Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition (Q41171500)

27 September 2017

Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition (English)

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20 April 2023

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20 April 2023

author name string

M. F. Moody

1

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20 April 2023

P. Vachette

2

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20 April 2023

A. M. Foote

3

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20 April 2023

language of work or name

English

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publication date

1 October 1979

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27 September 2017

9 October 1979

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National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=395314

full work available at URL

20 April 2023

https://api.elsevier.com/content/article/PII:0022283679904054?httpAccept=text/xml

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https://api.elsevier.com/content/article/PII:0022283679904054?httpAccept=text/plain

20 April 2023

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Journal of Molecular Biology

20 April 2023

published in

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27 September 2017

133

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27 September 2017

4

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27 September 2017

517-532

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

27 September 2017

1

1 reference

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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An effect of enzyme and ligand concentration on the state of aggregation of aspartate transcarbamylase of E. coli: I. The binding of CTP and ATP to the enzyme

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1 reference

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An improved procedure for protein staining in polyacrylamide gels with a new type of Coomassie Brilliant Blue

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Effect of succinate on the translational diffusion coefficient of aspartate transcarbamylase

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Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit

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Aqueous Central Cavity in Aspartate Transcarbamylase from Escherichia coli

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A Position Sensitive Proportional Detector for X-Ray Crystallography

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

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

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

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

20 April 2023

23

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

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

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

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Local and gross conformational changes in aspartate transcarbamylase

20 April 2023

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Feedback inhibition and ionizing radiation. Mechanism of inactivation of allosteric properties of aspartate transcarbamylase by X-rays

20 April 2023

30

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Role for zinc in the quaternary structure of aspartate transcarbamylase from Escherichia coli

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Modified methods for the determination of carbamyl aspartate

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Shape and size of bovine rhodopsin: a small-angle x-ray scattering study of a rhodopsin-detergent complex

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The use of X-ray synchrotron radiation for structural research in biology

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Structure of human serum lipoproteins in solution. II. Small-angle x-ray scattering study of HDL and LDL.

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The stimulation of Escherichia coli aspartate transcarbamylase activity by adenosine triphosphate. Relation with the other regulatory conformational changes; a model

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Regulation of glutamine synthetase. XII. Electron microscopy of the enzyme from Escherichia coli.

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20 April 2023

Identifiers

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27 September 2017

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