in eukaryotes.Active Control of Repetitive Structural Transitions between Replication Forks and Holliday Junctions by Werner Syndrome Helicase.Strand invasion by HLTF as a mechanism for template switch in fork rescue.Risks at the DNA Replication Fork: Effects upon Carcinogenesis and Tumor Heterogeneity The Intra-S Checkpoint Responses to DNA Damage.Bending Forks and Wagging Dogs--It's about the DNA 3' Tail.Replication fork dynamics and the DNA damage response.Resolving branched DNA intermediates with structure-specific nucleases during replication in eukaryotes.

P2860

Q24339475-E2C27C2D-9260-443C-9977-2363E5845D83 Q26744520-49B4409A-1996-4F13-BE69-C8262D27E8BE Q27301898-1DA6BC1E-57B0-4EC1-B9E2-FD56ADF4B36E Q27683756-E6B690D5-B487-4A7F-BE7E-163EDBDA2F33 Q27861055-51BC8A74-C748-4144-A11E-192482DE6B3A Q28067138-2D706CF1-34B6-47DE-8FCA-CB9804AEA446 Q28119166-F5788B13-3123-4B79-9C21-E6C9829D5EA8 Q28275269-FC8948B5-43A6-4031-AFBE-362229384C8C Q29871514-E83B9294-B9B7-471D-AE1A-535002D25BF3 Q29871515-44B25039-F35F-490B-B7C5-256E968BD039 Q30373537-968D16B1-9323-4350-886E-44C8C3AFDE37 Q30434300-93F7D1DB-4F8C-4F86-8E00-40C6B8FF053F Q33629544-F2772DE0-B097-4310-BDF0-31E5D85AD4A2 Q33973384-58477695-D896-4C91-ADF9-EF6145746EBF Q34170371-960D805D-E076-4BCE-8E9D-28C47D2DED3D Q34369330-79B7A0AC-182B-47A4-B8F4-C8972EFA8164 Q34679192-B90BA984-FCBC-4EC7-B029-9B5FDE8C7B5D Q34723611-1E573C96-6CEA-4312-92F3-FB2110F4FBDD Q34796010-1AE09CBE-C253-4F19-B37A-E2CF7D0C1C60 Q34816098-18D00F45-FAFF-4B49-84C1-508555CAF102 Q35141185-27A0AFEF-AC81-4D28-A67C-8DE9B2B96FDF Q35180818-6AE8D63D-80DF-47DD-BFE7-7621CE5D686C Q35532916-20A7B33A-21C9-4B1E-9C4A-2AD383D17994 Q35668778-464B7A28-E32A-44A2-8A8D-B67DC4862F5F Q35762843-14E57CF6-08FD-4FAA-915A-A56AD72E9908 Q35833998-0F46FA5F-41B0-4972-946E-544E7CC11E82 Q36074455-E8EF7E02-D235-49D1-AA29-288686178455 Q36214221-17631B8E-F13D-40D9-9FA6-3879E3183FAE Q36354812-7DAC01F2-BFBA-4528-B2EC-2A6F3BC19E6B Q36781920-CD30EB8B-1CF3-4850-9B33-936D67EE4331 Q36817937-1F66FD32-358C-4E90-9AD5-C73333093062 Q36904912-0B0EE8D6-53EB-4362-9819-A388138C428E Q37340387-43D3E13F-1E62-4364-9A9F-44A77B8F4B24 Q37515731-2F5D4895-6480-4F90-AC08-9AD67A16CC39 Q37574250-480A4A79-CB32-4896-AD28-4D3AEDA5A499 Q37628288-082AB689-5FFB-4F70-BB22-D0B323A73C64 Q37676255-90E27DA3-6F68-40C9-B230-1B7F3AA09DD5 Q37708501-F4562764-3390-4CDD-90DA-AEDDDD233CA5 Q37993652-FA1F7A88-BCDD-4EA0-A3E9-150279709158 Q38134624-C1BD3C49-28A6-4B6B-AFB4-D17B38E1AAA1

