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Volumn 6, Issue 2, 2012, Pages 265-276

Intrinsic fibrillation of fast-acting insulin analogs

Author keywords

Amyloid; Circular dichroism; Excipients; Fibrils; Insulin; Insulin stability; Intrinsic fibrillation; Protein aggregation; Protein precipitation; Thioflavine T

Indexed keywords

AMYLOID BETA PROTEIN; BUFFER; EXCIPIENT; HUMAN INSULIN; INSULIN ASPART; INSULIN DERIVATIVE; INSULIN GLULISINE; INSULIN LISPRO; ISOPHANE INSULIN; PHOSPHATE BUFFERED SALINE; ANTIDIABETIC AGENT; DRUG DERIVATIVE; INSULIN;

EID: 84865114967     PISSN: None     EISSN: 19322968     Source Type: Journal    
DOI: 10.1177/193229681200600209     Document Type: Article
Times cited : (59)

References (69)
  • 1
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: Pathways, induction factors and analysis
    • Mahler HC, Friess W, Grauschopf U, Kiese S. Protein aggregation: pathways, induction factors and analysis. J Pharm Sci. 2009;98(9):2909-34.
    • (2009) J Pharm Sci , vol.98 , Issue.9 , pp. 2909-2934
    • Mahler, H.C.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 3
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • Weiss WF 4th, Young TM, Roberts CJ. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci. 2009;98(4):1246-77.
    • (2009) J Pharm Sci , vol.98 , Issue.4 , pp. 1246-1277
    • Weiss IV, W.F.1    Young, T.M.2    Roberts, C.J.3
  • 5
    • 34248369818 scopus 로고    scopus 로고
    • A false paradise - Mixed blessings in the protein universe: The amyloid as a new challenge in drug development
    • DOI 10.2174/092986707780597989
    • Morozova-Roche L, Malisauskas M. A false paradise - mixed blessings in the protein universe: the amyloid as a new challenge in drug development. Curr Med Chem. 2007;14(11):1221-30. (Pubitemid 46739323)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.11 , pp. 1221-1230
    • Morozova-Roche, L.1    Malisauskas, M.2
  • 6
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • DOI 10.1016/j.ijpharm.2004.11.014, PII S0378517304006908
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm. 2005;289(1-2):1-30. (Pubitemid 40093537)
    • (2005) International Journal of Pharmaceutics , vol.289 , Issue.1-2 , pp. 1-30
    • Wang, W.1
  • 8
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An Immunologic perspective
    • DOI 10.1208/aapsj080359, 59
    • Rosenberg AS. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006;8(3):E501-7. (Pubitemid 44294011)
    • (2006) AAPS Journal , vol.8 , Issue.3
    • Rosenberg, A.S.1
  • 10
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • DOI 10.1126/science.1067122
    • Taylor JP, Hardy J, Fischbeck KH. Toxic proteins in neurodegenerative disease. Science. 2002;296(5575):1991-5. (Pubitemid 34627514)
    • (2002) Science , vol.296 , Issue.5575 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 11
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • DOI 10.1038/nm1066
    • Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med. 2004;10 Suppl:S10-7. (Pubitemid 38901862)
    • (2004) Nature Medicine , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 12
    • 0033977086 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis: Themes and variations
    • Rochet JC, Lansbury PT Jr. Amyloid fibrillogenesis: themes and variations. Curr Opin Struct Biol. 2000;10(1):60-8.
    • (2000) Curr Opin Struct Biol , vol.10 , Issue.1 , pp. 60-68
    • Rochet, J.C.1    Lansbury Jr., P.T.2
  • 15
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • DOI 10.1016/j.sbi.2003.12.002
    • Tycko R. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr Opin Struct Biol. 2004;14(1):96-103. (Pubitemid 38249598)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.1 , pp. 96-103
    • Tycko, R.1
  • 17
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • DOI 10.1021/bi002555c
    • Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry. 2001;40(20):6036-46. (Pubitemid 32466306)
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 19
    • 0026698922 scopus 로고
    • Mechanism of insulin aggregation and stabilization in agitated aqueous solutions
    • Sluzky V, Klibanov AM, Langer R. Mechanism of insulin aggregation and stabilization in agitated aqueous solutions. Biotechnol Bioeng. 1992;40(8):895-903.
