alpha-aminobutyric acid has been researched along with Diabetes Mellitus in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Flatt, PR; Gault, VA; Harriott, P; O'Harte, FP | 1 |
Flatt, PR; Gault, VA; Green, BD; Greer, B; Harriott, P; O'Harte, FP | 1 |
Chan, SJ; Chu, YC; De Meyts, P; Hua, QX; Huang, K; Jia, W; Katsoyannis, PG; Klaproth, B; Nakagawa, SH; Steiner, DF; Wang, RY; Weiss, MA; Whittaker, J | 1 |
3 other study(ies) available for alpha-aminobutyric acid and Diabetes Mellitus
Article | Year |
---|---|
Degradation, cyclic adenosine monophosphate production, insulin secretion, and glycemic effects of two novel N-terminal Ala2-substituted analogs of glucose-dependent insulinotropic polypeptide with preserved biological activity in vivo.
Topics: Alanine; Amino Acid Substitution; Aminobutyrates; Animals; Blood; Cell Line; Cricetinae; Cricetulus; Cyclic AMP; Diabetes Mellitus; Dipeptidyl Peptidase 4; Gastric Inhibitory Polypeptide; Glucose; Homeostasis; Humans; Hypoglycemic Agents; Insulin; Insulin Secretion; Lung; Mice; Obesity; Sarcosine; Spectrometry, Mass, Electrospray Ionization | 2003 |
Comparative effects of GLP-1 and GIP on cAMP production, insulin secretion, and in vivo antidiabetic actions following substitution of Ala8/Ala2 with 2-aminobutyric acid.
Topics: Adenylyl Cyclases; Alanine; Aminobutyrates; Animals; Cells, Cultured; Chromatography, High Pressure Liquid; Cyclic AMP; Diabetes Mellitus; Dipeptidyl Peptidase 4; Dose-Response Relationship, Drug; Gastric Inhibitory Polypeptide; Glucagon; Glucagon-Like Peptide 1; Glucose; Humans; Insulin; Insulin Secretion; Islets of Langerhans; Mice; Mice, Obese; Models, Chemical; Peptide Fragments; Peptides; Protein Precursors; Protein Structure, Tertiary; Spectrometry, Mass, Electrospray Ionization; Time Factors | 2004 |
The A-chain of insulin contacts the insert domain of the insulin receptor. Photo-cross-linking and mutagenesis of a diabetes-related crevice.
Topics: Aminobutyrates; Animals; Cross-Linking Reagents; Diabetes Mellitus; Humans; Insulin; Light; Magnetic Resonance Spectroscopy; Mice; Mutagenesis; Mutation; Photochemistry; Protein Conformation; Protein Isoforms; Protein Structure, Tertiary; Receptor, Insulin; Swine; Valine | 2007 |