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Volumn 58, Issue 3, 2015, Pages 1020-1037

Glucagon-like peptide-1 (GLP-1) analogs: Recent advances, new possibilities, and therapeutic implications

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALBIGLUTIDE; CYCLIC AMP; DAVALINTIDE; DIPEPTIDYL PEPTIDASE IV INHIBITOR; DULAGLUTIDE; EFPEGLENATIDE; EXENDIN 4; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 1 DERIVATIVE; GLUTAMIC ACID; GLYCINE; IMIDAZOLE; ISOLEUCINE; LIRAGLUTIDE; PHENYLALANINE; SEMAGLUTIDE; SERINE; TASPOGLUTIDE; VALINE;

EID: 84922771356     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm500810s     Document Type: Article
Times cited : (137)

References (174)
  • 1
    • 0026596851 scopus 로고
    • Antidiabetogenic effect of glucagon-like peptide-1 (7-36)amide in normal subjects and patients with diabetes mellitus
    • Gutniak, M.; Ørkov, C.; Holst, J. J.; Ahrén, B.; Efendić, S. Antidiabetogenic effect of glucagon-like peptide-1 (7-36)amide in normal subjects and patients with diabetes mellitus N. Engl. J. Med. 1992, 326, 1316-1322
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1316-1322
    • Gutniak, M.1    Ørkov, C.2    Holst, J.J.3    Ahrén, B.4    Efendić, S.5
  • 2
    • 3242730474 scopus 로고    scopus 로고
    • Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans
    • Holst, J. J.; Gromada, J. Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans Am. J. Physiol.: Endocrinol. Metabol. 2004, 287, E199-E206
    • (2004) Am. J. Physiol.: Endocrinol. Metabol. , vol.287 , pp. 199-E206
    • Holst, J.J.1    Gromada, J.2
  • 4
    • 2542479899 scopus 로고    scopus 로고
    • Minireview: Glucagon-like peptides regulate cell proliferation and apoptosis in the pancreas, gut, and central nervous system
    • Brubaker, P. L.; Drucker, D. J. Minireview: glucagon-like peptides regulate cell proliferation and apoptosis in the pancreas, gut, and central nervous system Endocrinology 2004, 145, 2653-2659
    • (2004) Endocrinology , vol.145 , pp. 2653-2659
    • Brubaker, P.L.1    Drucker, D.J.2
  • 5
    • 4344675057 scopus 로고    scopus 로고
    • Therapeutic strategies based on glucagon-like peptide 1
    • Deacon, C. F. Therapeutic strategies based on glucagon-like peptide 1 Diabetes 2004, 53, 2181-2189
    • (2004) Diabetes , vol.53 , pp. 2181-2189
    • Deacon, C.F.1
  • 6
    • 0033304603 scopus 로고    scopus 로고
    • The glucagon-like peptides
    • Kieffer, T. J.; Habener, J. F. The glucagon-like peptides Endocr. Rev. 1999, 20, 876-913
    • (1999) Endocr. Rev. , vol.20 , pp. 876-913
    • Kieffer, T.J.1    Habener, J.F.2
  • 7
    • 0028325376 scopus 로고
    • Divergent tissue-specific and developmental expression of receptors for glucagon and glucagon-like peptide-1 in the mouse
    • Campos, R. V.; Lee, Y. C.; Drucker, D. J. Divergent tissue-specific and developmental expression of receptors for glucagon and glucagon-like peptide-1 in the mouse Endocrinology 1994, 134, 2156-2164
    • (1994) Endocrinology , vol.134 , pp. 2156-2164
    • Campos, R.V.1    Lee, Y.C.2    Drucker, D.J.3
  • 8
    • 0030013475 scopus 로고    scopus 로고
    • Tissue distribution of messenger ribonucleic acid encoding the rat glucagon-like peptide-1 receptor
    • Bullock, B. P.; Heller, R. S.; Habener, J. F. Tissue distribution of messenger ribonucleic acid encoding the rat glucagon-like peptide-1 receptor Endocrinology 1996, 137, 2968-2978
    • (1996) Endocrinology , vol.137 , pp. 2968-2978
    • Bullock, B.P.1    Heller, R.S.2    Habener, J.F.3
  • 11
    • 0020596734 scopus 로고
    • Hamster preproglucagon contains the sequence of glucagon and two related peptides
    • Bell, G. I.; Santerre, R. F.; Mullenbach, G. T. Hamster preproglucagon contains the sequence of glucagon and two related peptides Nature 1983, 302, 716-718
    • (1983) Nature , vol.302 , pp. 716-718
    • Bell, G.I.1    Santerre, R.F.2    Mullenbach, G.T.3
  • 12
    • 0020026919 scopus 로고
    • Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem
    • Lund, P. K.; Goodman, R. H.; Dee, P. C.; Habener, J. F. Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem Proc. Natl. Acad. Sci. U.S.A. 1982, 79, 345-349
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 345-349
    • Lund, P.K.1    Goodman, R.H.2    Dee, P.C.3    Habener, J.F.4
  • 13
    • 0041733259 scopus 로고    scopus 로고
    • The glucagon-like peptides: A double-edged therapeutic sword?
    • Perry, T.; Greig, N. H. The glucagon-like peptides: a double-edged therapeutic sword? Trends Pharmacol. Sci. 2003, 24, 377-383
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 377-383
    • Perry, T.1    Greig, N.H.2
  • 14
    • 35748957503 scopus 로고    scopus 로고
    • The physiology of glucagon-like peptide 1
    • Holst, J. J. The physiology of glucagon-like peptide 1 Physiol. Rev. 2007, 87, 1409-1439
    • (2007) Physiol. Rev. , vol.87 , pp. 1409-1439
    • Holst, J.J.1
  • 15
    • 0030758090 scopus 로고    scopus 로고
    • Endoproteolysis of glucagon-like peptide (GLP)-1(7-36) amide by ectopeptidases in RINm5F cells
    • Hupe-Sodmann, K.; Göke, R.; Göke, B.; Thole, H. H.; Zimmermann, B.; Voigt, K.; McGregor, G. P. Endoproteolysis of glucagon-like peptide (GLP)-1(7-36) amide by ectopeptidases in RINm5F cells Peptides 1997, 18, 625-632
    • (1997) Peptides , vol.18 , pp. 625-632
    • Hupe-Sodmann, K.1    Göke, R.2    Göke, B.3    Thole, H.H.4    Zimmermann, B.5    Voigt, K.6    McGregor, G.P.7
  • 16
    • 0027215348 scopus 로고
    • Dipeptidyl peptidase-IV hydrolyzes gastric-inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein, R.; G, B.; Schmidt, W. E. Dipeptidyl peptidase-IV hydrolyzes gastric-inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum Eur. J. Biochem. 1993, 214, 829-835
    • (1993) Eur. J. Biochem. , vol.214 , pp. 829-835
    • Mentlein, R.1    Schmidt, W.E.2
  • 18
    • 0028803336 scopus 로고
    • Both subcutaneously and intravenously administered glucagon-like peptide i are rapidly degraded from the NH2-terminus in type II diabetic patients and in healthy subjects
    • Deacon, C. F.; Nauck, M. A.; Toft-Nielsen, M.; Pridal, L.; Willms, B.; Holst, J. J. Both subcutaneously and intravenously administered glucagon-like peptide I are rapidly degraded from the NH2-terminus in type II diabetic patients and in healthy subjects Diabetes 1995, 44, 1126-1131
    • (1995) Diabetes , vol.44 , pp. 1126-1131
    • Deacon, C.F.1    Nauck, M.A.2    Toft-Nielsen, M.3    Pridal, L.4    Willms, B.5    Holst, J.J.6
  • 19
    • 0038359686 scopus 로고    scopus 로고
    • Effects of GLP-1-(7-36)NH2, GLP-1-(7-37), and GLP-1- (9-36)NH2 on intravenous glucose tolerance and glucose-induced insulin secretion in healthy humans
    • Vahl, T. P.; Paty, B. W.; Fuller, B. D.; Prigeon, R. L.; DAlessio, D. A. Effects of GLP-1-(7-36)NH2, GLP-1-(7-37), and GLP-1- (9-36)NH2 on intravenous glucose tolerance and glucose-induced insulin secretion in healthy humans J. Clin. Endocrinol. Metab. 2003, 88, 1772-1779
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 1772-1779
    • Vahl, T.P.1    Paty, B.W.2    Fuller, B.D.3    Prigeon, R.L.4    Dalessio, D.A.5
  • 20
  • 21
    • 0036081143 scopus 로고    scopus 로고
    • GLP-1-(9-36) amide reduces blood glucose in anesthetized pigs by a mechanism that does not involve insulin secretion
    • Deacon, C. F.; Plamboeck, A.; Møller, S.; Holst, J. J. GLP-1-(9-36) amide reduces blood glucose in anesthetized pigs by a mechanism that does not involve insulin secretion Am. J. Physiol.: Endocrinol. Metabol. 2002, 282, E873-E879
    • (2002) Am. J. Physiol.: Endocrinol. Metabol. , vol.282 , pp. 873-E879
    • Deacon, C.F.1    Plamboeck, A.2    Møller, S.3    Holst, J.J.4
  • 22
    • 28144441354 scopus 로고    scopus 로고
    • Active metabolite of GLP-1 mediates myocardial glucose uptake and improves left ventricular performance in conscious dogs with dilated cardiomyopathy
