A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase. - Wikidata - awgldk - TriplyDB

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

http://www.wikidata.org/entity/Q34036878

about

In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.Mapping structural perturbations in Escherichia coli aspartate transcarbamylase by medium resolution hydrogen exchange Metal cation influence on activity and regulation of aspartate carbamoyltransferase.Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli.A survey of x-ray diffraction studies of enzyme-other molecule interactions as possible models for receptor sites.Relation between structure and function of alpha/beta-proteins.

P2860

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P2860

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

http://www.wikidata.org/entity/Q34036878

description

1979 nî lūn-bûn

@nan

1979 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1979 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

1979年の論文

@ja

1979年論文

@yue

1979年論文

@zh-hant

1979年論文

@zh-hk

1979年論文

@zh-mo

1979年論文

@zh-tw

1979年论文

@wuu

name

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@ast

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@en

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@nl

type

label

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@ast

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@en

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@nl

prefLabel

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@ast

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@en

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@nl

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PNAS.76.10.5105

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Proceedings of the National Academy of Sciences of the United States of America

P1476

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.

@en

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Honzatko RB

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Lipscomb WN

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Monaco HL

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P2860

Quantitative determination of the conformation of ATP in aqueous solution using the lanthanide cations as nuclear-magnetic-resonance probes.

The enzymology of control by feedback inhibition.

The 5.5 Angstrom resolution structure of the regulatory enzyme, asparate transcarbamylase.

Complex of aspartate carbamoyltransferase from Escherichia coli with its allosteric inhibitor, cytidine triphosphate: electron density at 5.9-angstroms resolution.

The structure of aspartate transcarbamylase, I. A molecular twofold axis in the complex with cytidine triphosphate.

Agonist-mediated changes of the acetylcholine receptor in its membrane environment.

The role of coordinated water in metal ion--adenine ring binding in complexes of adenosine triphosphate.

ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. III. THE INCORPORATION OF PYRIMIDINE AND PURINE ANALOGUES INTO DEOXYRIBONUCLEIC ACID.

Regulation of aspartate carbamoyltransferase of Escherichia coli by the interrelationship of magnesium and nucleotides.

An effect of enzyme and ligand concentration on the state of aggregation of aspartate transcarbamylase of E. coli: I. The binding of CTP and ATP to the enzyme.

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5105-5109

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scholarly article

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10.1073/PNAS.76.10.5105

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10

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388429

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