    • (1992) Biotechnol Bioeng , vol.40 , Issue.8 , pp. 895-903
    • Sluzky, V.1    Klibanov, A.M.2    Langer, R.3
  • 20
    • 0141483330 scopus 로고    scopus 로고
    • Partially folded intermediates in insulin fibrillation
    • DOI 10.1021/bi034868o
    • Ahmad A, Millett IS, Doniach S, Uversky VN, Fink AL. Partially folded intermediates in insulin fibrillation. Biochemistry. 2003;42(39):11404-16. (Pubitemid 37205734)
    • (2003) Biochemistry , vol.42 , Issue.39 , pp. 11404-11416
    • Ahmad, A.1    Millett, I.S.2    Doniach, S.3    Uversky, V.N.4    Fink, A.L.5
  • 23
  • 25
    • 70349505749 scopus 로고    scopus 로고
    • Formation mechanism of insulin fibrils and structural aspects of the insulin fibrillation process
    • Groenning M, Frokjaer S, Vestergaard B. Formation mechanism of insulin fibrils and structural aspects of the insulin fibrillation process. Curr Protein Pept Sci. 2009;10(5):509-28.
    • (2009) Curr Protein Pept Sci , vol.10 , Issue.5 , pp. 509-528
    • Groenning, M.1    Frokjaer, S.2    Vestergaard, B.3
  • 27
    • 67649119859 scopus 로고    scopus 로고
    • Diabetic ketoacidosis caused by exposure of insulin pump to heat and sunlight
    • Pryce R. Diabetic ketoacidosis caused by exposure of insulin pump to heat and sunlight. BMJ. 2009;338:a2218.
    • (2009) BMJ , vol.338
    • Pryce, R.1
  • 28
    • 0031010619 scopus 로고    scopus 로고
    • Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions
    • DOI 10.1021/bi963038q
    • Rahuel-Clermont S, French CA, Kaarsholm NC, Dunn MF, Chou CI. Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions. Biochemistry. 1997;36(19):5837-45. (Pubitemid 27214935)
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5837-5845
    • Rahuel-Clermont, S.1    French, C.A.2    Kaarsholm, N.C.3    Dunn, M.F.4
  • 29
    • 0032544188 scopus 로고    scopus 로고
    • Interactions of phenol and m-cresol in the insulin hexamer, and their effect on the association properties of B28 Pro > Asp insulin analogues
    • DOI 10.1021/bi980807s
    • Whittingham JL, Edwards DJ, Antson AA, Clarkson JM, Dodson GG. Interactions of phenol and m-cresol in the insulin hexamer, and their effect on the association properties of B28 pro - > Asp insulin analogues. Biochemistry. 1998;37(33):11516-23. (Pubitemid 28388193)
    • (1998) Biochemistry , vol.37 , Issue.33 , pp. 11516-11523
    • Whittingham, J.L.1    Edwards, D.J.2    Antson, A.A.3    Clarkson, J.M.4    Dodson, G.G.5
  • 32
    • 0029644942 scopus 로고
    • Role of C-terminal B-chain residues in insulin assembly: The structure of hexameric LysB28ProB29-human insulin
    • .Ciszak E, Beals JM, Frank BH, Baker JC, Carter ND, Smith GD. Role of C-terminal B-chain residues in insulin assembly: the structure of hexameric LysB28ProB29-human insulin. Structure. 1995;3(6):615-22.
