bay-k-8644 and glucagon-like peptide 1

bay-k-8644 has been researched along with glucagon-like peptide 1 in 2 studies

Research

Studies (2)

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

Authors

Authors	Studies
Bataille, D; Blache, P; Dalle, S; Le Brigand, L; Le-Nguyen, D	1
Gaisano, HY; MacDonald, PE; Salapatek, AM; Wheeler, MB	1

Other Studies

2 other study(ies) available for bay-k-8644 and glucagon-like peptide 1

Article	Year
Miniglucagon: a local regulator of islet physiology. Annals of the New York Academy of Sciences, 1998, Dec-11, Volume: 865 Topics: 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester; Animals; Calcium; Calcium Channels; Calcium Channels, L-Type; Cell Line; Cell Membrane; Glucagon; Glucagon-Like Peptide 1; Glucagon-Like Peptides; Glucose; Glyburide; Homeostasis; Insulin; Insulin Secretion; Islets of Langerhans; Kinetics; Membrane Potentials; Peptide Fragments; Peptides	1998
Mutations to the third cytoplasmic domain of the glucagon-like peptide 1 (GLP-1) receptor can functionally uncouple GLP-1-stimulated insulin secretion in HIT-T15 cells. Molecular endocrinology (Baltimore, Md.), 1999, Volume: 13, Issue:8 Topics: 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester; Animals; Barium; Calcium Channel Agonists; Cell Line; Cyclic AMP; Electric Conductivity; Gene Deletion; Glucagon; Glucagon-Like Peptide 1; Glucagon-Like Peptide-1 Receptor; Glucose; Humans; Insulin; Insulin Secretion; Islets of Langerhans; Mutagenesis; Peptide Fragments; Protein Precursors; Rats; Receptors, Glucagon; Structure-Activity Relationship; Transfection	1999

Article

Year

Miniglucagon: a local regulator of islet physiology.

Annals of the New York Academy of Sciences, 1998, Dec-11, Volume: 865

Topics: 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester; Animals; Calcium; Calcium Channels; Calcium Channels, L-Type; Cell Line; Cell Membrane; Glucagon; Glucagon-Like Peptide 1; Glucagon-Like Peptides; Glucose; Glyburide; Homeostasis; Insulin; Insulin Secretion; Islets of Langerhans; Kinetics; Membrane Potentials; Peptide Fragments; Peptides

1998

Mutations to the third cytoplasmic domain of the glucagon-like peptide 1 (GLP-1) receptor can functionally uncouple GLP-1-stimulated insulin secretion in HIT-T15 cells.

Molecular endocrinology (Baltimore, Md.), 1999, Volume: 13, Issue:8

Topics: 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester; Animals; Barium; Calcium Channel Agonists; Cell Line; Cyclic AMP; Electric Conductivity; Gene Deletion; Glucagon; Glucagon-Like Peptide 1; Glucagon-Like Peptide-1 Receptor; Glucose; Humans; Insulin; Insulin Secretion; Islets of Langerhans; Mutagenesis; Peptide Fragments; Protein Precursors; Rats; Receptors, Glucagon; Structure-Activity Relationship; Transfection

1999