(Q33907815)

English

The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase

scientific article

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

J B Sakash

1

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

E R Kantrowitz

2

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

language of work or name

0 references

publication date

1 September 2000

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

275

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

37

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

28701-28707

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Overproduction and purification of the regulatory subunit of Escherichia coli aspartate transcarbamoylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

NEGATIVE AND POSITIVE ION MASS ANALYSIS OF DICARBOXYLIC ACIDS IN STUDIES ON THE MECHANISM OF THE METHYLMALONYL ISOMERASE REACTION

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

An improved colorimetric assay for aspartate and ornithine transcarbamylases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M005079200

21 January 2018

Identifiers

10.1074/JBC.M005079200

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q33907815&oldid=1784277901"