    • (1995) Structure , vol.3 , Issue.6 , pp. 615-622
    • Ciszak, E.1    Beals, J.M.2    Frank, B.H.3    Baker, J.C.4    Carter, N.D.5    Smith, G.D.6
  • 34
    • 0034109079 scopus 로고    scopus 로고
    • Use of insulin aspart, a fast-acting insulin analog, as the mealtime insulin in the management of patients with type 1 diabetes
    • .Raskin P, Guthrie RA, Leiter L, Riis A, Jovanovic L. Use of insulin aspart, a fast-acting insulin analog, as the mealtime insulin in the management of patients with type 1 diabetes. Diabetes Care. 2000;23(5):583-8. (Pubitemid 30321534)
    • (2000) Diabetes Care , vol.23 , Issue.5 , pp. 583-588
    • Raskin, P.1    Guthrie, R.A.2    Leiter, L.3    Riis, A.4    Jovanovic, L.5
  • 35
    • 0032969538 scopus 로고    scopus 로고
    • Insulin analogs with improved pharmacokinetic profiles
    • DOI 10.1016/S0169-409X(98)00079-9, PII S0169409X98000799
    • Brange J, Vølund A. Insulin analogs with improved pharmacokinetic profiles. Adv Drug Deliv Rev. 1999;35(2-3):307-35. (Pubitemid 29073621)
    • (1999) Advanced Drug Delivery Reviews , vol.35 , Issue.2-3 , pp. 307-335
    • Brange, J.1    Volund, A.2
  • 36
    • 11844250564 scopus 로고    scopus 로고
    • Insulin analogues
    • DOI 10.1056/NEJMra040832
    • Hirsch IB. Insulin analogues. N Engl J Med. 2005;352(2):174-83. (Pubitemid 40096614)
    • (2005) New England Journal of Medicine , vol.352 , Issue.2 , pp. 174-183
    • Hirsch, I.B.1
  • 37
    • 33847208863 scopus 로고    scopus 로고
    • Insulin glulisine complementing basal insulins: A review of structure and activity
    • Becker RH. Insulin glulisine complementing basal insulins: a review of structure and activity. Diabetes Technol Ther. 2007;9(1):109-21.
    • (2007) Diabetes Technol Ther , vol.9 , Issue.1 , pp. 109-121
    • Becker, R.H.1
  • 39
    • 52449090177 scopus 로고    scopus 로고
    • Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: Structure and degradation pathways
    • Kerwin BA. Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: structure and degradation pathways. J Pharm Sci. 2008;97(8):2924-35.
    • (2008) J Pharm Sci , vol.97 , Issue.8 , pp. 2924-2935
    • Kerwin, B.A.1
  • 40
    • 0014543411 scopus 로고
    • The accurate measurement of insulin molarity
    • Harrison DM, Garratt CJ. The accurate measurement of insulin molarity. Biochem J. 1969;113(4):733-4.
    • (1969) Biochem J , vol.113 , Issue.4 , pp. 733-734
    • Harrison, D.M.1    Garratt, C.J.2
  • 41
    • 0025125376 scopus 로고
    • Cooperativity and intermediate states in the T>R-structural transformation of insulin
    • Krüger P, Gilge G, Cabuk Y, Wollmer A. Cooperativity and intermediate states in the T - R-structural transformation of insulin. Biol Chem Hoppe Seyler. 1990;371(8):669-73. (Pubitemid 20277174)
    • (1990) Biological Chemistry Hoppe-Seyler , vol.371 , Issue.8 , pp. 669-673
    • Kruger, P.1    Gilge, G.2    Cabuk, Y.3    Wollmer, A.4
  • 42
    • 84900559584 scopus 로고    scopus 로고
    • Effect of phenol and m-cresol depletion on analog insulin conformational stability
    • Accessed January 12, 2012
    • Teska B, Alarcon J, Pettis RJ, Randolph T, Carpenter J. Effect of phenol and m-cresol depletion on analog insulin conformational stability. AAPS J. 2011;12:S1. http://www.aapsj.org/abstracts/NBC-2011/T2077.pdf. Accessed January 12, 2012.
