The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision Repair
Open Access
- 31 December 2005
- journal article
- research article
- Published by Elsevier
- Vol. 13 (12) , 1849-1858
- https://doi.org/10.1016/j.str.2005.08.014
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Biophysical Characterization of the Interaction Domains and Mapping of the Contact Residues in the XPF-ERCC1 ComplexJournal of Biological Chemistry, 2005
- Crystal structure of the Holliday junction DNA in complex with a single RuvA tetramerProceedings of the National Academy of Sciences, 2000
- Nucleotide excision repair and human syndromesCarcinogenesis: Integrative Cancer Research, 2000
- Protein complexes in nucleotide excision repairMutation Research/DNA Repair, 1999
- Molecular mechanism of nucleotide excision repairGenes & Development, 1999
- Protein backbone angle restraints from searching a database for chemical shift and sequence homologyJournal of Biomolecular NMR, 1999
- Mapping of interaction domains between human repair proteins ERCC1 and XPFNucleic Acids Research, 1998
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- DNA Structural Elements Required for ERCC1-XPF Endonuclease ActivityJournal of Biological Chemistry, 1998
- Reconstitution of Human Excision Nuclease with Recombinant XPF-ERCC1 ComplexJournal of Biological Chemistry, 1997