메뉴 건너뛰기




Volumn 93, Issue 9, 2007, Pages 3132-3141

Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMYLIN;

EID: 36049013172     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.110635     Document Type: Article
Times cited : (167)

References (67)
  • 1
    • 23444450224 scopus 로고    scopus 로고
    • Protein fibers as performance proteins: New technologies and applications
    • Scheibel, T. 2005. Protein fibers as performance proteins: new technologies and applications. Curr. Opin. Biotechnol. 16:427-433.
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 427-433
    • Scheibel, T.1
  • 2
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathway
    • Kelly, J. W. 1998. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathway. Curr. Opin. Struct. Biol. 8:101-106.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 3
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. 2001. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond. B Biol. Sci. 356:133-145.
    • (2001) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 4
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert, M. 2001. Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2:492-501.
    • (2001) Nat. Rev. Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 5
    • 0036975682 scopus 로고    scopus 로고
    • β-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease
    • De Felice, F. G., and S. T. Ferreira. 2002. β-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease. Cell. Mol. Neurobiol. 22:545-563.
    • (2002) Cell. Mol. Neurobiol , vol.22 , pp. 545-563
    • De Felice, F.G.1    Ferreira, S.T.2
  • 6
    • 32444432146 scopus 로고    scopus 로고
    • Aβ and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease
    • Guo, J.-P., T. Arai, J. Miklossy, and P. L. McGeer. 2006. Aβ and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease. Proc. Natl. Acad. Sci. USA. 103:1953-1958.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1953-1958
    • Guo, J.-P.1    Arai, T.2    Miklossy, J.3    McGeer, P.L.4
  • 7
    • 33646155955 scopus 로고    scopus 로고
    • Structure of core domain of fibril-forming PHF/tau fragments
    • Inouye, H., D. Sharma, W. J. Goux, and D. A. Kirschner. 2006. Structure of core domain of fibril-forming PHF/tau fragments. Biophys. J. 90:1774-1789.
    • (2006) Biophys. J , vol.90 , pp. 1774-1789
    • Inouye, H.1    Sharma, D.2    Goux, W.J.3    Kirschner, D.A.4
  • 9
    • 33645669165 scopus 로고    scopus 로고
    • Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides
    • Rojas Quijano, F. A., D. Morrow, B. M. Wise, F. L. Brancia, and W. J. Goux. 2006. Prediction of nucleating sequences from amyloidogenic propensities of tau-related peptides. Biochemistry. 45:4638-4652.
    • (2006) Biochemistry , vol.45 , pp. 4638-4652
    • Rojas Quijano, F.A.1    Morrow, D.2    Wise, B.M.3    Brancia, F.L.4    Goux, W.J.5
  • 11
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • Tycko, R. 2004. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14:96-103.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 96-103
    • Tycko, R.1
  • 12
    • 33746780089 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin
    • Cordeiro, Y., J. Kraineva, M. C. Suarez, A. G. Tempesta, J. W. Kelly, J. L. Silva, R. Winter, and D. Foguel. 2006. Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin. Biophys. J. 91:957-967.
    • (2006) Biophys. J , vol.91 , pp. 957-967
    • Cordeiro, Y.1    Kraineva, J.2    Suarez, M.C.3    Tempesta, A.G.4    Kelly, J.W.5    Silva, J.L.6    Winter, R.7    Foguel, D.8
  • 13
    • 30744469843 scopus 로고    scopus 로고
    • Solvation-assisted pressure tuning of insulin fibrillation: From novel aggregation pathways to biotechnological applications
    • Grudzielanek, S., V. Smirnovas, and R. Winter. 2006. Solvation-assisted pressure tuning of insulin fibrillation: from novel aggregation pathways to biotechnological applications. J. Mol. Biol. 356:497-509.
