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Volumn 95, Issue 1, 2008, Pages 366-377

Early stages of amyloid fibril formation studied by liquid-state NMR: The peptide hormone glucagon

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; GLUCAGON;

EID: 46749110019     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.122895     Document Type: Article
Times cited : (34)

References (71)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and F. 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, F.M.2
  • 2
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B., and P. T. Lansbury Jr. 2003. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:267-298.
    • (2003) Annu. Rev. Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury Jr., P.T.2
  • 3
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko, R. 2006. Molecular structure of amyloid fibrils: insights from solid-state NMR. Q. Rev. Biophys. 39:1-55.
    • (2006) Q. Rev. Biophys , vol.39 , pp. 1-55
    • Tycko, R.1
  • 4
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe, J. D., and A. S. Cohen. 2000. Review: history of the amyloid fibril. J. Struct. Biol. 130:88-98.
    • (2000) J. Struct. Biol , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 5
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer, S., and D. E. Otzen. 2005. Protein drug stability: a formulation challenge. Nat. Rev. Drug. Disc. 4:298-306.
    • (2005) Nat. Rev. Drug. Disc , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 6
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. 2003. Protein folding and misfolding. Nature. 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 7
    • 0037041441 scopus 로고    scopus 로고
    • Medicine: Danger misfolding proteins
    • Ellis, R. J., and T. J. T. Pinheiro. 2002. Medicine: danger misfolding proteins. Nature. 416:483-484.
    • (2002) Nature , vol.416 , pp. 483-484
    • Ellis, R.J.1    Pinheiro, T.J.T.2
  • 8
    • 0000079910 scopus 로고    scopus 로고
    • Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro
    • Naiki, H., N. Hashimoto, S. Suzuki, H. Kimura, K. Nakakuki, and F. Gejyo. 1997. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro. Amyloid. 4:223-232.
    • (1997) Amyloid , vol.4 , pp. 223-232
    • Naiki, H.1    Hashimoto, N.2    Suzuki, S.3    Kimura, H.4    Nakakuki, K.5    Gejyo, F.6
  • 10
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of α-synuclein assembly by β- and γ-synucleins
    • Uversky, V. N., J. Li, P. Souillac, I. S. Millett, S. Doniach, R. Jakes, M. Goedert, and M. L. Fink. 2002. Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of α-synuclein assembly by β- and γ-synucleins. J. Biol. Chem. 277:11970-11978.
    • (2002) J. Biol. Chem , vol.277 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Millett, I.S.4    Doniach, S.5    Jakes, R.6    Goedert, M.7    Fink, M.L.8
  • 11
    • 3342902033 scopus 로고    scopus 로고
    • Modulation of S6 fibrillation by unfolding rates and gatekeeper residues
    • Pedersen, J. S., G. Christensen, and D. E. Otzen. 2004. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. J. Mol. Biol. 341:575-588.
    • (2004) J. Mol. Biol , vol.341 , pp. 575-588
    • Pedersen, J.S.1    Christensen, G.2    Otzen, D.E.3
  • 12
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • Zandomeneghi, G., M. R. H. Krebs, M. G. McCammon, and M. Fändrich. 2004. FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci. 13:3314-3321.
    • (2004) Protein Sci , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.H.2    McCammon, M.G.3    Fändrich, M.4
  • 13
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard, M., J. Zurdo, E. J. Nettleton, C. M. Dobson, and C. V. Robinson. 2000. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9:1960-1967.
    • (2000) Protein Sci , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 14
    • 28944433479 scopus 로고    scopus 로고
    • The changing face of glucagon fibrillation: Structural polymorphism and conformational imprinting
    • Pedersen, J. S., D. Dikov, J. L. Fink, H. A. Hjuler, G. Christiansen, and D. E. Otzen. 2006. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J. Mol. Biol. 355:501-523.
    • (2006) J. Mol. Biol , vol.355 , pp. 501-523
    • Pedersen, J.S.1    Dikov, D.2    Fink, J.L.3    Hjuler, H.A.4    Christiansen, G.5    Otzen, D.E.6
  • 17
    • 0016329537 scopus 로고
    • β-pleated sheet fibrils - comparison of native amyloid with synthetic protein fibrils
    • Glenner, G. G., E. D. Eanes, H. A. Bladen, R. P. Linke, and J. D. Termine. 1974. β-pleated sheet fibrils - comparison of native amyloid with synthetic protein fibrils. J. Histochem. Cytochem. 22:1141-1158.
