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Volumn 56, Issue 21, 2013, Pages 8339-8351

A general method for making peptide therapeutics resistant to serine protease degradation: Application to dipeptidyl peptidase IV substrates

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LYTIC PROTEINASE; CHYMOTRYPSIN; DIPEPTIDYL PEPTIDASE 8; DIPEPTIDYL PEPTIDASE IV; GLUCAGON LIKE PEPTIDE 1 [7-36] AMIDE; GLUCAGON LIKE PEPTIDE 1 DERIVATIVE; GLUCOSE; PEPTIDE DERIVATIVE; SEPRASE; SERINE PROTEINASE; TRYPSIN; UNCLASSIFIED DRUG;

EID: 84887965583     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400423p     Document Type: Article
Times cited : (15)

References (58)
  • 1
    • 54849425126 scopus 로고    scopus 로고
    • Discovering and improving novel peptide therapeutics
    • McGregor, D. P. Discovering and improving novel peptide therapeutics Curr. Opin. Pharmacol. 2008, 8 (5) 616-619
    • (2008) Curr. Opin. Pharmacol. , vol.8 , Issue.5 , pp. 616-619
    • McGregor, D.P.1
  • 2
    • 71249091175 scopus 로고    scopus 로고
    • Current trends in the clinical development of peptide therapeutics
    • Saladin, P. M.; Zhang, B. D.; Reichert, J. M. Current trends in the clinical development of peptide therapeutics IDrugs 2009, 12 (12) 779-784
    • (2009) IDrugs , vol.12 , Issue.12 , pp. 779-784
    • Saladin, P.M.1    Zhang, B.D.2    Reichert, J.M.3
  • 3
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo
    • Deacon, C. F.; Johnsen, A. H.; Holst, J. J. Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo J. Clin. Endocrinol. Metab. 1995, 80 (3) 952-957
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , Issue.3 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3
  • 4
    • 0033766716 scopus 로고    scopus 로고
    • Degradation of endogenous and exogenous gastric inhibitory polypeptide in healthy and in type 2 diabetic subjects as revealed using a new assay for the intact peptide
    • Deacon, C. F.; Nauck, M. A.; Meier, J.; Hucking, K.; Holst, J. J. Degradation of endogenous and exogenous gastric inhibitory polypeptide in healthy and in type 2 diabetic subjects as revealed using a new assay for the intact peptide J. Clin. Endocrinol. Metab. 2000, 85 (10) 3575-3581
    • (2000) J. Clin. Endocrinol. Metab. , vol.85 , Issue.10 , pp. 3575-3581
    • Deacon, C.F.1    Nauck, M.A.2    Meier, J.3    Hucking, K.4    Holst, J.J.5
  • 5
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26) - Role in the inactivation of regulatory peptides
    • Mentlein, R. Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides Regul. Pept. 1999, 85 (1) 9-24
    • (1999) Regul. Pept. , vol.85 , Issue.1 , pp. 9-24
    • Mentlein, R.1
  • 7
    • 0023714388 scopus 로고
    • Oxyntomodulin: A potential hormone from the distal gut. Pharmacokinetics and effects on gastric acid and insulin secretion in man
    • Schjoldager, B. T.; Baldissera, F. G.; Mortensen, P. E.; Holst, J. J.; Christiansen, J. Oxyntomodulin: a potential hormone from the distal gut. Pharmacokinetics and effects on gastric acid and insulin secretion in man Eur. J. Clin. Invest. 1988, 18 (5) 499-503
    • (1988) Eur. J. Clin. Invest. , vol.18 , Issue.5 , pp. 499-503
    • Schjoldager, B.T.1    Baldissera, F.G.2    Mortensen, P.E.3    Holst, J.J.4    Christiansen, J.5
  • 8
    • 0035010093 scopus 로고    scopus 로고
    • Disappearance rate of catecholamines, total metanephrines, and neuropeptide y from the plasma of patients after resection of pheochromocytoma
    • Grouzmann, E.; Fathi, M.; Gillet, M.; de Torrente, A.; Cavadas, C.; Brunner, H.; Buclin, T. Disappearance rate of catecholamines, total metanephrines, and neuropeptide Y from the plasma of patients after resection of pheochromocytoma Clin. Chem. 2001, 47 (6) 1075-1082
