메뉴 건너뛰기




Volumn 3, Issue 3, 2014, Pages 293-300

A glucagon analog chemically stabilized for immediate treatment of life-threatening hypoglycemia

Author keywords

Glucagon; Hypoglycemia; Insulin dependent diabetes; Peptide synthesis

Indexed keywords

ASPARAGINE; ASPARTIC ACID; CYCLIC AMP; GLUCAGON DERIVATIVE; GLUTAMINE; GLYCINE; HISTIDINE; LEUCINE; LYSINE; METHIONINE; PHENYLALANINE; SERINE; THREONINE; TRYPTOPHAN; TYROSINE; VALINE;

EID: 84897116097     PISSN: 22128778     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmet.2014.01.006     Document Type: Article
Times cited : (33)

References (28)
  • 1
    • 0017171586 scopus 로고
    • Physiology and pathophysiology of glucagon
    • Unger R.H., Orci L. Physiology and pathophysiology of glucagon. Physiological Reviews 1976, 56(4):778-826.
    • (1976) Physiological Reviews , vol.56 , Issue.4 , pp. 778-826
    • Unger, R.H.1    Orci, L.2
  • 2
    • 0014661159 scopus 로고
    • Glucagon-sensitive adenyl cylase in plasma membrane of hepatic parenchymal cells
    • Pohl S.L., Birnbaum L, Rodbell M. Glucagon-sensitive adenyl cylase in plasma membrane of hepatic parenchymal cells. Science 1969, 164(3879):566-567.
    • (1969) Science , vol.164 , Issue.3879 , pp. 566-567
    • Pohl, S.L.1    Birnbaum, L.2    Rodbell, M.3
  • 3
    • 0015901935 scopus 로고
    • Lack of glucagon response to hypoglycemia in diabetes: evidence for an intrinsic pancreatic alpha cell defect
    • Gerich J.E., Langlois M., Noacco C., Karam J.H., Forsham P.H. Lack of glucagon response to hypoglycemia in diabetes: evidence for an intrinsic pancreatic alpha cell defect. Science. 182 1973, (108):171-173.
    • (1973) Science. 182 , Issue.108 , pp. 171-173
    • Gerich, J.E.1    Langlois, M.2    Noacco, C.3    Karam, J.H.4    Forsham, P.H.5
  • 4
    • 0021716348 scopus 로고
    • Duration of type I diabetes affects glucagon and glucose responses to insulin-induced hypoglycemia
    • Lorenzi M., Bohannon N., Tsalikian E., Karam J.H. Duration of type I diabetes affects glucagon and glucose responses to insulin-induced hypoglycemia. Western Journal of Medicine 1984, 141(4):467-471.
    • (1984) Western Journal of Medicine , vol.141 , Issue.4 , pp. 467-471
    • Lorenzi, M.1    Bohannon, N.2    Tsalikian, E.3    Karam, J.H.4
  • 5
    • 0028607457 scopus 로고
    • Banting lecture. hypoglycemia: the limiting factor in the management of IDDM
    • Cryer P.E. Banting lecture. hypoglycemia: the limiting factor in the management of IDDM. Diabetes 1994, 43(11):1378-1389.
    • (1994) Diabetes , vol.43 , Issue.11 , pp. 1378-1389
    • Cryer, P.E.1
  • 6
    • 0027370108 scopus 로고
    • The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes-mellitus
    • Shamoon H., et al. The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes-mellitus. New England Journal of Medicine 1993, 329(14):977-986.
    • (1993) New England Journal of Medicine , vol.329 , Issue.14 , pp. 977-986
    • Shamoon, H.1
  • 9
    • 27644506040 scopus 로고    scopus 로고
    • Studies on the mechanism of aspartic acid cleavage and glutamine deamidation in the acidic degradation of glucagon
    • Joshi A.B., Sawai M., Kearney W.M., Kirsch L.E. Studies on the mechanism of aspartic acid cleavage and glutamine deamidation in the acidic degradation of glucagon. Journal of Pharmaceutical Sciences 2005, 94(9):1912-1927.
    • (2005) Journal of Pharmaceutical Sciences , vol.94 , Issue.9 , pp. 1912-1927
    • Joshi, A.B.1    Sawai, M.2    Kearney, W.M.3    Kirsch, L.E.4
  • 12
    • 3242735868 scopus 로고    scopus 로고
    • Mishandling of the therapeutic peptide glucagon generates cytotoxic amyloidogenic fibrils
    • Onoue S., Ohshima K., Debari K., Koh K., Shioda S., Iwasa S., et al. Mishandling of the therapeutic peptide glucagon generates cytotoxic amyloidogenic fibrils. Pharmaceutical Research 2004, 21(7):1274-1283.
    • (2004) Pharmaceutical Research , vol.21 , Issue.7 , pp. 1274-1283
    • Onoue, S.1    Ohshima, K.2    Debari, K.3    Koh, K.4    Shioda, S.5    Iwasa, S.6
  • 14
    • 0026648961 scopus 로고
    • Isolation and characterization of exendin-4, an exendin-3 analog, 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 analog, from heloderma-suspectum venom - further evidence for an exendin receptor on dispersed acini from guinea-pig pancreas. Journal of Biological Chemistry 1992, 267(11):7402-7405.
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.11 , pp. 7402-7405
    • Eng, J.1    Kleinman, W.A.2    Singh, L.3    Singh, G.4    Raufman, J.P.5
  • 15
    • 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(44):13188-13200.
    • (2001) Biochemistry , vol.40 , Issue.44 , pp. 13188-13200