    • (2006) J. Mol. Biol , vol.356 , pp. 497-509
    • Grudzielanek, S.1    Smirnovas, V.2    Winter, R.3
  • 14
    • 0024804095 scopus 로고
    • Amylin and the amylin gene: Structure, function and relationship to islet amyloid and to diabetes mellitus
    • Cooper, G. J. S., A. J. Day, A. C. Willis, A. N. Roberts, K. B. M. Reid, and B. Leighton. 1989. Amylin and the amylin gene: structure, function and relationship to islet amyloid and to diabetes mellitus. Biochim. Biophys. Acta. 1014:247-258.
    • (1989) Biochim. Biophys. Acta , vol.1014 , pp. 247-258
    • Cooper, G.J.S.1    Day, A.J.2    Willis, A.C.3    Roberts, A.N.4    Reid, K.B.M.5    Leighton, B.6
  • 16
    • 0024362027 scopus 로고
    • Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion fromisolated rat pancreatic islets
    • Ohsawa, H., A. Kanatsuka, T. Yamaguchi, H. Makino, and S. Yoshida. 1989. Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion fromisolated rat pancreatic islets. Biochem. Biophys. Res. Commun. 160:961-967.
    • (1989) Biochem. Biophys. Res. Commun , vol.160 , pp. 961-967
    • Ohsawa, H.1    Kanatsuka, A.2    Yamaguchi, T.3    Makino, H.4    Yoshida, S.5
  • 17
    • 0025364139 scopus 로고
    • Islet amyloid polypeptide (IAPP;amylin) influences the endocrine but not the exocrine rat pancreas
    • Fehmann, H. C., V. Weber, R. Goke, B. Goke, R. Eissele, and R. Arnold. 1990. Islet amyloid polypeptide (IAPP;amylin) influences the endocrine but not the exocrine rat pancreas. Biochem. Biophys. Res. Commun. 167:1102-1108.
    • (1990) Biochem. Biophys. Res. Commun , vol.167 , pp. 1102-1108
    • Fehmann, H.C.1    Weber, V.2    Goke, R.3    Goke, B.4    Eissele, R.5    Arnold, R.6
  • 18
    • 0026654926 scopus 로고
    • Islet amyloid polypeptide: Mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus
    • Johnson, K. H., T. D. O'Brien, C. Betsholtz, and P. Westermark. 1992. Islet amyloid polypeptide: mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus. Lab. Invest. 66:522-535.
    • (1992) Lab. Invest , vol.66 , pp. 522-535
    • Johnson, K.H.1    O'Brien, T.D.2    Betsholtz, C.3    Westermark, P.4
  • 21
    • 1842425710 scopus 로고    scopus 로고
    • Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation
    • Green, J. D., C. Goldsbury, J. Kistler, G. J. S. Cooper, and U. Aebi. 2004. Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation. J. Biol. Chem. 279:12206-12212.
    • (2004) J. Biol. Chem , vol.279 , pp. 12206-12212
    • Green, J.D.1    Goldsbury, C.2    Kistler, J.3    Cooper, G.J.S.4    Aebi, U.5
  • 24
    • 0141653970 scopus 로고    scopus 로고
    • The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies
    • Porat, Y., S. Kolusheva, R. Jelinek, and E. Gazit. 2003. The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies. Biochemistry. 42:10971-10977.
    • (2003) Biochemistry , vol.42 , pp. 10971-10977
    • Porat, Y.1    Kolusheva, S.2    Jelinek, R.3    Gazit, E.4
  • 25
    • 0035955455 scopus 로고    scopus 로고
    • Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation
    • Harroun, T. A., J. P. Bradshaw, and R. H. Ashley. 2001. Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation. FEBS Lett. 507:200-204.
    • (2001) FEBS Lett , vol.507 , pp. 200-204
    • Harroun, T.A.1    Bradshaw, J.P.2    Ashley, R.H.3
  • 26
    • 4243516677 scopus 로고    scopus 로고
    • High islet amyloid polypeptide secretion results in transient hyperglycemia without beta-cell death
    • Janson, J., P. C. Butler, and W. Soeller. 1998. High islet amyloid polypeptide secretion results in transient hyperglycemia without beta-cell death. Diabetes. 47(Suppl. 1):A30.