P2860

Role of double-stranded DNA translocase activity of human HLTF in replication of damaged DNA

http://www.wikidata.org/entity/Q33614018

description

2009 nî lūn-bûn

@nan

2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Role of double-stranded DNA tr ...... in replication of damaged DNA

@ast

Role of double-stranded DNA tr ...... in replication of damaged DNA

@en

type

label

Role of double-stranded DNA tr ...... in replication of damaged DNA

@ast

Role of double-stranded DNA tr ...... in replication of damaged DNA

@en

prefLabel

Role of double-stranded DNA tr ...... in replication of damaged DNA

@ast

Role of double-stranded DNA tr ...... in replication of damaged DNA

@en

P1433

Q33614018-46A05796-E3B8-48D2-B6A6-DD7EE5C1C626

P1476

Q33614018-186AE5A2-3AC3-4E07-BD5A-9EF23D57D2F2

P2093

Q33614018-05ED1258-715B-4591-AC9E-3E5781396480

Q33614018-5EB0F8FE-5D5C-44F4-B9F3-FA00086AC670

Q33614018-BDD99E75-C48E-4903-9110-49D4586E62B4

Q33614018-C033DCA9-6F1C-4370-AEC3-885C9BD575B6

P2860

Q33614018-0621B0E2-F362-4590-B633-6C4D188629FC

Q33614018-1010EB63-FB9B-4755-A0AF-B45E90F2154E

Q33614018-1AC3662B-8D35-49D8-BF47-C27E66893847

Q33614018-2AA30BE8-7E80-46F6-8D88-A4253D3D31E7

Q33614018-2B058F06-665A-4F7B-B13A-E8DAE5B841E5

Q33614018-2B8E1BDC-2839-411D-92B8-2904BE50DF74

Q33614018-3086ACFE-CE0A-4611-94C3-5CED50445295

Q33614018-32339042-54ED-4B03-B80A-5CAF14D1BEE0

Q33614018-3A22B55A-ED40-4C0A-8FC5-2CF05C67E1D3

Q33614018-3AF7E52B-2F43-4054-AC45-BEB3AAEF1C3A

P304

Q33614018-3A84C306-B8C0-440F-948E-37692A7C5B65

P31

Q33614018-CF364756-B824-4F78-AF11-17A7839F9E98

P356

Q33614018-DD5EE1D2-945E-4993-9C59-BD8910837F9F

P407

Q33614018-A977942A-B271-40B1-9051-010D91BCCF49

P433

Q33614018-DE1EECC6-2912-4F44-8517-1BCD41854910

P478

Q33614018-6532039A-7F33-4DFF-9655-EA48E2FBCFAF

P577

Q33614018-18C3BF9B-9E4B-47F0-97D3-7E0F1D42BA4E

P5875

Q33614018-EEE2E673-24ED-46E7-A89B-7B38218963B9

P698

Q33614018-4E19CFF0-DACA-41E4-8B84-E06C5DDDE884

P932

Q33614018-7AF00883-3221-4F5C-8BE2-0562E369542F

P356

P1433

Molecular and Cellular Biology

P1476

Role of double-stranded DNA tr ...... in replication of damaged DNA

@en

P2093

András Blastyák

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

Ildikó Hajdú

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

Ildikó Unk

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

Lajos Haracska

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

P2860

Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen

Cloning of an SNF2/SWI2-related protein that binds specifically to the SPH motifs of the SV40 enhancer and to the HIV-1 promoter

HLTF gene silencing in human colon cancer.

Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks

Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination

A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M

Human cancers express a mutator phenotype

Human RECQ5beta helicase promotes strand exchange on synthetic DNA structures resembling a stalled replication fork

Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination

Structural analysis of DNA replication fork reversal by RecG

P304

684-693

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

P31

scholarly article

P356

10.1128/MCB.00863-09

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

P407

P433

3

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

P478

30

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

P577

2009-11-30T00:00:00Z

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

P5875

40041984

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

P698

19948885

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

P932

2812231

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