    • Neidigh, J.W.1    Fesinmeyer, R.M.2    Prickett, K.S.3    Andersen, N.H.4
  • 16
    • 33845989145 scopus 로고    scopus 로고
    • Stability of synthetic exendin-4 in human plasma in vitro
    • Chen J., Yu L., Fang X., Li L., Li W. Stability of synthetic exendin-4 in human plasma in vitro. Protein and Peptide Letters 2007, 14(1):19-25.
    • (2007) Protein and Peptide Letters , vol.14 , Issue.1 , pp. 19-25
    • Chen, J.1    Yu, L.2    Fang, X.3    Li, L.4    Li, W.5
  • 17
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnolzer M., Alewood P., Jones A., Alewood D., Kent S.B. In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences. International Journal of Peptide and Protein Research 1992, 40(3-4):180-193.
    • (1992) International Journal of Peptide and Protein Research , vol.40 , Issue.3-4 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 19
    • 1542358755 scopus 로고    scopus 로고
    • The estimation of glutaminyl deamidation and aspartyl cleavage rates in glucagon
    • Joshi A.B., Kirsch L.E. The estimation of glutaminyl deamidation and aspartyl cleavage rates in glucagon. International Journal of Pharmaceutics 2004, 273(1-2):213-219.
    • (2004) International Journal of Pharmaceutics , vol.273 , Issue.1-2 , pp. 213-219
    • Joshi, A.B.1    Kirsch, L.E.2
  • 20
    • 0023464863 scopus 로고
    • Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins
    • Clarke S. Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. International Journal of Peptide and Protein Research 1987, 30(6):808-821.
    • (1987) International Journal of Peptide and Protein Research , vol.30 , Issue.6 , pp. 808-821
    • Clarke, S.1
  • 21
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides - succinimide-linked reactions that contribute to protein-degradation
    • Geiger T., Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides - succinimide-linked reactions that contribute to protein-degradation. Journal of Biological Chemistry 1987, 262(2):785-794.
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.2 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 22
    • 0026419837 scopus 로고
    • Structures of polypeptides from alpha-amino-acids disubstituted at the alpha-carbon
    • Toniolo C., Benedetti E. Structures of polypeptides from alpha-amino-acids disubstituted at the alpha-carbon. Macromolecules 1991, 24(14):4004-4009.
    • (1991) Macromolecules , vol.24 , Issue.14 , pp. 4004-4009
    • Toniolo, C.1    Benedetti, E.2
  • 23
    • 0345352748 scopus 로고    scopus 로고
    • Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib
    • Kumita J.R., Weston C.J., Choo-Smith L.P., Woolley G.A., Smart O.S. Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib. Biochemistry 2003, 42(15):4492-4498.
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4492-4498
    • Kumita, J.R.1    Weston, C.J.2    Choo-Smith, L.P.3    Woolley, G.A.4    Smart, O.S.5
  • 24
    • 0016687342 scopus 로고
    • The conformation of glucagon: predictions and consequences
    • Chou P.Y., Fasman G.D. The conformation of glucagon: predictions and consequences. Biochemistry 1975, 14(11):2536-2541.
    • (1975) Biochemistry , vol.14 , Issue.11 , pp. 2536-2541
    • Chou, P.Y.1    Fasman, G.D.2
  • 25
    • 0025345233 scopus 로고
    • Structural characteristics of alpha-helical peptide molecules containing Aib residues
    • Karle I.L., Balaram P. Structural characteristics of alpha-helical peptide molecules containing Aib residues. Biochemistry 1990, 29(29):6747-6756.
    • (1990) Biochemistry , vol.29 , Issue.29 , pp. 6747-6756
    • Karle, I.L.1    Balaram, P.2
  • 26
    • 0024700331 scopus 로고
    • Comparison of the effect of 5 guest residues on the beta-sheet conformation of host (l-Val)N oligopeptides
    • Moretto V., Crisma M., Bonora G.M., Toniolo C., Balaram H., Balaram P. Comparison of the effect of 5 guest residues on the beta-sheet conformation of host (l-Val)N oligopeptides. Macromolecules 1989, 22(7):2939-2944.
    • (1989) Macromolecules , vol.22 , Issue.7 , pp. 2939-2944
    • Moretto, V.1    Crisma, M.2    Bonora, G.M.3    Toniolo, C.4    Balaram, H.5    Balaram, P.6
  • 28
    • 0345352748 scopus 로고    scopus 로고
    • Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib
    • Kumita J.R., Weston C.J., Choo-Smith L.P., Wooley G.A., Smart O.S. Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib. Biochemistry 2003, 42(15):4492-4498.
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4492-4498
    • Kumita, J.R.1    Weston, C.J.2    Choo-Smith, L.P.3    Wooley, G.A.4    Smart, O.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.