2--3--o-(2-4-6-trinitrophenyl)adenosine-5--triphosphate and Bone-Diseases--Developmental

2--3--o-(2-4-6-trinitrophenyl)adenosine-5--triphosphate has been researched along with Bone-Diseases--Developmental* in 1 studies

Other Studies

1 other study(ies) available for 2--3--o-(2-4-6-trinitrophenyl)adenosine-5--triphosphate and Bone-Diseases--Developmental

Article	Year
Skeletal overgrowth-causing mutations mimic an allosterically activated conformation of guanylyl cyclase-B that is inhibited by 2,4,6,-trinitrophenyl ATP. The Journal of biological chemistry, 2017, 06-16, Volume: 292, Issue:24 Activating mutations in the receptor for C-type natriuretic peptide (CNP), guanylyl cyclase B (GC-B, also known as Npr2 or NPR-B), increase cellular cGMP and cause skeletal overgrowth, but how these mutations affect GTP catalysis is poorly understood. The A488P and R655C mutations were compared with the known mutation V883M. Neither mutation affected GC-B concentrations. The A488P mutation decreased the EC Topics: Adenosine Triphosphate; Allosteric Regulation; Amino Acid Substitution; Bone Diseases, Developmental; Cyclic GMP; Enzyme Inhibitors; Guanosine Triphosphate; HEK293 Cells; Humans; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Mutation, Missense; Natriuretic Peptide, C-Type; Phosphorylation; Protein Conformation; Protein Processing, Post-Translational; Receptors, Atrial Natriuretic Factor; Recombinant Proteins	2017

Article

Year

Skeletal overgrowth-causing mutations mimic an allosterically activated conformation of guanylyl cyclase-B that is inhibited by 2,4,6,-trinitrophenyl ATP.

The Journal of biological chemistry, 2017, 06-16, Volume: 292, Issue:24

Activating mutations in the receptor for C-type natriuretic peptide (CNP), guanylyl cyclase B (GC-B, also known as Npr2 or NPR-B), increase cellular cGMP and cause skeletal overgrowth, but how these mutations affect GTP catalysis is poorly understood. The A488P and R655C mutations were compared with the known mutation V883M. Neither mutation affected GC-B concentrations. The A488P mutation decreased the EC

Topics: Adenosine Triphosphate; Allosteric Regulation; Amino Acid Substitution; Bone Diseases, Developmental; Cyclic GMP; Enzyme Inhibitors; Guanosine Triphosphate; HEK293 Cells; Humans; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Mutation, Missense; Natriuretic Peptide, C-Type; Phosphorylation; Protein Conformation; Protein Processing, Post-Translational; Receptors, Atrial Natriuretic Factor; Recombinant Proteins

2017