DNA Polymerases and Aminoacyl-tRNA Synthetases: Shared Mechanisms for Ensuring the Fidelity of Gene Expression
- 14 October 2008
- journal article
- review article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 47 (45), 11695-11703
- https://doi.org/10.1021/bi801500z
Abstract
No abstract availableKeywords
This publication has 70 references indexed in Scilit:
- Structures of DNA Polymerase β with Active-Site Mismatches Suggest a Transient Abasic Site Intermediate during MisincorporationMolecular Cell, 2008
- In vitro assays for the determination of aminoacyl-tRNA synthetase editing activityMethods, 2008
- Amino Acid Toxicities of Escherichia coli That Are Prevented by Leucyl-tRNA Synthetase Amino Acid EditingJournal of Bacteriology, 2007
- What a difference a decade makes: Insights into translesion DNA synthesisProceedings of the National Academy of Sciences of the United States of America, 2007
- Kinetic Discrimination of tRNA Identity by the Conserved Motif 2 Loop of a Class II Aminoacyl-tRNA SynthetaseMolecular Cell, 2007
- Regulation of DNA Repair Fidelity by Molecular Checkpoints: “Gates” in DNA Polymerase β's Substrate SelectionBiochemistry, 2006
- Visualizing polynucleotide polymerase machines at workThe EMBO Journal, 2006
- Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69Cell, 1997
- CONFORMATIONAL COUPLING IN DNA POLYMERASE FIDELITYAnnual Review of Biochemistry, 1993
- Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifsNature, 1990