Dimerization of human XPA and formation of XPA2-RPA protein complex. - sprookjes - yvandenbroek - TriplyDB

Dimerization of human XPA and formation of XPA2-RPA protein complex.

Dimerization of human XPA and formation of XPA2-RPA protein complex.

http://www.wikidata.org/entity/Q31114827

about

Nucleotide excision repair is associated with the replisome and its efficiency depends on a direct interaction between XPA and PCNA Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells Nucleotide excision repair by mutant xeroderma pigmentosum group A (XPA) proteins with deficiency in interaction with RPA Preferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damage Role of the XPA protein in the NER pathway: A perspective on the function of structural disorder in macromolecular assembly Binding of the human nucleotide excision repair proteins XPA and XPC/HR23B to the 5R-thymine glycol lesion and structure of the cis-(5R,6S) thymine glycol epimer in the 5'-GTgG-3' sequence: destabilization of two base pairs at the lesion site Structure and conformational change of a replication protein A heterotrimer bound to ssDNA Structure of (5′ S )-8,5′-Cyclo-2′-deoxyguanosine in DNA Structural Basis for Bulky-Adduct DNA-Lesion Recognition by the Nucleotide Excision Repair Protein Rad14 Biochemical analysis of DNA polymerase η fidelity in the presence of replication protein A A dynamic model for replication protein A (RPA) function in DNA processing pathways Interactions of human replication protein A with single-stranded DNA adducts.Mass spectrometric identification of lysines involved in the interaction of human replication protein a with single-stranded DNA.Cooperative interaction of human XPA stabilizes and enhances specific binding of XPA to DNA damage.Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B.Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair.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.Specific and efficient binding of xeroderma pigmentosum complementation group A to double-strand/single-strand DNA junctions with 3'- and/or 5'-ssDNA branches.Structural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Transcriptome profiling of developmental and xenobiotic responses in a keystone soil animal, the oligochaete annelid Lumbricus rubellus.Cyclosporin A inhibits nucleotide excision repair via downregulation of the xeroderma pigmentosum group A and G proteins, which is mediated by calcineurin inhibition.Replication-mediated disassociation of replication protein A-XPA complex upon DNA damage: implications for RPA handing off.DNA-PK, ATM and ATR collaboratively regulate p53-RPA interaction to facilitate homologous recombination DNA repair XPA: A key scaffold for human nucleotide excision repair.A new structural insight into XPA-DNA interactions.Structural insights into the recognition of cisplatin and AAF-dG lesion by Rad14 (XPA)Molecular mechanisms of xeroderma pigmentosum (XP) proteins.Characterization of oligomeric human half-ABC transporter ATP-binding cassette G2.Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates.Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.RPA and XPA interaction with DNA structures mimicking intermediates of the late stages in nucleotide excision repair.

P2860

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P2860

Dimerization of human XPA and formation of XPA2-RPA protein complex.

http://www.wikidata.org/entity/Q31114827

description

2002 nî lūn-bûn

@nan

2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Dimerization of human XPA and formation of XPA2-RPA protein complex.

@ast

Dimerization of human XPA and formation of XPA2-RPA protein complex.

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type

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Dimerization of human XPA and formation of XPA2-RPA protein complex.

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Dimerization of human XPA and formation of XPA2-RPA protein complex.

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prefLabel

Dimerization of human XPA and formation of XPA2-RPA protein complex.

@ast

Dimerization of human XPA and formation of XPA2-RPA protein complex.

@en

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Dimerization of human XPA and formation of XPA2-RPA protein complex.

@en

P2093

Jian-Ting Zhang

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

Leslie Y Mao

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Yang Liu

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

Yue Zou

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

Zheng-guan Yang

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

P2860

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

RPA involvement in the damage-recognition and incision steps of nucleotide excision repair

Formation of a ternary complex by human XPA, ERCC1, and ERCC4(XPF) excision repair proteins

Specific association between the human DNA repair proteins XPA and ERCC1

An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair

Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies

Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA

Three-dimensional structural views of damaged-DNA recognition: T4 endonuclease V, E. coli Vsr protein, and human nucleotide excision repair factor XPA

The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor

Enhancement of damage-specific DNA binding of XPA by interaction with the ERCC1 DNA repair protein

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13012-13020

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10.1021/BI026064Z

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