    • Nikolaidis, L. A.; Elahi, D.; Shen, Y.-T.; Shannon, R. P. Active metabolite of GLP-1 mediates myocardial glucose uptake and improves left ventricular performance in conscious dogs with dilated cardiomyopathy Am. J. Physiol.: Heart Circ. Physiol. 2005, 289, H2401-H2408
    • (2005) Am. J. Physiol.: Heart Circ. Physiol. , vol.289 , pp. 2401-H2408
    • Nikolaidis, L.A.1    Elahi, D.2    Shen, Y.-T.3    Shannon, R.P.4
  • 23
    • 24944436267 scopus 로고    scopus 로고
    • Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig
    • Plamboeck, A.; Holst, J.; Carr, R.; Deacon, C. Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig Diabetologia 2005, 48, 1882-1890
    • (2005) Diabetologia , vol.48 , pp. 1882-1890
    • Plamboeck, A.1    Holst, J.2    Carr, R.3    Deacon, C.4
  • 26
    • 34249891874 scopus 로고    scopus 로고
    • Effects of once-weekly dosing of a long-acting release formulation of exenatide on glucose control and body weight in subjects with type 2 diabetes
    • Kim, D.; MacConell, L.; Zhuang, D.; Kothare, P. A.; Trautmann, M.; Fineman, M.; Taylor, K. Effects of once-weekly dosing of a long-acting release formulation of exenatide on glucose control and body weight in subjects with type 2 diabetes Diabetes Care 2007, 30, 1487-1493
    • (2007) Diabetes Care , vol.30 , pp. 1487-1493
    • Kim, D.1    Macconell, L.2    Zhuang, D.3    Kothare, P.A.4    Trautmann, M.5    Fineman, M.6    Taylor, K.7
  • 30
    • 0031465992 scopus 로고    scopus 로고
    • The positive charge of the imidazole side chain of histidine7 is crucial for GLP-1 action
    • Hareter, A.; Hoffmann, E.; Bode, H. P.; Goke, B.; Goke, R. The positive charge of the imidazole side chain of histidine7 is crucial for GLP-1 action Endocr. J. 1997, 44, 701-705
    • (1997) Endocr. J. , vol.44 , pp. 701-705
    • Hareter, A.1    Hoffmann, E.2    Bode, H.P.3    Goke, B.4    Goke, R.5
  • 33
    • 1842530457 scopus 로고    scopus 로고
    • N-terminal His(7)-modification of glucagon-like peptide-1(7-36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity
    • Green, B. D.; Mooney, M. H.; Gault, V. A.; Irwin, N.; Bailey, C. J.; Harriott, P.; Greer, B.; OHarte, F. P.; Flatt, P. R. N-terminal His(7)-modification of glucagon-like peptide-1(7-36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity J. Endocrinol. 2004, 180, 379-388
    • (2004) J. Endocrinol. , vol.180 , pp. 379-388
    • Green, B.D.1    Mooney, M.H.2    Gault, V.A.3    Irwin, N.4    Bailey, C.J.5    Harriott, P.6    Greer, B.7    Oharte, F.P.8    Flatt, P.R.9
  • 34
    • 0033974696 scopus 로고    scopus 로고
    • N-terminally modified glucagon-like peptide-1(7-36) amide exhibits resistance to enzymatic degradation while maintaining its antihyperglycaemic activity in vivo
    • OHarte, F. P.; Mooney, M. H.; Lawlor, A.; Flatt, P. R. N-terminally modified glucagon-like peptide-1(7-36) amide exhibits resistance to enzymatic degradation while maintaining its antihyperglycaemic activity in vivo Biochim. Biophys. Acta 2000, 1474, 13-22
    • (2000) Biochim. Biophys. Acta , vol.1474 , pp. 13-22
    • Oharte, F.P.1    Mooney, M.H.2    Lawlor, A.3    Flatt, P.R.4
  • 35
    • 33845207048 scopus 로고    scopus 로고
    • Evaluation of therapeutic potentials of site-specific PEGylated glucagon-like peptide-1 isomers as a type 2 anti-diabetic treatment: Insulinotropic activity, glucose-stabilizing capability, and proteolytic stability
    • Youn, Y. S.; Chae, S. Y.; Lee, S.; Jeon, J. E.; Shin, H. G.; Lee, K. C. Evaluation of therapeutic potentials of site-specific PEGylated glucagon-like peptide-1 isomers as a type 2 anti-diabetic treatment: insulinotropic activity, glucose-stabilizing capability, and proteolytic stability Biochem. Pharmacol. 2007, 73, 84-93
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 84-93
    • Youn, Y.S.1    Chae, S.Y.2    Lee, S.3    Jeon, J.E.4    Shin, H.G.5    Lee, K.C.6
  • 36
    • 0033005873 scopus 로고    scopus 로고
    • Long-lasting antidiabetic effect of a dipeptidyl peptidase IV-resistant analog of glucagon-like peptide-1
    • Burcelin, R.; Dolci, W.; Thorens, B. Long-lasting antidiabetic effect of a dipeptidyl peptidase IV-resistant analog of glucagon-like peptide-1 Metabolism 1999, 48, 252-258
    • (1999) Metabolism , vol.48 , pp. 252-258
    • Burcelin, R.1    Dolci, W.2    Thorens, B.3
  • 37
    • 0031782440 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity
    • Deacon, C. F.; Knudsen, L. B.; Madsen, K.; Wiberg, F. C.; Jacobsen, O.; Holst, J. J. Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity Diabetologia 1998, 41, 271-278
    • (1998) Diabetologia , vol.41 , pp. 271-278
    • Deacon, C.F.1    Knudsen, L.B.2    Madsen, K.3    Wiberg, F.C.4    Jacobsen, O.5    Holst, J.J.6
  • 39
    • 0842284596 scopus 로고    scopus 로고
    • Lys9 for Glu9 substitution in glucagon-like peptide-1(7-36)amide confers dipeptidylpeptidase IV resistance with cellular and metabolic actions similar to those of established antagonists glucagon-like peptide-1(9-36)amide and exendin (9-39)
    • Green, B. D.; Mooney, M. H.; Gault, V. A.; Irwin, N.; Bailey, C. J.; Harriott, P.; Greer, B.; Flatt, P. R.; OHarte, F. P. Lys9 for Glu9 substitution in glucagon-like peptide-1(7-36)amide confers dipeptidylpeptidase IV resistance with cellular and metabolic actions similar to those of established antagonists glucagon-like peptide-1(9-36)amide and exendin (9-39) Metabolism 2004, 53, 252-259
    • (2004) Metabolism , vol.53 , pp. 252-259
    • Green, B.D.1    Mooney, M.H.2    Gault, V.A.3    Irwin, N.4    Bailey, C.J.5    Harriott, P.6    Greer, B.7    Flatt, P.R.8    Oharte, F.P.9
  • 40
    • 0346728540 scopus 로고    scopus 로고
    • Metabolic stability, receptor binding, cAMP generation, insulin secretion and antihyperglycaemic activity of novel N-terminal Glu9-substituted analogues of glucagon-like peptide-1
    • Green, B. D.; Gault, V. A.; Irwin, N.; Mooney, M. H.; Bailey, C. J.; Harriott, P.; Greer, B.; Flatt, P. R.; OHarte, F. P. Metabolic stability, receptor binding, cAMP generation, insulin secretion and antihyperglycaemic activity of novel N-terminal Glu9-substituted analogues of glucagon-like peptide-1 Biol. Chem. 2003, 384, 1543-1551
    • (2003) Biol. Chem. , vol.384 , pp. 1543-1551
    • Green, B.D.1    Gault, V.A.2    Irwin, N.3    Mooney, M.H.4    Bailey, C.J.5    Harriott, P.6    Greer, B.7    Flatt, P.R.8    Oharte, F.P.9
  • 41
    • 56749149571 scopus 로고    scopus 로고
    • Influence of selective fluorination on the biological activity and proteolytic stability of glucagon-like peptide-1
    • Meng, H.; Krishnaji, S. T.; Beinborn, M.; Kumar, K. Influence of selective fluorination on the biological activity and proteolytic stability of glucagon-like peptide-1 J. Med. Chem. 2008, 51, 7303-7307
    • (2008) J. Med. Chem. , vol.51 , pp. 7303-7307
    • Meng, H.1    Krishnaji, S.T.2    Beinborn, M.3    Kumar, K.4
  • 42
    • 0028215420 scopus 로고
    • Structure-activity relationships of glucagon-like peptide-1(7-36)amide: Insulinotropic activities in perfused rat pancreases, and receptor binding and cyclic AMP production in RINm5F cells
    • Watanabe, Y.; Kawai, K.; Ohashi, S.; Yokota, C.; Suzuki, S.; Yamashita, K. Structure-activity relationships of glucagon-like peptide-1(7-36)amide: insulinotropic activities in perfused rat pancreases, and receptor binding and cyclic AMP production in RINm5F cells J. Endocrinol. 1994, 140, 45-52
    • (1994) J. Endocrinol. , vol.140 , pp. 45-52
    • Watanabe, Y.1    Kawai, K.2    Ohashi, S.3    Yokota, C.4    Suzuki, S.5    Yamashita, K.6
  • 43
    • 0003288306 scopus 로고    scopus 로고
    • The insulinotropic gut hormone glucagon like peptide-1
    • Belfiore, F. Karger: Basel, Switzerland
    • Fehmann, H. C.; Goke, B. The insulinotropic gut hormone glucagon like peptide-1. In Frontiers in Diabetes; Belfiore, F., Ed.; Karger: Basel, Switzerland, 1997; Vol. 13, pp 1-99.