    • (1974) J. Histochem. Cytochem , vol.22 , pp. 1141-1158
    • Glenner, G.G.1    Eanes, E.D.2    Bladen, H.A.3    Linke, R.P.4    Termine, J.D.5
  • 21
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova, A. T., R. D. Leapman, Z. Guo, W.-M. Yau, M. P. Mattson, and R. Tycko. 2005. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science. 307:262-265.
    • (2005) Science , vol.307 , 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
  • 22
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec, C. P., C. E. MacPhee, V. S. Bajaj, M. T. McMahon, C. M. Dobson, and R. G. Griffin. 2004. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc. Natl. Acad. Sci. USA. 101:711-716.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1    MacPhee, C.E.2    Bajaj, V.S.3    McMahon, M.T.4    Dobson, C.M.5    Griffin, R.G.6
  • 24
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
    • Heise, H., W. Hoyer, S. Becker, O. C. Andronesi, D. Riedel, and M. Baldus. 2005. Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. USA. 102:15871-15876.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 25
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes, E. D., and G. G. Glenner. 1968. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16:673-677.
    • (1968) J. Histochem. Cytochem , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 26
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases: Importance of seeding
    • Come, J. H., P. E. Fraser, and P. T. Lansbury, Jr. 1993. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc. Natl. Acad. Sci. USA. 90:5959-5963.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury Jr., P.T.3
  • 27
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • Jarrett, J. T., and P. T. Lansbury, Jr. 1992. Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry. 31:12345-12352.
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 28
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon, W., and J. W. Kelly. 1992. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry. 31:8654-8660.
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 30
    • 34250872212 scopus 로고    scopus 로고
    • Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition
    • Andersen, C. B., D. Otzen, G. Christiansen, and C. Rischel. 2007. Glucagon amyloid-like fibril morphology is selected via morphology-dependent growth inhibition. Biochemistry. 46:7314-7324.
    • (2007) Biochemistry , vol.46 , pp. 7314-7324
    • Andersen, C.B.1    Otzen, D.2    Christiansen, G.3    Rischel, C.4
  • 31
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti, F., M. Stefani, N. Taddei, G. Ramponi, and C. M. Dobson. 2003. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature. 424:805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 32
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D. M., D. M. Walsh, C. P. Ye, T. Diehl, S. Vasquez, P. M. Vassilev, D. B. Teplow, and D. J. Selkoe. 1999. Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19:8876-8884.
    • (1999) J. Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 34
    • 33644816759 scopus 로고    scopus 로고
    • Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
    • Soto, C., L. Estrada, and J. Castilla. 2006. Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem. Sci. 31:150-155.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 150-155
    • Soto, C.1    Estrada, L.2    Castilla, J.3
  • 35
    • 34548718786 scopus 로고    scopus 로고
    • Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface
    • Hovgaard, M. B., M. Dong, D. E. Otzen, and F. Besenbacher. 2007. Quartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interface. Biophys. J. 93:2162-2169.
    • (2007) Biophys. J , vol.93 , pp. 2162-2169
    • Hovgaard, M.B.1    Dong, M.2    Otzen, D.E.3    Besenbacher, F.4
  • 36
    • 33748450346 scopus 로고    scopus 로고
    • Amyloid fibrils of glucagon characterized by high-resolution atomic force microscopy
    • De Jong, K. L., B. Incledon, C. M. Yip, and M. R. DeFelippis. 2006. Amyloid fibrils of glucagon characterized by high-resolution atomic force microscopy. Biophys. J. 91:1905-1914.
    • (2006) Biophys. J , vol.91 , pp. 1905-1914
    • De Jong, K.L.1    Incledon, B.2    Yip, C.M.3    DeFelippis, M.R.4
  • 37
    • 33748892027 scopus 로고    scopus 로고
    • AFM study of glucagon fibrillation via oligomeric structures resulting in interwoven fibrils
    • Dong, M. D., M. B. Hovgaard, S. L. Xu, D. E. Otzen, and F. Besenbacher. 2006. AFM study of glucagon fibrillation via oligomeric structures resulting in interwoven fibrils. Nanotechnology. 17:4003-4009.