    • (1998) Diabetes , vol.47 , Issue.SUPPL. 1
    • Janson, J.1    Butler, P.C.2    Soeller, W.3
  • 27
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov, T. A., M. C. Lin, and B. L. Kagan. 1996. Pore formation by the cytotoxic islet amyloid peptide amylin. J. Biol. Chem. 271:1988-1992.
    • (1996) J. Biol. Chem , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 28
    • 33747119677 scopus 로고    scopus 로고
    • Conserved and cooperative assembly of membrane-bound α-helical states of islet amyloid polypeptide
    • Knight, J. D., J. A. Hebda, and A. D. Miranker. 2006. Conserved and cooperative assembly of membrane-bound α-helical states of islet amyloid polypeptide. Biochemistry. 45:9496-9508.
    • (2006) Biochemistry , vol.45 , pp. 9496-9508
    • Knight, J.D.1    Hebda, J.A.2    Miranker, A.D.3
  • 29
    • 24644502612 scopus 로고    scopus 로고
    • Lipid membranes modulate the structure of islet amyloid polyp
    • Jayasinghe, S. A., and R. Langen. 2005. Lipid membranes modulate the structure of islet amyloid polyp. Biochemistry. 44:12113-12119.
    • (2005) Biochemistry , vol.44 , pp. 12113-12119
    • Jayasinghe, S.A.1    Langen, R.2
  • 30
    • 0018146301 scopus 로고
    • The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus
    • Westermark, P., and E. Wilander. 1978. The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus. Diabetologia. 15:417-421.
    • (1978) Diabetologia , vol.15 , pp. 417-421
    • Westermark, P.1    Wilander, E.2
  • 31
    • 0019805122 scopus 로고
    • The relation of islet amyloid to the clinical type of diabetes
    • Maloy, A. L., D. S. Longnecker, and E. R. Greenberg. 1981. The relation of islet amyloid to the clinical type of diabetes. Hum. Pathol. 12:917-922.
    • (1981) Hum. Pathol , vol.12 , pp. 917-922
    • Maloy, A.L.1    Longnecker, D.S.2    Greenberg, E.R.3
  • 32
    • 0036716508 scopus 로고    scopus 로고
    • Pancreatic islet amyloid in type 2 diabetes mellitus: A clinical and historical review
    • Hayden, M. R. 2002. Pancreatic islet amyloid in type 2 diabetes mellitus: a clinical and historical review. Mo. Med. 99:495-498.
    • (2002) Mo. Med , vol.99 , pp. 495-498
    • Hayden, M.R.1
  • 33
    • 4444292588 scopus 로고    scopus 로고
    • Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide
    • Green, J. D., L. Kreplak, C. Goldsbury, X. Li Blatter, M. Stolz, G. Cooper, A. Seelig, J. Kistler, and U. Aebi. 2004. Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide. J. Mol. Biol. 342:877-887.
    • (2004) J. Mol. Biol , vol.342 , pp. 877-887
    • Green, J.D.1    Kreplak, L.2    Goldsbury, C.3    Li Blatter, X.4    Stolz, M.5    Cooper, G.6    Seelig, A.7    Kistler, J.8    Aebi, U.9
  • 34
    • 13844303627 scopus 로고    scopus 로고
    • Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin
    • Balali-Mood, K., R. H. Ashley, T. Hauss, and J. P. Bradshaw. 2005. Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin. FEBS Lett. 579:1143-1148.
    • (2005) FEBS Lett , vol.579 , pp. 1143-1148
    • Balali-Mood, K.1    Ashley, R.H.2    Hauss, T.3    Bradshaw, J.P.4
  • 35
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • Knight, J. D., and A. D. Miranker. 2004. Phospholipid catalysis of diabetic amyloid assembly. J. Mol. Biol. 341:1175-1187.
