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Article

The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision Repair

1 Dec 2005

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 16338413
DOI: 10.1016/j.str.2005.08.014

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision RepairPMID 16338413Read ↗

Function and Interactions of ERCC1-XPF in DNA Damage ResponseSemantic proximity Read ↗

Multiple DNA binding domains mediate the function of the ERCC1-XPF protein in nucleotide excision repair.Semantic proximity Read ↗

Mapping of interaction domains between human repair proteins ERCC1 and XPFSemantic proximity Read ↗

DNA repair endonuclease ERCC1-XPF as a novel therapeutic target to overcome chemoresistance in cancer therapy.Semantic proximity Read ↗

Activity of individual ERCC1 and XPF subunits in DNA nucleotide excision repair.Semantic proximity Read ↗

The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways.Semantic proximity Read ↗

Genomic sequence comparison of the human and mouse XRCC1 DNA repair gene regionsSemantic proximity Read ↗

XPA: A key scaffold for human nucleotide excision repair.Semantic proximity Read ↗

Physiological consequences of defects in ERCC1-XPF DNA repair endonuclease.Semantic proximity Read ↗

Every protagonist has a sidekick: Structural aspects of human xeroderma pigmentosum-binding proteins in nucleotide excision repair.Semantic proximity Read ↗

ERCC1 mutations impede DNA damage repair and cause liver and kidney dysfunction in patients.Semantic proximity Read ↗

Physical and Functional Interaction between the XPF/ERCC1 Endonuclease and hRad52Semantic proximity Read ↗

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