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Biochemistry|December 7, 1993
A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putidaB Mitra, J A Gerlt, P C Babbitt, et al.
The Journal of Biological Chemistry|December 10, 1983
Molecular anatomy of the antibody binding siteJ Novotný, R Bruccoleri, J Newell, et al.
Proteins|December 1, 1986
Isolation and analysis of arc repressor mutants: evidence for an unusual mechanism of DNA bindingA K Vershon, J U Bowie, T M Karplus, et al.
The Journal of Biological Chemistry|April 25, 1993
Three-dimensional models of four mouse mast cell chymases. Identification of proteoglycan binding regions and protease-specific antigenic epitopesA Sali, R Matsumoto, H P McNeil, et al.
American Journal of Medical Genetics|January 1, 1980
Malformation syndrome associated with small extra chromosomeR Carmi, D Abeliovich, J Bar-Ziv, et al.
Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences|June 26, 1981
On the three-dimensional structure and catalytic mechanism of triose phosphate isomeraseT Alber, D W Banner, A C Bloomer, et al.
Acta Crystallographica. Section D, Biological Crystallography|May 1, 1997
Characterization of two crystal forms of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putidaM S Hasson, I Schlichting, M M McGowen, et al.
Biochemistry|March 1, 1994
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzymeK M Bohren, C E Grimshaw, C J Lai, et al.
Biochemistry|March 7, 1995
Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317B Mitra, A T Kallarakal, J W Kozarich, et al.
Biochemistry|December 14, 1993
Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxisA M Stock, E Martinez-Hackert, B F Rasmussen, et al.
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