Published in Biochemistry on October 04, 1988
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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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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
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The kinetics of cytochalasin D binding to monomeric actin. J Biol Chem (1986) 1.05
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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
Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Biochemistry (1996) 0.99
Interaction of microtubule-associated proteins with actin filaments. Studies using the fluorescence-photobleaching recovery technique. J Biol Chem (1984) 0.98
Intestinal fatty acid binding protein: characterization of mutant proteins containing inserted cysteine residues. Biochemistry (1993) 0.98
The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes. Proc Natl Acad Sci U S A (1998) 0.98
Intestinal fatty acid binding protein: a specific residue in one turn appears to stabilize the native structure and be responsible for slow refolding. Protein Sci (1997) 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
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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
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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
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
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A small computer system for the routine analysis of enzyme kinetic mechanisms. Comput Biomed Res (1973) 0.93
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
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Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy. Biochemistry (1996) 0.90
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
Effect of filamin and controlled linear shear on the microheterogeneity of F-actin/gelsolin gels. Cell Motil Cytoskeleton (1990) 0.89
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GroEL-mediated folding of structurally homologous dihydrofolate reductases. J Mol Biol (1997) 0.89
Rabbit muscle phosphofructokinase. A model for regulatory kinetic behavior. J Biol Chem (1979) 0.88
Purification of GroEL with low fluorescence background. Methods Enzymol (1998) 0.87
Effect of trinitrophenylation of specific lysyl residues on the catalytic, regulatory, and molecular properties of bovine liver glutamate dehydrogenase. Biochemistry (1971) 0.87
Effect of temperature on the mechanism of actin polymerization. Biochemistry (1986) 0.87
The three-dimensional structure of a helix-less variant of intestinal fatty acid-binding protein. Protein Sci (1998) 0.86
Refolding of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: a stopped-flow NMR spectroscopy study. Biochemistry (1998) 0.85
Analysis of the cold lability behavior of rabbit muscle phosphofructokinase. Biochem Biophys Res Commun (1975) 0.85
An NADH-induced conformational change that mediates the sequential 3 beta-hydroxysteroid dehydrogenase/isomerase activities is supported by affinity labeling and the time-dependent activation of isomerase. J Biol Chem (1995) 0.85
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Catalytic strategy of citrate synthase: subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site. Biochemistry (1995) 0.83
The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: implications for the mechanism. Biochemistry (1992) 0.83
Crystallographic studies of glutamate dehydrogenase. Preliminary crystal data. J Biol Chem (1979) 0.83
Crystallographic studies of glutamate dehydrogenase. II. Preliminary crystal data for the tuna liver enzyme. J Mol Biol (1980) 0.83
Adenylate deaminase: potent inhibition by 2'-deoxycoformycin 5'-phosphate. Biochem Biophys Res Commun (1979) 0.83
pH-induced cold lability of rabbit skeletal muscle phosphofructokinase. Biochemistry (1974) 0.82
pH-induced changes in G-actin conformation and metal affinity. Biochemistry (1988) 0.82
Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase. Biochemistry (1991) 0.82
Chemical modification of actin. Acceleration of polymerization and reduction of network formation by reaction with N-ethylmaleimide, (iodoacetamido)tetramethylrhodamine, or 7-chloro-4-nitro-2,1,3-benzoxadiazole. Biochemistry (1982) 0.81
Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase. J Biol Chem (1985) 0.81
The tyrosine B10 hydroxyl is crucial for oxygen avidity of Ascaris hemoglobin. J Biol Chem (1994) 0.81
Adenosine deaminase converts purine riboside into an analogue of a reactive intermediate: a 13C NMR and kinetic study. Biochemistry (1987) 0.81