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Volumn 396, Issue 1, 2010, Pages 60-74

Lability Landscape and Protease Resistance of Human Insulin Amyloid: A New Insight into Its Molecular Properties

Author keywords

amyloid; atomic force microscopy; insulin; lability; seeding

Indexed keywords

AMYLOID; HUMAN INSULIN; THIOFLAVINE;

EID: 74649083540     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.11.012     Document Type: Article
Times cited : (18)

References (62)
  • 1
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M., and Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81 (2003) 678-699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 2
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • Ferreira S.T., Vieira M.N., and De Felice F.G. Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases. IUBMB Life 59 (2007) 332-345
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 5
    • 28244446220 scopus 로고    scopus 로고
    • Aspects on human amyloid forms and their fibril polypeptides
    • Westermark P. Aspects on human amyloid forms and their fibril polypeptides. FEBS J. 272 (2005) 5942-5949
    • (2005) FEBS J. , vol.272 , pp. 5942-5949
    • Westermark, P.1
  • 8
    • 0033849915 scopus 로고    scopus 로고
    • Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants
    • Morozova-Roche L.A., Zurdo J., Spencer A., Noppe W., Receveur V., Archer D.B., et al. Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J. Struct. Biol. 130 (2000) 339-351
    • (2000) J. Struct. Biol. , vol.130 , pp. 339-351
    • Morozova-Roche, L.A.1    Zurdo, J.2    Spencer, A.3    Noppe, W.4    Receveur, V.5    Archer, D.B.6
  • 9
    • 64649090221 scopus 로고    scopus 로고
    • At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to α-synuclein and prevents its fibrillation
    • Zhou W., Gallagher A., Hong D.P., Long C., Fink A.L., and Uversky V.N. At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to α-synuclein and prevents its fibrillation. J. Mol. Biol. 388 (2009) 597-610
    • (2009) J. Mol. Biol. , vol.388 , pp. 597-610
    • Zhou, W.1    Gallagher, A.2    Hong, D.P.3    Long, C.4    Fink, A.L.5    Uversky, V.N.6
  • 10
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • Arnaudov L.N., and de Vries R. Thermally induced fibrillar aggregation of hen egg white lysozyme. Biophys. J. 88 (2005) 515-526
    • (2005) Biophys. J. , vol.88 , pp. 515-526
    • Arnaudov, L.N.1    de Vries, R.2
  • 11
    • 9444299029 scopus 로고    scopus 로고
    • Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure
    • De Felice F.G., Vieira M.N., Meirelles M.N., Morozova-Roche L.A., Dobson C.M., and Ferreira S.T. Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure. FASEB J. 18 (2004) 1099-1101
    • (2004) FASEB J. , vol.18 , pp. 1099-1101
    • De Felice, F.G.1    Vieira, M.N.2    Meirelles, M.N.3    Morozova-Roche, L.A.4    Dobson, C.M.5    Ferreira, S.T.6
  • 12
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde M., and Blake C.C.F. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50 (1997) 123-159
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.C.F.2
  • 13
    • 22844447714 scopus 로고    scopus 로고
    • X-ray diffraction studies of amyloid structure
    • Makin O.S., and Serpell L.C. X-ray diffraction studies of amyloid structure. Methods Mol. Biol. 299 (2005) 67-80
    • (2005) Methods Mol. Biol. , vol.299 , pp. 67-80
    • Makin, O.S.1    Serpell, L.C.2
  • 14
    • 0035823520 scopus 로고    scopus 로고
    • Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation
    • Azriel R., and Gazit E. Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation. J. Biol. Chem. 276 (2001) 34156-34161
    • (2001) J. Biol. Chem. , vol.276 , pp. 34156-34161
    • Azriel, R.1    Gazit, E.2
  • 16
    • 50349089799 scopus 로고    scopus 로고
    • Temperature-induced dissociation of Aβ monomers from amyloid fibril
    • Takeda T., and Klimov D.K. Temperature-induced dissociation of Aβ monomers from amyloid fibril. Biophys. J. 95 (2008) 1758-1772
    • (2008) Biophys. J. , vol.95 , pp. 1758-1772
    • Takeda, T.1    Klimov, D.K.2
  • 17
    • 33646088595 scopus 로고    scopus 로고
    • Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties
    • Meersman F., and Christopher M.D. Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties. Biochim. Biophys. Acta 1764 (2006) 452-460
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 452-460
    • Meersman, F.1    Christopher, M.D.2
  • 18
    • 27744499932 scopus 로고    scopus 로고
    • Kinetic analysis of the polymerization and depolymerization of β(2)-microglobulin-related amyloid fibrils in vitro
    • Yamamoto S., Hasegawa K., Yamaguchi I., Goto Y., Gejyo F., and Naiki H. Kinetic analysis of the polymerization and depolymerization of β(2)-microglobulin-related amyloid fibrils in vitro. Biochim. Biophys. Acta 1753 (2005) 34-43
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 34-43
    • Yamamoto, S.1    Hasegawa, K.2    Yamaguchi, I.3    Goto, Y.4    Gejyo, F.5    Naiki, H.6
  • 20
    • 0037126833 scopus 로고    scopus 로고
    • The "correctly folded" state of proteins: is it a metastable state?