    • (2001) Clin. Chem. , vol.47 , Issue.6 , pp. 1075-1082
    • Grouzmann, E.1    Fathi, M.2    Gillet, M.3    De Torrente, A.4    Cavadas, C.5    Brunner, H.6    Buclin, T.7
  • 9
    • 0032748389 scopus 로고    scopus 로고
    • Pathophysiologic relevance of measuring the plasma levels of cardiac natriuretic peptide hormones in humans
    • Clerico, A.; Iervasi, G.; Mariani, G. Pathophysiologic relevance of measuring the plasma levels of cardiac natriuretic peptide hormones in humans Horm. Metab. Res. 1999, 31 (9) 487-498
    • (1999) Horm. Metab. Res. , vol.31 , Issue.9 , pp. 487-498
    • Clerico, A.1    Iervasi, G.2    Mariani, G.3
  • 10
    • 0029044968 scopus 로고
    • Metabolism of enterostatin in rat intestine, brain membranes, and serum: Differential involvement of proline-specific peptidases
    • Bouras, M.; Huneau, J. F.; Luengo, C.; Erlanson-Albertsson, C.; Tome, D. Metabolism of enterostatin in rat intestine, brain membranes, and serum: differential involvement of proline-specific peptidases Peptides 1995, 16 (3) 399-405
    • (1995) Peptides , vol.16 , Issue.3 , pp. 399-405
    • Bouras, M.1    Huneau, J.F.2    Luengo, C.3    Erlanson-Albertsson, C.4    Tome, D.5
  • 11
    • 58149467276 scopus 로고    scopus 로고
    • Four weeks of near-normalisation of blood glucose improves the insulin response to glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide in patients with type 2 diabetes
    • Hojberg, P. V.; Vilsboll, T.; Rabol, R.; Knop, F. K.; Bache, M.; Krarup, T.; Holst, J. J.; Madsbad, S. Four weeks of near-normalisation of blood glucose improves the insulin response to glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide in patients with type 2 diabetes Diabetologia 2009, 52 (2) 199-207
    • (2009) Diabetologia , vol.52 , Issue.2 , pp. 199-207
    • Hojberg, P.V.1    Vilsboll, T.2    Rabol, R.3    Knop, F.K.4    Bache, M.5    Krarup, T.6    Holst, J.J.7    Madsbad, S.8
  • 12
    • 0027248866 scopus 로고
    • Normalization of fasting hyperglycaemia by exogenous glucagon-like peptide 1 (7-36 amide) in type 2 (non-insulin-dependent) diabetic patients
    • Nauck, M. A.; Kleine, N.; Orskov, C.; Holst, J. J.; Willms, B.; Creutzfeldt, W. Normalization of fasting hyperglycaemia by exogenous glucagon-like peptide 1 (7-36 amide) in type 2 (non-insulin-dependent) diabetic patients Diabetologia 1993, 36 (8) 741-744
    • (1993) Diabetologia , vol.36 , Issue.8 , pp. 741-744
    • Nauck, M.A.1    Kleine, N.2    Orskov, C.3    Holst, J.J.4    Willms, B.5    Creutzfeldt, W.6
  • 13
    • 0032976939 scopus 로고    scopus 로고
    • Continuous subcutaneous infusion of glucagon-like peptide 1 lowers plasma glucose and reduces appetite in type 2 diabetic patients
    • Toft-Nielsen, M. B.; Madsbad, S.; Holst, J. J. Continuous subcutaneous infusion of glucagon-like peptide 1 lowers plasma glucose and reduces appetite in type 2 diabetic patients Diabetes Care 1999, 22 (7) 1137-1143
    • (1999) Diabetes Care , vol.22 , Issue.7 , pp. 1137-1143
    • Toft-Nielsen, M.B.1    Madsbad, S.2    Holst, J.J.3
  • 16
    • 77957890652 scopus 로고    scopus 로고
    • (d-Ser2)Oxm[mPEG-PAL]: A novel chemically modified analogue of oxyntomodulin with antihyperglycaemic, insulinotropic and anorexigenic actions
    • Kerr, B. D.; Flatt, P. R.; Gault, V. A. (d -Ser2)Oxm[mPEG-PAL]: a novel chemically modified analogue of oxyntomodulin with antihyperglycaemic, insulinotropic and anorexigenic actions Biochem. Pharmacol. 2010, 80 (11) 1727-1735
