Fidelity of DNA replication under conditions used for oligodeoxynucleotide-directed mutagenesis
J Mol Biol
(1984)
177
269
(doi: 10.1016/0022-2836(84)90456-x)
Basis of biological specificity
Trends in Biochemical Sciences
(1984)
9
145
(doi: 10.1016/0968-0004(84)90122-1)
Genetic dissection of tyrosyl-tRNA synthetase
Biochemical Society Transactions
(1984)
12
224
(doi: 10.1042/bst0120224)
A large increase in enzyme-substrate affinity by protein engineering.
Nature
(1984)
307
187
(doi: 10.1038/307187a0)
Fidelity of DNA Replication in Vitro
Advances in experimental medicine and biology
(1984)
179
525
(doi: 10.1007/978-1-4684-8730-5_55)
REPLICATION OF PHI-X174 DNA BY CALF THYMUS DNA POLYMERASE-ALPHA - MEASUREMENT OF ERROR RATES AT THE AMBER-16 CODON
Advances in experimental medicine and biology
(1984)
179
535
(doi: 10.1007/978-1-4684-8730-5_56)
Deletion mutagenesis using an ‘M13 splint’: the N‐terminal structural domain of tyrosyl‐tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate.
The EMBO Journal
(1983)
2
1827
Accuracy of DNA polymerase-alpha in copying natural DNA.
The EMBO journal
(1983)
2
1515
Fidelity of replication of bacteriophage phi X174 DNA in vitro and in vivo.
Journal of molecular biology
(1983)
165
633
Kinetics of base misinsertion by DNA polymerase I of Escherichia coli.
Journal of molecular biology
(1983)
165
655
Contribution of 3′ → 5′ exonuclease activity of DNA polymerase III holoenzyme from Escherichia coli to specificity
J Mol Biol
(1983)
165
669
ACCURACY OF DNA POLYMERASE-ALPHA IN COPYING NATURAL DNA
HOPPE-SEYLERS ZEITSCHRIFT FUR PHYSIOLOGISCHE CHEMIE
(1983)
364
1133
Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding.
Nature
(1982)
299
756
(doi: 10.1038/299756a0)
Kinetic basis of spontaneous mutation Misinsertion frequencies, proofreading specificities and cost of proofreading by DNA polymerases of Escherichia coli
J Mol Biol
(1982)
156
37
(doi: 10.1016/0022-2836(82)90457-0)
Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli
Nucleic Acids Research
(1981)
9
4627
(doi: 10.1093/nar/9.18.4627)
Enzymic editing mechanisms and the genetic code.
Proceedings of the Royal Society of London. Series B, Biological sciences
(1981)
212
351
(doi: 10.1098/rspb.1981.0044)
Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases.
Nucleic Acids Research
(1981)
9
3105
(doi: 10.1093/nar/9.13.3105)
DNA polymerase accuracy and spontaneous mutation rates: frequencies of purine.purine, purine.pyrimidine, and pyrimidine.pyrimidine mismatches during DNA replication.
Proceedings of the National Academy of Sciences
(1981)
78
4251
(doi: 10.1073/pnas.78.7.4251)
INTRODUCTORY-REMARKS TO THE 3RD SESSION
Philosophical Transactions of the Royal Society of London. B, Biological Sciences
(1981)
293
119
(doi: 10.1098/rstb.1981.0065)