A kinetic model of cooperativity in aspartate transcarbamylase (Q40796205)

23 September 2017

A kinetic model of cooperativity in aspartate transcarbamylase (English)

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https://api.crossref.org/works/10.1016/S0006-3495(77)85611-7

modelling biological systems

21 June 2022

main subject

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:329911

21 June 2022

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https://api.crossref.org/works/10.1016/S0006-3495(77)85611-7

21 June 2022

author name string

M. Dembo

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:329911

21 June 2022

S. I. Rubinow

series ordinal

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:329911

21 June 2022

language of work or name

English

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publication date

1 June 1977

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23 September 2017

23

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full work available at URL

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https://europepmc.org/articles/PMC1473294

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC:MED AND EXT_ID:329911

https://europepmc.org/articles/PMC1473294?pdf=render

21 June 2022

1 reference

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https://api.elsevier.com/content/article/PII:S0006349577856117?httpAccept=text/xml

21 June 2022

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https://api.crossref.org/works/10.1016/S0006-3495(77)85611-7

https://api.elsevier.com/content/article/PII:S0006349577856117?httpAccept=text/plain

21 June 2022

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https://api.crossref.org/works/10.1016/S0006-3495(77)85611-7

21 June 2022

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23 September 2017

18

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23 September 2017

3

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23 September 2017

245-267

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

23 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

The enzymology of control by feedback inhibition.

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

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

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Localization of the zinc binding site of aspartate transcarbamoylase in the regulatory subunit

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Aspartate Transcarbamoylase Molecules Lacking One Regulatory Subunit

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

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

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Kinetics of allosteric enzymes

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Quaternary constraint in hybrid of aspartate transcarbamylase containing wild-type and mutant catalytic subunits

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of cytosine 5'-triphosphate and adenosine 5'-triphosphate

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Subunit interactions in aspartate transcarbamylase. Characterization of a complex between the catalytic and the regulatory subunits

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase

24 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Conformational changes in proteins as measured by difference sedimentation studies. I. Technique for measuring small changes in sedimentation coefficient

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

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

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Subunit Structure of Aspartate Transcarbamylase from Escherichia coli

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

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

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

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

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Aspartate transcarbamylase of Escherichia coli. Mechanisms of inhibition and activation by dicarboxylic acids and other anions

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

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

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Local and gross conformational changes in aspartate transcarbamylase

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Determination of ligand binding: partial and full saturation of aspartate transcarbamylase. Applicability of a filter assay to weakly binding ligands

17 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1473294

Determination of the number of regulatory and catalytic sites on aspartate transcarbamylase

19 August 2018

1 reference

12 December 2020

Interaction of Aspartate Transcarbamylase with Regulatory Nucleotides

1 reference

12 December 2020

Aspartate transcarbamylase. Studies of the catalytic subunit by ultraviolet difference spectroscopy

1 reference

12 December 2020

Anatomy and physiology of a regulatory enzyme-aspartate transcarbamylase

1 reference

12 December 2020

Carbamyl phosphate binding to aspartate transcarbamylase. Partial saturation and its alteration by succinate

1 reference

12 December 2020

An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate

1 reference

12 December 2020

Structure and arrangement of the regulatory subunits in aspartate transcarbamylase

1 reference

12 December 2020

Electron microscopy of aspartate transcarbamylase and its catalytic subunit

1 reference

12 December 2020

Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with aspartate analogs

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

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

1 reference

12 December 2020

Interpretation of nonhyperbolic behavior in enzymic systems. II. Quantitative characteristics of rate and binding functions

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

1 reference

23 September 2017

1 reference

PMC publication ID

1473294

23 September 2017

1 reference

PMC publication ID

1473294