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Volumn 64, Issue 1, 2012, Pages 29-44

Amyloid-Like Fibril Formation by Tachykinin Neuropeptides and Its Relevance to Amyloid β-Protein Aggregation and Toxicity

Author keywords

Amyloids; Fibrils; Functions; Neuropeptides; Peptide

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (25 35); AMYLOID BETA-PROTEIN (25-35); CONGO RED; HEPARIN; KASSININ; PEPTIDE FRAGMENT; PHYSALAEMIN; SUBSTANCE P; THIAZOLE DERIVATIVE; THIOFLAVINE;

EID: 84865560144     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-012-9364-z     Document Type: Article
Times cited : (22)

References (65)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., & Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75, 333-366.
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 68649086842 scopus 로고    scopus 로고
    • Structure-activity relationship of amyloid fibrils
    • Maji, S. K., Wang, L., Greenwald, J., & Riek, R. (2009). Structure-activity relationship of amyloid fibrils. FEBS Letters, 583, 2610-2617.
    • (2009) FEBS Letters , vol.583 , pp. 2610-2617
    • Maji, S.K.1    Wang, L.2    Greenwald, J.3    Riek, R.4
  • 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. Quarterly Reviews of Biophysics, 39, 1-55.
    • (2006) Quarterly Reviews of Biophysics , vol.39 , pp. 1-55
    • Tycko, R.1
  • 4
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk, W. E., Jacob, R. F., & Mason, R. P. (1999). Quantifying amyloid by Congo red spectral shift assay. Methods in Enzymology, 309, 285-305.
    • (1999) Methods in Enzymology , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 5
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine, H. (1999). Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods in Enzymology, 309, 274-284.
    • (1999) Methods in Enzymology , vol.309 , pp. 274-284
    • Levine, H.1
  • 6
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M., & Blake, C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advances in Protein Chemistry, 50, 123-159.
    • (1997) Advances in Protein Chemistry , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 8
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. (1999). Protein misfolding, evolution and disease. Trends in Biochemical Sciences, 24, 329-332.
    • (1999) Trends in Biochemical Sciences , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 9
    • 0347481472 scopus 로고    scopus 로고
    • Pathological and functional amyloid formation orchestrated by the secretory pathway
    • Huff, M. E., Balch, W. E., & Kelly, J. W. (2003). Pathological and functional amyloid formation orchestrated by the secretory pathway. Current Opinion in Structural Biology, 13, 674-682.
    • (2003) Current Opinion in Structural Biology , vol.13 , pp. 674-682
    • Huff, M.E.1    Balch, W.E.2    Kelly, J.W.3
  • 12
    • 84857771844 scopus 로고    scopus 로고
    • Native Functions of Amyloid
    • D. A. Stein (Ed.), New York: Nova Science Publishers, Inc
    • Jacob, R., Anoop, A., Singh, P., & Maji, S. (2010). Native Functions of Amyloid. In D. A. Stein (Ed.), Protein aggregation (pp. 79-109). New York: Nova Science Publishers, Inc.
    • (2010) Protein Aggregation , pp. 79-109
    • Jacob, R.1    Anoop, A.2    Singh, P.3    Maji, S.4
  • 14
    • 84860315046 scopus 로고    scopus 로고
    • Nanomaterials: Amyloids reflect their brighter side
    • doi:10.3402/nano.v2i0.6032
    • Mankar, S., Anoop, A., Sen, S., & Maji, S. K. (2011). Nanomaterials: Amyloids reflect their brighter side. Nano Reviews, 2, 6032. doi: 10. 3402/nano. v2i0. 6032.
    • (2011) Nano Reviews , vol.2 , pp. 6032
    • Mankar, S.1    Anoop, A.2    Sen, S.3    Maji, S.K.4
  • 15
    • 62549087388 scopus 로고    scopus 로고
    • Surface- and solution-based assembly of amyloid fibrils for biomedical and nanotechnology applications
    • Gras, S. L. (2009). Surface- and solution-based assembly of amyloid fibrils for biomedical and nanotechnology applications. Advances in Chemical Engineering, 35, 161-209.
    • (2009) Advances in Chemical Engineering , vol.35 , pp. 161-209
    • Gras, S.L.1
  • 17
    • 34547316314 scopus 로고    scopus 로고
    • Self-assembled peptide nanostructures: The design of molecular building blocks and their technological utilization
    • Gazit, E. (2007). Self-assembled peptide nanostructures: The design of molecular building blocks and their technological utilization. Chemical Society Reviews, 36, 1263-1269.
    • (2007) Chemical Society Reviews , vol.36 , pp. 1263-1269
    • Gazit, E.1
  • 18
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • Zhang, S., Marini, D. M., Hwang, W., & Santoso, S. (2002). Design of nanostructured biological materials through self-assembly of peptides and proteins. Current Opinion in Chemical Biology, 6, 865-871.
    • (2002) Current Opinion in Chemical Biology , vol.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Hwang, W.3    Santoso, S.4
