(Q36295568)

English

Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study (English)

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

author name string

J E Ladner

1

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

J P Kitchell

2

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

R B Honzatko

3

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

H M Ke

4

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

K W Volz

5

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

A J Kalb

6

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

R C Ladner

7

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

W N Lipscomb

8

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

language of work or name

0 references

publication date

1 May 1982

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Europe PubMed Central

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13 August 2017

number of pages

4

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

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Europe PubMed Central

PMC publication ID

13 August 2017

79

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Europe PubMed Central

PMC publication ID

13 August 2017

10

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

3125-3128

1 reference

Europe PubMed Central

PMC publication ID

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=346366

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=346366

30 September 2017

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=346366

30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=346366

30 September 2017

The 5.5 A Resolution Structure of the Regulatory Enzyme, Aspartate Transcarbamylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=346366

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=346366

30 September 2017

Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=346366

30 September 2017

Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analog 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=346366

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=346366

29 June 2018

Allosteric Interactions in Aspartate Transcarbamylase. II. Evidence for Different Conformational States of the Protein in the Presence and Absence of Specific Ligands

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=346366

29 June 2018

Subunit interactions in aspartate transcarbamylase. A model for the allosteric mechanism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=346366

29 June 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/6954462

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide Chain

1 reference

https://pubmed.ncbi.nlm.nih.gov/6954462

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The use of non-crystallographic symmetry for phase determination

1 reference

https://pubmed.ncbi.nlm.nih.gov/6954462

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Conformational changes in aspartate transcarbamylase. 3. A functional model for allosteric behavior

1 reference

https://pubmed.ncbi.nlm.nih.gov/6954462

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Effect of pH on local and gross conformational changes in aspartate transcarbamylase

1 reference

https://pubmed.ncbi.nlm.nih.gov/6954462

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION

1 reference

https://pubmed.ncbi.nlm.nih.gov/6954462

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.79.10.3125

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

1982PNAS...79.3125L

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

ResearchGate publication ID

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