    • (2010) Biochem. Pharmacol. , vol.80 , Issue.11 , pp. 1727-1735
    • Kerr, B.D.1    Flatt, P.R.2    Gault, V.A.3
  • 17
    • 24944459820 scopus 로고    scopus 로고
    • Secretion of incretin hormones and the insulinotropic effect of gastric inhibitory polypeptide in women with a history of gestational diabetes
    • Meier, J. J.; Gallwitz, B.; Askenas, M.; Vollmer, K.; Deacon, C. F.; Holst, J. J.; Schmidt, W. E.; Nauck, M. A. Secretion of incretin hormones and the insulinotropic effect of gastric inhibitory polypeptide in women with a history of gestational diabetes Diabetologia 2005, 48 (9) 1872-1881
    • (2005) Diabetologia , vol.48 , Issue.9 , pp. 1872-1881
    • Meier, J.J.1    Gallwitz, B.2    Askenas, M.3    Vollmer, K.4    Deacon, C.F.5    Holst, J.J.6    Schmidt, W.E.7    Nauck, M.A.8
  • 18
    • 0027510970 scopus 로고
    • The effect of glyburide on beta-cell sensitivity to glucose-dependent insulinotropic polypeptide
    • Meneilly, G. S.; Bryer-Ash, M.; Elahi, D. The effect of glyburide on beta-cell sensitivity to glucose-dependent insulinotropic polypeptide Diabetes Care 1993, 16 (1) 110-114
    • (1993) Diabetes Care , vol.16 , Issue.1 , pp. 110-114
    • Meneilly, G.S.1    Bryer-Ash, M.2    Elahi, D.3
  • 19
    • 33749339257 scopus 로고    scopus 로고
    • Oxyntomodulin increases energy expenditure in addition to decreasing energy intake in overweight and obese humans: A randomised controlled trial
    • Wynne, K.; Park, A. J.; Small, C. J.; Meeran, K.; Ghatei, M. A.; Frost, G. S.; Bloom, S. R. Oxyntomodulin increases energy expenditure in addition to decreasing energy intake in overweight and obese humans: a randomised controlled trial Int. J. Obes. 2006, 30 (12) 1729-1736
    • (2006) Int. J. Obes. , vol.30 , Issue.12 , pp. 1729-1736
    • Wynne, K.1    Park, A.J.2    Small, C.J.3    Meeran, K.4    Ghatei, M.A.5    Frost, G.S.6    Bloom, S.R.7
  • 21
    • 0031179155 scopus 로고    scopus 로고
    • Enterostatin - A peptide regulating fat intake
    • Erlanson-Albertsson, C.; York, D. Enterostatin-a peptide regulating fat intake Obes. Res. 1997, 5 (4) 360-372
    • (1997) Obes. Res. , vol.5 , Issue.4 , pp. 360-372
    • Erlanson-Albertsson, C.1    York, D.2
  • 22
    • 33846818749 scopus 로고    scopus 로고
    • Enterostatin inhibition of dietary fat intake is modulated through the melanocortin system
    • Lin, L.; Park, M.; York, D. A. Enterostatin inhibition of dietary fat intake is modulated through the melanocortin system Peptides 2007, 28 (3) 643-649
    • (2007) Peptides , vol.28 , Issue.3 , pp. 643-649
    • Lin, L.1    Park, M.2    York, D.A.3
  • 23
    • 0026808316 scopus 로고
    • Effect of enterostatin given intravenously and intracerebroventricularly on high-fat feeding in rats
    • Mei, J.; Erlanson-Albertsson, C. Effect of enterostatin given intravenously and intracerebroventricularly on high-fat feeding in rats Regul. Pept. 1992, 41 (3) 209-218
    • (1992) Regul. Pept. , vol.41 , Issue.3 , pp. 209-218
    • Mei, J.1    Erlanson-Albertsson, C.2
  • 24
    • 0033457358 scopus 로고    scopus 로고
    • Multiple receptors for neuropeptide y in the hippocampus: Putative roles in seizures and cognition
    • Redrobe, J. P.; Dumont, Y.; St-Pierre, J. A.; Quirion, R. Multiple receptors for neuropeptide Y in the hippocampus: putative roles in seizures and cognition Brain Res. 1999, 848 (1-2) 153-166
    • (1999) Brain Res. , vol.848 , Issue.12 , pp. 153-166
    • Redrobe, J.P.1    Dumont, Y.2    St-Pierre, J.A.3    Quirion, R.4
  • 25
    • 33644843588 scopus 로고    scopus 로고
    • NPY in alcoholism and psychiatric disorders
