Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity. - Wikidata - awgldk - TriplyDB

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

http://www.wikidata.org/entity/Q37700587

about

Influence of XPB helicase on recruitment and redistribution of nucleotide excision repair proteins at sites of UV-induced DNA damage Skin cancer in organ transplant recipients: effects of immunosuppressive medications on DNA repair Structure of the C-terminal half of human XPB helicase and the impact of the disease-causing mutation XP11BE Transcriptional and Posttranslational Regulation of Nucleotide Excision Repair: The Guardian of the Genome against Ultraviolet Radiation Phosphorylation of nucleotide excision repair factor xeroderma pigmentosum group A by ataxia telangiectasia mutated and Rad3-related-dependent checkpoint pathway promotes cell survival in response to UV irradiation.Sequential recruitment of the repair factors during NER: the role of XPG in initiating the resynthesis step.A unified model for the molecular basis of Xeroderma pigmentosum-Cockayne Syndrome.Other proteins interacting with XP proteins.The oncogenic phosphatase WIP1 negatively regulates nucleotide excision repair Newly identified CHO ERCC3/XPB mutations and phenotype characterization.Cyclosporin A inhibits nucleotide excision repair via downregulation of the xeroderma pigmentosum group A and G proteins, which is mediated by calcineurin inhibition.Multiple DNA binding domains mediate the function of the ERCC1-XPF protein in nucleotide excision repair.Control of the function of the transcription and repair factor TFIIH by the action of the cochaperone Ydj1.Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair.Telomere attrition and genomic instability in xeroderma pigmentosum type-b deficient fibroblasts under oxidative stress Molecular insights into the recruitment of TFIIH to sites of DNA damage Human JC virus small tumour antigen inhibits nucleotide excision repair and sensitises cells to DNA-damaging agents.Recruitment of the nucleotide excision repair endonuclease XPG to sites of UV-induced dna damage depends on functional TFIIH.Cyclosporin A, but not everolimus, inhibits DNA repair mediated by calcineurin: implications for tumorigenesis under immunosuppression.Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition.Single-stranded DNA binding activity of XPBI, but not XPBII, from Sulfolobus tokodaii causes double-stranded DNA melting.The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity.Phosphorylation of xeroderma pigmentosum group C regulates ultraviolet-induced DNA damage repair.

P2860

Q24306173-12F74917-C720-4CE3-AF55-6B84AAE7BD70 Q26822549-7C1A4A08-4E05-4290-9D3F-26E7EECADC6E Q27683946-4D2A647A-8072-44FF-96E8-5D8E8CB96A0B Q28070128-4A6890FD-6E49-485B-A7A9-9E81D3537196 Q33236676-A0E56F61-F8D7-4B2A-A83B-69C758C57ED9 Q33310274-6B6FF79C-B6A4-4156-8FEF-43F0A1CCE0A5 Q33361700-5D5382B9-E3F9-4798-A8C5-C1F63FCD5812 Q33404215-F68BFFC8-A127-4FB6-84AD-C75B6AE7D417 Q33572384-187D597F-95DD-411F-BC7B-3B86ABF293DE Q33672978-7CFE881D-AD7E-4FCB-B04E-D300D529C42F Q33943659-A70DC4B9-02FF-42AC-87C4-57BB952FAF2B Q34252316-614E2B5F-AFD0-4165-BEB3-99A5B165B436 Q35217152-BEED757E-80A1-4F27-8404-3348831D6892 Q35865533-8B1C0DEC-F847-46D6-861F-9A52DCD76D32 Q37335006-749EF755-D8A9-405D-8740-20B1F90D4B86 Q37383019-F7E4FC8C-4A7B-44DA-9039-ACB4F68190B9 Q38903158-F37BDA65-197A-4142-A65C-5B8AE575EA7C Q39127506-5341C9AD-E2B6-4842-9EED-424747931CAD Q39591754-4365F7D5-08C1-4B66-A284-D886BE9CF1AB Q41376744-EA51E337-7803-409D-9211-221B0E73AE94 Q43029877-6DF1DCC3-FEA8-46AD-A117-92797AE419E1 Q45345104-586AEA47-87B1-425D-8E76-12ECDCB3D35F Q52585806-FBF4B201-9933-4EED-BF6C-EBD8FC661D8F

