Ku heterodimer binds to both ends of the Werner protein and functional interaction occurs at the Werner N-terminus - Wikidata - awgldk - TriplyDB

Ku heterodimer binds to both ends of the Werner protein and functional interaction occurs at the Werner N-terminus

Ku heterodimer binds to both ends of the Werner protein and functional interaction occurs at the Werner N-terminus

http://www.wikidata.org/entity/Q24538401

about

APLF promotes the assembly and activity of non-homologous end joining protein complexes Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein A Up-regulation of WRN and DNA ligase IIIalpha in chronic myeloid leukemia: consequences for the repair of DNA double-strand breaks Roles of Werner syndrome protein in protection of genome integrity Model of human aging: recent findings on Werner's and Hutchinson-Gilford progeria syndromes The role of RecQ helicases in non-homologous end-joining DNA-PK: a dynamic enzyme in a versatile DSB repair pathway Nucleolin inhibits G4 oligonucleotide unwinding by Werner helicase RecQ helicases in DNA double strand break repair and telomere maintenance.Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8.Nonhomologous end joining: a good solution for bad ends Characterization of the DNA-unwinding activity of human RECQ1, a helicase specifically stimulated by human replication protein A.RECQ helicase RECQL4 participates in non-homologous end joining and interacts with the Ku complex Suppression of gross chromosomal rearrangements by yKu70-yKu80 heterodimer through DNA damage checkpoints.Non-homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair process.Human RECQ1 interacts with Ku70/80 and modulates DNA end-joining of double-strand breaks Mismatch-repair protein MSH6 is associated with Ku70 and regulates DNA double-strand break repair.Identification and functional characterization of a Ku-binding motif in aprataxin polynucleotide kinase/phosphatase-like factor (APLF)RecQ helicases: suppressors of tumorigenesis and premature aging.The role of the non-homologous end-joining pathway in lymphocyte development.Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair.Depletion of WRN protein causes RACK1 to activate several protein kinase C isoforms Human RecQ helicases in DNA repair, recombination, and replication.DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities.A new phosphorylated form of Ku70 identified in resistant leukemic cells confers fast but unfaithful DNA repair in cancer cell lines.Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability RECQ helicases are deregulated in hematological malignancies in association with a prognostic value WRN Exonuclease activity is blocked by specific oxidatively induced base lesions positioned in either DNA strand.Werner syndrome protein, WRN, protects cells from DNA damage induced by the benzene metabolite hydroquinone DNA double strand break repair via non-homologous end-joining.Poly(ADP-ribose) polymerase 1 regulates both the exonuclease and helicase activities of the Werner syndrome protein.Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining.Serines 440 and 467 in the Werner syndrome protein are phosphorylated by DNA-PK and affects its dynamics in response to DNA double strand breaks Different non-synonymous polymorphisms modulate the interaction of the WRN protein to its protein partners and its enzymatic activities.RecQ helicases; at the crossroad of genome replication, repair, and recombination.Detection and repair of ionizing radiation-induced DNA double strand breaks: new developments in nonhomologous end joining.The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins.Divergent cellular phenotypes of human and mouse cells lacking the Werner syndrome RecQ helicase.Depletion of Werner helicase results in mitotic hyperrecombination and pleiotropic homologous and nonhomologous recombination phenotypes.

P2860

Q24304501-F8DEEF76-79E5-41A4-BB75-F32069072734 Q24563590-ABACB274-45D4-41D4-8D12-EF705BBC3220 Q24619366-F955A01B-CD7A-49BF-BE97-3A446C80DAEB Q24643050-8B04149E-8785-47A3-A1EA-D4B717C3733C Q24644033-373CA870-5DA7-4B68-9C2B-54C766F3697B Q26829119-87CA7D0F-F8AF-42D1-9012-2560BB0063D7 Q26866928-CD9DEEC6-F098-49CC-8051-A070D0B48B88 Q27304621-3D4FF19B-B545-4DB5-B191-7AFD0CBD2AA3 Q27692685-C0F8450A-68D2-4E75-96B0-3F6BDB01338A Q28486710-B3FCBB57-C219-4612-837D-E1EBEA10ACD7 Q33202888-C1CB787C-C471-41F2-8145-B8903480B61E Q33625010-228F3A6B-AC18-435A-B4B5-4B9ADFE998C3 Q34158015-493F10A2-1167-4638-9B86-B2ACA2B991F3 Q34425537-64781CC7-1ED8-45BF-84DD-42124C6F17FC Q34478480-356A6CAB-CF30-4D07-BE19-FE94D3DA92D2 Q34550224-808DC5FD-2012-460E-865A-42A5FB0A8964 Q34708378-07A81C92-A4DF-4AAC-BE0A-C2DC0F69F5BD Q34723491-BB74796F-C2A1-4D2A-9FFC-8564B197C4A6 Q34729427-6EFD514B-5990-48EF-B6F2-5CDC3C9C5403 Q35152970-B9B0F013-424B-4549-857D-B05735571030 Q35830410-DFE62C1B-30C4-42E3-981A-0BFD1F47C4E0 Q35865533-8A80A4F7-B475-4D7F-9213-B4A4CAE4572A Q36100863-FD19B0FB-15DF-42CA-B875-5BCBB28BE792 Q36101160-91C261AA-AE89-4649-AB7B-E143FE76742C Q36132407-0F7F4CD1-318A-4E6A-8018-69E44F18E054 Q36413959-6300050C-251F-4315-86B2-929C03800D05 Q36573932-861D60FC-ABF7-481B-BD40-D84BB1EB4F28 Q36577713-58D41018-DFCB-460D-B6CF-119E0EE0D1E5 Q36859249-203FE74C-0396-40D1-8D08-DB23596F0596 Q37091544-ED0770B6-590F-46CC-B3FF-F96541770CA5 Q37135926-3D1BC4D9-B177-4105-BF85-3A1995150F50 Q37346311-FDFDB0DA-3427-4F14-AD59-3B3E7BE3C961 Q37365625-135AC016-25CD-4334-BA5C-5EC9487B4450 Q37590850-7FB3115A-75D1-4CC8-8B4A-4687D793C879 Q37699107-A7257867-88D5-4F38-BFAD-8A01FDE8882D Q37938856-9E71F6BF-12C7-4B60-8B05-A57C3E9E7951 Q38083939-6283CFFB-C31C-48F3-9E7B-D5F4383F92AE Q40150704-19AAEEB7-29C6-408E-8E90-3B6FE5C8A308 Q42130385-4BFF97EE-7862-4DE4-BFBC-35FE1B992180 Q42199897-0003A992-B995-4FEA-B6A4-A875E07B9B98