    • (2004) J. Mol. Biol , vol.341 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 36
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro, A., E. Mina, R. Kayed, S. C. Milton, I. Parker, and C. G. Glabe. 2005. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280:17294-17300.
    • (2005) J. Biol. Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 37
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., E. Head, J. L. Thompson, T. M. McIntire, S. C. Milton, C. W. Cotman, and C. G. Glabe. 2003. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 300:486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 38
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed, R., Y. Sokolov, B. Edmonds, T. M. McIntire, S. C. Milton, J. E. Hall, and C. G. Glabe. 2004. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 279:46363-46366.
    • (2004) J. Biol. Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 39
    • 0037167613 scopus 로고    scopus 로고
    • Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes
    • Anguiano, M., R. J. Nowak, and P. T. Lansbury Jr. 2002. Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry. 41:11338-11343.
    • (2002) Biochemistry , vol.41 , pp. 11338-11343
    • Anguiano, M.1    Nowak, R.J.2    Lansbury Jr., P.T.3
  • 41
    • 0141780910 scopus 로고    scopus 로고
    • Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: Pathogenesis of diabetes in a mouse model
    • Hoppener, J. W., C. Oosterwijk, M. G. Nieuwenhuis, G. Posthuma, J. H. Thijssen, T. M. Vroom, B. Ahren, and C. J. Lips. 1999. Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: pathogenesis of diabetes in a mouse model. Diabetologia. 42:427-434.
    • (1999) Diabetologia , vol.42 , pp. 427-434
    • Hoppener, J.W.1    Oosterwijk, C.2    Nieuwenhuis, M.G.3    Posthuma, G.4    Thijssen, J.H.5    Vroom, T.M.6    Ahren, B.7    Lips, C.J.8
  • 42
    • 2542581025 scopus 로고    scopus 로고
    • Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): A new model for type 2 diabetes
    • Butler, A. E., J. Jang, T. Gurlo, M. D. Carty, W. C. Soeller, and P. C. Butler. 2004. Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes. Diabetes. 53:1509-1516.
    • (2004) Diabetes , vol.53 , pp. 1509-1516
    • Butler, A.E.1    Jang, J.2    Gurlo, T.3    Carty, M.D.4    Soeller, W.C.5    Butler, P.C.6
  • 43
    • 0028237335 scopus 로고
    • External reflection FTIR of peptide monolayer films in situ at the air/water interface: Experimental design, spectra-structure correlations, and effects of hydrogen-deuterium exchange
    • Flach, C. R., J. W. Brauner, J. W. Taylor, R. C. Baldwin, and R. Mendelsohn. 1994. External reflection FTIR of peptide monolayer films in situ at the air/water interface: experimental design, spectra-structure correlations, and effects of hydrogen-deuterium exchange. Biophys. J. 67:402-410.
    • (1994) Biophys. J , vol.67 , pp. 402-410
    • Flach, C.R.1    Brauner, J.W.2    Taylor, J.W.3    Baldwin, R.C.4    Mendelsohn, R.5
  • 45
    • 18844362604 scopus 로고    scopus 로고
    • Monolayer-multilayer transitions in a lung surfactant model: IR reflection-absorption spectroscopy and atomic force microscopy
    • Wang, L., P. Cai, H.-J. Galla, H. He, C. R. Flach, and R. Mendelsohn. 2005. Monolayer-multilayer transitions in a lung surfactant model: IR reflection-absorption spectroscopy and atomic force microscopy. Eur. Biophys. J. 34:243-254.
    • (2005) Eur. Biophys. J , vol.34 , pp. 243-254
    • Wang, L.1    Cai, P.2    Galla, H.-J.3    He, H.4    Flach, C.R.5    Mendelsohn, R.6
  • 46
    • 2342473919 scopus 로고    scopus 로고
    • Orientation of peptides in aqueous monolayer films. Infrared reflection-absorption spectroscopy studies of a synthetic amphipathic β-sheet
    • Xu, Z., J. W. Brauner, C. R. Flach, and R. Mendelsohn. 2004. Orientation of peptides in aqueous monolayer films. Infrared reflection-absorption spectroscopy studies of a synthetic amphipathic β-sheet. Langmuir. 20:3730-3733.