    • Gazit E. The "correctly folded" state of proteins: is it a metastable state?. Angew. Chem. 41 (2002) 257-259
    • (2002) Angew. Chem. , vol.41 , pp. 257-259
    • Gazit, E.1
  • 22
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • Paravastu A.K., Leapman R.D., Yau W.-M., and Tycko R. Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils. Proc. Natl Acad. Sci. USA 102 (2008) 18349-18354
    • (2008) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.-M.3    Tycko, R.4
  • 23
    • 34249051698 scopus 로고    scopus 로고
    • Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions
    • Olofsson A., Lindhagen-Persson M., Sauer-Eriksson A.E., and Ohman A. Amide solvent protection analysis demonstrates that amyloid-β(1-40) and amyloid-β(1-42) form different fibrillar structures under identical conditions. Biochem. J. 404 (2007) 63-70
    • (2007) Biochem. J. , vol.404 , pp. 63-70
    • Olofsson, A.1    Lindhagen-Persson, M.2    Sauer-Eriksson, A.E.3    Ohman, A.4
  • 24
    • 33644817349 scopus 로고    scopus 로고
    • Scanning cysteine mutagenesis analysis of Aβ-(1-40) amyloid fibrils
    • Shivaprasad S., and Wetzel R. Scanning cysteine mutagenesis analysis of Aβ-(1-40) amyloid fibrils. J. Biol. Chem. 281 (2006) 993-1000
    • (2006) J. Biol. Chem. , vol.281 , pp. 993-1000
    • Shivaprasad, S.1    Wetzel, R.2
  • 25
    • 3342906956 scopus 로고    scopus 로고
    • Fibrillation of carrier protein albebetin and its biologically active constructs. Multiple oligomeric intermediates and pathways
    • Morozova-Roche L.A., Zamotin V., Malisauskas M., Ohman A., Chertkova R., Lavrikova M.A., et al. Fibrillation of carrier protein albebetin and its biologically active constructs. Multiple oligomeric intermediates and pathways. Biochemistry 43 (2004) 9610-9619
    • (2004) Biochemistry , vol.43 , pp. 9610-9619
    • Morozova-Roche, L.A.1    Zamotin, V.2    Malisauskas, M.3    Ohman, A.4    Chertkova, R.5    Lavrikova, M.A.6
  • 26
    • 0042744699 scopus 로고    scopus 로고
    • Amyloid protofilaments from the calcium-binding protein equine lysozyme: formation of ring and linear structures depends on pH and metal ion concentration
    • Malisauskas M., Zamotin V., Jass J., Noppe W., Dobson C.M., and Morozova-Roche L.A. Amyloid protofilaments from the calcium-binding protein equine lysozyme: formation of ring and linear structures depends on pH and metal ion concentration. J. Mol. Biol. 330 (2003) 879-890
    • (2003) J. Mol. Biol. , vol.330 , pp. 879-890
    • Malisauskas, M.1    Zamotin, V.2    Jass, J.3    Noppe, W.4    Dobson, C.M.5    Morozova-Roche, L.A.6
  • 28
    • 39049119728 scopus 로고    scopus 로고
    • Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size
    • Sun Y., Makarava N., Lee C.I., Laksanalamai P., Robb F.T., and Baskakov I.V. Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J. Mol. Biol. 376 (2008) 1155-1167
    • (2008) J. Mol. Biol. , vol.376 , pp. 1155-1167
    • Sun, Y.1    Makarava, N.2    Lee, C.I.3    Laksanalamai, P.4    Robb, F.T.5    Baskakov, I.V.6
  • 29
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., and Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66 (1997) 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 30