    • Thorsell, A.; Karlsson, R. M.; Heilig, M. NPY in alcoholism and psychiatric disorders EXS 2006, 95, 183-192
    • (2006) EXS , vol.95 , pp. 183-192
    • Thorsell, A.1    Karlsson, R.M.2    Heilig, M.3
  • 26
    • 33644898815 scopus 로고    scopus 로고
    • The effects of social isolation on neuropeptide y levels, exploratory and anxiety-related behaviors in rats
    • Thorsell, A.; Slawecki, C. J.; El Khoury, A.; Mathe, A. A.; Ehlers, C. L. The effects of social isolation on neuropeptide Y levels, exploratory and anxiety-related behaviors in rats Pharmacol., Biochem. Behav. 2006, 83 (1) 28-34
    • (2006) Pharmacol., Biochem. Behav. , vol.83 , Issue.1 , pp. 28-34
    • Thorsell, A.1    Slawecki, C.J.2    El Khoury, A.3    Mathe, A.A.4    Ehlers, C.L.5
  • 27
    • 0036082757 scopus 로고    scopus 로고
    • Nesiritide: Review of clinical pharmacology and role in heart failure management
    • Cheng, J. W. Nesiritide: review of clinical pharmacology and role in heart failure management Heart Dis. 2002, 4 (3) 199-203
    • (2002) Heart Dis. , vol.4 , Issue.3 , pp. 199-203
    • Cheng, J.W.1
  • 28
    • 33745413893 scopus 로고    scopus 로고
    • BNP: Pathophysiological and potential therapeutic roles in acute congestive heart failure
    • Grantham, J. A.; Borgeson, D. D.; Burnett, J. C., Jr. BNP: pathophysiological and potential therapeutic roles in acute congestive heart failure Am. J. Physiol. 1997, 272 (4 Pt 2) R1077-R1083
    • (1997) Am. J. Physiol. , vol.272 , Issue.4 PART 2
    • Grantham, J.A.1    Borgeson, D.D.2    Burnett Jr., J.C.3
  • 29
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sonnichsen, F. D.; Van Eyk, J. E.; Hodges, R. S.; Sykes, B. D. Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide Biochemistry 1992, 31 (37) 8790-8798
    • (1992) Biochemistry , vol.31 , Issue.37 , pp. 8790-8798
    • Sonnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 30
    • 34247588747 scopus 로고    scopus 로고
    • Selectivity among dipeptidyl peptidases of the S9b family
    • Bjelke, J. R.; Kanstrup, A. B.; Rasmussen, H. B. Selectivity among dipeptidyl peptidases of the S9b family Cell. Mol. Biol. 2006, 52 (4) 3-7
    • (2006) Cell. Mol. Biol. , vol.52 , Issue.4 , pp. 3-7
    • Bjelke, J.R.1    Kanstrup, A.B.2    Rasmussen, H.B.3
  • 31
    • 79953729051 scopus 로고    scopus 로고
    • Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-alpha
    • Keane, F. M.; Nadvi, N. A.; Yao, T. W.; Gorrell, M. D. Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-alpha FEBS J. 2011, 278 (8) 1316-1332
    • (2011) FEBS J. , vol.278 , Issue.8 , pp. 1316-1332
    • Keane, F.M.1    Nadvi, N.A.2    Yao, T.W.3    Gorrell, M.D.4
  • 32
    • 0029948534 scopus 로고    scopus 로고
    • Proteases involved in the metabolism of angiotensin II, bradykinin, calcitonin gene-related peptide (CGRP), and neuropeptide y by vascular smooth muscle cells
    • Mentlein, R.; Roos, T. Proteases involved in the metabolism of angiotensin II, bradykinin, calcitonin gene-related peptide (CGRP), and neuropeptide Y by vascular smooth muscle cells Peptides 1996, 17 (4) 709-720
    • (1996) Peptides , vol.17 , Issue.4 , pp. 709-720
    • Mentlein, R.1    Roos, T.2
  • 33
  • 34
    • 0027494070 scopus 로고
    • Proteolytic processing of neuropeptide y and peptide YY by dipeptidyl peptidase IV
    • Mentlein, R.; Dahms, P.; Grandt, D.; Kruger, R. Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV Regul. Pept. 1993, 49 (2) 133-144
    • (1993) Regul. Pept. , vol.49 , Issue.2 , pp. 133-144
    • Mentlein, R.1    Dahms, P.2    Grandt, D.3    Kruger, R.4
  • 35