  • 21
    • 0023394274 scopus 로고
    • Membrane-assisted molecular mechanism of neurokinin receptor subtype selection
    • Schwyzer, R. (1987). Membrane-assisted molecular mechanism of neurokinin receptor subtype selection. EMBO Journal, 6, 2255-2259.
    • (1987) EMBO Journal , vol.6 , pp. 2255-2259
    • Schwyzer, R.1
  • 22
    • 80052908978 scopus 로고    scopus 로고
    • Solution conformation of non-mammalian tachykinin physalaemin in lipid micelles by NMR
    • Grace, C. R., & Cowsik, S. M. (2011). Solution conformation of non-mammalian tachykinin physalaemin in lipid micelles by NMR. Biopolymers, 96, 252-259.
    • (2011) Biopolymers , vol.96 , pp. 252-259
    • Grace, C.R.1    Cowsik, S.M.2
  • 24
    • 0025305263 scopus 로고
    • Diversity in mammalian tachykinin peptidergic neurons: Multiple peptides, receptors, and regulatory mechanisms
    • Helke, C. J., Krause, J. E., Mantyh, P. W., Couture, R., & Bannon, M. J. (1990). Diversity in mammalian tachykinin peptidergic neurons: Multiple peptides, receptors, and regulatory mechanisms. FASEB Journal, 4, 1606-1615.
    • (1990) FASEB Journal , vol.4 , pp. 1606-1615
    • Helke, C.J.1    Krause, J.E.2    Mantyh, P.W.3    Couture, R.4    Bannon, M.J.5
  • 25
    • 0023713984 scopus 로고
    • Ultrastructural studies on calcitonin gene-related peptide-, tachykinins- and somatostatin-immunoreactive neurones in rat dorsal root ganglia: Evidence for the colocalization of different peptides in single secretory granules
    • Merighi, A., Polak, J. M., Gibson, S. J., Gulbenkian, S., Valentino, K. L., & Peirone, S. M. (1988). Ultrastructural studies on calcitonin gene-related peptide-, tachykinins- and somatostatin-immunoreactive neurones in rat dorsal root ganglia: Evidence for the colocalization of different peptides in single secretory granules. Cell and Tissue Research, 254, 101-109.
    • (1988) Cell and Tissue Research , vol.254 , pp. 101-109
    • Merighi, A.1    Polak, J.M.2    Gibson, S.J.3    Gulbenkian, S.4    Valentino, K.L.5    Peirone, S.M.6
  • 26
    • 56149106018 scopus 로고    scopus 로고
    • Short elements with charged amino acids form clusters to sort protachykinin into large dense-core vesicles
    • Ma, G. Q., Wang, B., Wang, H. B., Wang, Q., & Bao, L. (2008). Short elements with charged amino acids form clusters to sort protachykinin into large dense-core vesicles. Traffic, 9, 2165-2179.
    • (2008) Traffic , vol.9 , pp. 2165-2179
    • Ma, G.Q.1    Wang, B.2    Wang, H.B.3    Wang, Q.4    Bao, L.5
  • 27
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990). Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides. Science, 250, 279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 28
    • 0032374061 scopus 로고    scopus 로고
    • Comparative studies on peptides representing the so-called tachykinin-like region of the Alzheimer Aβ peptide [Aβ(25-35)]
    • El-Agnaf, O. M., Irvine, G. B., Fitzpatrick, G., Glass, W. K., & Guthrie, D. J. (1998). Comparative studies on peptides representing the so-called tachykinin-like region of the Alzheimer Aβ peptide [Aβ(25-35)]. Biochemical Journal, 336(Pt 2), 419-427.
    • (1998) Biochemical Journal , vol.336 , Issue.Pt 2 , pp. 419-427
    • El-Agnaf, O.M.1    Irvine, G.B.2    Fitzpatrick, G.3    Glass, W.K.4    Guthrie, D.J.5
  • 30
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla, A. M., Rousseau, F., Schymkowitz, J., & Serrano, L. (2004). Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nature Biotechnology, 22, 1302-1306.
    • (2004) Nature Biotechnology , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 33
    • 0033865052 scopus 로고    scopus 로고
    • Review: Amyloidogenesis-Unquestioned answers and unanswered questions
    • Kisilevsky, R. (2000). Review: Amyloidogenesis-Unquestioned answers and unanswered questions. Journal of Structural Biology, 130, 99-108.
    • (2000) Journal of Structural Biology , vol.130 , pp. 99-108
    • Kisilevsky, R.1
  • 34
    • 0346103697 scopus 로고    scopus 로고
    • Glycosaminoglycans enhance the trifluoroethanol-induced extension of β2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamamoto, S., Yamaguchi, I., Hasegawa, K., Tsutsumi, S., Goto, Y., Gejyo, F., et al. (2004). Glycosaminoglycans enhance the trifluoroethanol-induced extension of β2-microglobulin-related amyloid fibrils at a neutral pH. Journal of the American Society of Nephrology, 15, 126-133.
    • (2004) Journal of the American Society of Nephrology , vol.15 , pp. 126-133
    • Yamamoto, S.1    Yamaguchi, I.2    Hasegawa, K.3    Tsutsumi, S.4    Goto, Y.5    Gejyo, F.6
  • 35
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro
    • Cohlberg, J. A., Li, J., Uversky, V. N., & Fink, A. L. (2002). Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro. Biochemistry, 41, 1502-1511.
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 36
  • 37
