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Straus, D., Raines, R., Kawashima, E., Knowles, J. R., Gilbert, W. (1985) Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme. Proceedings of the National Academy of Sciences, 82 (8) 2272-2276 doi:10.1073/pnas.82.8.2272

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Reference TypeJournal (article/letter/editorial)
TitleActive site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme.
JournalProceedings of the National Academy of Sciences
AuthorsStraus, D.Author
Raines, R.Author
Kawashima, E.Author
Knowles, J. R.Author
Gilbert, W.Author
Year1985 (April 1)Volume82
Issue8
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.82.8.2272Search in ResearchGate
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Mindat Ref. ID1448103Long-form Identifiermindat:1:5:1448103:9
GUID0
Full ReferenceStraus, D., Raines, R., Kawashima, E., Knowles, J. R., Gilbert, W. (1985) Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme. Proceedings of the National Academy of Sciences, 82 (8) 2272-2276 doi:10.1073/pnas.82.8.2272
Plain TextStraus, D., Raines, R., Kawashima, E., Knowles, J. R., Gilbert, W. (1985) Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme. Proceedings of the National Academy of Sciences, 82 (8) 2272-2276 doi:10.1073/pnas.82.8.2272
In(1985, April) Proceedings of the National Academy of Sciences Vol. 82 (8) Proceedings of the National Academy of Sciences

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Straus, D., Gilbert, W. (1985) Chicken triosephosphate isomerase complements an Escherichia coli deficiency. Proceedings of the National Academy of Sciences, 82 (7) 2014-2018 doi:10.1073/pnas.82.7.2014
Hermes, J. D., Blacklow, S. C., Knowles, J. R. (1990) Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme. Proceedings of the National Academy of Sciences, 87 (2) 696-700 doi:10.1073/pnas.87.2.696
Rozovsky, S., McDermott, A. E. (2007) Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase. Proceedings of the National Academy of Sciences, 104 (7) 2080-2085 doi:10.1073/pnas.0608876104
Borchert, T. V., Abagyan, R., Jaenicke, R., Wierenga, R. K. (1994) Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. Proceedings of the National Academy of Sciences, 91 (4) 1515-1518 doi:10.1073/pnas.91.4.1515
Stenkamp, R. E., Sieker, L. C., Jensen, L. H., McCallum, J. D., Sanders-Loehr, J. (1985) Active site structures of deoxyhemerythrin and oxyhemerythrin. Proceedings of the National Academy of Sciences, 82 (3) 713-716 doi:10.1073/pnas.82.3.713
Straus, E., Malesci, A., Yalow, R. S. (1978) Characterization of a nontrypsin cholecystokinin converting enzyme in mammalian brain. Proceedings of the National Academy of Sciences, 75 (11) 5711-5714 doi:10.1073/pnas.75.11.5711
RAINES, RONALD T., KNOWLES, JEREMY R. (1986) The Mechanistic Pathway of a Mutant Triosephosphate Isomerase. Annals of the New York Academy of Sciences, 471 (1) 266-271 doi:10.1111/j.1749-6632.1986.tb48042.x
Hook, V. Y., Mezey, E., Fricker, L. D., Pruss, R. M., Siegel, R. E., Brownstein, M. J. (1985) Immunochemical characterization of carboxypeptidase B-like peptide-hormone-processing enzyme. Proceedings of the National Academy of Sciences, 82 (14) 4745-4749 doi:10.1073/pnas.82.14.4745
Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proceedings of the National Academy of Sciences, 82 (2) 488-492 doi:10.1073/pnas.82.2.488
Eisenbeis, S. J., Nasoff, M. S., Noble, S. A., Bracco, L. P., Dodds, D. R., Caruthers, M. H. (1985) Altered Cro repressors from engineered mutagenesis of a synthetic cro gene. Proceedings of the National Academy of Sciences, 82 (4) 1084-1088 doi:10.1073/pnas.82.4.1084
Flavell, R. A., Sabo, D. L., Bandle, E. F., Weissmann, C. (1975) Site-directed mutagenesis: effect of an extracistronic mutation on the in vitro propagation of bacteriophage Qbeta RNA. Proceedings of the National Academy of Sciences, 72 (1) 367-371 doi:10.1073/pnas.72.1.367
 
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