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Biochemistry|July 1, 1999
Evidence that pcpA encodes 2,6-dichlorohydroquinone dioxygenase, the ring cleavage enzyme required for pentachlorophenol degradation in Sphingomonas chlorophenolica strain ATCC 39723L Xu, K Resing, S L Lawson, et al.
Biochemistry|October 17, 1998
Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putidaA M Gulick, D R Palmer, P C Babbitt, et al.
The Journal of Biological Chemistry|June 27, 1997
Cloning and functional characterization of a rat renal organic cation transporter isoform (rOCT1A)L Zhang, M J Dresser, J K Chun, et al.
Biochemistry|October 17, 1998
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coliB K Hubbard, M Koch, D R Palmer, et al.
Biochemistry|November 19, 1996
Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamilyD L McCarthy, S Navarrete, W S Willett, et al.
Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing|March 27, 2001
ViewFeature: integrated feature analysis and visualizationD R Banatao, C C Huang, P C Babbitt, et al.
The Journal of Biological Chemistry|June 25, 1991
Cloning and expression of functional rabbit muscle creatine kinase in Escherichia coli. Addressing the problem of microheterogeneityL H Chen, P C Babbitt, J R Vásquez, et al.
Bio/Technology (Nature Publishing Company)|October 1, 1990
Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzymeP C Babbitt, B L West, D D Buechter, et al.
Journal of Protein Chemistry|July 6, 2000
A comparative study of human muscle and brain creatine kinases expressed in Escherichia coliL H Chen, C B White, P C Babbitt, et al.
Biochemistry|December 4, 1990
Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifsD J Pocalyko, L J Carroll, B M Martin, et al.
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