Crystallization and preliminary X-ray study of the catalytic subunit of aspartate transcarbamylase (Q70879879)

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14 October 2019

title

Crystallization and preliminary x-ray study of the catalytic subunit of aspartate transcarbamylase (English)

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14 October 2019

Crystallization and preliminary X-ray study of the catalytic subunit of aspartate transcarbamylase (English)

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5 April 2024

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5 April 2024

author name string

A. M. Foote

1

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5 April 2024

F. K. Winkler

2

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M. F. Moody

3

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5 April 2024

language of work or name

English

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National Center for Biotechnology Information

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5 April 2024

publication date

1 March 1981

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14 October 2019

5 March 1981

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National Center for Biotechnology Information

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full work available at URL

5 April 2024

https://api.elsevier.com/content/article/PII:0022283681903958?httpAccept=text/xml

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https://api.elsevier.com/content/article/PII:0022283681903958?httpAccept=text/plain

5 April 2024

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Journal of Molecular Biology

5 April 2024

published in

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14 October 2019

volume

146

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14 October 2019

issue

3

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14 October 2019

page(s)

389-391

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Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer

14 October 2019

cites work

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Assembly of catalytic subunits of aspartate transcarbamoylase from Escherichia coli

5 April 2024

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Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits

5 April 2024

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Effect of succinate on the translational diffusion coefficient of aspartate transcarbamylase

5 April 2024

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

5 April 2024

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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

5 April 2024

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A unifying concept for the active site region in aspartate transcarbamylase

5 April 2024

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

5 April 2024

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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

5 April 2024

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

5 April 2024

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Substrate positions and induced-fit in crystalline adenylate kinase

5 April 2024

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Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

5 April 2024

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5 Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits

5 April 2024

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5 April 2024

Identifiers

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14 October 2019

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