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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

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Reference TypeJournal (article/letter/editorial)
TitleSubstrate product equilibrium on a reversible enzyme, triosephosphate isomerase
JournalProceedings of the National Academy of Sciences
AuthorsRozovsky, S.Author
McDermott, A. E.Author
Year2007 (February 13)Volume104
Issue7
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0608876104Search in ResearchGate
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Mindat Ref. ID1746650Long-form Identifiermindat:1:5:1746650:9
GUID0
Full ReferenceRozovsky, 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
Plain TextRozovsky, 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
In(2007, February) Proceedings of the National Academy of Sciences Vol. 104 (7) Proceedings of the National Academy of Sciences

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Jogl, G., Rozovsky, S., McDermott, A. E., Tong, L. (2003) Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. Proceedings of the National Academy of Sciences, 100 (1) 50-55 doi:10.1073/pnas.0233793100
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
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
Sasnauskas, G., Connolly, B. A., Halford, S. E., Siksnys, V. (2007) Site-specific DNA transesterification catalyzed by a restriction enzyme. Proceedings of the National Academy of Sciences, 104 (7) 2115-2120 doi:10.1073/pnas.0608689104
Keeling, P. J., Doolittle, W. F. (1997) Evidence that eukaryotic triosephosphate isomerase is of alpha-proteobacterial origin. Proceedings of the National Academy of Sciences, 94 (4) 1270-1275 doi:10.1073/pnas.94.4.1270
Pincus, M. R., Zimmerman, S. S., Scheraga, H. A. (1977) Structures of enzyme-substrate complexes of lysozyme. Proceedings of the National Academy of Sciences, 74 (7) 2629-2633 doi:10.1073/pnas.74.7.2629
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
Gnerer, J. P., Kreber, R. A., Ganetzky, B. (2006) wasted away, a Drosophila mutation in triosephosphate isomerase, causes paralysis, neurodegeneration, and early death. Proceedings of the National Academy of Sciences, 103 (41) 14987-14993 doi:10.1073/pnas.0606887103
Wright, B. E. (1960) ON ENZYME-SUBSTRATE RELATIONSHIPS DURING BIOCHEMICAL DIFFERENTIATION. Proceedings of the National Academy of Sciences, 46 (6) 798-803 doi:10.1073/pnas.46.6.798
Spiegelman, S., DeLorenzo, W. F. (1952) Substrate Stabilization of Enzyme-Forming Capacity During the Segregation of a Heterozygote. Proceedings of the National Academy of Sciences, 38 (7) 583-592 doi:10.1073/pnas.38.7.583
McDermott, B. M., Baucom, J. M., Hudspeth, A. J. (2007) Analysis and functional evaluation of the hair-cell transcriptome. Proceedings of the National Academy of Sciences, 104 (28) 11820-11825 doi:10.1073/pnas.0704476104
 
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