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barium and glucagon-like peptide 1

barium has been researched along with glucagon-like peptide 1 in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Kato, M; Ma, HT; Tatemoto, K1
Dobashi, Y; Kanno, T; Suga, S; Wakui, M1
Dobashi, Y; Kanno, T; Nakano, K; Suga, S; Takeo, T; Wakui, M1
Gaisano, HY; MacDonald, PE; Salapatek, AM; Wheeler, MB1

Other Studies

4 other study(ies) available for barium and glucagon-like peptide 1

ArticleYear
GLP-1 depolarizes the rat pancreatic beta cell in a Na(+)-dependent manner.
    Regulatory peptides, 1996, Apr-09, Volume: 62, Issue:1

    Topics: Animals; Barium; Calcium Channel Blockers; Cell Polarity; Cells, Cultured; Cyclic AMP-Dependent Protein Kinases; Glucagon; Glucagon-Like Peptide 1; Glucose; Insulin; Insulin Secretion; Islets of Langerhans; Isoquinolines; Male; Meglumine; Membrane Potentials; Pancreatic Hormones; Patch-Clamp Techniques; Peptides; Protein Precursors; Rats; Rats, Wistar; Sodium; Sulfonamides

1996
GLP-1 (7-36) amide activates L-type Ca2+ channels of pancreatic B-cells through c-AMP signaling.
    The Japanese journal of physiology, 1997, Volume: 47 Suppl 1

    Topics: Action Potentials; Animals; Barium; Calcium Channels; Cyclic AMP; Electric Conductivity; Glucagon; Glucagon-Like Peptide 1; Glucagon-Like Peptides; Islets of Langerhans; Male; Peptide Fragments; Rats; Signal Transduction

1997
GLP-I(7-36) amide augments Ba2+ current through L-type Ca2+ channel of rat pancreatic beta-cell in a cAMP-dependent manner.
    Diabetes, 1997, Volume: 46, Issue:11

    Topics: Action Potentials; Adenosine Triphosphate; Animals; Barium; Bucladesine; Calcium Channels; Calcium Channels, L-Type; Cells, Cultured; Cyclic AMP; Electric Stimulation; Glucagon; Glucagon-Like Peptide 1; Glucagon-Like Peptides; Glucose; Islets of Langerhans; Kinetics; Membrane Potentials; Peptide Fragments; Rats; Thionucleotides; Tolbutamide

1997
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