    • (2011) AAPS J , vol.12
    • Teska, B.1    Alarcon, J.2    Pettis, R.J.3    Randolph, T.4    Carpenter, J.5
  • 43
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • DOI 10.1016/j.sbi.2007.01.007, PII S0959440X07000085, Foldinf and Binding / Protein-Nucleic Interactions
    • Kodali R, Wetzel R. Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struct Biol. 2007;17(1):48-57. (Pubitemid 46242190)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 44
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H 3rd. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods in Enzymol. 1999;309:274-84.
    • (1999) Methods in Enzymol , vol.309 , pp. 274-284
    • LeVine III, H.1
  • 46
    • 59649110455 scopus 로고    scopus 로고
    • Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils
    • Meinhardt J, Sachse C, Hortschansky P, Grigorief N, Fändrich M. Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J Mol Biol. 2009;386(3):869-77.
    • (2009) J Mol Biol , vol.386 , Issue.3 , pp. 869-877
    • Meinhardt, J.1    Sachse, C.2    Hortschansky, P.3    Grigorief, N.4    Fändrich, M.5
  • 48
    • 28944433479 scopus 로고    scopus 로고
    • The changing face of glucagon fibrillation: Structural polymorphism and conformational imprinting
    • DOI 10.1016/j.jmb.2005.09.100, PII S0022283605012970
    • Pedersen JS, Dikov D, Flink JL, Hjuler HA, Christiansen G, Otzen DE. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J Mol Biol. 2006;355(3):501-23. (Pubitemid 41785753)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.3 , pp. 501-523
    • Pedersen, J.S.1    Dikov, D.2    Flink, J.L.3    Hjuler, H.A.4    Christiansen, G.5    Otzen, D.E.6
  • 49
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation
    • DOI 10.1110/ps.041266605
    • Hortschansky P, Schroeckh V, Christopeit T, Zandomeneghi G, Fändrich M. The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation. Protein Sci. 2005;14(7):1753-9. (Pubitemid 40994145)
    • (2005) Protein Science , vol.14 , Issue.7 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fandrich, M.5
  • 50
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • .Xue WF, Homans SW, Radford SE. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA. 2008;105(26):8926-31.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.26 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 51
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a Partially Folded Intermediate in alpha-Synuclein Fibril Formation
    • DOI 10.1074/jbc.M010907200
    • Uversky VN, Li J, Fink AL. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J Biol Chem. 2001;276(14):10737-44. (Pubitemid 38089246)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 53
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. Rationalization of the efects of mutations on peptide and protein aggregation rates. Nature. 2003;424(6950):805-8. (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 56
    • 34250872212 scopus 로고    scopus 로고
    • Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition
    • DOI 10.1021/bi6025374
    • .Andersen CB, Otzen D, Christiansen G, Rischel C. Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition. Biochemistry. 2007;46(24):7314-24. (Pubitemid 46974004)
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7314-7324
    • Andersen, C.B.1    Otzen, D.2    Christiansen, G.3    Rischel, C.4
  • 57
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard M, Zurdo J, Nettleton EJ, Dobson CM, Robinson CV. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 2000;9(10):1960-7.
    • (2000) Protein Sci , vol.9 , Issue.10 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 58
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils
    • Paravastu AK, Leapman RD, Yau WM, Tycko R. Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci USA. 2008;105(47):18349-54.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.47 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 59
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • DOI 10.1126/science.1105850
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science. 2005;307(5707):262-5. (Pubitemid 40116242)
    • (2005) Science , vol.307 , Issue.5707 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 60
    • 33744830833 scopus 로고    scopus 로고
    • Kinetics of insulin aggregation: Disentanglement of amyloid fibrillation from large-size cluster formation
    • DOI 10.1529/biophysj.105.077636
    • Manno M, Craparo EF, Martorana V, Bulone D, San Biagio PL. Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation. Biophys J. 2006;90(12):4585-91. (Pubitemid 43830902)
    • (2006) Biophysical Journal , vol.90 , Issue.12 , pp. 4585-4591
    • Manno, M.1    Craparo, E.F.2    Martorana, V.3    Bulone, D.4    San, B.P.L.5
  • 62
    • 77950689601 scopus 로고    scopus 로고
    • Strategies to increase the reproducibility of protein fibrillization in plate reader assays
    • Giehm L, Otzen DE. Strategies to increase the reproducibility of protein fibrillization in plate reader assays. Anal Biochem. 2010;400(2):270-81.