    • (1997) Frontiers in Diabetes , vol.13 , pp. 1-99
    • Fehmann, H.C.1    Goke, B.2
  • 45
    • 75449096219 scopus 로고    scopus 로고
    • Design, synthesis and in vitro characterization of glucagon-like peptide-1 derivatives for pancreatic beta cell imaging by SPECT
    • Behnam Azad, B.; Rota, V. A.; Breadner, D.; Dhanvantari, S.; Luyt, L. G. Design, synthesis and in vitro characterization of glucagon-like peptide-1 derivatives for pancreatic beta cell imaging by SPECT Bioorg. Med. Chem. 2010, 18, 1265-1272
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 1265-1272
    • Behnam Azad, B.1    Rota, V.A.2    Breadner, D.3    Dhanvantari, S.4    Luyt, L.G.5
  • 46
    • 1842687009 scopus 로고    scopus 로고
    • Degradation, receptor binding, insulin secreting and antihyperglycaemic actions of palmitate-derivatised native and Ala8-substituted GLP-1 analogues
    • Green, B. D.; Gault, V. A.; Mooney, M. H.; Irwin, N.; Harriott, P.; Greer, B.; Bailey, C. J.; OHarte, F. P.; Flatt, P. R. Degradation, receptor binding, insulin secreting and antihyperglycaemic actions of palmitate-derivatised native and Ala8-substituted GLP-1 analogues Biol. Chem. 2004, 385, 169-177
    • (2004) Biol. Chem. , vol.385 , pp. 169-177
    • Green, B.D.1    Gault, V.A.2    Mooney, M.H.3    Irwin, N.4    Harriott, P.5    Greer, B.6    Bailey, C.J.7    Oharte, F.P.8    Flatt, P.R.9
  • 49
    • 78649707525 scopus 로고    scopus 로고
    • Discovery and characterization of taspoglutide, a novel analogue of human glucagon-like peptide-1, engineered for sustained therapeutic activity in type 2 diabetes
    • Dong, J. Z.; Shen, Y.; Zhang, J.; Tsomaia, N.; Mierke, D. F.; Taylor, J. E. Discovery and characterization of taspoglutide, a novel analogue of human glucagon-like peptide-1, engineered for sustained therapeutic activity in type 2 diabetes Diabetes Obes. Metab. 2011, 13, 19-25
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 19-25
    • Dong, J.Z.1    Shen, Y.2    Zhang, J.3    Tsomaia, N.4    Mierke, D.F.5    Taylor, J.E.6
  • 50
    • 75249100556 scopus 로고    scopus 로고
    • Insulin-like actions of glucagon-like peptide-1: A dual receptor hypothesis
    • Tomas, E.; Habener, J. F. Insulin-like actions of glucagon-like peptide-1: a dual receptor hypothesis Trends Endocrinol. Metab. 2010, 21, 59-67
    • (2010) Trends Endocrinol. Metab. , vol.21 , pp. 59-67
    • Tomas, E.1    Habener, J.F.2
  • 52
    • 84901919235 scopus 로고    scopus 로고
    • GLP-1[28-36] exerts direct cardioprotective effects, activating pro-survival kinases and soluble adenylyl cyclase
    • Mundil, D.; Beca, S.; Cameron-Vendrig, A.; El-Mounayri, O.; Momen, A.; Backx, P. H.; Husain, M. GLP-1[28-36] exerts direct cardioprotective effects, activating pro-survival kinases and soluble adenylyl cyclase Circulation 2012, 126, 13657
    • (2012) Circulation , vol.126 , pp. 13657
    • Mundil, D.1    Beca, S.2    Cameron-Vendrig, A.3    El-Mounayri, O.4    Momen, A.5    Backx, P.H.6    Husain, M.7
  • 53
    • 84904541595 scopus 로고    scopus 로고
    • GLP-1(32-36)amide, a novel pentapeptide cleavage product of GLP-1, modulates whole body glucose metabolism in dogs
    • Elahi, D.; Angeli, F. S.; Vakilipour, A.; Carlson, O. D.; Tomas, E.; Egan, J. M.; Habener, J. F.; Shannon, R. P. GLP-1(32-36)amide, a novel pentapeptide cleavage product of GLP-1, modulates whole body glucose metabolism in dogs Peptides 2014, 59, 20-24
    • (2014) Peptides , vol.59 , pp. 20-24
    • Elahi, D.1    Angeli, F.S.2    Vakilipour, A.3    Carlson, O.D.4    Tomas, E.5    Egan, J.M.6    Habener, J.F.7    Shannon, R.P.8
  • 54
    • 84901943963 scopus 로고    scopus 로고
    • GLP-1(28-36)amide, the glucagon-like peptide-1 metabolite: Friend, foe, or pharmacological folly?
