Published in J Biol Chem on September 25, 1985
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Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. Biochemistry (1977) 1.50
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Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. Proc Natl Acad Sci U S A (1987) 1.23
Ultracentrifuge studies with Rayleigh interference optics. II. Low-speed sedimentation equilibrium of homogeneous systems. Biochemistry (1968) 1.22
Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1985) 1.20
Aspartate transcarbamoylase molecules lacking one regulatory subunit. Proc Natl Acad Sci U S A (1974) 1.12
Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP. J Biol Chem (1989) 1.09
Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit. Proc Natl Acad Sci U S A (1999) 1.08
Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity. J Biol Chem (1984) 1.06
Primary structure and properties of an inactive mutant aspartate transcarbamoylase. J Biol Chem (1979) 1.06
Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation. Proc Natl Acad Sci U S A (2000) 1.05
Genetic characterization of the folding domains of the catalytic chains in aspartate transcarbamoylase. J Biol Chem (1983) 1.03
Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains. Proc Natl Acad Sci U S A (1993) 1.02
A method for the separation of hybrids of chromatographically identical oligomeric proteins. Use of 3,4,5,6-tetrahydrophthaloyl groups as a reversible "chromatographic handle". Biochemistry (1976) 1.02
Purification and characterization of a mutant aspartate transcarbamoylase lacking enzyme activity. J Biol Chem (1979) 1.02
Measurement of partial specific volume by sedimentation equilibrium in H2O-D2O solutions. Methods Enzymol (1973) 1.01
Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits. Biochemistry (1977) 1.01
Regulation of aspartate transcarbamoylase synthesis in Escherichia coli: analysis of deletion mutations in the promoter region of the pyrBI operon. Proc Natl Acad Sci U S A (1985) 1.00
Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers. J Biol Chem (1982) 1.00
Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects. Biophys Chem (1990) 1.00
Conformational changes in proteins as measured by difference sedimentation studies. I. A technique for measuring small changes in sedimentation coefficient. Biochemistry (1971) 0.99
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase. Biochemistry (1990) 0.99
Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylase. Proc Natl Acad Sci U S A (1977) 0.98
Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1986) 0.98
Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1991) 0.97
Differential scanning calorimetry of asparate transcarbamoylase and its isolate subunits. J Biol Chem (1978) 0.96
Quaternary constraint in hybrid of aspartate transcarbamylase containing wild-type and mutant catalytic subunits. Proc Natl Acad Sci U S A (1975) 0.96
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Protein-ligand binding studies with a table-top, air-driven high-speed centrifuge. Arch Biochem Biophys (1978) 0.93
A sedimentation equilibrium method for determining molecular weights of proteins with a tabletop high speed air turbine centrifuge. J Biol Chem (1978) 0.93
A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity. Proc Natl Acad Sci U S A (1991) 0.92
Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments. J Mol Biol (1989) 0.92
Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains. Protein Sci (1993) 0.92
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On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase. J Mol Biol (1981) 0.91
Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains. Proc Natl Acad Sci U S A (1989) 0.90
Anatomy and physiology of a regulatory enzyme-aspartate transcarbamylase. Harvey Lect (1974) 0.90
Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase. Anal Biochem (1987) 0.90
Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate? J Mol Biol (1985) 0.90
In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains. Protein Sci (1993) 0.89
In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly. Protein Sci (1996) 0.88
Alteration of the allosteric properties of aspartate transcarbamoylase by pyridoxylation of the catalytic and regulatory subunits. Biochemistry (1976) 0.88
Communication between catalytic and regulatory subunits in Ni(II)- and Co(II)-aspartate transcarbamoylase. Ligand-promoted structural alterations at the intersubunit bonding domains. J Biol Chem (1983) 0.87
Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits. Proc Natl Acad Sci U S A (1974) 0.87
Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase. Biochemistry (1971) 0.87
Assembly of aspartate transcarbamoylase in Escherichia coli. Trans N Y Acad Sci (1983) 0.87
Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains. J Biol Chem (1982) 0.87
Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains. Proc Natl Acad Sci U S A (1980) 0.86
Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites. Biochemistry (1976) 0.86
Attenuation in the regulation of the pyrBI operon in Escherichia coli. In vivo studies of transcriptional termination. J Biol Chem (1989) 0.85
Communication between dissimilar subunits in aspartate transcarbamoylase: effect of inhibitor and activator on the conformation of the catalytic polypeptide chains. Proc Natl Acad Sci U S A (1979) 0.85
Cooperative interactions in aspartate transcarbamoylase. 1. Hybrids composed of native and chemically inactivated catalytic polypeptide chains. Proc Natl Acad Sci U S A (1974) 0.84
Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase. Protein Sci (1993) 0.84
A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits. J Biol Chem (1980) 0.84
The influence of quaternary structure on the active site of an oligomeric enzyme. Catalytic subunit of aspartate transcarbamoylase. J Biol Chem (1984) 0.84
Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase. Protein Sci (1996) 0.84
Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. I. Focusing of the camera and cylindrical lenses. Anal Biochem (1971) 0.83
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase. J Biol Chem (1988) 0.83
Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: effect of active-site ligands on the regulatory chains. Proc Natl Acad Sci U S A (1980) 0.83
Mechanism of disproportionation of asparate transcarbamoylase molecules lacking one regulatory subunit. J Biol Chem (1980) 0.83
Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function. Protein Sci (2001) 0.83
Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase. Biochemistry (1992) 0.82
Spectral alterations associated with the ligand-promoted gross conformational change in aspartate transcarbamoylase. J Biol Chem (1981) 0.82
Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli. J Biol Chem (1981) 0.82
Effect of D2O and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenase. Biochemistry (1973) 0.82
Kinetics of the interaction of N-(phosphonacetyl)-L-aspartate with the catalytic subunit of aspartate transcarbamoylase. A slow conformational change subsequent to binding. J Biol Chem (1986) 0.82
Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: implications for domain switching. Protein Sci (1996) 0.81
Hybridization of native and chemically modified enzymes. II. Native and succinylated glyceraldehyde 3-phosphate dehydrogenase. Biochemistry (1970) 0.81
Comparison of active mutants and wild-type aspartate transcarbamoylase of Escherichia coli. J Biol Chem (1984) 0.81
Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme. J Biol Chem (1991) 0.81
Local and gross conformational changes in aspartate transcarbamylase. Biochemistry (1973) 0.81
Communication between subunits in aspartate transcarbamoylase. Effect of active site ligands on the tertiary structure of regulatory chains. J Biol Chem (1981) 0.80
Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. II. A general procedure. Anal Biochem (1971) 0.80
19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits. J Biol Chem (1985) 0.80
Conformational studies on the nitrated catalytic subunit of aspartate transcarbamylase. Biochemistry (1973) 0.79
1H NMR studies on the catalytic subunit of aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1992) 0.79
Equilibrium and kinetic studies of the association of catalytic and regulatory subunits of aspartate transcarbamoylase. J Biol Chem (1980) 0.78
Communication between polypeptide chains in aspartate transcarbamoylase. Conformational changes at the active sites of unliganded chains resulting from ligand binding to other chains. J Biol Chem (1986) 0.78
Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability. Protein Sci (1994) 0.78