arginine and beryllium fluoride

arginine has been researched along with beryllium fluoride in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Braig, K; Kagawa, R; Leslie, AG; Montgomery, MG; Walker, JE	1
Aittoniemi, J; Ashcroft, FM; de Wet, H; Ellard, S; Flanagan, SE; Hattersley, AT; Patch, AM; Rees, MG; Sansom, MS; Shimomura, K	1

Other Studies

2 other study(ies) available for arginine and beryllium fluoride

Article	Year
The structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride. The EMBO journal, 2004, Jul-21, Volume: 23, Issue:14 Topics: Adenosine Diphosphate; Animals; Arginine; Beryllium; Binding Sites; Catalytic Domain; Cattle; Crystallography, X-Ray; Enzyme Inhibitors; Fluorides; Hydrolysis; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Proton-Translocating ATPases; Water	2004
Increased ATPase activity produced by mutations at arginine-1380 in nucleotide-binding domain 2 of ABCC8 causes neonatal diabetes. Proceedings of the National Academy of Sciences of the United States of America, 2007, Nov-27, Volume: 104, Issue:48 Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Substitution; Arginine; ATP-Binding Cassette Transporters; Beryllium; Binding Sites; Diabetes Mellitus, Type 1; Fluorides; Humans; Hydrolysis; Infant, Newborn; Insulin; Insulin Secretion; Ion Channel Gating; Kinetics; Models, Molecular; Mutation, Missense; Point Mutation; Potassium; Potassium Channels; Potassium Channels, Inwardly Rectifying; Protein Structure, Tertiary; Receptors, Drug; Structure-Activity Relationship; Sulfonylurea Receptors	2007

Article

Year

The structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride.

The EMBO journal, 2004, Jul-21, Volume: 23, Issue:14

Topics: Adenosine Diphosphate; Animals; Arginine; Beryllium; Binding Sites; Catalytic Domain; Cattle; Crystallography, X-Ray; Enzyme Inhibitors; Fluorides; Hydrolysis; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Proton-Translocating ATPases; Water

2004

Increased ATPase activity produced by mutations at arginine-1380 in nucleotide-binding domain 2 of ABCC8 causes neonatal diabetes.

Proceedings of the National Academy of Sciences of the United States of America, 2007, Nov-27, Volume: 104, Issue:48

Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Substitution; Arginine; ATP-Binding Cassette Transporters; Beryllium; Binding Sites; Diabetes Mellitus, Type 1; Fluorides; Humans; Hydrolysis; Infant, Newborn; Insulin; Insulin Secretion; Ion Channel Gating; Kinetics; Models, Molecular; Mutation, Missense; Point Mutation; Potassium; Potassium Channels; Potassium Channels, Inwardly Rectifying; Protein Structure, Tertiary; Receptors, Drug; Structure-Activity Relationship; Sulfonylurea Receptors

2007