    • Taing, M. W.; Rose, F. J.; Whitehead, J. P. GLP-1(28-36)amide, the glucagon-like peptide-1 metabolite: friend, foe, or pharmacological folly? Drug Des. Dev. Ther. 2014, 8, 677-688
    • (2014) Drug Des. Dev. Ther. , vol.8 , pp. 677-688
    • Taing, M.W.1    Rose, F.J.2    Whitehead, J.P.3
  • 56
    • 0028207562 scopus 로고
    • Structure of glucagon-like peptide(7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR
    • Thornton, K.; Gorenstein, D. G. Structure of glucagon-like peptide(7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR Biochemistry 1994, 33, 3532-3539
    • (1994) Biochemistry , vol.33 , pp. 3532-3539
    • Thornton, K.1    Gorenstein, D.G.2
  • 57
    • 0008739778 scopus 로고    scopus 로고
    • Structure and folding of glucagon-like peptide-1-(7-36)-amide in aqueous trifluoroethanol studied by NMR spectroscopy
    • Chang, X.; Keller, D.; Bjørn, S.; Led, J. J. Structure and folding of glucagon-like peptide-1-(7-36)-amide in aqueous trifluoroethanol studied by NMR spectroscopy Magn. Reson. Chem. 2001, 39, 477-483
    • (2001) Magn. Reson. Chem. , vol.39 , pp. 477-483
    • Chang, X.1    Keller, D.2    Bjørn, S.3    Led, J.J.4
  • 58
    • 0035818410 scopus 로고    scopus 로고
    • Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states
    • Neidigh, J. W.; Fesinmeyer, R. M.; Prickett, K. S.; Andersen, N. H. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states Biochemistry 2001, 40, 13188-13200
    • (2001) Biochemistry , vol.40 , pp. 13188-13200
    • Neidigh, J.W.1    Fesinmeyer, R.M.2    Prickett, K.S.3    Andersen, N.H.4
  • 59
    • 34248563781 scopus 로고    scopus 로고
    • Differential structural properties of GLP-1 and exendin-4 determine their relative affinity for the GLP-1 receptor N-terminal extracellular domain
    • Runge, S.; Schimmer, S.; Oschmann, J.; Schiødt, C. B.; Knudsen, S. M.; Jeppesen, C. B.; Madsen, K.; Lau, J.; Thøgersen, H.; Rudolph, R. Differential structural properties of GLP-1 and exendin-4 determine their relative affinity for the GLP-1 receptor N-terminal extracellular domain Biochemistry 2007, 46, 5830-5840
    • (2007) Biochemistry , vol.46 , pp. 5830-5840
    • Runge, S.1    Schimmer, S.2    Oschmann, J.3    Schiødt, C.B.4    Knudsen, S.M.5    Jeppesen, C.B.6    Madsen, K.7    Lau, J.8    Thøgersen, H.9    Rudolph, R.10
  • 60
    • 77954870787 scopus 로고    scopus 로고
    • The major determinant of exendin-4/glucagon-like peptide 1 differential affinity at the rat glucagon-like peptide 1 receptor N-terminal domain is a hydrogen bond from SER-32 of exendin-4
    • Mann, R. J.; Nasr, N. E.; Sinfield, J. K.; Paci, E.; Donnelly, D. The major determinant of exendin-4/glucagon-like peptide 1 differential affinity at the rat glucagon-like peptide 1 receptor N-terminal domain is a hydrogen bond from SER-32 of exendin-4 Br. J. Pharmacol. 2010, 160, 1973-1984
    • (2010) Br. J. Pharmacol. , vol.160 , pp. 1973-1984
    • Mann, R.J.1    Nasr, N.E.2    Sinfield, J.K.3    Paci, E.4    Donnelly, D.5
  • 61
    • 73649107900 scopus 로고    scopus 로고
    • Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor
    • Underwood, C. R.; Garibay, P.; Knudsen, L. B.; Hastrup, S.; Peters, G. H.; Rudolph, R.; Reedtz-Runge, S. Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor J. Biol. Chem. 2010, 285, 723-730
    • (2010) J. Biol. Chem. , vol.285 , pp. 723-730
    • Underwood, C.R.1    Garibay, P.2    Knudsen, L.B.3    Hastrup, S.4    Peters, G.H.5    Rudolph, R.6    Reedtz-Runge, S.7
  • 62
    • 77956419436 scopus 로고    scopus 로고
    • Recombinant expression, in vitro refolding, and biophysical characterization of the human glucagon-like peptide-1 receptor
    • Schröder-Tittmann, K.; Bosse-Doenecke, E.; Reedtz-Runge, S.; Ihling, C.; Sinz, A.; Tittmann, K.; Rudolph, R. Recombinant expression, in vitro refolding, and biophysical characterization of the human glucagon-like peptide-1 receptor Biochemistry 2010, 49, 7956-7965
    • (2010) Biochemistry , vol.49 , pp. 7956-7965
    • Schröder-Tittmann, K.1    Bosse-Doenecke, E.2    Reedtz-Runge, S.3    Ihling, C.4    Sinz, A.5    Tittmann, K.6    Rudolph, R.7
  • 63
    • 71749104270 scopus 로고    scopus 로고
    • Molecular basis of glucagon-like peptide 1 docking to its intact receptor studied with carboxyl-terminal photolabile probes
    • Chen, Q.; Pinon, D. I.; Miller, L. J.; Dong, M. Molecular basis of glucagon-like peptide 1 docking to its intact receptor studied with carboxyl-terminal photolabile probes J. Biol. Chem. 2009, 284, 34135-34144
    • (2009) J. Biol. Chem. , vol.284 , pp. 34135-34144
    • Chen, Q.1    Pinon, D.I.2    Miller, L.J.3    Dong, M.4
  • 64
    • 77955302857 scopus 로고    scopus 로고
    • Spatial approximations between residues 6 and 12 in the amino-terminal region of glucagon-like peptide 1 and its receptor
    • Chen, Q.; Pinon, D. I.; Miller, L. J.; Dong, M. Spatial approximations between residues 6 and 12 in the amino-terminal region of glucagon-like peptide 1 and its receptor J. Biol. Chem. 2010, 285, 24508-24518
    • (2010) J. Biol. Chem. , vol.285 , pp. 24508-24518
    • Chen, Q.1    Pinon, D.I.2    Miller, L.J.3    Dong, M.4
  • 65
    • 79955540676 scopus 로고    scopus 로고
    • Refinement of glucagon-like peptide 1 docking to its intact receptor using mid-region photolabile probes and molecular modeling
    • Miller, L. J.; Chen, Q.; Lam, P. C.-H.; Pinon, D. I.; Sexton, P. M.; Abagyan, R.; Dong, M. Refinement of glucagon-like peptide 1 docking to its intact receptor using mid-region photolabile probes and molecular modeling J. Biol. Chem. 2011, 286, 15895-15907
    • (2011) J. Biol. Chem. , vol.286 , pp. 15895-15907
    • Miller, L.J.1    Chen, Q.2    Lam, P.C.-H.3    Pinon, D.I.4    Sexton, P.M.5    Abagyan, R.6    Dong, M.7
  • 66
    • 1542578694 scopus 로고    scopus 로고
    • Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues
    • Lopez de Maturana, R.; Treece-Birch, J.; Abidi, F.; Findlay, J. B.; Donnelly, D. Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues Protein Pept. Lett. 2004, 11, 15-22
    • (2004) Protein Pept. Lett. , vol.11 , pp. 15-22
    • Lopez De Maturana, R.1    Treece-Birch, J.2    Abidi, F.3    Findlay, J.B.4    Donnelly, D.5
  • 67
    • 0142169387 scopus 로고    scopus 로고
    • The positive charge at Lys-288 of the glucagon-like peptide-1 (GLP-1) receptor is important for binding the N-terminus of peptide agonists
    • Al-Sabah, S.; Donnelly, D. The positive charge at Lys-288 of the glucagon-like peptide-1 (GLP-1) receptor is important for binding the N-terminus of peptide agonists FEBS Lett. 2003, 553, 342-346
    • (2003) FEBS Lett. , vol.553 , pp. 342-346
    • Al-Sabah, S.1    Donnelly, D.2
  • 68
    • 0037163906 scopus 로고    scopus 로고
    • The glucagon-like peptide-1 receptor binding site for the N-terminus of GLP-1 requires polarity at Asp198 rather than negative charge
    • Lopez de Maturana, R.; Donnelly, D. The glucagon-like peptide-1 receptor binding site for the N-terminus of GLP-1 requires polarity at Asp198 rather than negative charge FEBS Lett. 2002, 530, 244-248
    • (2002) FEBS Lett. , vol.530 , pp. 244-248
    • Lopez De Maturana, R.1    Donnelly, D.2
  • 69
    • 45549086826 scopus 로고    scopus 로고
    • Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
    • Runge, S.; Thogersen, H.; Madsen, K.; Lau, J.; Rudolph, R. Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain J. Biol. Chem. 2008, 283, 11340-11347
