(Q33834289)

29 July 2017

title

Structural transitions in crystals of native aspartate carbamoyltransferase (English)

1 reference

29 July 2017

J E Gouaux

1

1 reference

29 July 2017

W N Lipscomb

series ordinal

2

1 reference

29 July 2017

language of work or name

English

0 references

publication date

1 February 1989

1 reference

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

29 July 2017

published in

1 reference

29 July 2017

volume

86

1 reference

29 July 2017

issue

3

1 reference

29 July 2017

page(s)

845-848

1 reference

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

29 July 2017

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

The enzymology of control by feedback inhibition.

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Structure of dahlemense strain of tobacco mosaic virus: A periodically deformed helix

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

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

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

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

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Conformational changes in aspartate transcarbamylase. I. Proteolysis of the intact enzyme.

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

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

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

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

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

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

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

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

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Escherichia coli aspartate transcarbamylase: the relation between structure and function

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analog N-(phosphonacetyl)-L-aspartate

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

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

4 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286574

Liquid-like movements in crystalline insulin

29 October 2018

1 reference

12 December 2020

Pyrimidine biosynthesis in Escherichia coli

1 reference

12 December 2020

Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase*

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

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

1 reference

12 December 2020

Conformational changes in aspartate transcarbamylase. II. Concerted or sequential mechanism?

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.86.3.845

1 reference

29 July 2017

0 references

1 reference

29 July 2017

1 reference