Structure-activity studies of glucagon-like peptide-1.

[1]  B. Göke,et al.  Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting beta-cells. , 1993, The Journal of biological chemistry.

[2]  A. Vinther,et al.  Using capillary electrophoresis in the optimization of a carboxypeptidase Y catalyzed transpeptidation reaction , 1993, Electrophoresis.

[3]  S. Mojsov.  Structural requirements for biological activity of glucagon-like peptide-I. , 2009, International journal of peptide and protein research.

[4]  G. Singhg,et al.  Truncated glucagon-like peptide-1 interacts with exendin receptors on dispersed acini from guinea pig pancreas. Identification of a mammalian analogue of the reptilian peptide exendin-4. , 1992, The Journal of biological chemistry.

[5]  J. Holst,et al.  Antidiabetogenic effect of glucagon-like peptide-1 (7-36)amide in normal subjects and patients with diabetes mellitus. , 1992, The New England journal of medicine.

[6]  D. Nathan,et al.  Insulinotropic Action of Glucagonlike Peptide-I-(7–37) in Diabetic and Nondiabetic Subjects , 1992, Diabetes Care.

[7]  S. Ohashi,et al.  The structure-function relationship of GLP-1 related peptides in the endocrine function of the canine pancreas. , 1991, The Tohoku journal of experimental medicine.

[8]  S. Gammeltoft,et al.  Receptor Binding and Tyrosine Kinase Activation by Insulin Analogues With Extreme Affinities Studied in Human Hepatoma HepG2 Cells , 1991, Diabetes.

[9]  R. Garippa,et al.  Structure-activity studies of vasoactive intestinal polypeptide. , 1991, The Journal of biological chemistry.

[10]  R. B. Merrifield,et al.  Position 9 replacement analogs of glucagon uncouple biological activity and receptor binding. , 1991, The Journal of biological chemistry.

[11]  G. Weir,et al.  Glucagon-like peptide-I analogs: effects on insulin secretion and adenosine 3',5'-monophosphate formation. , 1990, Endocrinology.

[12]  J. Holst,et al.  Complete sequences of glucagon-like peptide-1 from human and pig small intestine. , 1989, The Journal of biological chemistry.

[13]  G. Weir,et al.  Insulinotropin: glucagon-like peptide I (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas. , 1987, The Journal of clinical investigation.

[14]  J. Holst,et al.  Truncated glucagon‐like peptide I, an insulin‐releasing hormone from the distal gut , 1987, FEBS letters.

[15]  J. Holst,et al.  Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas. , 1986, Endocrinology.

[16]  L. Orci,et al.  Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing. , 1986, The Journal of biological chemistry.

[17]  D. Steiner,et al.  Mutations in the guinea pig preproglucagon gene are restricted to a specific portion of the prohormone sequence , 1986, FEBS letters.

[18]  S. Mammi,et al.  Interaction of calcium ions with gastrin fragments of increasing chain length , 1986, Biopolymers.

[19]  G. Bell,et al.  Hamster preproglucagon contains the sequence of glucagon and two related peptides , 1983, Nature.

[20]  J. Thorell,et al.  Enzymatic iodination of polypeptides with 125I to high specific activity. , 1971, Biochimica et biophysica acta.