    • (2008) J. Biol. Chem. , vol.283 , pp. 11340-11347
    • Runge, S.1    Thogersen, H.2    Madsen, K.3    Lau, J.4    Rudolph, R.5
  • 70
    • 0037518197 scopus 로고    scopus 로고
    • The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1
    • Lopez de Maturana, R.; Willshaw, A.; Kuntzsch, A.; Rudolph, R.; Donnelly, D. The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1 J. Biol. Chem. 2003, 278, 10195-10200
    • (2003) J. Biol. Chem. , vol.278 , pp. 10195-10200
    • Lopez De Maturana, R.1    Willshaw, A.2    Kuntzsch, A.3    Rudolph, R.4    Donnelly, D.5
  • 71
    • 55749095379 scopus 로고    scopus 로고
    • Search for alpha-helical propensity in the receptor-bound conformation of glucagon-like peptide-1
    • Murage, E. N.; Schroeder, J. C.; Beinborn, M.; Ahn, J.-M. Search for alpha-helical propensity in the receptor-bound conformation of glucagon-like peptide-1 Bioorg. Med. Chem. 2008, 16, 10106-10112
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 10106-10112
    • Murage, E.N.1    Schroeder, J.C.2    Beinborn, M.3    Ahn, J.-M.4
  • 72
    • 0035855890 scopus 로고    scopus 로고
    • A new approach to search for the bioactive conformation of glucagon: Positional cyclization scanning
    • Ahn, J.-M.; Gitu, P. M.; Medeiros, M.; Swift, J. R.; Trivedi, D.; Hruby, V. J. A new approach to search for the bioactive conformation of glucagon: positional cyclization scanning J. Med. Chem. 2001, 44, 3109-3116
    • (2001) J. Med. Chem. , vol.44 , pp. 3109-3116
    • Ahn, J.-M.1    Gitu, P.M.2    Medeiros, M.3    Swift, J.R.4    Trivedi, D.5    Hruby, V.J.6
  • 73
    • 77956331314 scopus 로고    scopus 로고
    • Development of potent glucagon-like peptide-1 agonists with high enzyme stability via introduction of multiple lactam bridges
    • Murage, E. N.; Gao, G.; Bisello, A.; Ahn, J.-M. Development of potent glucagon-like peptide-1 agonists with high enzyme stability via introduction of multiple lactam bridges J. Med. Chem. 2010, 53, 6412-6420
    • (2010) J. Med. Chem. , vol.53 , pp. 6412-6420
    • Murage, E.N.1    Gao, G.2    Bisello, A.3    Ahn, J.-M.4
  • 74
    • 27844447147 scopus 로고    scopus 로고
    • Immunogenetics of type 1 diabetes
    • Kim, M. S.; Polychronakos, C. Immunogenetics of type 1 diabetes Horm. Res. 2005, 64, 180-188
    • (2005) Horm. Res. , vol.64 , pp. 180-188
    • Kim, M.S.1    Polychronakos, C.2
  • 76
    • 0027953703 scopus 로고
    • Banting Lecture. Insulin action, diabetogenes, and the cause of type II diabetes
    • Kahn, C. R. Banting Lecture. Insulin action, diabetogenes, and the cause of type II diabetes Diabetes 1994, 43, 1066-1084
    • (1994) Diabetes , vol.43 , pp. 1066-1084
    • Kahn, C.R.1
  • 78
    • 23044518919 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 (GLP-1) and the control of glucose metabolism in mammals and teleost fish
    • Mojsov, S. Glucagon-like peptide-1 (GLP-1) and the control of glucose metabolism in mammals and teleost fish Am. Zool. 2000, 40, 246-258
    • (2000) Am. Zool. , vol.40 , pp. 246-258
    • Mojsov, S.1
  • 80
    • 77649102941 scopus 로고    scopus 로고
    • Effects of incretin hormones on beta-cell mass and function, body weight, and hepatic and myocardial function
    • Mudaliar, S.; Henry, R. R. Effects of incretin hormones on beta-cell mass and function, body weight, and hepatic and myocardial function Am. J. Med. 2010, 123, S19-S27
    • (2010) Am. J. Med. , vol.123 , pp. 19-S27
    • Mudaliar, S.1    Henry, R.R.2
  • 81
    • 75149128665 scopus 로고    scopus 로고
    • Incretin-based therapies for the treatment of type 2 diabetes: Evaluation of the risks and benefits
    • Drucker, D. J.; Sherman, S. I.; Gorelick, F. S.; Bergenstal, R. M.; Sherwin, R. S.; Buse, J. B. Incretin-based therapies for the treatment of type 2 diabetes: evaluation of the risks and benefits Diabetes Care 2010, 33, 428-433
    • (2010) Diabetes Care , vol.33 , pp. 428-433
    • Drucker, D.J.1    Sherman, S.I.2    Gorelick, F.S.3    Bergenstal, R.M.4    Sherwin, R.S.5    Buse, J.B.6
  • 82
    • 75149182370 scopus 로고    scopus 로고
    • GLP-1-based therapy for diabetes: What you do not know can hurt you
    • Butler, P. C.; Dry, S.; Elashoff, R. GLP-1-based therapy for diabetes: What you do not know can hurt you Diabetes Care 2010, 33, 453-455
    • (2010) Diabetes Care , vol.33 , pp. 453-455
    • Butler, P.C.1    Dry, S.2    Elashoff, R.3
  • 83
    • 21744440422 scopus 로고    scopus 로고
    • Structure and function studies of glucagon-like peptide-1 (GLP-1): The designing of a novel pharmacological agent for the treatment of diabetes
    • Hui, H.; Zhao, X.; Perfetti, R. Structure and function studies of glucagon-like peptide-1 (GLP-1): the designing of a novel pharmacological agent for the treatment of diabetes Diabetes Metab. Res. Rev. 2005, 21, 313-331
    • (2005) Diabetes Metab. Res. Rev. , vol.21 , pp. 313-331
    • Hui, H.1    Zhao, X.2    Perfetti, R.3
  • 84
    • 67651173077 scopus 로고    scopus 로고
    • Incretin-based therapies for type 2 diabetes mellitus
    • Lovshin, J. A.; Drucker, D. J. Incretin-based therapies for type 2 diabetes mellitus Nat. Rev. Endocrinol. 2009, 5, 262-269
    • (2009) Nat. Rev. Endocrinol. , vol.5 , pp. 262-269
    • Lovshin, J.A.1    Drucker, D.J.2
  • 85
    • 57649232757 scopus 로고    scopus 로고
    • Molecular, pharmacological and clinical aspects of liraglutide, a once-daily human GLP-1 analogue
    • Russell-Jones, D. Molecular, pharmacological and clinical aspects of liraglutide, a once-daily human GLP-1 analogue Mol. Cell. Endocrinol. 2009, 297, 137-140
    • (2009) Mol. Cell. Endocrinol. , vol.297 , pp. 137-140
    • Russell-Jones, D.1
  • 88
    • 79955014687 scopus 로고    scopus 로고
    • Mono-PEGylated dimeric exendin-4 as high receptor binding and long-acting conjugates for type 2 anti-diabetes therapeutics
    • Kim, T. H.; Jiang, H. H.; Lee, S.; Youn, Y. S.; Park, C. W.; Byun, Y.; Chen, X.; Lee, K. C. Mono-PEGylated dimeric exendin-4 as high receptor binding and long-acting conjugates for type 2 anti-diabetes therapeutics Bioconjugate Chem. 2011, 22, 625-632
    • (2011) Bioconjugate Chem. , vol.22 , pp. 625-632
    • Kim, T.H.1    Jiang, H.H.2    Lee, S.3    Youn, Y.S.4    Park, C.W.5    Byun, Y.6    Chen, X.7    Lee, K.C.8
  • 89
    • 0026648961 scopus 로고
    • Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas
    • Eng, J.; Kleinman, W. A.; Singh, L.; Singh, G.; Raufman, J. P. Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas J. Biol. Chem. 1992, 267, 7402-7405
    • (1992) J. Biol. Chem. , vol.267 , pp. 7402-7405
    • Eng, J.1    Kleinman, W.A.2    Singh, L.3    Singh, G.4    Raufman, J.P.5
  • 90
    • 0036235563 scopus 로고    scopus 로고
    • Endoproteolysis by isolated membrane peptidases reveal metabolic stability of glucagon-like peptide-1 analogs, exendins-3 and -4
    • Thum, A.; Hupe-Sodmann, K.; Goke, R.; Voigt, K.; Goke, B.; McGregor, G. Endoproteolysis by isolated membrane peptidases reveal metabolic stability of glucagon-like peptide-1 analogs, exendins-3 and -4 Exp. Clin. Endocrinol. Diabetes 2002, 110, 113-118
    • (2002) Exp. Clin. Endocrinol. Diabetes , vol.110 , pp. 113-118
    • Thum, A.1    Hupe-Sodmann, K.2    Goke, R.3    Voigt, K.4    Goke, B.5    McGregor, G.6
  • 91
    • 67349176115 scopus 로고    scopus 로고
    • Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes
