Published in Biochemistry on September 14, 1971
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The Mg2+-induced conformational change in rabbit skeletal muscle G-actin. J Biol Chem (1982) 1.20
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Polymerization-induced changes in the fluorescence of actin labeled with iodoacetamidotetramethylrhodamine. Arch Biochem Biophys (1982) 1.14
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Divalent cation binding to the high- and low-affinity sites on G-actin. Biochemistry (1987) 1.13
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The effect of milk and lactobacillus feeding on human intestinal bacterial enzyme activity. Am J Clin Nutr (1984) 1.11
The relationship between diet and rat fecal bacterial enzymes implicated in colon cancer. J Natl Cancer Inst (1976) 1.11
Differences in G-actin containing bound ATP or ADP: the Mg2+-induced conformational change requires ATP. Biochemistry (1985) 1.11
Identification of the sites of modification of bovine liver glutamate dehydrogenase reacted with trinitrobenzenesulfonate. Biochemistry (1971) 1.10
Formation of actin dimers as studied by small angle neutron scattering. J Biol Chem (1986) 1.10
Intestinal fatty acid-binding protein: the structure and stability of a helix-less variant. Biochemistry (1996) 1.08
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The binding of cytochalasin D to monomeric actin. Biochem Biophys Res Commun (1985) 1.07
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The effect of pyridoxal phosphate modification on the catalytic and regulatory properties of bovine liver glutamate dehydrogenase. J Biol Chem (1972) 1.06
The kinetics of cytochalasin D binding to monomeric actin. J Biol Chem (1986) 1.05
Bacterially synthesized folate in rat large intestine is incorporated into host tissue folyl polyglutamates. J Nutr (1991) 1.05
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Rabbit muscle phosphofructokinase: the effect of the state of the enzyme and assay procedure on the kinetic properties. Arch Biochem Biophys (1975) 1.03
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Studies on the structure of actin gels using time correlation spectroscopy of fluorescent beads. Biophys J (1992) 1.02
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Full time course studies on the oxidation of reduced coenzyme by bovine liver glutamate dehydrogenase. Use of computer simulation to obtain rate and dissociation constants. J Biol Chem (1973) 1.00
Construction of a fol mutant strain of Escherichia coli for use in dihydrofolate reductase mutagenesis experiments. J Bacteriol (1988) 1.00
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Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Biochemistry (1996) 0.99
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Metalloporphyrin chelatase from barley. Biochim Biophys Acta (1969) 0.98
Adenosine deaminase: viscosity studies and the mechanism of binding of substrate and of ground- and transition-state analogue inhibitors. Biochemistry (1987) 0.98
19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies. Biochemistry (1994) 0.97
The purification and physical properties of glutamate dehydrogenase from rat liver. J Biol Chem (1970) 0.96
Immunofluorescent and histochemical localization of AMP deaminase in skeletal muscle. J Cell Biol (1979) 0.95
Rabbit muscle phosphofructokinase: studies of the subunit molecular weight and structure. Isolation of carboxymethylated cysteinyl peptides and sedimentation equilibrium studies. J Biol Chem (1973) 0.95
The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases. J Mol Biol (1999) 0.93
Adenylate deaminase. Kinetic and binding studies on the rabbit muscle enzyme. J Biol Chem (1978) 0.93
Rabbit muscle phosphofructokinase. Modification of molecular and regulatory kinetic properties with the affinity label 5'-p-(fluorosulfonyl)benzoyl adenosine. J Biol Chem (1978) 0.93
A small computer system for the routine analysis of enzyme kinetic mechanisms. Comput Biomed Res (1973) 0.93
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Protein fragments as probes in the study of protein folding mechanisms: differential effects of dihydrofolate reductase fragments on the refolding of the intact protein. Proc Natl Acad Sci U S A (1989) 0.91
Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzyme. J Biol Chem (1976) 0.91
Malate dehydrogenases. The lack of evidence for dissociation of the dimeric enzyme in kinetic analyses. J Biol Chem (1978) 0.91
Binding of regulatory ligands to rabbit muscle phosphofructokinase. A model for nucleotide binding as a function of temperature and pH. J Biol Chem (1979) 0.90
Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy. Biochemistry (1996) 0.90
Diet and the excretion and enterohepatic cycling of estrogens. Prev Med (1987) 0.90