    • (2010) Anal Biochem , vol.400 , Issue.2 , pp. 270-281
    • Giehm, L.1    Otzen, D.E.2
  • 63
    • 0028872558 scopus 로고
    • Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease
    • Evans KC, Berger EP, Cho CG, Weisgraber KH, Lansbury PT Jr. Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease. Proc Natl Acad Sci USA. 1995;92(3):763-7.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.3 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.G.3    Weisgraber, K.H.4    Lansbury Jr., P.T.5
  • 64
    • 0037178811 scopus 로고    scopus 로고
    • Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature, and co-solute studies
    • DOI 10.1074/jbc.M202492200
    • .Kim YS, Randolph TW, Stevens FJ, Carpenter JF. Kinetics and energetics of assembly, nucleation, and growth of aggregates and fibrils for an amyloidogenic protein. Insights into transition states from pressure, temperature, and co-solute studies. J Biol Chem. 2002;277(30):27240-6. (Pubitemid 34951741)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27240-27246
    • Kim, Y.-S.1    Randolph, T.W.2    Stevens, F.J.3    Carpenter, J.F.4
  • 65
    • 34250872212 scopus 로고    scopus 로고
    • Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition
    • DOI 10.1021/bi6025374
    • Andersen CB, Otzen D, Christiansen G, Rischel C. Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition. Biochemistry. 2007;46(24):7314-24. (Pubitemid 46974004)
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7314-7324
    • Andersen, C.B.1    Otzen, D.2    Christiansen, G.3    Rischel, C.4
  • 66
    • 0030805003 scopus 로고    scopus 로고
    • The new era of biotech insulin analogues
    • DOI 10.1007/s001250051400
    • Brange J. The new era of biotech insulin analogues. Diabetologia. 1997;40 Suppl 2:S48-53. (Pubitemid 27306922)
    • (1997) Diabetologia , vol.40 , Issue.SUPPL. 2
    • Brange, J.1
  • 67
    • 33846005437 scopus 로고    scopus 로고
    • Absolute Correlation between Lag Time and Growth Rate in the Spontaneous Formation of Several Amyloid-like Aggregates and Fibrils
    • DOI 10.1016/j.jmb.2006.11.009, PII S0022283606015385
    • Fändrich M 2007. Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrils. J Mol Biol. 2007;365(5):1266-70. (Pubitemid 46048846)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1266-1270
    • Fandrich, M.1
  • 68
    • 70349505749 scopus 로고    scopus 로고
    • Formation mechanism of insulin fibrils and structural aspects of the insulin fibrillation process
    • Groenning M, Frokjaer S, Vestergaard B. Formation mechanism of insulin fibrils and structural aspects of the insulin fibrillation process. Curr Protein Pept Sci. 2009;10(5):509-28.
    • (2009) Curr Protein Pept Sci , vol.10 , Issue.5 , pp. 509-528
    • Groenning, M.1    Frokjaer, S.2    Vestergaard, B.3
  • 69
    • 80051800704 scopus 로고    scopus 로고
    • Quaternary conformational stability: The efect of reversible self-association on the fibrillation of two insulin analogs
    • Epub ahead of print
    • Ludwig DB, Webb JN, Fernández C, Carpenter JF, Randolph TW. Quaternary conformational stability: The efect of reversible self-association on the fibrillation of two insulin analogs. Biotechnol Bioeng. 2011. Epub ahead of print.
    • (2011) Biotechnol Bioeng
    • Ludwig, D.B.1    Webb, J.N.2    Fernández, C.3    Carpenter, J.F.4    Randolph, T.W.5


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