(Q37339058)

English

Communication between dissimilar subunits in aspartate transcarbamoylase: Effect of inhibitor and activator on the conformation of the catalytic polypeptide chains

scientific article published on August 1, 1979

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

Communication between dissimilar subunits in aspartate transcarbamoylase: effect of inhibitor and activator on the conformation of the catalytic polypeptide chains (English)

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

Communication between dissimilar subunits in aspartate transcarbamoylase: Effect of inhibitor and activator on the conformation of the catalytic polypeptide chains (English)

1 reference

10.1073/PNAS.76.8.3732

https://api.crossref.org/works/10.1073/PNAS.76.8.3732

17 April 2023

author name string

P. Hensley

1

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A386346

17 April 2023

H. K. Schachman

2

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A386346

17 April 2023

language of work or name

0 references

publication date

1 August 1979

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

full work available at URL

https://europepmc.org/articles/PMC383907

online access status

content deliverer

Europe PubMed Central

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A386346

17 April 2023

https://europepmc.org/articles/PMC383907?pdf=render

Portable Document Format

online access status

content deliverer

Europe PubMed Central

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A386346

17 April 2023

https://pnas.org/doi/pdf/10.1073/pnas.76.8.3732

1 reference

10.1073/PNAS.76.8.3732

https://api.crossref.org/works/10.1073/PNAS.76.8.3732

17 April 2023

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

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

76

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

8

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

3732-3736

1 reference

Europe PubMed Central

PMC publication ID

19 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=383907

6 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=383907

6 September 2017

Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

6 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=383907

6 September 2017

Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

6 September 2017

Aspartate Transcarbamoylase Molecules Lacking One Regulatory Subunit

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

6 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=383907

6 September 2017

Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

6 September 2017

Pyridoxal 5'-phosphate, a fluorescent probe in the active site of aspartate transcarbamylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

14 September 2017

5 Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

28 September 2017

Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

28 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

28 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

28 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=383907

28 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=383907

26 June 2018

Subunit Structure 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=383907

26 June 2018

Aspartate transcarbamylase. Stereospecific restrictions on the binding site for L-aspartate.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 June 2018

Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 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=383907

26 June 2018

Local and gross conformational changes in aspartate transcarbamylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 June 2018

Conformational studies on the nitrated catalytic subunit of aspartate transcarbamylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 June 2018

Interaction of aspartate transcarbamylase with 5-bromocytidine 5'-tri-, di-, and monophosphates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 June 2018

Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with cytidine 5'-triphosphate.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 June 2018

Structure and subunit interaction of haemoglobin M Milwaukee.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 June 2018

Spin-labeling studies of aspartate transcarbamylase. I. Effects of nucleotide binding and subunit separation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

26 June 2018

Conformational changes in aspartate transcarbamylase. II. Circular dichroism evidence for the involvement of metal ions in allosteric interactions.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=383907

2 September 2018

Structural mapping of aspartate transcarbamoylase by fluorescence energy-transfer measurements: determination of the distance between catalytic sites of different subunits

1 reference

https://pubmed.ncbi.nlm.nih.gov/386346

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interaction of Aspartate Transcarbamylase with Regulatory Nucleotides

1 reference

https://pubmed.ncbi.nlm.nih.gov/386346

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

High resolution nuclear magnetic resonance spectra of hemoglobin. 3. The half-ligated state and allosteric interactions

1 reference

https://pubmed.ncbi.nlm.nih.gov/386346

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structure and arrangement of the regulatory subunits in aspartate transcarbamylase

1 reference

https://pubmed.ncbi.nlm.nih.gov/386346

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/386346

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Environmentally Sensitive Tyrosyl Residues. Nitration with Tetranitromethane*

1 reference

https://pubmed.ncbi.nlm.nih.gov/386346

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Nature of Haem–Haem Interaction

1 reference

https://pubmed.ncbi.nlm.nih.gov/386346

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.76.8.3732

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

1979PNAS...76.3732H

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

ResearchGate publication ID

0 references

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