(Q52418466)

1 May 2018

title

Is substrate inhibition a consequence of allostery in aspartate transcarbamylase? (English)

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1 May 2018

author name string

V J LiCata

series ordinal

1

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1 May 2018

N M Allewell

series ordinal

2

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1 May 2018

publication date

1 February 1997

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1 May 2018

published in

Biophysical Chemistry

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1 May 2018

volume

64

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1 May 2018

issue

1-3

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1 May 2018

page(s)

225-234

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1 May 2018

Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Thermodynamic approaches to understanding aspartate transcarbamylase

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Ionic-strength-dependent substrate inhibition of the lysis of Micrococcus luteus by hen egg-white lysozyme.

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

The allosteric nature of substrate inhibition of insect actomyosin ATPase in presence of magnesium

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Interactions of ionizable groups in Escherichia coli aspartate transcarbamylase with adenosine and cytidine 5'-triphosphates.

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Modified methods for the determination of carbamyl aspartate

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Effects of assembly and mutations outside the active site on the functional pH dependence of Escherichia coli aspartate transcarbamylase.

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

The molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutations

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Purification and properties of porcine liver ornithine transcarbamylase

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Linked functions in allosteric proteins. Extension of the concerted (MWC) model for ligand-linked subunit assembly and its application to human hemoglobins

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Oxygenation-linked subunit interactions in human hemoglobin: analysis of linkage functions for constituent energy terms

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Parameter estimation by least-squares methods

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

A unifying concept for the active site region in aspartate transcarbamylase

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

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://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Carbon-13 isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

L-alanosine: a noncooperative substrate for Escherichia coli aspartate transcarbamylase.

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

Molecular code for cooperativity in hemoglobin

1 reference

https://api.crossref.org/works/10.1016%2FS0301-4622%2896%2902204-1

7 January 2021

10.1016/S0301-4622(96)02204-1

Identifiers

DOI

1 reference

1 May 2018

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1 May 2018