    • (2006) Nanotechnology , vol.17 , pp. 4003-4009
    • Dong, M.D.1    Hovgaard, M.B.2    Xu, S.L.3    Otzen, D.E.4    Besenbacher, F.5
  • 39
    • 3242735868 scopus 로고    scopus 로고
    • Mishandling of the therapeutic peptide glucagon generates cytotoxic amyloidogenic fibrils
    • Onoue, S., K. Ohshima, K. Debari, K. Koh, S. Shioda, S. Iwasa, K. Kashimoto, and T. Yajima. 2004. Mishandling of the therapeutic peptide glucagon generates cytotoxic amyloidogenic fibrils. Pharm. Res. 21:1274-1283.
    • (2004) Pharm. Res , vol.21 , pp. 1274-1283
    • Onoue, S.1    Ohshima, K.2    Debari, K.3    Koh, K.4    Shioda, S.5    Iwasa, S.6    Kashimoto, K.7    Yajima, T.8
  • 40
    • 0001693313 scopus 로고
    • Aqueous extracts of pancreas III. Some precipitation reactions of insulin
    • Kimball, C. P., and J. R. Murlin. 1923. Aqueous extracts of pancreas III. Some precipitation reactions of insulin. J. Biol. Chem. 58:337-348.
    • (1923) J. Biol. Chem , vol.58 , pp. 337-348
    • Kimball, C.P.1    Murlin, J.R.2
  • 41
    • 50449154488 scopus 로고
    • Glucagon; the hyperglycaemic glycogenolytic factor of the pancreas
    • De Duve, C. 1953. Glucagon; the hyperglycaemic glycogenolytic factor of the pancreas. Lancet. 265:99-104.
    • (1953) Lancet , vol.265 , pp. 99-104
    • De Duve, C.1
  • 43
    • 0014599351 scopus 로고
    • Formation and structure of gels and fibrils from glucagon
    • Beaven, G. H., W. B. Gratzer, and H. G. Davies. 1969. Formation and structure of gels and fibrils from glucagon. Eur. J. Biochem. 11:37-42.
    • (1969) Eur. J. Biochem , vol.11 , pp. 37-42
    • Beaven, G.H.1    Gratzer, W.B.2    Davies, H.G.3
  • 44
    • 0017700305 scopus 로고
    • Conformational transitions of glucagon in solution: The a to b transition
    • Moran, E. C., P. Y. Chou, and G. D. Fasman. 1977. Conformational transitions of glucagon in solution: the a to b transition. Biochem. Biophys. Res. Commun. 77:1300-1306.
    • (1977) Biochem. Biophys. Res. Commun , vol.77 , pp. 1300-1306
    • Moran, E.C.1    Chou, P.Y.2    Fasman, G.D.3
  • 45
    • 0016709043 scopus 로고
    • X-ray analysis of glucagon and its relationship to receptor binding
    • Sasaki, K., S. Dockerill, D. A. Adamiak, I. J. Tickle, and T. Blundell. 1975. X-ray analysis of glucagon and its relationship to receptor binding. Nature. 257:751-757.
    • (1975) Nature , vol.257 , pp. 751-757
    • Sasaki, K.1    Dockerill, S.2    Adamiak, D.A.3    Tickle, I.J.4    Blundell, T.5
  • 46
    • 0018196016 scopus 로고
    • 1H nuclear magnetic resonance studies of the molecular conformation of monomeric glucagon in aqueous solution
    • 1H nuclear magnetic resonance studies of the molecular conformation of monomeric glucagon in aqueous solution. Eur. J. Biochem. 91:204-214.
    • (1978) Eur. J. Biochem , vol.91 , pp. 204-214
    • Bösch, C.1    Bundi, A.2    Oppliger, M.3    Wüthrich, K.4
  • 48
    • 0019297405 scopus 로고
    • Proton NMR studies of the association and folding of glucagon in solution
    • Wagman, M. E., C. M. Dobson, and M. Karplus. 1980. Proton NMR studies of the association and folding of glucagon in solution. FEBS Lett. 119:265-270.
    • (1980) FEBS Lett , vol.119 , pp. 265-270
    • Wagman, M.E.1    Dobson, C.M.2    Karplus, M.3
  • 50
    • 0001098519 scopus 로고
    • Diffusion-ordered two-dimensional nuclear magnetic resonance spectroscopy
    • Morris, K. F., and C. S. Johnson. 1992. Diffusion-ordered two-dimensional nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 114:3139-3141.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 3139-3141
    • Morris, K.F.1    Johnson, C.S.2
  • 51
    • 0000600340 scopus 로고
    • General intelligence objectivity determined and measured
    • Spearman, C. H. 1904. General intelligence objectivity determined and measured. Am. J. Psychol. 15:201-293.
