The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain.

DNA sequencing with chain-terminating inhibitors

1977 • 69,181 citations

[1] Production of single-stranded plasmid DNA

1987 • 2,642 citations

The Enzymology of Control by Feedback Inhibition

1962 • 1,003 citations

Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment of DNA

1982 • 764 citations

Improved oligonudeotide site-directed rautagenesis using M13 vectors

1985 • 545 citations

Aspartate Transcarbamylase

1971 • 422 citations

Aspartate Transcarbamylase

1969 • 305 citations

Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli

1982 • 227 citations

2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-l-aspartate

1987 • 210 citations

Complex of N-phosphonacetyl-l-aspartate with aspartate carbamoyltransferase

1988 • 175 citations

Escherichia coli Aspartate Transcarbamylase: the Relation Between Structure and Function

1988 • 157 citations

Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli

1987 • 135 citations

An improved colorimetric assay for aspartate and ornithine transcarbamylases

1981 • 124 citations

Attenuation control of pyrBI operon expression in Escherichia coli K-12.

1983 • 119 citations

In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.

1989 • 119 citations

[20] Improved oligonucleotide-directed mutagenesis using M13 vectors

1987 • 112 citations

Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate.

1985 • 110 citations

Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.

1968 • 106 citations

The organization and regulation of the pyrBI operon in E. coli includes a rho-independent attenuator sequence

1982 • 93 citations

The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli

1978 • 91 citations

A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies

1988 • 81 citations

Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5'-triphosphate analog

1973 • 77 citations

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.

1988 • 74 citations

Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-.ANG. resolution and neutral pH

1990 • 69 citations

Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase

1989 • 67 citations

Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase

1988 • 66 citations

Synthesis of aspartate transcarbamoylase in Escherichia coli: transcriptional regulation of the pyrB-pyrI operon.

1983 • 55 citations

Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions

1983 • 50 citations

Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.

1986 • 45 citations

Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.

1989 • 37 citations

Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase

1988 • 36 citations

Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase.

1986 • 35 citations

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase

1989 • 30 citations

Stabilization of the relaxed state of aspartate transcarbamoylase by modification with a bifunctional reagent.

1978 • 29 citations

Catalytic-regulatory subunit interactions and allosteric effects in aspartate transcarbamylase.

1987 • 20 citations

Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.

1989 • 17 citations