    • 17844367336 scopus 로고    scopus 로고
    • Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism
    • Lundmark K., Westermark G.T., Olsen A., and Westermark P. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism. Proc. Natl Acad. Sci. USA 102 (2005) 6098-6102
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6098-6102
    • Lundmark, K.1    Westermark, G.T.2    Olsen, A.3    Westermark, P.4
  • 31
    • 0030959947 scopus 로고    scopus 로고
    • Towards understanding insulin fibrillation
    • Brange J. Towards understanding insulin fibrillation. J. Pharm. Sci. 86 (1997) 517-525
    • (1997) J. Pharm. Sci. , vol.86 , pp. 517-525
    • Brange, J.1
  • 33
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton E.J., Tito P., Sunde M., Bouchard M., Dobson C.M., and Robinson C.V. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 79 (2000) 1053-1065
    • (2000) Biophys. J. , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 34
    • 2442468092 scopus 로고    scopus 로고
    • Stimulation of insulin fibrillation by urea-induced intermediates
    • Ahmad A., Millett I.S., Doniach S., Uversky V., and Fink A.L. Stimulation of insulin fibrillation by urea-induced intermediates. J. Biol. Chem. 279 (2004) 14999-15013
    • (2004) J. Biol. Chem. , vol.279 , pp. 14999-15013
    • Ahmad, A.1    Millett, I.S.2    Doniach, S.3    Uversky, V.4    Fink, A.L.5
  • 35
    • 0030907673 scopus 로고    scopus 로고
    • A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin)
    • Brange J., Dodson G.G., Edwards D.J., Holden P.H., and Whittingham J.L. A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin). Proteins 27 (1997) 507-516
    • (1997) Proteins , vol.27 , pp. 507-516
    • Brange, J.1    Dodson, G.G.2    Edwards, D.J.3    Holden, P.H.4    Whittingham, J.L.5
  • 36
    • 33745610089 scopus 로고    scopus 로고
    • New insights into the self-assembly of insulin amyloid fibrils: an H-D exchange FT-IR study
    • Dzwolak W., Loksztejn A., and Smirnovas V. New insights into the self-assembly of insulin amyloid fibrils: an H-D exchange FT-IR study. Biochemistry 45 (2006) 8143-8151
    • (2006) Biochemistry , vol.45 , pp. 8143-8151
    • Dzwolak, W.1    Loksztejn, A.2    Smirnovas, V.3
  • 37
    • 42749089759 scopus 로고    scopus 로고
    • Chiral bifurcation in aggregating insulin: an induced circular dichroism study
    • Loksztejn A., and Dzwolak W. Chiral bifurcation in aggregating insulin: an induced circular dichroism study. J. Mol. Biol. 379 (2008) 9-16
    • (2008) J. Mol. Biol. , vol.379 , pp. 9-16
    • Loksztejn, A.1    Dzwolak, W.2
  • 38
    • 59849109485 scopus 로고    scopus 로고
    • A universal pathway for amyloid nucleus and precursor formation for insulin
    • Nayak A., Sorci M., Krueger S., and Belfort G. A universal pathway for amyloid nucleus and precursor formation for insulin. Proteins 74 (2009) 556-565
    • (2009) Proteins , vol.74 , pp. 556-565
    • Nayak, A.1    Sorci, M.2    Krueger, S.3    Belfort, G.4
  • 39
    • 34250897912 scopus 로고    scopus 로고
    • Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin
