(Q37588042)

21 August 2017

Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue (English)

2 references

21 August 2017

10.1073/PNAS.75.6.2654

https://api.crossref.org/works/10.1073/PNAS.75.6.2654

26 March 2022

1

S. M. Landfear

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A26914

26 March 2022

author name string

D. R. Evans

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A26914

26 March 2022

W. N. Lipscomb

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A26914

26 March 2022

language of work or name

English

0 references

publication date

1 June 1978

1 reference

PMCID

392621

full work available at URL

21 August 2017

https://europepmc.org/articles/PMC392621

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A26914

https://europepmc.org/articles/PMC392621?pdf=render

26 March 2022

file format

Portable Document Format

online access status

open access

content deliverer

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A26914

https://syndication.highwire.org/content/doi/10.1073/pnas.75.6.2654

26 March 2022

1 reference

Crossref

DOI

10.1073/PNAS.75.6.2654

https://api.crossref.org/works/10.1073/PNAS.75.6.2654

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

26 March 2022

published in

1 reference

21 August 2017

75

1 reference

21 August 2017

2654-2658

1 reference

21 August 2017

6

1 reference

The enzymology of control by feedback inhibition.

21 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

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

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Aspartate Transcarbamoylase from Escherichia coli : Electron Density at 5.5 Å Resolution

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Aqueous Central Cavity in Aspartate Transcarbamylase from Escherichia coli

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

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

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Functional modifications of aspartate transcarbamylase induced by nitration with tetranitromethane

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Functionally important arginine residues of aspartate transcarbamylase

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Subunit Structure of Aspartate Transcarbamylase from Escherichia coli

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Aspartate transcarbamylase. Stereospecific restrictions on the binding site for L-aspartate.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Thin-layer chromatography of sub-nanomole amounts of phenylthiohydantoin (PTH) amino acids on polyamide sheets.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Spin-labeling studies of aspartate transcarbamylase. I. Effects of nucleotide binding and subunit separation

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Aspartate transcarbamylase of Escherichia coli. Mechanisms of inhibition and activation by dicarboxylic acids and other anions

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Conformational changes in aspartate transcarbamylase. II. Circular dichroism evidence for the involvement of metal ions in allosteric interactions.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392621

Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins

1 September 2018

1 reference

12 December 2020

The amino acid sequence of porcine parathyroid hormone

1 reference

12 December 2020

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

1 reference

12 December 2020

Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism

1 reference

12 December 2020

Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis

1 reference

12 December 2020

Probable protein crosslinking with tetranitromethane

1 reference

12 December 2020

Biosynthesis of an aspartate transcarbamylase lacking co-operative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil

1 reference

12 December 2020

Regulation of enzyme activity. The activity of enzymes can be controlled by a multiplicity of conformational equilibria

1 reference

12 December 2020

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

1 reference

12 December 2020

Tetranitromethane. A Reagent for the Nitration of Tyrosyl Residues in Proteins*

1 reference

12 December 2020

Reduction of nitrotyrosyl residues in proteins

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.75.6.2654

1 reference

21 August 2017

0 references

1 reference

21 August 2017

1 reference

PMCID

392621