(Q44634047)

4 December 2017

title

A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state (English)

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4 December 2017

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Jay M West

1

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4 December 2017

Hiro Tsuruta

series ordinal

2

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4 December 2017

Evan R Kantrowitz

series ordinal

3

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4 December 2017

language of work or name

English

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publication date

26 October 2003

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Journal of Biological Chemistry

4 December 2017

number of pages

7

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based on heuristic

inferred from page(s)

published in

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4 December 2017

volume

279

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4 December 2017

issue

2

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4 December 2017

page(s)

945-951

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

4 December 2017

cites work

1 reference

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In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase

21 January 2018

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Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions

21 January 2018

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Interactions of metal-nucleotide complexes with aspartate carbamoyltransferase in the crystalline state

21 January 2018

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Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH

21 January 2018

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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

21 January 2018

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

21 January 2018

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Escherichia coli aspartate transcarbamylase: the relation between structure and function

21 January 2018

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Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution

21 January 2018

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

21 January 2018

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Structural kinetics of the allosteric transition of aspartate transcarbamylase produced by physiological substrates.

21 January 2018

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A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies.

21 January 2018

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Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation

21 January 2018

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Intramolecular pyrene excimer fluorescence: a probe of proximity and protein conformational change

21 January 2018

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2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

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

21 January 2018

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Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli

21 January 2018

1 reference

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Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion

21 January 2018

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Tryptophan residues at subunit interfaces used as fluorescence probes to investigate homotropic and heterotropic regulation of aspartate transcarbamylase

21 January 2018

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The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain

21 January 2018

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

21 January 2018

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Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

21 January 2018

1 reference

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A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase

21 January 2018

1 reference

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Trapping specific quaternary states of the allosteric enzyme aspartate transcarbamoylase in silica matrix sol-gels

21 January 2018

1 reference

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

21 January 2018

1 reference

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Raster3D: photorealistic molecular graphics

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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NEGATIVE AND POSITIVE ION MASS ANALYSIS OF DICARBOXYLIC ACIDS IN STUDIES ON THE MECHANISM OF THE METHYLMALONYL ISOMERASE REACTION

21 January 2018

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A colorimetric method for determining low concentrations of mercaptans

21 January 2018

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An improved colorimetric assay for aspartate and ornithine transcarbamylases

21 January 2018

1 reference

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Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304018200

Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304018200

Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304018200

Kinetic consequences of site-specific mutation of Glu-239----Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304018200

Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304018200

X-ray Scattering Titration of the Quaternary Structure Transition of Aspartate Transcarbamylase with a Bisubstrate Analogue: Influence of Nucleotide Effectors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M304018200

21 January 2018

Identifiers

DOI

10.1074/JBC.M304018200

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4 December 2017

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