    • Dzwolak W., Loksztejn A., Galinska-Rakoczy A., Adachi R., Goto Y., and Rupnicki L. Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin. J. Am. Chem. Soc. 20 (2007) 7517-7522
    • (2007) J. Am. Chem. Soc. , vol.20 , pp. 7517-7522
    • Dzwolak, W.1    Loksztejn, A.2    Galinska-Rakoczy, A.3    Adachi, R.4    Goto, Y.5    Rupnicki, L.6
  • 40
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: a formulation challenge
    • Frokjaer S., and Otzen D.E. Protein drug stability: a formulation challenge. Nat. Rev., Drug Discov. 4 (2005) 298-306
    • (2005) Nat. Rev., Drug Discov. , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 41
    • 0027048535 scopus 로고
    • Chemical stability of insulin: 5. Isolation, characterization and identification of insulin transformation products
    • Brange J., Hallund O., and Sørensen E. Chemical stability of insulin: 5. Isolation, characterization and identification of insulin transformation products. Acta Pharm. Nord. 4 (1992) 223-232
    • (1992) Acta Pharm. Nord. , vol.4 , pp. 223-232
    • Brange, J.1    Hallund, O.2    Sørensen, E.3
  • 42
    • 0030805003 scopus 로고    scopus 로고
    • The new era of biotech insulin analogues
    • Brange J. The new era of biotech insulin analogues. Diabetalogia 40 (1997) S48-S53
    • (1997) Diabetalogia , vol.40
    • Brange, J.1
  • 43
    • 26944499416 scopus 로고    scopus 로고
    • Biopharmaceuticals: recent approvals and likely directions
    • Welsh G. Biopharmaceuticals: recent approvals and likely directions. Trends Biotechnol. 23 (2005) 553-558
    • (2005) Trends Biotechnol. , vol.23 , pp. 553-558
    • Welsh, G.1
  • 44
    • 34248369818 scopus 로고    scopus 로고
    • False paradise-mixed blessings in the protein universe: the amyloid as a new challenge in drug development
    • Morozova-Roche L.A., and Malisauskas M.A. False paradise-mixed blessings in the protein universe: the amyloid as a new challenge in drug development. Curr. Med. Chem. 14 (2007) 1221-1230
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1221-1230
    • Morozova-Roche, L.A.1    Malisauskas, M.A.2
  • 45
    • 0025286235 scopus 로고
    • Persistent cutaneous insulin allergy resulting from high-molecular-weight insulin aggregates
    • Ratner R.E., Philips T.M., and Steiner M. Persistent cutaneous insulin allergy resulting from high-molecular-weight insulin aggregates. Diabetes 39 (1990) 728-733
    • (1990) Diabetes , vol.39 , pp. 728-733
    • Ratner, R.E.1    Philips, T.M.2    Steiner, M.3
  • 47
    • 0023948509 scopus 로고
    • Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient
    • Dische F.E., Wernstedt C., Westermark G.T., Westermark P., Pepys M.B., Rennie J.A., et al. Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient. Diabetologia 31 (1988) 158-161
    • (1988) Diabetologia , vol.31 , pp. 158-161
    • Dische, F.E.1    Wernstedt, C.2    Westermark, G.T.3    Westermark, P.4    Pepys, M.B.5    Rennie, J.A.6
  • 48
    • 14844323613 scopus 로고    scopus 로고
    • Does the cytotoxic effect of transient amyloid oligomers from common equine lysozyme in vitro imply innate amyloid toxicity?