    • Ahren, B. Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes Nat. Rev. Drug Discovery 2009, 8, 369-385
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 369-385
    • Ahren, B.1
  • 92
    • 75649136250 scopus 로고    scopus 로고
    • Benefit-risk assessment of exenatide in the therapy of type 2 diabetes mellitus
    • Gallwitz, B. Benefit-risk assessment of exenatide in the therapy of type 2 diabetes mellitus Drug Saf. 2010, 33, 87-100
    • (2010) Drug Saf. , vol.33 , pp. 87-100
    • Gallwitz, B.1
  • 93
    • 77955847376 scopus 로고    scopus 로고
    • Pharmacological profile of lixisenatide: A new GLP-1 receptor agonist for the treatment of type 2 diabetes
    • Werner, U.; Haschke, G.; Herling, A. W.; Kramer, W. Pharmacological profile of lixisenatide: A new GLP-1 receptor agonist for the treatment of type 2 diabetes Regul. Pept. 2010, 164, 58-64
    • (2010) Regul. Pept. , vol.164 , pp. 58-64
    • Werner, U.1    Haschke, G.2    Herling, A.W.3    Kramer, W.4
  • 94
    • 68549099651 scopus 로고    scopus 로고
    • Lixisenatide, a novel GLP-1 receptor agonist for the treatment of type 2 diabetes mellitus
    • Christensen, M.; Knop, F. K.; Holst, J. J.; Vilsboll, T. Lixisenatide, a novel GLP-1 receptor agonist for the treatment of type 2 diabetes mellitus IDrugs 2009, 12, 503-513
    • (2009) IDrugs , vol.12 , pp. 503-513
    • Christensen, M.1    Knop, F.K.2    Holst, J.J.3    Vilsboll, T.4
  • 95
    • 0036676385 scopus 로고    scopus 로고
    • Pharmacokinetics, pharmacodynamics, safety, and tolerability of a single-dose of NN2211, a long-acting glucagon-like peptide 1 derivative, in healthy male subjects
    • Elbrond, B.; Jakobsen, G.; Larsen, S.; Agerso, H.; Jensen, L. B.; Rolan, P.; Sturis, J.; Hatorp, V.; Zdravkovic, M. Pharmacokinetics, pharmacodynamics, safety, and tolerability of a single-dose of NN2211, a long-acting glucagon-like peptide 1 derivative, in healthy male subjects Diabetes Care 2002, 25, 1398-1404
    • (2002) Diabetes Care , vol.25 , pp. 1398-1404
    • Elbrond, B.1    Jakobsen, G.2    Larsen, S.3    Agerso, H.4    Jensen, L.B.5    Rolan, P.6    Sturis, J.7    Hatorp, V.8    Zdravkovic, M.9
  • 96
    • 37849026464 scopus 로고    scopus 로고
    • Structure-activity and protraction relationship of long-acting glucagon-like peptide-1 derivatives: Importance of fatty acid length, polarity, and bulkiness
    • Madsen, K.; Knudsen, L. B.; Agersoe, H.; Nielsen, P. F.; Thøgersen, H.; Wilken, M.; Johansen, N. L. Structure-activity and protraction relationship of long-acting glucagon-like peptide-1 derivatives: importance of fatty acid length, polarity, and bulkiness J. Med. Chem. 2007, 50, 6126-6132
    • (2007) J. Med. Chem. , vol.50 , pp. 6126-6132
    • Madsen, K.1    Knudsen, L.B.2    Agersoe, H.3    Nielsen, P.F.4    Thøgersen, H.5    Wilken, M.6    Johansen, N.L.7
  • 97
    • 79953040963 scopus 로고    scopus 로고
    • An overview of once-weekly GLP-1 receptor agonists-available efficacy and safety data and perspectives for the future
    • Madsbad, S.; Kielgast, U.; Asmar, M.; Deacon, C.; Torekov, S. S.; Holst, J. J. An overview of once-weekly GLP-1 receptor agonists-available efficacy and safety data and perspectives for the future Diabetes Obes. Metab. 2011, 13, 394-407
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 394-407
    • Madsbad, S.1    Kielgast, U.2    Asmar, M.3    Deacon, C.4    Torekov, S.S.5    Holst, J.J.6
  • 98
    • 70350764845 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic properties of taspoglutide, a once-weekly, human GLP-1 analogue, after single-dose administration in patients with type 2 diabetes
    • Kapitza, C.; Heise, T.; Birman, P.; Jallet, K.; Ramis, J.; Balena, R. Pharmacokinetic and pharmacodynamic properties of taspoglutide, a once-weekly, human GLP-1 analogue, after single-dose administration in patients with type 2 diabetes Diabet. Med. 2009, 26, 1156-1164
    • (2009) Diabet. Med. , vol.26 , pp. 1156-1164
    • Kapitza, C.1    Heise, T.2    Birman, P.3    Jallet, K.4    Ramis, J.5    Balena, R.6
  • 99
    • 71049141403 scopus 로고    scopus 로고
    • Preparation and structural, biochemical, and pharmaceutical characterizations of bile acid-modified long-acting exendin-4 derivatives
    • Son, S.; Chae, S. Y.; Kim, C. W.; Choi, Y. G.; Jung, S. Y.; Lee, S.; Lee, K. C. Preparation and structural, biochemical, and pharmaceutical characterizations of bile acid-modified long-acting exendin-4 derivatives J. Med. Chem. 2009, 52, 6889-6896
    • (2009) J. Med. Chem. , vol.52 , pp. 6889-6896
    • Son, S.1    Chae, S.Y.2    Kim, C.W.3    Choi, Y.G.4    Jung, S.Y.5    Lee, S.6    Lee, K.C.7
  • 102
    • 41349098117 scopus 로고    scopus 로고
    • An albumin-exendin-4 conjugate engages central and peripheral circuits regulating murine energy and glucose homeostasis
    • Baggio, L. L.; Huang, Q.; Cao, X.; Drucker, D. J. An albumin-exendin-4 conjugate engages central and peripheral circuits regulating murine energy and glucose homeostasis Gastroenterology 2008, 134, 1137-1147
    • (2008) Gastroenterology , vol.134 , pp. 1137-1147
    • Baggio, L.L.1    Huang, Q.2    Cao, X.3    Drucker, D.J.4
  • 103
    • 84866435806 scopus 로고    scopus 로고
    • Monotherapy with the once-weekly GLP-1 analogue dulaglutide for 12 weeks in patients with type 2 diabetes: Dose-dependent effects on glycaemic control in a randomized, double-blind, placebo-controlled study
    • Grunberger, G.; Chang, A.; Garcia Soria, G.; Botros, F. T.; Bsharat, R.; Milicevic, Z. Monotherapy with the once-weekly GLP-1 analogue dulaglutide for 12 weeks in patients with type 2 diabetes: dose-dependent effects on glycaemic control in a randomized, double-blind, placebo-controlled study Diabetic Med. 2012, 29, 1260-1267
    • (2012) Diabetic Med. , vol.29 , pp. 1260-1267
    • Grunberger, G.1    Chang, A.2    Garcia Soria, G.3    Botros, F.T.4    Bsharat, R.5    Milicevic, Z.6
  • 105
    • 84922829599 scopus 로고    scopus 로고
    • Diartis presents VRS-859 positive clinical results for type 2 diabetes at 48th EASD annual meeting. (accessed Aug 21)
    • Diartis presents VRS-859 positive clinical results for type 2 diabetes at 48th EASD annual meeting. http://www.marketwired.com/press-release/diartis-presents-vrs-859-positive-clinical-results-type-2-diabetes-48th-easd-annual-1708016.htm (accessed Aug 21, 2013).
    • (2013)
  • 110
    • 84867314257 scopus 로고    scopus 로고
    • Combination of long-acting insulin with the dual GluGLP-1 agonist ZP2929 causes improved glycemic control without body weight gain in db/db mice
    • Fosgerau, K.; Skovgaard, M.; Larsen, S. A.; Baek, C. A.; Meier, E.; Groendahl, C.; Bak, H. H. Combination of long-acting insulin with the dual GluGLP-1 agonist ZP2929 causes improved glycemic control without body weight gain in db/db mice Diabetes 2011, 60, A418
    • (2011) Diabetes , vol.60 , pp. 418
    • Fosgerau, K.1    Skovgaard, M.2    Larsen, S.A.3    Baek, C.A.4    Meier, E.5    Groendahl, C.6    Bak, H.H.7
  • 111
    • 84922831353 scopus 로고    scopus 로고
    • Transition Therapeutics announces results of clinical study of type 2 diabetes drug candidate TT-401. (archived Apr 30, 2013) (accessed Aug 21)
    • Transition Therapeutics announces results of clinical study of type 2 diabetes drug candidate TT-401. http://www.transitiontherapeutics.com/media/archive.php# (archived Apr 30, 2013) (accessed Aug 21, 2013).
