(Q36278364)

English

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

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scholarly article

1 reference

Europe PubMed Central

13 August 2017

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

1 reference

Europe PubMed Central

13 August 2017

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

P Tauc

1

1 reference

Europe PubMed Central

13 August 2017

R T Keiser

2

1 reference

Europe PubMed Central

13 August 2017

E R Kantrowitz

3

1 reference

Europe PubMed Central

13 August 2017

P Vachette

4

1 reference

Europe PubMed Central

13 August 2017

publication date

1 November 1994

1 reference

Europe PubMed Central

13 August 2017

Protein Science

1 reference

Europe PubMed Central

13 August 2017

3

1 reference

Europe PubMed Central

13 August 2017

11

1 reference

Europe PubMed Central

13 August 2017

1998-2004

1 reference

Europe PubMed Central

13 August 2017

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

The enzymology of control by feedback inhibition.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

Aspartate transcarbamylase from Escherichia coli: activity and regulation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

Can a simple model account for the allosteric transition of aspartate transcarbamoylase?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

30 September 2017

Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

Kinetic mechanism of native Escherichia coli aspartate transcarbamylase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

Structural kinetics of the allosteric transition of aspartate transcarbamylase produced by physiological substrates.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

29 June 2018

Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142631

22 September 2018

The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein Subunits

1 reference

https://pubmed.ncbi.nlm.nih.gov/7703847

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/7703847

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/7703847

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/PRO.5560031112

1 reference

Europe PubMed Central

13 August 2017

1 reference

Europe PubMed Central

13 August 2017

1 reference

Europe PubMed Central

13 August 2017

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