    • Malisauskas M., Ostman J., Darinskas A., Zamotin V., Liutkevicius E., Lundgren E., and Morozova-Roche L.A. Does the cytotoxic effect of transient amyloid oligomers from common equine lysozyme in vitro imply innate amyloid toxicity?. J. Biol. Chem. 280 (2005) 6269-6275
    • (2005) J. Biol. Chem. , vol.280 , pp. 6269-6275
    • Malisauskas, M.1    Ostman, J.2    Darinskas, A.3    Zamotin, V.4    Liutkevicius, E.5    Lundgren, E.6    Morozova-Roche, L.A.7
  • 49
    • 56249090429 scopus 로고    scopus 로고
    • Ultrathin silver nanowires produced by amyloid biotemplating
    • Malisauskas M., Meskys R., and Morozova-Roche L.A. Ultrathin silver nanowires produced by amyloid biotemplating. Biotechnol. Prog. 24 (2008) 1166-1170
    • (2008) Biotechnol. Prog. , vol.24 , pp. 1166-1170
    • Malisauskas, M.1    Meskys, R.2    Morozova-Roche, L.A.3
  • 50
    • 8344266799 scopus 로고    scopus 로고
    • Age- and sex-related reference values for serum insulin concentration and its biological determinants in a French healthy population. The STANISLAS cohort
    • Francois A., Maumus S., Vincent-Viry M., Gueguen R., Siest G., and Visvikis S. Age- and sex-related reference values for serum insulin concentration and its biological determinants in a French healthy population. The STANISLAS cohort. Clin. Chem. Lab. Med. 42 (2004) 1140-1149
    • (2004) Clin. Chem. Lab. Med. , vol.42 , pp. 1140-1149
    • Francois, A.1    Maumus, S.2    Vincent-Viry, M.3    Gueguen, R.4    Siest, G.5    Visvikis, S.6
  • 53
    • 43049164334 scopus 로고    scopus 로고
    • Secondary nucleation and accessible surface in insulin amyloid fibril formation
    • Foderà V., Librizzi F., Groenning M., van de Weert M., and Leone M. Secondary nucleation and accessible surface in insulin amyloid fibril formation. J. Phys. Chem. B. 112 (2008) 3853-3858
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 3853-3858
    • Foderà, V.1    Librizzi, F.2    Groenning, M.3    van de Weert, M.4    Leone, M.5
  • 55
    • 68149099439 scopus 로고    scopus 로고
    • Self-organization pathways and spatial heterogeneity in insulin amyloid fibril formation
    • Foderà V., Cataldo S., Librizzi F., Pignataro B., Spiccia P., and Leone M. Self-organization pathways and spatial heterogeneity in insulin amyloid fibril formation. J. Phys. Chem. B. 113 (2009) 10830-10837
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 10830-10837
    • Foderà, V.1    Cataldo, S.2    Librizzi, F.3    Pignataro, B.4    Spiccia, P.5    Leone, M.6
  • 56
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • Jansen R., Dzwolak W., and Winter R. Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. Biophys. J. 88 (2005) 1344-1353
    • (2005) Biophys. J. , vol.88 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 57
    • 28844482969 scopus 로고    scopus 로고
    • The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways
    • Librizzi F., and Rischel C. The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways. Protein Sci. 14 (2005) 3129-3134
    • (2005) Protein Sci. , vol.14 , pp. 3129-3134
    • Librizzi, F.1    Rischel, C.2
  • 58
    • 12544259221 scopus 로고    scopus 로고
    • Reversal of protein aggregation provides evidence for multiple aggregated states
    • Calamai M., Canale C., Telini A., Stefani M., Chiti F., and Dobson C.M. Reversal of protein aggregation provides evidence for multiple aggregated states. J. Mol. Biol. 346 (2005) 603-616
    • (2005) J. Mol. Biol. , vol.346 , pp. 603-616
    • Calamai, M.1    Canale, C.2    Telini, A.3    Stefani, M.4    Chiti, F.5    Dobson, C.M.6
  • 59
    • 0142164890 scopus 로고    scopus 로고
    • Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis
    • Polverino de Laureto P., Taddei N., Frare E., Capanni C., Costantini S., Zurdo J., et al. Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. J. Mol. Biol. 334 (2003) 129-141
    • (2003) J. Mol. Biol. , vol.334 , pp. 129-141
    • Polverino de Laureto, P.1    Taddei, N.2    Frare, E.3    Capanni, C.4    Costantini, S.5    Zurdo, J.6
  • 61
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine III H. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 62


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