    • (1904) Am. J. Psychol , vol.15 , pp. 201-293
    • Spearman, C.H.1
  • 52
    • 84860107456 scopus 로고    scopus 로고
    • The R project for statistical computing. Web-page: http://www.r-project. org/index.html
    • Web-page
  • 53
    • 0038004458 scopus 로고    scopus 로고
    • A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils
    • Claessen, D., R. Rink, W. de Jong, J. Siebring, P. de Vreugd, F. G. Boersma, L. Dijkhuizen, and H. A. Wosten. 2003. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev. 17:1714-1726.
    • (2003) Genes Dev , vol.17 , pp. 1714-1726
    • Claessen, D.1    Rink, R.2    de Jong, W.3    Siebring, J.4    de Vreugd, P.5    Boersma, F.G.6    Dijkhuizen, L.7    Wosten, H.A.8
  • 55
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins, S. R., A. Douglass, R. D. Vale, and J. S. Weissman. 2004. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2:e321.
    • (2004) PLoS Biol , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 57
    • 13444310701 scopus 로고    scopus 로고
    • Characterization of chemical exchange between soluble and aggregated states of β-amyloid by solution-state NMR upon variation of salt conditions
    • Narayanan, S., and B. Reif. 2005. Characterization of chemical exchange between soluble and aggregated states of β-amyloid by solution-state NMR upon variation of salt conditions. Biochemistry. 44:1444-1452.
    • (2005) Biochemistry , vol.44 , pp. 1444-1452
    • Narayanan, S.1    Reif, B.2
  • 58
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer, M., and B. Meyer. 1999. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem. Int. Ed. 38:1784-1788.
    • (1999) Angew. Chem. Int. Ed , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 59
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar, A. P., K. F. DuBay, J. Zurdo, F. Chiti, M. Vendruscolo, and C. M. Dobson. 2005. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350:379-392.
    • (2005) J. Mol. Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    DuBay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 60
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., B. D. Sykes, and F. M. Richards. 1992. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 61
    • 33745356391 scopus 로고
    • Contact electron-spin coupling of nuclear magnetic moments
    • Karplus, M. 1959. Contact electron-spin coupling of nuclear magnetic moments. J. Chem. Phys. 30:11-15.
    • (1959) J. Chem. Phys , vol.30 , pp. 11-15
    • Karplus, M.1
  • 63
    • 0028966761 scopus 로고
    • Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR
    • Zhang, Y. Z., Y. Paterson, and H. Roder. 1995. Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR. Protein Sci. 4:804-814.
    • (1995) Protein Sci , vol.4 , pp. 804-814
    • Zhang, Y.Z.1    Paterson, Y.2    Roder, H.3
  • 64
    • 0345598918 scopus 로고    scopus 로고
    • NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126
    • Kuwata, K., T. Matumoto, H. Cheng, K. Nagayama, T. L. James, and H. Roder. 2003. NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. Proc. Natl. Acad. Sci. USA. 100:14790-14795.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14790-14795
    • Kuwata, K.1    Matumoto, T.2    Cheng, H.3    Nagayama, K.4    James, T.L.5    Roder, H.6
  • 67
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla, A. M., F. Rousseau, J. Schymkowitz, and L. Serrano. 2004. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 22:1240-1241.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1240-1241
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 68
    • 33845251797 scopus 로고    scopus 로고
    • N- and C-terminal hydrophobic patches are involved in fibrillation of glucagon
    • Pedersen, J. S., D. Dikov, and D. E. Otzen. 2006. N- and C-terminal hydrophobic patches are involved in fibrillation of glucagon. Biochemistry. 45:14503-14512.
    • (2006) Biochemistry , vol.45 , pp. 14503-14512
    • Pedersen, J.S.1    Dikov, D.2    Otzen, D.E.3
  • 69
    • 33845978790 scopus 로고    scopus 로고
    • Trovato, A., F. Chiti, A. Maritan, and F. Seno. 2006. Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comp. Biol. 2:e170.
    • Trovato, A., F. Chiti, A. Maritan, and F. Seno. 2006. Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comp. Biol. 2:e170.
  • 70
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584-599.
    • (1993) J. Mol. Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.