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein, R.; Gallwitz, B.; Schmidt, W. E. Dipeptidyl-peptidase IV hydrolyses 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 (3) 829-835
    • (1993) Eur. J. Biochem. , vol.214 , Issue.3 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 36
    • 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.; O'Harte, 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 (12) 1543-1551
    • (2003) Biol. Chem. , vol.384 , Issue.12 , 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    O'Harte, F.P.9
  • 37
    • 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.; O'Harte, 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 (2) 252-259
    • (2004) Metabolism , vol.53 , Issue.2 , 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    O'Harte, F.P.9
  • 41
    • 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 (3) 342-346
    • (2003) FEBS Lett. , vol.553 , Issue.3 , pp. 342-346
    • Al-Sabah, S.1    Donnelly, D.2
  • 42
    • 0141992171 scopus 로고    scopus 로고
    • A model for receptor-peptide binding at the glucagon-like peptide-1 (GLP-1) receptor through the analysis of truncated ligands and receptors
    • Al-Sabah, S.; Donnelly, D. A model for receptor-peptide binding at the glucagon-like peptide-1 (GLP-1) receptor through the analysis of truncated ligands and receptors Br. J. Pharmacol. 2003, 140 (2) 339-346
    • (2003) Br. J. Pharmacol. , vol.140 , Issue.2 , pp. 339-346
    • Al-Sabah, S.1    Donnelly, D.2
  • 43
    • 0034031434 scopus 로고    scopus 로고
    • Molecular characterization of the ligand-receptor interaction of the neuropeptide y family
    • Cabrele, C.; Beck-Sickinger, A. G. Molecular characterization of the ligand-receptor interaction of the neuropeptide Y family J. Pept. Sci. 2000, 6 (3) 97-122
    • (2000) J. Pept. Sci. , vol.6 , Issue.3 , pp. 97-122
    • Cabrele, C.1    Beck-Sickinger, A.G.2
  • 44
    • 0028941516 scopus 로고
    • Evaluation of conformational and binding characteristics of various natriuretic peptides and related analogs
    • Mimeault, M.; De Lean, A.; Lafleur, M.; Bonenfant, D.; Fournier, A. Evaluation of conformational and binding characteristics of various natriuretic peptides and related analogs Biochemistry 1995, 34 (3) 955-964
    • (1995) Biochemistry , vol.34 , Issue.3 , pp. 955-964
    • Mimeault, M.1    De Lean, A.2    Lafleur, M.3    Bonenfant, D.4    Fournier, A.5
  • 46
    • 4043168530 scopus 로고    scopus 로고
    • In depth analysis of the N-terminal bioactive domain of gastric inhibitory polypeptide
    • Hinke, S. A.; Manhart, S.; Speck, M.; Pederson, R. A.; Demuth, H. U.; McIntosh, C. H. In depth analysis of the N-terminal bioactive domain of gastric inhibitory polypeptide Life Sci. 2004, 75 (15) 1857-1870
    • (2004) Life Sci. , vol.75 , Issue.15 , pp. 1857-1870
    • Hinke, S.A.1    Manhart, S.2    Speck, M.3    Pederson, R.A.4    Demuth, H.U.5    McIntosh, C.H.6
  • 47
    • 0036289106 scopus 로고    scopus 로고
    • Characterization of the cellular and metabolic effects of a novel enzyme-resistant antagonist of glucose-dependent insulinotropic polypeptide
    • Gault, V. A.; O'Harte, F. P.; Harriott, P.; Flatt, P. R. Characterization of the cellular and metabolic effects of a novel enzyme-resistant antagonist of glucose-dependent insulinotropic polypeptide Biochem. Biophys. Res. Commun. 2002, 290 (5) 1420-1426
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , Issue.5 , pp. 1420-1426
    • Gault, V.A.1    O'Harte, F.P.2    Harriott, P.3    Flatt, P.R.4
  • 48
    • 0023910424 scopus 로고
    • Oxyntomodulin (glicentin-(33-69)): Pharmacokinetics, binding to liver cell membranes, effects on isolated perfused pig pancreas, and secretion from isolated perfused lower small intestine of pigs
