(Q39089545)

9 September 2017

title

An essential residue at the active site of aspartate transcarbamylase (English)

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

11 March 2022

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https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

11 March 2022

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https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

11 March 2022

author name string

E. R. Kantrowitz

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A4457

11 March 2022

W. N. Lipscomb

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A4457

11 March 2022

language of work or name

English

0 references

publication date

1 May 1976

1 reference

9 September 2017

10 May 1976

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=4457

full work available at URL

11 March 2022

http://intl.jbc.org/cgi/content/abstract/251/9/2688

online access status

open access

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A4457

https://api.elsevier.com/content/article/PII:S0021925817335421?httpAccept=text/xml

11 March 2022

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

https://api.elsevier.com/content/article/PII:S0021925817335421?httpAccept=text/plain

11 March 2022

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Journal of Biological Chemistry

11 March 2022

published in

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9 September 2017

volume

251

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9 September 2017

issue

9

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9 September 2017

page(s)

2688-2695

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CARBAMYL PHOSPHATE, THE CARBAMYL DONOR IN ENZYMATIC CITRULLINE SYNTHESIS1

9 September 2017

cites work

1

77

819

Jones

1955

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Aspartate Carbamyl Transferase from Escherichia coli

11 March 2022

2

10

548

Reichard

1956

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

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

11 March 2022

5

4

1054

Gerhart

1965

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

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

11 March 2022

6

218

1116

Weber

1968

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

11 March 2022

7

218

1119

Wiley

1968

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

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

11 March 2022

8

65

234

Meighen

1970

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

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

11 March 2022

9

36

285

Wiley

1971

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

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

11 March 2022

10

70

1117

Warren

1973

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Complex of Aspartate Carbamoyltransferase from Escherichia coli with Its Allosteric Inhibitor, Cytidine Triphosphate: Electron Density at 5.9-Å Resolution

11 March 2022

11

71

4437

Edwards

1974

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate

11 March 2022

15

10

1046

Hammes

1971

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Fluorescence energy transfer between ligand binding sites on aspartate transcarbamylase

11 March 2022

20

14

214

Matsumoto

1975

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Functional arginyl residues as ATP binding sites of glutamine synthetase and carbamyl phosphate synthetase

11 March 2022

series ordinal

24

0 references

Essential arginyl residue at the nucleotide binding site of creatine kinase

25

14

4699

Borders

1975

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Functional arginyl residues as NADH binding sites of alcohol dehydrogenases

11 March 2022

28

13

4361

Lange

1974

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Arginine as the C-1 phosphate binding site in rabbit muscle aldolase

11 March 2022

29

54

70

Lobb

1975

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Essential arginyl residues in Escherichia coli alkaline phosphatase

11 March 2022

30

13

2865

Daemen

1974

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

The structure of carboxypeptidase a, vi. Some results at 2.0-a resolution, and the complex with glycyl-tyrosine at 2.8-a resolution

11 March 2022

31

58

2220

Reeke

1967

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Inactivation of bovine carboxypeptidase A by specific modification of arginine residues with phenylglyoxal

11 March 2022

32

75

455

Ikenaga

1973

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Functional arginyl residues in carboxypeptidase A. Modification with butanedione

11 March 2022

33

12

3915

Riordan

1973

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Simple trimerization of 2,3-butanedione yielding a selective reagent for the modification of arginine in proteins

11 March 2022

35

90

1664

Yankeelov

1968

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

A new class of chromophoric organomercurials and their reactions with d-glyceraldehyde 3-phosphate dehydrogenase

11 March 2022

38

115

913

McMurray

1969

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Protein measurement with the Folin phenol reagent

11 March 2022

41

193

265

Lowry

1951

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

Two new staining procedures for quantitative estimation of proteins on electrophoretic strips

11 March 2022

42

71

377

Fazekas de St. Groth

1963

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

The thiol group in the catalytic chains of aspartate transcarbamoylase

11 March 2022

43

69

3638

Evans

1972

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

A nuclear magnetic resonance study of the binding of substrate analogues to a modified aspartate transcarbamylase

11 March 2022

45

48

572

McMurray

1972

0 references

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

46

10

1919

Kirschner

1971

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

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

11 March 2022

47

2

531

Changeux

1968

1 reference

https://api.crossref.org/works/10.1016/S0021-9258(17)33542-1

11 March 2022

Identifiers

1 reference