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Article

Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair.

Nature structural & molecular biology - 1 Mar 2006

Camenisch Ulrike, Dip Ramiro, Schumacher Sylvie Briand, Schuler Benjamin, Naegeli Hanspeter

Abstract excerpt

The function of human XPA protein, a key subunit of the nucleotide excision repair pathway, has been examined with site-directed substitutions in its putative DNA-binding cleft. After screening for repair activity in a host-cell reactivation assay, we analyzed mutants by comparing their affinities for different substrate architectures, including DNA junctions that provide a surrogate for distorted reaction...

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Source

Identifiers

PMID: 16491090
DOI: 10.1038/nsmb1061

Genes

XPA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair.PMID 16491090Read ↗

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The rem mutations in the ATP-binding groove of the Rad3/XPD helicase lead to Xeroderma pigmentosum-Cockayne syndrome-like phenotypes.Semantic proximity Read ↗

Conserved Residues of Human XPG Protein Important for Nuclease Activity and Function in Nucleotide Excision RepairSemantic proximity Read ↗

A disease-associated XPA allele interferes with TFIIH binding and primarily affects transcription-coupled nucleotide excision repair.Semantic proximity Read ↗

Does the XPA–FEN1 Interaction Concern to Nucleotide Excision Repair or Beyond?Semantic proximity Read ↗

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