    • (2004) Langmuir , vol.20 , pp. 3730-3733
    • Xu, Z.1    Brauner, J.W.2    Flach, C.R.3    Mendelsohn, R.4
  • 47
    • 2942690094 scopus 로고    scopus 로고
    • Infrared reflection absorption spectroscopy of amphipathic model peptides at the air/water interface
    • Kerth, A., A. Erbe, M. Dathe, and A. Blume. 2004. Infrared reflection absorption spectroscopy of amphipathic model peptides at the air/water interface. Biophys. J. 86:3750-3758.
    • (2004) Biophys. J , vol.86 , pp. 3750-3758
    • Kerth, A.1    Erbe, A.2    Dathe, M.3    Blume, A.4
  • 48
    • 26944494925 scopus 로고    scopus 로고
    • Adsorption of amyloid beta (1-40) peptide at phospholipid monolayers
    • Maltseva, E., A. Kerth, A. Blume, H. Möhwald, and G. Brezesinski. 2005. Adsorption of amyloid beta (1-40) peptide at phospholipid monolayers. ChemBioChem. 6:1817-1824.
    • (2005) ChemBioChem , vol.6 , pp. 1817-1824
    • Maltseva, E.1    Kerth, A.2    Blume, A.3    Möhwald, H.4    Brezesinski, G.5
  • 49
    • 33746858605 scopus 로고    scopus 로고
    • Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS)
    • Meister, A., C. Nicolini, H. Waldmann, J. Kuhlmann, A. Kerth, R. Winter, and A. Blume. 2006. Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS). Biophys. J. 91:1388-1401.
    • (2006) Biophys. J , vol.91 , pp. 1388-1401
    • Meister, A.1    Nicolini, C.2    Waldmann, H.3    Kuhlmann, J.4    Kerth, A.5    Winter, R.6    Blume, A.7
  • 50
    • 0016717097 scopus 로고
    • Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers
    • Demel, R. A., W. S. Geurts van Kessel, R. F. Zwaal, B. Roelofsen, and L. L. van Deenen. 1975. Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers. Biochim. Biophys. Acta. 406:97-107.
    • (1975) Biochim. Biophys. Acta , vol.406 , pp. 97-107
    • Demel, R.A.1    Geurts van Kessel, W.S.2    Zwaal, R.F.3    Roelofsen, B.4    van Deenen, L.L.5
  • 51
    • 0034677739 scopus 로고    scopus 로고
    • Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils
    • Higham, C. E., E. T. A. S. Jaikaran, P. E. Fraser, M. Gross, and A. Clark. 2000. Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils. FEBS Lett. 470:55-60.
    • (2000) FEBS Lett , vol.470 , pp. 55-60
    • Higham, C.E.1    Jaikaran, E.T.A.S.2    Fraser, P.E.3    Gross, M.4    Clark, A.5
  • 52
    • 0035969513 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes: From molecular misfolding to islet pathophysiology
    • Jaikaran, E. T., and A. Clark. 2001. Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochim. Biophys. Acta. 1537:179-203.
    • (2001) Biochim. Biophys. Acta , vol.1537 , pp. 179-203
    • Jaikaran, E.T.1    Clark, A.2
  • 53
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin
    • Kajava, A. V., U. Aebi, and A. C. Steven. 2005. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 348:247-252.
    • (2005) J. Mol. Biol , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 54
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • Lorenzo, A., B. Razzaboni, G. C. Weir, and B. A. Yankner. 1994. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature. 368:756-760.
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Weir, G.C.3    Yankner, B.A.4
  • 55
    • 0001040367 scopus 로고
    • An algorithm for protein secondary structure prediction based on class prediction
    • Deleage, G., and B. Roux. 1987. An algorithm for protein secondary structure prediction based on class prediction. Protein Eng. 1:289-294.
