Published in Proc Natl Acad Sci U S A on August 01, 1979
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
Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association. Proc Natl Acad Sci U S A (1981) 0.88
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
Thermodynamics of assembly of Escherichia coli aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1983) 0.85
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
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Subunit structure of aspartate transcarbamylase from Escherichia coli. J Biol Chem (1971) 1.72
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High resolution nuclear magnetic resonance spectra of hemoglobin. 3. The half-ligated state and allosteric interactions. J Mol Biol (1972) 1.32
Structural mapping of aspartate transcarbamoylase by fluorescence energy-transfer measurements: determination of the distance between catalytic sites of different subunits. Biochemistry (1978) 1.31
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Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue. Proc Natl Acad Sci U S A (1978) 1.03
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Interaction of aspartate transcarbamylase with regulatory nucleotides. J Biol Chem (1973) 0.98
Conformational changes in aspartate transcarbamylase. II. Circular dichroism evidence for the involvement of metal ions in allosteric interactions. J Biol Chem (1973) 0.91
Interaction of aspartate transcarbamylase with 5-bromocytidine 5'-tri-, di-, and monophosphates. Biochemistry (1974) 0.86
Spin-labeling studies of aspartate transcarbamylase. I. Effects of nucleotide binding and subunit separation. Biochemistry (1970) 0.82
Local and gross conformational changes in aspartate transcarbamylase. Biochemistry (1973) 0.81
Conformational studies on the nitrated catalytic subunit of aspartate transcarbamylase. Biochemistry (1973) 0.79
Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with cytidine 5'-triphosphate. Biochemistry (1973) 0.77
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Energetics of the HIV gp120-CD4 binding reaction. Proc Natl Acad Sci U S A (2000) 4.44
Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal Biochem (1993) 2.51
Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin. Neuron (1996) 2.25
The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. J Biol Chem (1967) 2.23
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Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits. Biochemistry (1968) 1.71
cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. Proc Natl Acad Sci U S A (1987) 1.66
Herpesvirus entry mediator ligand (HVEM-L), a novel ligand for HVEM/TR2, stimulates proliferation of T cells and inhibits HT29 cell growth. J Biol Chem (1998) 1.60
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
Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase. Proc Natl Acad Sci U S A (1970) 1.54
ON THE MACROMOLECULAR STRUCTURE OF DEOXYRIBONUCLEIC ACID: AN INTERRUPTED TWO-STRAND MODEL. Proc Natl Acad Sci U S A (1954) 1.54
Self-activation of guanosine triphosphatase activity by oligomerization of the bacterial cell division protein FtsZ. Biochemistry (1999) 1.53
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
Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases. Biochemistry (1992) 1.38
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
The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction. J Biomol Tech (2003) 1.29
Mercurial-promoted Zn2+ release from Escherichia coli aspartate transcarbamoylase. J Biol Chem (1984) 1.27
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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
Characterization of HIV-1 p24 self-association using analytical affinity chromatography. Proteins (1992) 1.20
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
Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. J Biol Chem (1996) 1.19
Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface. Proc Natl Acad Sci U S A (1995) 1.13
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
Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins. J Biol Chem (1995) 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
Purification and characterization of a mutant aspartate transcarbamoylase lacking enzyme activity. J Biol Chem (1979) 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
Amino acid sequence of the N-terminal domain of calf thymus histone H2A.Z. FEBS Lett (1983) 1.02
Molecular characteristics of recombinant human CD4 as deduced from polymorphic crystals. Proc Natl Acad Sci U S A (1990) 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
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
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase. Biochemistry (1990) 0.99
Conformational changes in proteins as measured by difference sedimentation studies. I. A technique for measuring small changes in sedimentation coefficient. Biochemistry (1971) 0.99
Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase. Proc Natl Acad Sci U S A (1986) 0.98
Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylase. Proc Natl Acad Sci U S A (1977) 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
Physical properties of a single-motif erythrocyte spectrin peptide: a highly stable independently folding unit. Biochemistry (1997) 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
Protein-ligand binding studies with a table-top, air-driven high-speed centrifuge. Arch Biochem Biophys (1978) 0.93
Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase. J Biol Chem (2000) 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
Critical amino acids in the transcriptional activation domain of the herpesvirus protein VP16 are solvent-exposed in highly mobile protein segments. An intrinsic fluorescence study. J Biol Chem (1996) 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
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
On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase. J Mol Biol (1981) 0.91
Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein. Biochemistry (1997) 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
A molecular model of the inducer binding domain of the galactose repressor of Escherichia coli. J Biol Chem (1994) 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
Overexpression in Escherichia coli, folding, purification, and characterization of the first three short consensus repeat modules of human complement receptor type 1. Protein Expr Purif (1995) 0.89
Determination of rate and equilibrium binding constants for macromolecular interactions by surface plasmon resonance. Methods Enzymol (1994) 0.89
Factor X-activating glycoprotein of Russell's viper venom. Polypeptide composition and characterization of the carbohydrate moieties. J Biol Chem (1994) 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
Determining confidence intervals for parameters derived from analysis of equilibrium analytical ultracentrifugation data. Methods Enzymol (1994) 0.88
Purification and characterization of ornithine transcarbamoylase from Saccharomyces cerevisiae. J Biol Chem (1984) 0.88
Alteration of the allosteric properties of aspartate transcarbamoylase by pyridoxylation of the catalytic and regulatory subunits. Biochemistry (1976) 0.88
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
Influence of inositol hexaphosphate binding on subunit dissociation in methemoglobin. J Biol Chem (1975) 0.87
Roles of metal ions in the maintenance of the tertiary and quaternary structure of arginase from Saccharomyces cerevisiae. J Biol Chem (1991) 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
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
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
The effects of metal ions and temperature on the interaction of cobra venom factor and human complement factor B. J Biol Chem (1986) 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
A model for the assembly of aspartate transcarbamoylase from catalytic and regulatory subunits. J Biol Chem (1980) 0.84