Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution (Q24595328)

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English	Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution	scientific article

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instance of

scholarly article

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title

Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution (English)

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H M Ke

1

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R B Honzatko

series ordinal

2

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W N Lipscomb

series ordinal

3

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language of work or name

English

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publication date

July 1984

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

81

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issue

13

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page(s)

4037-40

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cites work

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

24 March 2017

The enzymology of control by feedback inhibition.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

The 5.5 A Resolution Structure of the Regulatory Enzyme, Aspartate Transcarbamylase

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

A unifying concept for the active site region in aspartate transcarbamylase

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

27 September 2017

Modification of three active site lysine residues in the catalytic subunit of aspartate transcarbamylase by D- and L-bromosuccinate.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=345363

retrieved

30 May 2018

The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein Subunits

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/6377306

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide Chain

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/6377306

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/6377306

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/6377306

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1073/PNAS.81.13.4037

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PubMed publication ID

6377306

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Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution (Q24595328)

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Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution (Q24595328)

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