Published in Annu Rev Biochem on January 01, 1979
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Cytochalasin D and platelet gelsolin accelerate actin polymer formation. A model for regulation of the extent of actin polymer formation in vivo. Biochemistry (1982) 1.79
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Kinetic studies on the effect of yeast cofilin on yeast actin polymerization. Biochemistry (1998) 1.46
Treatment of enzyme kinetic data. II. The multisite case: comparison of allosteric models and a possible new mechanism. J Biol Chem (1967) 1.45
Polymerization and gelation of actin studied by fluorescence photobleaching recovery. Biochemistry (1982) 1.44
Actin polymerization induces a shape change in actin-containing vesicles. Proc Natl Acad Sci U S A (1989) 1.42
On the role of amino groups in the structure and function of glutamate dehydrogenase. II. Effect of acetylation on molecular properties. J Biol Chem (1966) 1.41
Folding of a predominantly beta-structure protein: rat intestinal fatty acid binding protein. Biochemistry (1990) 1.37
Interaction of AMP-aminohydrolase with myosin and its subfragments. J Biol Chem (1977) 1.34
Microheterogeneity of actin gels formed under controlled linear shear. J Cell Biol (1988) 1.33
A fluorescent probe for conformational changes in skeletal muscle G-actin. J Biol Chem (1980) 1.32
Kinetic studies on pig heart cytoplasmic malate dehydrogenase. J Biol Chem (1975) 1.32
Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies. Biochemistry (2001) 1.28
Actin polymerization. The effect of brevin on filament size and rate of polymerization. J Biol Chem (1984) 1.27
Fatty acid interactions with a helix-less variant of intestinal fatty acid-binding protein. Biochemistry (1996) 1.24
Yeast actin: polymerization kinetic studies of wild type and a poorly polymerizing mutant. Proc Natl Acad Sci U S A (1996) 1.24
Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase. J Biol Chem (1987) 1.24
The Mg2+-induced conformational change in rabbit skeletal muscle G-actin. J Biol Chem (1982) 1.20
Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase. Proc Natl Acad Sci U S A (1995) 1.14
Polymerization-induced changes in the fluorescence of actin labeled with iodoacetamidotetramethylrhodamine. Arch Biochem Biophys (1982) 1.14
Divalent cation binding to the high- and low-affinity sites on G-actin. Biochemistry (1987) 1.13
New PC versions of the kinetic-simulation and fitting programs, KINSIM and FITSIM. Trends Biochem Sci (1997) 1.13
Effect of pH on the mechanism of actin polymerization. Biochemistry (1988) 1.12
Differences in G-actin containing bound ATP or ADP: the Mg2+-induced conformational change requires ATP. Biochemistry (1985) 1.11
Formation of actin dimers as studied by small angle neutron scattering. J Biol Chem (1986) 1.10
Identification of the sites of modification of bovine liver glutamate dehydrogenase reacted with trinitrobenzenesulfonate. Biochemistry (1971) 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
Glutamate dehydrogenase concentration as a determinant in the effect of purine nucleotides on enzymatic activity. J Biol Chem (1967) 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
Localization and mobility of gelsolin in cells. J Cell Biol (1988) 1.03
Rabbit muscle phosphofructokinase: the effect of the state of the enzyme and assay procedure on the kinetic properties. Arch Biochem Biophys (1975) 1.03
Studies on the structure of actin gels using time correlation spectroscopy of fluorescent beads. Biophys J (1992) 1.02
Rabbit muscle phosphofructokinase: studies on the polymerization. The behavior of the enzyme at pH 8, pH 6, and intermediate pH values. J Biol Chem (1972) 1.01
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
Adenosine deaminase: viscosity studies and the mechanism of binding of substrate and of ground- and transition-state analogue inhibitors. Biochemistry (1987) 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
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: characterization of mutant proteins containing inserted cysteine residues. Biochemistry (1993) 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
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
Adenylate deaminase. Kinetic and binding studies on the rabbit muscle enzyme. J Biol Chem (1978) 0.93
A small computer system for the routine analysis of enzyme kinetic mechanisms. Comput Biomed Res (1973) 0.93
Malate dehydrogenases. The lack of evidence for dissociation of the dimeric enzyme in kinetic analyses. J Biol Chem (1978) 0.91
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
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
GroEL-mediated folding of structurally homologous dihydrofolate reductases. J Mol Biol (1997) 0.89
Phosphofructokinase. III. Correlation of the regulatory kinetic and molecular properties of the rabbit muscle enzyme. J Biol Chem (1976) 0.89
Effect of filamin and controlled linear shear on the microheterogeneity of F-actin/gelsolin gels. Cell Motil Cytoskeleton (1990) 0.89
Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures. J Mol Biol (1999) 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
Analysis of the cold lability behavior of rabbit muscle phosphofructokinase. Biochem Biophys Res Commun (1975) 0.85
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
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
Phosphofructokinase. I. Mechanism of the pH-dependent inactivation and reactivation of the rabbit muscle enzyme. J Biol Chem (1976) 0.85
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 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
pH-induced cold lability of rabbit skeletal muscle phosphofructokinase. Biochemistry (1974) 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
Adenosine deaminase converts purine riboside into an analogue of a reactive intermediate: a 13C NMR and kinetic study. Biochemistry (1987) 0.81
The tyrosine B10 hydroxyl is crucial for oxygen avidity of Ascaris hemoglobin. J Biol Chem (1994) 0.81
Cooperative interaction between the GTP binding sites of glutamate dehydrogenase. Biochem Biophys Res Commun (1966) 0.80
Protein structural changes accompanying formation of enzymatic transition states: tryptophan environment in ground-state and transition-state analogue complexes of adenosine deaminase. Biochemistry (1985) 0.80