(Q36405397)

English

Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains (English)

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

1 reference

based on heuristic

inferred from title

author name string

Y R Yang

1

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

H K Schachman

2

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

language of work or name

0 references

publication date

1 September 1980

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

number of pages

5

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inferred from page(s)

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

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

77

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

9

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

5187-5191

1 reference

Europe PubMed Central

PMC publication ID

14 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=350022

30 September 2017

The enzymology of control by feedback inhibition.

1 reference

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30 September 2017

Propagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: effect of active-site ligands on the regulatory chains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

30 September 2017

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

1 reference

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30 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=350022

30 September 2017

Cooperative Interactions in Aspartate Transcarbamoylase. 1. Hybrids Composed of Native and Chemically Inactivated Catalytic Polypeptide Chains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

30 September 2017

Aspartate Transcarbamoylase from Escherichia coli : Electron Density at 5.5 Å Resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

30 September 2017

A method for the separation of hybrids of chromatographically identical oligomeric proteins. Use of 3,4,5,6-tetrahydrophthaloyl groups as a reversible "chromatographic handle"

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

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=350022

30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

30 September 2017

Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

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=350022

30 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=350022

30 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=350022

30 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=350022

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=350022

30 September 2017

Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

30 September 2017

Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

30 September 2017

Reactivation of enzymes by light-stimulated cleavage of reduced pyridoxal 5'-phosphate-enzyme complexes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

30 September 2017

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=350022

28 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=350022

28 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=350022

28 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=350022

28 June 2018

Aspartate transcarbamylase from Escherichia coli. The use of pyridoxal 5'-phosphate as a probe in the active site.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

28 June 2018

Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

28 June 2018

Alteration of the allosteric properties of aspartate transcarbamoylase by pyridoxylation of the catalytic and regulatory subunits

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=350022

28 June 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/6933552

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/6933552

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/6933552

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/6933552

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Effect of succinate on the translational diffusion coefficient of aspartate transcarbamylase

1 reference

https://pubmed.ncbi.nlm.nih.gov/6933552

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.77.9.5187

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

1980PNAS...77.5187Y

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

ResearchGate publication ID

0 references

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