메뉴 건너뛰기




Volumn 49, Issue 25, 2006, Pages 7545-7548

Engineering of a VPAC2 receptor peptide agonist to impart dipeptidyl peptidase IV stability and enhance in vivo glucose disposal

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; GLUCOSE; INSULIN; VASOACTIVE INTESTINAL POLYPEPTIDE DERIVATIVE; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 2; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 2 AGONIST;

EID: 33845477003     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0609059     Document Type: Article
Times cited : (8)

References (19)
  • 1
    • 33644902945 scopus 로고    scopus 로고
    • GLP-1 based therapy for type 2 diabetes
    • Arulmozhi, D. K.; Portha, B. GLP-1 based therapy for type 2 diabetes. Eur. J. Pharm. Sci. 2006, 28, 96-108.
    • (2006) Eur. J. Pharm. Sci. , vol.28 , pp. 96-108
    • Arulmozhi, D.K.1    Portha, B.2
  • 2
    • 33644842108 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitors: A promising new therapeutic approach for the management of type 2 diabetes
    • Deacon, C. F.; Holst, J. J. Dipeptidyl peptidase IV inhibitors: A promising new therapeutic approach for the management of type 2 diabetes. Int. J. Biochem. Cell Biol. 2006, 38, 831-844.
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 831-844
    • Deacon, C.F.1    Holst, J.J.2
  • 3
    • 33646353949 scopus 로고    scopus 로고
    • Emerging therapies mimicking the effects of amylin and glucagon-like peptide 1
    • Riddle, M. C.; Drucker, D. J. Emerging therapies mimicking the effects of amylin and glucagon-like peptide 1. Diabetes Care 2006, 29, 435-449.
    • (2006) Diabetes Care , vol.29 , pp. 435-449
    • Riddle, M.C.1    Drucker, D.J.2
  • 5
    • 0034048147 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide and its receptors: From structure to functions
    • Vaudry, D.; Gonzalez, B. J.; Basille, M.; Yon, L.; Fournier, A.; Vaudry, H. Pituitary adenylate cyclase-activating polypeptide and its receptors: From structure to functions. Pharmacol. Rev. 2000, 52, 269-324.
    • (2000) Pharmacol. Rev. , vol.52 , pp. 269-324
    • Vaudry, D.1    Gonzalez, B.J.2    Basille, M.3    Yon, L.4    Fournier, A.5    Vaudry, H.6
  • 6
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris, J. M.; Chess, R. B. Effect of PEGylation on pharmaceuticals. Nat. Rev. Drug Discovery 2003, 2, 214-221.
    • (2003) Nat. Rev. Drug Discovery , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 8
    • 33845483757 scopus 로고    scopus 로고
    • 7
    • 7
  • 9
    • 0035798196 scopus 로고    scopus 로고
    • Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion
    • Lambeir, A. M.; Durinx, C.; Proost, P.; Van Damme, J.; Scharpe, S.; De Meester, I. Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett. 2001, 507, 327-330.
    • (2001) FEBS Lett. , vol.507 , pp. 327-330
    • Lambeir, A.M.1    Durinx, C.2    Proost, P.3    Van Damme, J.4    Scharpe, S.5    De Meester, I.6
  • 12
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • Rasmussen, H. B.; Branner, S.; Wiberg, F. C.; Wagtmann, N. Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat. Struct. Biol. 2003, 10, 19-25.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4
  • 13
    • 23644439921 scopus 로고    scopus 로고
    • Contribution of site-specific PEGylation to the dipeptidyl peptidase IV stability of glucose-dependent insulinotropic polypeptide
    • Salhanick, A. I.; Clairmont, K. B.; Buckholz, T. M.; Pellegrino, C. M.; Ha, S.; Lumb, K. J. Contribution of site-specific PEGylation to the dipeptidyl peptidase IV stability of glucose-dependent insulinotropic polypeptide. Bioorg. Med. Chem. Lett. 2005, 15, 4114-4117.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 4114-4117
    • Salhanick, A.I.1    Clairmont, K.B.2    Buckholz, T.M.3    Pellegrino, C.M.4    Ha, S.5    Lumb, K.J.6
  • 14
    • 0032211606 scopus 로고    scopus 로고
    • Polyethylene glycol-conjugated pharmaceutical proteins
    • Bailon, P.; Berthold, W. Polyethylene glycol-conjugated pharmaceutical proteins. Pharm. Sci. Technol. Today 1998, 1, 352.
    • (1998) Pharm. Sci. Technol. Today , vol.1 , pp. 352
    • Bailon, P.1    Berthold, W.2
  • 15
    • 0025265384 scopus 로고
    • Site-directed PEGylation of recombinant interleukin-2 at its glycosylation site
    • Goodson, R. J.; Katre, N. V. Site-directed PEGylation of recombinant interleukin-2 at its glycosylation site. Biotechnology 1990, 8, 343-346.
    • (1990) Biotechnology , vol.8 , pp. 343-346
    • Goodson, R.J.1    Katre, N.V.2
  • 18
    • 0033533402 scopus 로고    scopus 로고
    • NVP-DPP728 (1-[[[2-[(5-cyanopyridin-2-yl)amino]ethyl]amino]-acetyl]-2- cyano-(S)-pyrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV
    • Hughes, T. E.; Mone, M. D.; Russell, M. E.; Weldon, S. C.; Villhauer, E. B. NVP-DPP728 (1-[[[2-[(5-cyanopyridin-2-yl)amino]ethyl]amino]-acetyl]-2-cyano- (S)-pyrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV. Biochemistry 1999, 38, 11597-11603.
    • (1999) Biochemistry , vol.38 , pp. 11597-11603
    • Hughes, T.E.1    Mone, M.D.2    Russell, M.E.3    Weldon, S.C.4    Villhauer, E.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.