Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Non-catalytic Function of XPG Protein during Dual Incision in Human Nucleotide Excision Repair

1 Jun 1997

Abstract excerpt

XPG is a member of the FEN-1 structure-specific endonuclease family. It has 3'-junction cutting activity on bubble substrates and makes the 3'-incision in the human dual incision (excision nuclease) repair system. To investigate the precise role of XPG in nucleotide excision repair, we mutagenized two amino acid residues thought to be involved in DNA binding and catalysis, overproduced the mutant proteins using a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to CRISPR and Genetic Engineering
Share to DNA Repair Mechanisms
Share to Prenatal Screening and Diagnostics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 9188507
DOI: 10.1074/jbc.272.25.16030

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Non-catalytic Function of XPG Protein during Dual Incision in Human Nucleotide Excision RepairPMID 9188507Read ↗

Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG.Semantic proximity Read ↗

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

Replication Protein A Confers Structure-specific Endonuclease Activities to the XPF-ERCC1 and XPG Subunits of Human DNA Repair Excision NucleaseSemantic proximity Read ↗

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

The DNA-protein interaction modes of FEN-1 with gap substrates and their implication in preventing duplication mutations.Semantic proximity Read ↗

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

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

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

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

Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations.Semantic proximity Read ↗

Functional Role of N-Terminal Extension of Human AP Endonuclease 1 In Coordination of Base Excision DNA Repair via Protein-Protein Interactions.Semantic proximity Read ↗

The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.