Phage ø29 DNA polymerase residues involved in the proper stabilisation of the primer-terminus at the 3′-5′ exonuclease active site
- 17 November 2000
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 304 (1) , 1-9
- https://doi.org/10.1006/jmbi.2000.4178
Abstract
No abstract availableKeywords
Funding Information
- Comunidad de Madrid
- European Commission (07B/0032/1999)
- National Institutes of Health (PB98-0645)
- Dirección General de Investigación Científica y Técnica (ERBFMRX CT97 0125)
- Fundación Ramón Areces
This publication has 30 references indexed in Scilit:
- Mutational analysis of ø29 DNA polymerase residues acting as ssDNA ligands for 3′-5′ exonucleolysisJournal of Molecular Biology, 1998
- DNA Polymerase β: Structure−Fidelity Relationship from Pre-Steady-State Kinetic Analyses of All Possible Correct and Incorrect Base Pairs for Wild Type and R283A MutantBiochemistry, 1997
- [28] Structure-function analysis of 3′ → 5′-exonuclease of DNA polymerasesPublished by Elsevier ,1995
- Structure of DNA Polymerase I Klenow Fragment Bound to Duplex DNAScience, 1993
- Compilation, alignment, and phylogenetic relationships of DNA polymerasesNucleic Acids Research, 1993
- Fidelity of the reverse transcriptase of human immunodeficiency virus type 2FEBS Letters, 1992
- A conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerasesCell, 1989
- An RNA polymerase II transcription factor binds to an upstream element in the adenovirus major late promoterCell, 1985
- Characterization of a 3′ → 5′ exonuclease activity in the phage φ29-encoded DNA polymeraseNucleic Acids Research, 1985
- Enzymatic Synthesis of Deoxyribonucleic AcidJournal of Biological Chemistry, 1972