P2860

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

http://www.wikidata.org/entity/Q37700587

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh

2004年學術文章

@zh-hant

name

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

@en

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

@nl

type

label

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

@en

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

@nl

prefLabel

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

@en

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

@nl

P1433

Q37700587-830D06DC-4D4A-443A-9DF1-F56BD1A68981

P1476

Q37700587-29861F19-497E-43DE-BF07-A590F417AA64

P2093

Q37700587-0754D02B-7BF9-4C58-8AB4-6D3C02865EC5

Q37700587-33FB5FAE-C8C0-4A9A-9F2D-033D5F7C713E

Q37700587-8BC1C5DD-CE03-4941-8247-C14B097E2234

Q37700587-B064F60F-5FF0-413E-BAC9-BCC1A47700A1

Q37700587-DACE72F8-44DB-4533-B5D3-D75F7995C850

Q37700587-F2E20AFD-E98D-4D3A-97C1-2C3B6E981F3F

P2860

Q37700587-04B3E138-C846-45C6-92A3-A72FA4957D6F

Q37700587-06AF77FA-3453-4A17-958F-D8988B65335C

Q37700587-0AAAAFDD-634C-452D-BFAA-C96E2D82A6AB

Q37700587-0F402849-687B-4E18-8814-E0D7F2890C0D

Q37700587-166FF4C8-4F96-41E0-9C93-D6634F1746FC

Q37700587-1E1A9B5E-69F3-4927-9861-E65408201365

Q37700587-2197E00D-6F86-48D5-8631-150190543AA8

Q37700587-26B20DCB-E3CB-4201-A2F6-C29B8BC79CA6

Q37700587-2785AAE3-9FAC-4D21-B6DF-35EFA6493817

Q37700587-2B037FFB-24CD-4D5B-B706-B6ABD53088F8

P304

Q37700587-6AEFB33B-1F81-4788-A627-D9A048D2D62C

P31

Q37700587-66C51C7A-1F25-451B-A400-B275C2D4E7F1

P356

Q37700587-AED01A5B-4073-4991-A894-F15B171B07A5

P407

Q37700587-D82DD238-FCEF-4044-9E1D-E2B573904EB5

P433

Q37700587-5679D706-00E4-47B3-931C-24C9A489BA64

P478

Q37700587-8434CE65-8920-4E07-BB7A-F6E2F0724B65

P577

Q37700587-FE040047-F38D-4FAA-9591-9B2697336DE5

P5875

Q37700587-0185B920-54F1-49B8-920D-B1EE74A20A67

P698

Q37700587-A18568D5-454A-47DD-9D5F-1C09356CC426

P921

Q37700587-F14C665D-CDB7-48F0-9C06-C2F4A0C91B11

P932

Q37700587-015C3321-2892-4298-8795-12BD3DBB3044

P356

SJ.EMBOJ.7600480

P1433

The EMBO Journal

P1476

Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity.

@en

P2093

Angel Tapias

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

Frédéric Coin

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

Jean-Marc Egly

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

Jérome Auriol

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

Pascale Clivio

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

Wim Vermeulen

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

P2860

A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders xeroderma pigmentosum and Cockayne's syndrome

Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair

Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH

XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair

A 3' --> 5' XPB helicase defect in repair/transcription factor TFIIH of xeroderma pigmentosum group B affects both DNA repair and transcription

Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease

MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH

Molecular cloning and biological characterization of the human excision repair gene ERCC-3

Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK

A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein

P304

4835-4846

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

P31

scholarly article

P356

10.1038/SJ.EMBOJ.7600480

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

P407

P433

24

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

P478

23

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

P577

2004-11-18T00:00:00Z

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

P5875

8178362

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

P698

15549133

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

P921

phosphorylation

P932

535092

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