P2860

Ku heterodimer binds to both ends of the Werner protein and functional interaction occurs at the Werner N-terminus

http://www.wikidata.org/entity/Q24538401

description

2002 nî lūn-bûn

@nan

2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@ast

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@en

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@nl

type

label

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@ast

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@en

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@nl

prefLabel

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@ast

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@en

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@nl

P1433

Q24538401-37936C3D-AC5E-45D3-BEDB-A62DE542CCF4

P1476

Q24538401-0299AEA5-2DC3-4EAC-A41F-5C7BF2CA58FE

P2093

Q24538401-4F22315B-48A1-42C2-907E-14C9C8D3A050

Q24538401-5161C492-D101-4A1E-A3C7-67DE9AD565C4

Q24538401-9C04EBEB-866C-4D8D-8A48-C77B13067524

Q24538401-A14D58C2-6B1C-412C-A5BF-C85011D03AAB

P2860

Q24538401-10259322-3554-4037-BFE2-CF52E0DCEE31

Q24538401-22949856-FAAA-47F6-A6F7-0B9E80AEFE37

Q24538401-282FF0CA-C6DE-43FF-B2B5-52E4DB6293E7

Q24538401-2B5784F4-83EA-4A83-BE31-F6DA62BA3501

Q24538401-2C563BA1-F553-4888-986D-48DA0302A9F5

Q24538401-4D6ECA7B-392B-4F01-9589-06DB5C2EC197

Q24538401-4EE5F7E8-E151-4F3C-9F8C-C315C30CD521

Q24538401-5253CE3A-9CD8-4616-98FD-7BDC7D7CC511

Q24538401-5282879F-EDF5-4E34-9EFD-A07D6523612C

Q24538401-5A20CB84-D2FC-4270-B025-24617509A02F

P304

Q24538401-B0288B20-FE9B-4DF6-A2E8-468D010D087F

P31

Q24538401-E132CD3B-275D-4757-9C1B-382C20BC7E01

P3181

Q24538401-5B97C5C0-05D0-4BD3-8B50-DF041DC23378

P356

Q24538401-4F33AAFA-0891-4EA4-84D2-8263738E28DC

P407

Q24538401-BCEE3593-D8CA-44AA-96E8-BE198042D684

P433

Q24538401-74EFF9F9-0A64-41C8-8D8B-03EBF7A322DA

P478

Q24538401-FEF6508F-73C9-4DFF-93FD-E92613755210

P577

Q24538401-BB02B51A-8038-400B-A57B-48A277A88C26

P5875

Q24538401-1831897D-FAB9-4FF6-8ACA-D45DC71A063F

P698

Q24538401-0694B6AA-F2FF-43D3-8B36-08638771FE80

P932

Q24538401-7ED1D909-516D-4BE3-ACF2-47BBE3633590

P3181

P356

P1433

Nucleic Acids Research

P1476

Ku heterodimer binds to both e ...... ccurs at the Werner N-terminus

@en

P2093

Carey M Snowden

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

Dale A Ramsden

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

Parimal Karmakar

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

Vilhelm A Bohr

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

P2860

Functional and physical interaction between WRN helicase and human replication protein A

Ku is associated with the telomere in mammals

Ku complex interacts with and stimulates the Werner protein

Replication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activity

A functional interaction of Ku with Werner exonuclease facilitates digestion of damaged DNA

p53 Modulates the exonuclease activity of Werner syndrome protein

Werner syndrome protein interacts with human flap endonuclease 1 and stimulates its cleavage activity

Mapping of protein-protein interactions within the DNA-dependent protein kinase complex

Ku recruits the XRCC4-ligase IV complex to DNA ends

The C terminus of Ku80 activates the DNA-dependent protein kinase catalytic subunit

P304

3583-91

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

P31

scholarly article

P3181

2393496

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

P356

10.1093/NAR/GKF482

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

P407

P433

16

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

P478

30

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

P577

2002-08-15T00:00:00Z

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

P5875

279869851

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

P698

12177300

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

P932

134248

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