(Q27619230)

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Structural basis of the allosteric behaviour of phosphofructokinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 A resolution and 100 K: the role of the water structure and its contribution to binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Quantifying the allosteric properties of Escherichia coli carbamyl phosphate synthetase: determination of thermodynamic linked-function parameters in an ordered kinetic mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Evidence for the presence of two nonidentical subunits in carbamyl phosphate synthetase of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Reversible dissociation of carbamyl phosphate synthetase into a regulated synthesis subunit and a subunit required for glutamine utilization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Regulatory Changes in the Control of Carbamoyl Phosphate Synthetase Induced by Truncation and Mutagenesis of the Allosteric Binding Domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Photoaffinity labeling with UMP of lysine 992 of carbamyl phosphate synthetase from Escherichia coli allows identification of the binding site for the pyrimidine inhibitor.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Interactive binding between the substrate and allosteric sites of carbamoyl-phosphate synthetase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Binding of allosteric effectors to carbamyl-phosphate synthetase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Role of the four conserved histidine residues in the amidotransferase domain of carbamoyl phosphate synthetase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

AMoRe: an automated package for molecular replacement

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Activator anion binding site in pyridoxal phosphorylase b: the binding of phosphite, phosphate, and fluorophosphate in the crystal.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Photoaffinity Labeling with the Activator IMP and Site-Directed Mutagenesis of Histidine 995 of Carbamoyl Phosphate Synthetase fromEscherichia coliDemonstrate That the Binding Site for IMP Overlaps with That for the Inhibitor UMP†

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Allosteric effects of carbamoyl phosphate synthetase from Escherichia coli are entropy-driven

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

Allosteric dominance in carbamoyl phosphate synthetase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.32.22502

release_th5mic33wbaitpkvwz4gsfomdy

21 January 2018

Identifiers

DOI

10.1074/JBC.274.32.22502

0 references

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/th5mic33wbaitpkvwz4gsfomdy