Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair. - Wikidata - awgldk - TriplyDB

Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair.

Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair.

http://www.wikidata.org/entity/Q30684974

about

Nucleotide excision repair is associated with the replisome and its efficiency depends on a direct interaction between XPA and PCNA Human single-stranded DNA binding proteins are essential for maintaining genomic stability Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization Human XPC-hHR23B interacts with XPA-RPA in the recognition of triplex-directed psoralen DNA interstrand crosslinks.Global-genome Nucleotide Excision Repair Controlled by Ubiquitin/Sumo Modifiers Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation Nucleotide excision repair in eukaryotes Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA Structural Basis for Bulky-Adduct DNA-Lesion Recognition by the Nucleotide Excision Repair Protein Rad14 The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif.A dynamic model for replication protein A (RPA) function in DNA processing pathways Differential nucleotide excision repair susceptibility of bulky DNA adducts in different sequence contexts: hierarchies of recognition signals Domains in the XPA protein important in its role as a processivity factor.Quantitative analysis of the binding affinity of poly(ADP-ribose) to specific binding proteins as a function of chain length The phosphorylation domain of the 32-kDa subunit of replication protein A (RPA) modulates RPA-DNA interactions. Evidence for an intersubunit interaction.Xeroderma pigmentosum group A protein loads as a separate factor onto DNA lesions.Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease.Psoralen interstrand cross-link repair is specifically altered by an adjacent triple-stranded structure Molecular anatomy of the human excision nuclease assembled at sites of DNA damage.Interactions of human replication protein A with single-stranded DNA adducts.Dimerization of human XPA and formation of XPA2-RPA protein complex.Potentially functional variants in the core nucleotide excision repair genes predict survival in Japanese gastric cancer patients.Ordered conformational changes in damaged DNA induced by nucleotide excision repair factors.Cooperative interaction of human XPA stabilizes and enhances specific binding of XPA to DNA damage.Initiation of DNA repair mediated by a stalled RNA polymerase IIO.Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair.Specific and efficient binding of xeroderma pigmentosum complementation group A to double-strand/single-strand DNA junctions with 3'- and/or 5'-ssDNA branches.Other proteins interacting with XP proteins.Replication protein A: directing traffic at the intersection of replication and repair.Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair.Hydrogen peroxide induced genomic instability in nucleotide excision repair-deficient lymphoblastoid cells Base sequence context effects on nucleotide excision repair.Platelet-activating factor receptor agonists mediate xeroderma pigmentosum A photosensitivity.Poly(ADP-ribose)-mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function.A protein array screen for Kaposi's sarcoma-associated herpesvirus LANA interactors links LANA to TIP60, PP2A activity, and telomere shortening.Simulating structural and thermodynamic properties of carcinogen-damaged DNA.DNA repair deficiency in neurodegeneration.Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum complementation group A in nucleotide excision repair.Polymorphisms of nucleotide excision repair genes predict melanoma survival.

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Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair.

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2001 nî lūn-bûn

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2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2001 թվականի հուլիսին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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The EMBO Journal

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Double-check probing of DNA be ...... ctural function in DNA repair.

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Brabec V

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Buterin T

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Hindges R

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Hübscher U

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Kaspárková J

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Missura M

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Naegeli H

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P2860

The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA

Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites

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

Human DNA repair excision nuclease. Analysis of the roles of the subunits involved in dual incisions by using anti-XPG and anti-ERCC1 antibodies

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

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

Crystal structure of a DNA Holliday junction

Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA

Crystal structure of double-stranded DNA containing the major adduct of the anticancer drug cisplatin

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11432842

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