    • (2013)
  • 113
    • 34249067690 scopus 로고    scopus 로고
    • Review: DPP IV inhibitors-current evidence and future directions
    • Vilsbøll, T.; Knop, F. K. Review: DPP IV inhibitors-current evidence and future directions Br. J. Diabetes Vasc. Dis. 2007, 7, 69-74
    • (2007) Br. J. Diabetes Vasc. Dis. , vol.7 , pp. 69-74
    • Vilsbøll, T.1    Knop, F.K.2
  • 114
    • 33845468278 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (DPP IV) inhibitors: A newly emerging drug class for the treatment of type 2 diabetes
    • Green, B. D.; Flatt, P. R.; Bailey, C. J. Dipeptidyl peptidase IV (DPP IV) inhibitors: a newly emerging drug class for the treatment of type 2 diabetes Diabetes Vasc. Dis. Res. 2006, 3, 159-165
    • (2006) Diabetes Vasc. Dis. Res. , vol.3 , pp. 159-165
    • Green, B.D.1    Flatt, P.R.2    Bailey, C.J.3
  • 115
    • 63049125578 scopus 로고    scopus 로고
    • Emerging drug candidates of dipeptidyl peptidase IV (DPP IV) inhibitor class for the treatment of type 2 diabetes
    • Gupta, R.; Walunj, S. S.; Tokala, R. K.; Parsa, K. V.; Singh, S. K.; Pal, M. Emerging drug candidates of dipeptidyl peptidase IV (DPP IV) inhibitor class for the treatment of type 2 diabetes Curr. Drug Targets 2009, 10, 71-87
    • (2009) Curr. Drug Targets , vol.10 , pp. 71-87
    • Gupta, R.1    Walunj, S.S.2    Tokala, R.K.3    Parsa, K.V.4    Singh, S.K.5    Pal, M.6
  • 116
    • 79959773411 scopus 로고    scopus 로고
    • DPP-4 inhibitors
    • Dicker, D. DPP-4 inhibitors Diabetes Care 2011, 34, S276-S278
    • (2011) Diabetes Care , vol.34 , pp. 276-S278
    • Dicker, D.1
  • 117
    • 33846548176 scopus 로고    scopus 로고
    • Nonpeptidic glucagon-like peptide 1 receptor agonists: A magic bullet for diabetes?
    • Murphy, K. G.; Bloom, S. R. Nonpeptidic glucagon-like peptide 1 receptor agonists: A magic bullet for diabetes? Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 689-690
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 689-690
    • Murphy, K.G.1    Bloom, S.R.2
  • 119
    • 73649135313 scopus 로고    scopus 로고
    • Insulin-releasing and metabolic effects of small molecule GLP-1 receptor agonist 6,7-dichloro-2-methylsulfonyl-3- N - Tert -butylaminoquinoxaline
    • Irwin, N.; Flatt, P. R.; Patterson, S.; Green, B. D. Insulin-releasing and metabolic effects of small molecule GLP-1 receptor agonist 6,7-dichloro-2-methylsulfonyl-3- N-tert -butylaminoquinoxaline Eur. J. Pharmacol. 2010, 628, 268-273
    • (2010) Eur. J. Pharmacol. , vol.628 , pp. 268-273
    • Irwin, N.1    Flatt, P.R.2    Patterson, S.3    Green, B.D.4
  • 123
    • 78650399197 scopus 로고    scopus 로고
    • A novel 3-(8-chloro-6-(trifluoromethyl)imidazo[1,2- A ]pyridine-2-yl)phenyl acetate skeleton and pharmacophore model as glucagon-like peptide 1 receptor agonists
    • Gong, Y.-D.; Cheon, H. G.; Lee, T.; Kang, N. S. A novel 3-(8-chloro-6-(trifluoromethyl)imidazo[1,2- a ]pyridine-2-yl)phenyl acetate skeleton and pharmacophore model as glucagon-like peptide 1 receptor agonists Bull. Korean Chem. Soc. 2010, 31, 3760-3764
    • (2010) Bull. Korean Chem. Soc. , vol.31 , pp. 3760-3764
    • Gong, Y.-D.1    Cheon, H.G.2    Lee, T.3    Kang, N.S.4
  • 125
    • 84922800370 scopus 로고    scopus 로고
    • Solution structure of a GLP-1 receptor peptidomimetic agonist, Ac-SH3-GLP-1(22-36)-NH2
    • Proceedings of the 22nd American Peptide Symposium; Lebl, M. Prompt Scientific Publishing: San Diego, CA
    • Kumarasinghe, I. R.; Murage, E.; Ahn, J.-M. Solution structure of a GLP-1 receptor peptidomimetic agonist, Ac-SH3-GLP-1(22-36)-NH2. In Peptides:Building Bridges, Proceedings of the 22nd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, CA, 2011; pp 182-183.
    • (2011) Peptides:Building Bridges , pp. 182-183
    • Kumarasinghe, I.R.1    Murage, E.2    Ahn, J.-M.3
  • 126
    • 66349084499 scopus 로고    scopus 로고
    • Rational design of peptidomimetics for class B GPCRs: Potent non-peptide GLP-1 receptor agonists
    • Proceedings of the 20th American Peptide Symposium; Escher, E. Lubell, W. D. Valle, S. D. Springer: New York, NY
    • Ahn, J.-M.; Han, S.-Y.; Murage, E.; Beinborn, M. Rational design of peptidomimetics for class B GPCRs: potent non-peptide GLP-1 receptor agonists. In Peptides: Chemistry, Structure and Biology, Proceedings of the 20th American Peptide Symposium; Escher, E.; Lubell, W. D.; Valle, S. D., Eds.; Springer: New York, NY, 2009; pp 125-126.
    • (2009) Peptides: Chemistry, Structure and Biology , pp. 125-126
    • Ahn, J.-M.1    Han, S.-Y.2    Murage, E.3    Beinborn, M.4
  • 128
    • 34247138372 scopus 로고    scopus 로고
    • Facile synthesis of benzamides to mimic an a-helix
    • Ahn, J.-M.; Han, S.-Y. Facile synthesis of benzamides to mimic an a-helix Tetrahedron Lett. 2007, 48, 3543-3547
    • (2007) Tetrahedron Lett. , vol.48 , pp. 3543-3547
    • Ahn, J.-M.1    Han, S.-Y.2
  • 129
    • 79955370176 scopus 로고    scopus 로고
    • Solid-phase synthesis of tris-benzamides as α-helix mimetics
    • Lee, T.-K.; Ahn, J.-M. Solid-phase synthesis of tris-benzamides as α-helix mimetics ACS Comb. Sci. 2011, 13, 107-111
    • (2011) ACS Comb. Sci. , vol.13 , pp. 107-111
    • Lee, T.-K.1    Ahn, J.-M.2
  • 130
    • 64849087911 scopus 로고    scopus 로고
    • Biocompatible microspheres based on acetylated polysaccharide prepared from water-in-oil-in-water (W1/O/W2) double-emulsion method for delivery of type II diabetic drug (exenatide)
    • Yang, H. J.; Park, I. S.; Na, K. Biocompatible microspheres based on acetylated polysaccharide prepared from water-in-oil-in-water (W1/O/W2) double-emulsion method for delivery of type II diabetic drug (exenatide) Colloids Surf. Physicochem. Eng. Aspects 2009, 340, 115-120
    • (2009) Colloids Surf. Physicochem. Eng. Aspects , vol.340 , pp. 115-120
    • Yang, H.J.1    Park, I.S.2    Na, K.3
  • 131
    • 84873096405 scopus 로고    scopus 로고
    • A long-acting formulation of a polypeptide drug exenatide in treatment of diabetes using an injectable block copolymer hydrogel
    • Li, K.; Yu, L.; Liu, X.; Chen, C.; Chen, Q.; Ding, J. A long-acting formulation of a polypeptide drug exenatide in treatment of diabetes using an injectable block copolymer hydrogel Biomaterials 2013, 34, 2834-2842
    • (2013) Biomaterials , vol.34 , pp. 2834-2842
    • Li, K.1    Yu, L.2    Liu, X.3    Chen, C.4    Chen, Q.5    Ding, J.6
  • 133
    • 84874245248 scopus 로고    scopus 로고
    • Injectable protease-operated depots of glucagon-like peptide-1 provide extended and tunable glucose control
    • Amiram, M.; Luginbuhl, K. M.; Li, X.; Feinglos, M. N.; Chilkoti, A. Injectable protease-operated depots of glucagon-like peptide-1 provide extended and tunable glucose control Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 2792-2797
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 2792-2797
    • Amiram, M.1    Luginbuhl, K.M.2    Li, X.3    Feinglos, M.N.4    Chilkoti, A.5
  • 135
    • 79961172157 scopus 로고    scopus 로고
    • Albumin-coated porous hollow poly(lactic- co -glycolic acid) microparticles bound with palmityl-acylated exendin-4 as a long-acting inhalation delivery system for the treatment of diabetes
    • Kim, H.; Lee, J.; Kim, T.; Lee, E.; Oh, K.; Lee, D.; Park, E.-S.; Bae, Y.; Lee, K.; Youn, Y. Albumin-coated porous hollow poly(lactic- co -glycolic acid) microparticles bound with palmityl-acylated exendin-4 as a long-acting inhalation delivery system for the treatment of diabetes Pharm. Res. 2011, 28, 2008-2019
    • (2011) Pharm. Res. , vol.28 , pp. 2008-2019
    • Kim, H.1    Lee, J.2    Kim, T.3    Lee, E.4    Oh, K.5    Lee, D.6    Park, E.-S.7    Bae, Y.8    Lee, K.9    Youn, Y.10
  • 137
    • 84864648267 scopus 로고    scopus 로고
    • Delivery of two-step transcription amplification exendin-4 plasmid system with arginine-grafted bioreducible polymer in type 2 diabetes animal model
    • Kim, P.-H.; Lee, M.; Kim, S. W. Delivery of two-step transcription amplification exendin-4 plasmid system with arginine-grafted bioreducible polymer in type 2 diabetes animal model J. Controlled Release 2012, 162, 9-18
    • (2012) J. Controlled Release , vol.162 , pp. 9-18
    • Kim, P.-H.1    Lee, M.2    Kim, S.W.3
  • 138
    • 75149180515 scopus 로고    scopus 로고
    • ADA. Standards of Medical Care in Diabetes-2010
    • ADA. Standards of Medical Care in Diabetes-2010. Diabetes Care 2010, 33, S11-S61.