    • Baldissera, F. G.; Holst, J. J.; Knuhtsen, S.; Hilsted, L.; Nielsen, O. V. Oxyntomodulin (glicentin-(33-69)): pharmacokinetics, binding to liver cell membranes, effects on isolated perfused pig pancreas, and secretion from isolated perfused lower small intestine of pigs Regul. Pept. 1988, 21 (1-2) 151-166
    • (1988) Regul. Pept. , vol.21 , Issue.12 , pp. 151-166
    • Baldissera, F.G.1    Holst, J.J.2    Knuhtsen, S.3    Hilsted, L.4    Nielsen, O.V.5
  • 49
    • 0027220436 scopus 로고
    • Glucagon-like peptide-1-(7-36) amide, oxyntomodulin, and glucagon interact with a common receptor in a somatostatin-secreting cell line
    • Gros, L.; Thorens, B.; Bataille, D.; Kervran, A. Glucagon-like peptide-1-(7-36) amide, oxyntomodulin, and glucagon interact with a common receptor in a somatostatin-secreting cell line Endocrinology 1993, 133 (2) 631-638
    • (1993) Endocrinology , vol.133 , Issue.2 , pp. 631-638
    • Gros, L.1    Thorens, B.2    Bataille, D.3    Kervran, A.4
  • 50
    • 0041344589 scopus 로고    scopus 로고
    • Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus
    • Runge, S.; Gram, C.; Brauner-Osborne, H.; Madsen, K.; Knudsen, L. B.; Wulff, B. S. Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus J. Biol. Chem. 2003, 278 (30) 28005-28010
    • (2003) J. Biol. Chem. , vol.278 , Issue.30 , pp. 28005-28010
    • Runge, S.1    Gram, C.2    Brauner-Osborne, H.3    Madsen, K.4    Knudsen, L.B.5    Wulff, B.S.6
  • 51
    • 0028097051 scopus 로고
    • Complete l -alanine scan of neuropeptide y reveals ligands binding to Y1 and Y2 receptors with distinguished conformations
    • Beck-Sickinger, A. G.; Wieland, H. A.; Wittneben, H.; Willim, K. D.; Rudolf, K.; Jung, G. Complete l -alanine scan of neuropeptide Y reveals ligands binding to Y1 and Y2 receptors with distinguished conformations Eur. J. Biochem. 1994, 225 (3) 947-958
    • (1994) Eur. J. Biochem. , vol.225 , Issue.3 , pp. 947-958
    • Beck-Sickinger, A.G.1    Wieland, H.A.2    Wittneben, H.3    Willim, K.D.4    Rudolf, K.5    Jung, G.6
  • 53
    • 79953713734 scopus 로고    scopus 로고
    • Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site
    • Kuhn-Wache, K.; Bar, J. W.; Hoffmann, T.; Wolf, R.; Rahfeld, J. U.; Demuth, H. U. Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site Biol. Chem. 2011, 392 (3) 223-231
    • (2011) Biol. Chem. , vol.392 , Issue.3 , pp. 223-231
    • Kuhn-Wache, K.1    Bar, J.W.2    Hoffmann, T.3    Wolf, R.4    Rahfeld, J.U.5    Demuth, H.U.6
  • 54
    • 0028237726 scopus 로고
    • Substrate specificity of aminopeptidase P from Escherichia coli: Comparison with membrane-bound forms from rat and bovine lung
    • Yoshimoto, T.; Orawski, A. T.; Simmons, W. H. Substrate specificity of aminopeptidase P from Escherichia coli: comparison with membrane-bound forms from rat and bovine lung Arch. Biochem. Biophys. 1994, 311 (1) 28-34
    • (1994) Arch. Biochem. Biophys. , vol.311 , Issue.1 , pp. 28-34
    • Yoshimoto, T.1    Orawski, A.T.2    Simmons, W.H.3
  • 57
    • 0035851103 scopus 로고    scopus 로고
    • A small molecule ligand of the glucagon-like peptide 1 receptor targets its amino-terminal hormone binding domain
    • Tibaduiza, E. C.; Chen, C.; Beinborn, M. A small molecule ligand of the glucagon-like peptide 1 receptor targets its amino-terminal hormone binding domain J. Biol. Chem. 2001, 276 (41) 37787-37793
    • (2001) J. Biol. Chem. , vol.276 , Issue.41 , pp. 37787-37793
    • Tibaduiza, E.C.1    Chen, C.2    Beinborn, M.3


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