    • (1987) Protein Eng , vol.1 , pp. 289-294
    • Deleage, G.1    Roux, B.2
  • 56
    • 0024283401 scopus 로고
    • Improvements in a secondary structure prediction method based on a search for local sequence homologies and its use as a model building tool
    • Levin, T. M., and J. Garnier. 1988. Improvements in a secondary structure prediction method based on a search for local sequence homologies and its use as a model building tool. Biochim. Biochim. Acta. 955:283-295.
    • (1988) Biochim. Biochim. Acta , vol.955 , pp. 283-295
    • Levin, T.M.1    Garnier, J.2
  • 57
    • 0028009149 scopus 로고
    • SOPM: A self-optimized method for protein secondary structure prediction
    • Geourjon, C., and G. Deleage. 1994. SOPM: a self-optimized method for protein secondary structure prediction. Protein Eng. 7:157-164.
    • (1994) Protein Eng , vol.7 , pp. 157-164
    • Geourjon, C.1    Deleage, G.2
  • 59
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • Jansen, R., W. Dzwolak, and R. Winter. 2005. Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. Biophys. J. 88:1344-1353.
    • (2005) Biophys. J , vol.88 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 60
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis
    • Jaikaran, E. T., C. E. Higham, L. C. Serpell, J. Zurdo, M. Gross, A. Clark, and P. E. Fraser. 2001. Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 308:515-525.
    • (2001) J. Mol. Biol , vol.308 , pp. 515-525
    • Jaikaran, E.T.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6    Fraser, P.E.7
  • 61
    • 33845960266 scopus 로고    scopus 로고
    • Direct detection of transient alpha-helical states in islet amyloid polypeptide
    • Williamson, J. A., and A. D. Miranker. 2007. Direct detection of transient alpha-helical states in islet amyloid polypeptide. Protein Sci. 16:1-8.
    • (2007) Protein Sci , vol.16 , pp. 1-8
    • Williamson, J.A.1    Miranker, A.D.2
  • 62
    • 0033555275 scopus 로고    scopus 로고
    • Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease
    • Shao, H., S.-C. Jao, K. Ma, and M. G. Zagorski. 1999. Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease. J. Mol. Biol. 285:755-773.
    • (1999) J. Mol. Biol , vol.285 , pp. 755-773
    • Shao, H.1    Jao, S.-C.2    Ma, K.3    Zagorski, M.G.4
  • 63
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis
    • Kirkitadze, M. D., M. M. Condron, and D. B. Teplow. 2001. Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis. J. Mol. Biol. 312:1103-1119.
    • (2001) J. Mol. Biol , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 64
    • 0037469147 scopus 로고    scopus 로고
    • The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation
    • Kessler, J. C., J. C. Rochet, and P. T. Lansbury Jr. 2003. The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation. Biochemistry. 42:672-678.
    • (2003) Biochemistry , vol.42 , pp. 672-678
    • Kessler, J.C.1    Rochet, J.C.2    Lansbury Jr., P.T.3
  • 65
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and C. M. Dobson. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 66
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin
    • Kajava, A. V., E. Aebi, and A. C. Steven. 2005. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J. Mol. Biol. 348:247-252.
    • (2005) J. Mol. Biol , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, E.2    Steven, A.C.3
  • 67
    • 0033534397 scopus 로고    scopus 로고
    • Watching amyloid fibrils grow by time-lapse atomic force microscopy
    • Goldsbury, C., J. Kistler, U. Aebi, T. Arvinte, and G. J. S. Cooper. 1999. Watching amyloid fibrils grow by time-lapse atomic force microscopy. J. Mol. Biol. 285:33-39.
    • (1999) J. Mol. Biol , vol.285 , pp. 33-39
    • Goldsbury, C.1    Kistler, J.2    Aebi, U.3    Arvinte, T.4    Cooper, G.J.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.