    • (2010) Diabetes Care , vol.33 , pp. 11-S61
  • 139
    • 53549130683 scopus 로고    scopus 로고
    • An examination of β-cell function measures and their potential use for estimating β-cell mass
    • Kahn, S. E.; Carr, D. B.; Faulenbach, M. V.; Utzschneider, K. M. An examination of β-cell function measures and their potential use for estimating β-cell mass Diabetes Obes. Metab. 2008, 10, 63-76
    • (2008) Diabetes Obes. Metab. , vol.10 , pp. 63-76
    • Kahn, S.E.1    Carr, D.B.2    Faulenbach, M.V.3    Utzschneider, K.M.4
  • 140
    • 0019887842 scopus 로고
    • Glycosylated hemoglobin as an index of diabetes mellitus control (authors transl)
    • Gomis, R.; Figuerola, D.; Micalo, T.; Millan, M.; Peig, M. Glycosylated hemoglobin as an index of diabetes mellitus control (authors transl) Med. Clin. 1981, 76, 251-254
    • (1981) Med. Clin. , vol.76 , pp. 251-254
    • Gomis, R.1    Figuerola, D.2    Micalo, T.3    Millan, M.4    Peig, M.5
  • 142
    • 53549094111 scopus 로고    scopus 로고
    • Relationship between β-cell mass and diabetes onset
    • Matveyenko, A. V.; Butler, P. C. Relationship between β-cell mass and diabetes onset Diabetes Obes. Metab. 2008, 10, 23-31
    • (2008) Diabetes Obes. Metab. , vol.10 , pp. 23-31
    • Matveyenko, A.V.1    Butler, P.C.2
  • 143
    • 33644749322 scopus 로고    scopus 로고
    • Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: Many differences, few similarities
    • Cnop, M.; Welsh, N.; Jonas, J.-C.; Jörns, A.; Lenzen, S.; Eizirik, D. L. Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: many differences, few similarities Diabetes 2005, 54 (Suppl. 2) S97-107
    • (2005) Diabetes , vol.54 , pp. 97-107
    • Cnop, M.1    Welsh, N.2    Jonas, J.-C.3    Jörns, A.4    Lenzen, S.5    Eizirik, D.L.6
  • 145
    • 7944228597 scopus 로고    scopus 로고
    • Cellular sources of new pancreatic beta cells and therapeutic implications for regenerative medicine
    • Halban, P. A. Cellular sources of new pancreatic beta cells and therapeutic implications for regenerative medicine Nat. Cell Biol. 2004, 6, 1021-1025
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1021-1025
    • Halban, P.A.1
  • 147
    • 67349225011 scopus 로고    scopus 로고
    • Advances in beta-cell imaging
    • Moore, A. Advances in beta-cell imaging Eur. J. Radiol. 2009, 70, 254-257
    • (2009) Eur. J. Radiol. , vol.70 , pp. 254-257
    • Moore, A.1
  • 149
    • 77954988574 scopus 로고    scopus 로고
    • Imaging of β-cell mass and function
    • Ichise, M.; Harris, P. E. Imaging of β-cell mass and function J. Nucl. Med. 2010, 51, 1001-1004
    • (2010) J. Nucl. Med. , vol.51 , pp. 1001-1004
    • Ichise, M.1    Harris, P.E.2
  • 152
    • 53549099095 scopus 로고    scopus 로고
    • Efforts to develop methods for in vivo evaluation of the native β-cell mass
    • Schneider, S. Efforts to develop methods for in vivo evaluation of the native β-cell mass Diabetes Obes. Metab. 2008, 10, 109-118
    • (2008) Diabetes Obes. Metab. , vol.10 , pp. 109-118
    • Schneider, S.1
  • 155
    • 38349073954 scopus 로고    scopus 로고
    • VMAT2 gene expression and function as it applies to imaging β-cell mass
    • Harris, P.; Ferrara, C.; Barba, P.; Polito, T.; Freeby, M.; Maffei, A. VMAT2 gene expression and function as it applies to imaging β-cell mass J. Mol. Med. 2008, 86, 5-16
    • (2008) J. Mol. Med. , vol.86 , pp. 5-16
    • Harris, P.1    Ferrara, C.2    Barba, P.3    Polito, T.4    Freeby, M.5    Maffei, A.6
  • 166
    • 84922793164 scopus 로고    scopus 로고
    • Highly constrained GLP-1 analogues as non-invasive PET imaging agents for the assessment of pancreatic beta-cell mass
    • Proceedings of the 22nd American Peptide Symposium; Lebl, M. Prompt Scientific Publishing: San Diego, CA
    • Ahn, J.-M.; Murage, E. N.; Lo, S.-T.; Lin, M.; Sun, X. Highly constrained GLP-1 analogues as non-invasive PET imaging agents for the assessment of pancreatic beta-cell mass. In Peptides:Building Bridges, Proceedings of the 22nd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, CA, 2011; pp 220-221.
    • (2011) Peptides:Building Bridges , pp. 220-221
    • Ahn, J.-M.1    Murage, E.N.2    Lo, S.-T.3    Lin, M.4    Sun, X.5
  • 169
    • 77957134846 scopus 로고    scopus 로고
    • GLP-1-receptor scanning for imaging of human beta cells transplanted in muscle
    • Pattou, F.; Kerr-Conte, J.; Wild, D. GLP-1-receptor scanning for imaging of human beta cells transplanted in muscle N. Engl. J. Med. 2010, 363, 1289-1290
    • (2010) N. Engl. J. Med. , vol.363 , pp. 1289-1290
    • Pattou, F.1    Kerr-Conte, J.2    Wild, D.3
  • 173
    • 84922761526 scopus 로고    scopus 로고
    • Targeting GLP-1R for non-invasive assessment of pancreatic beta-cell mass
    • Proceedings of the 23rd American Peptide Symposium; Lebl, M. Ed. Prompt Scientific Publishing: San Diego, CA
    • Manandhar, B.; Lo, S.-T.; Murage, E.; Lin, M.; Sun, X.; Ahn, J.-M. Targeting GLP-1R for non-invasive assessment of pancreatic beta-cell mass. In Peptides across the Pacific, Proceedings of the 23rd American Peptide Symposium; Lebl, M., Ed. Prompt Scientific Publishing: San Diego, CA, 2013; pp 172-173.
    • (2013) Peptides Across the Pacific , pp. 172-173
    • Manandhar, B.1    Lo, S.-T.2    Murage, E.3    Lin, M.4    Sun, X.5    Ahn, J.-M.6


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