Published in Biochemistry on March 23, 1976
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
Modification of mouse testicular lactate dehydrogenase by pyridoxal 5'-phosphate. Biochem J (1980) 0.80
A cooperative Escherichia coli aspartate transcarbamoylase without regulatory subunits . Biochemistry (2010) 0.78
Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase. Biochemistry (1965) 4.76
The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. J Biol Chem (1967) 2.23
Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry (1968) 2.16
An Ultracentrifuge Cell for Producing Boundaries Synthetically by a Layering Technique. Proc Natl Acad Sci U S A (1952) 1.98
Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits. Biochemistry (1968) 1.71
Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1996) 1.56
Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation. Proc Natl Acad Sci U S A (1984) 1.56
ON THE MACROMOLECULAR STRUCTURE OF DEOXYRIBONUCLEIC ACID: AN INTERRUPTED TWO-STRAND MODEL. Proc Natl Acad Sci U S A (1954) 1.54
Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase. Proc Natl Acad Sci U S A (1970) 1.54
Synthesis of aspartate transcarbamoylase in Escherichia coli: transcriptional regulation of the pyrB-pyrI operon. Proc Natl Acad Sci U S A (1983) 1.50
Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. Biochemistry (1977) 1.50
Characterization of cyanobacterial phycobilisomes in zwitterionic detergents. Proc Natl Acad Sci U S A (1979) 1.40
Dissociation of hemoglobin into subunits. Monomer formation and the influence of ligands. J Mol Biol (1971) 1.38
Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model. Biochemistry (1977) 1.38
Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon. Proc Natl Acad Sci U S A (1982) 1.37
Structure and arrangement of the regulatory subunits in aspartate transcarbamylase. Biochemistry (1972) 1.36
Ultracentrifuge studies with absorption optics. IV. Molecular weight determinations at the microgram level. Biochemistry (1966) 1.33
Aspartate transcarbamoylase (Escherichia coli): preparation of subunits. Methods Enzymol (1978) 1.27
Mercurial-promoted Zn2+ release from Escherichia coli aspartate transcarbamoylase. J Biol Chem (1984) 1.27
A role for zinc in the quaternary structure of aspartate transcarbamylase from Escherichia coli. Biochemistry (1972) 1.27
Sedimentation equilibrium studies on glutamic dehydrogenase. Biochemistry (1971) 1.25
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
Preclinical efficacy and safety of pascolizumab (SB 240683): a humanized anti-interleukin-4 antibody with therapeutic potential in asthma. Clin Exp Immunol (2002) 1.07
Primary structure and properties of an inactive mutant aspartate transcarbamoylase. J Biol Chem (1979) 1.06
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
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
The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence. J Biol Chem (1984) 1.04
Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. J Biol Chem (1985) 1.04
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
Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits. Biochemistry (1977) 1.01
Measurement of partial specific volume by sedimentation equilibrium in H2O-D2O solutions. Methods Enzymol (1973) 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
Quaternary constraint in hybrid of aspartate transcarbamylase containing wild-type and mutant catalytic subunits. Proc Natl Acad Sci U S A (1975) 0.96
Differential scanning calorimetry of asparate transcarbamoylase and its isolate subunits. J Biol Chem (1978) 0.96
Hybridization of native and chemically modified enzymes. I. Development of a general method and its application to the study of the subunit structure of aldolase. Biochemistry (1970) 0.95
Antithrombotic efficacy of a novel murine antihuman factor IX antibody in rats. Arterioscler Thromb Vasc Biol (1999) 0.94
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
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
The heparin binding site of antithrombin III. Evidence for a critical tryptophan residue. J Biol Chem (1980) 0.92
Pseudoisoenzymes of rabbit muscle phosphoglucose isomerase. J Biol Chem (1972) 0.92
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
Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains. Protein Sci (1993) 0.92
pryB mutations as suppressors of arginine auxotrophy in Salmonella typhimurium. J Bacteriol (1980) 0.91
Molecular weight and amino acid composition of five-times-crystallized phosphoglucose isomerase from rabbit skeletal muscle. Biochemistry (1970) 0.91
On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase. J Mol Biol (1981) 0.91
Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase. Anal Biochem (1987) 0.90
Anatomy and physiology of a regulatory enzyme-aspartate transcarbamylase. Harvey Lect (1974) 0.90
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
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
Dependence of antithrombin III and thrombin binding stoichiometries and catalytic activity on the molecular weight of affinity-purified heparin. J Biol Chem (1986) 0.89
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
Characterization of the denaturation and renaturation of human plasma vitronectin. I. Biophysical characterization of protein unfolding and multimerization. J Biol Chem (1996) 0.88
Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits. Proc Natl Acad Sci U S A (1974) 0.87
Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains. J Biol Chem (1982) 0.87
Site-directed mutagenesis probing the catalytic role of arginines 165 and 166 of human cytomegalovirus protease. Biochemistry (1998) 0.87
Assembly of aspartate transcarbamoylase in Escherichia coli. Trans N Y Acad Sci (1983) 0.87
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
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
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
Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases. Biochemistry (1999) 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
The influence of quaternary structure on the active site of an oligomeric enzyme. Catalytic subunit of aspartate transcarbamoylase. J Biol Chem (1984) 0.84
Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase. Protein Sci (1993) 0.84
Histidine-rich glycoprotein modulation of the anticoagulant activity of heparin. Evidence for a mechanism involving competition with both antithrombin and thrombin for heparin binding. J Biol Chem (1987) 0.84
Subunit structure and function of porcine factor Xa-activated factor VIII. Biochemistry (1997) 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
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
A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits. J Biol Chem (1980) 0.84
Measurement of protein interaction bioenergetics: application to structural variants of anti-sCD4 antibody. Methods Enzymol (2000) 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
Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. I. Focusing of the camera and cylindrical lenses. Anal Biochem (1971) 0.83
Pyridoxylation of essential lysines in the heparin-binding site of antithrombin III. J Biol Chem (1984) 0.83
Mechanism of disproportionation of asparate transcarbamoylase molecules lacking one regulatory subunit. J Biol Chem (1980) 0.83
Identification of a lysyl residue in antithrombin which is essential for heparin binding. J Biol Chem (1987) 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
Effect of D2O and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenase. Biochemistry (1973) 0.82