Replication Protein A Confers Structure-specific Endonuclease Activities to the XPF-ERCC1 and XPG Subunits of Human DNA Repair Excision Nuclease
Open Access
- 1 May 1996
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 271 (19), 11047-11050
- https://doi.org/10.1074/jbc.271.19.11047
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- DNA EXCISION REPAIRAnnual Review of Biochemistry, 1996
- Purification and Characterization of the XPF-ERCC1 Complex of Human DNA Repair Excision NucleasePublished by Elsevier BV ,1995
- Human DNA Repair Excision NucleasePublished by Elsevier BV ,1995
- Reconstitution of Yeast Nucleotide Excision Repair with Purified Rad Proteins, Replication Protein A, and Transcription Factor TFIIHJournal of Biological Chemistry, 1995
- Mammalian DNA nucleotide excision repair reconstituted with purified protein componentsCell, 1995
- Reconstitution of Human DNA Repair Excision Nuclease in a Highly Defined SystemPublished by Elsevier BV ,1995
- Specific Cleavage of Model Recombination and Repair Intermediates by the Yeast Rad1-Rad10 DNA EndonucleaseScience, 1994
- XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repairNature, 1994
- Human xeroderma pigmentosum group G gene encodes a DNA endonucleaseNucleic Acids Research, 1994
- Human nucleotide excision nuclease removes thymine dimers from DNA by incising the 22nd phosphodiester bond 5' and the 6th phosphodiester bond 3' to the photodimer.Proceedings of the National Academy of Sciences of the United States of America, 1992