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996). Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature, 383, 550-553.
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 40
    • 0018973612 scopus 로고
    • Molecular organization of prolactin granules. II. Characterization of glycosaminoglycans and glycoproteins of the bovine prolactin matrix
    • Zanini, A., Giannattasio, G., Nussdorfer, G., Margolis, R. K., Margolis, R. U., & Meldolesi, J. (1980). Molecular organization of prolactin granules. II. Characterization of glycosaminoglycans and glycoproteins of the bovine prolactin matrix. Journal of Cell Biology, 86, 260-272.
    • (1980) Journal of Cell Biology , vol.86 , pp. 260-272
    • Zanini, A.1    Giannattasio, G.2    Nussdorfer, G.3    Margolis, R.K.4    Margolis, R.U.5    Meldolesi, J.6
  • 41
    • 26444556824 scopus 로고    scopus 로고
    • Conformational dynamics of amyloid β-protein assembly probed using intrinsic fluorescence
    • Maji, S. K., Amsden, J. J., Rothschild, K. J., Condron, M. M., & Teplow, D. B. (2005). Conformational dynamics of amyloid β-protein assembly probed using intrinsic fluorescence. Biochemistry, 44, 13365-13376.
    • (2005) Biochemistry , vol.44 , pp. 13365-13376
    • Maji, S.K.1    Amsden, J.J.2    Rothschild, K.J.3    Condron, M.M.4    Teplow, D.B.5
  • 43
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
    • Buck, M. (1998). Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins. Quarterly Reviews of Biophysics, 31, 297-355.
    • (1998) Quarterly Reviews of Biophysics , vol.31 , pp. 297-355
    • Buck, M.1
  • 44
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid β-protein fibril assembly-Differential effects of α-helix stabilization
    • Fezoui, Y., & Teplow, D. B. (2002). Kinetic studies of amyloid β-protein fibril assembly-Differential effects of α-helix stabilization. Journal of Biological Chemistry, 277, 36948-36954.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 46
    • 0037432332 scopus 로고    scopus 로고
    • Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes
    • Munishkina, L. A., Phelan, C., Uversky, V. N., & Fink, A. L. (2003). Conformational behavior and aggregation of α-synuclein in organic solvents: Modeling the effects of membranes. Biochemistry, 42, 2720-2730.
    • (2003) Biochemistry , vol.42 , pp. 2720-2730
    • Munishkina, L.A.1    Phelan, C.2    Uversky, V.N.3    Fink, A.L.4
  • 47
    • 0037135111 scopus 로고    scopus 로고
    • Medicine-The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., & Selkoe, D. J. (2002). Medicine-The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 48
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein, W. L., Stine, W. B., Jr, & Teplow, D. B. (2004). Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiology of Aging, 25, 569-580.
    • (2004) Neurobiology of Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr., W.B.2    Teplow, D.B.3
  • 50
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., et al. (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
  • 51
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann, T. (1983). Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. Journal of Immunological Methods, 65, 55-63.
    • (1983) Journal of Immunological Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 52
    • 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., & Lansbury, P. T., Jr. (1997). Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annual Review of Biochemistry, 66, 385-407.
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 53
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • Wright, C. F., Teichmann, S. A., Clarke, J., & Dobson, C. M. (2005). The importance of sequence diversity in the aggregation and evolution of proteins. Nature, 438, 878-881.
    • (2005) Nature , vol.438 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 54
    • 0029257497 scopus 로고
    • The core Alzheimer's peptide Nac forms amyloid fibrils which seed and are seeded by β-Amyloid-Is NAC a common trigger or target in neurodegenerative disease?
    • Han, H. Y., Weinreb, P. H., & Lansbury, P. T. (1995). The core Alzheimer's peptide Nac forms amyloid fibrils which seed and are seeded by β-Amyloid-Is NAC a common trigger or target in neurodegenerative disease? Chemistry & Biology, 2, 163-169.
    • (1995) Chemistry & Biology , vol.2 , pp. 163-169
    • Han, H.Y.1    Weinreb, P.H.2    Lansbury, P.T.3
  • 55
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: Not only pathological agents but also ordered nanomaterials
    • (International Ed. In English)
    • Cherny, I., & Gazit, E. (2008). Amyloids: Not only pathological agents but also ordered nanomaterials. Angewandte Chemie (International ed. in English), 47, 4062-4069.
    • (2008) Angewandte Chemie , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 56
    • 79960023029 scopus 로고    scopus 로고
    • Protein aggregation and amyloid fibril formation prediction software from primary sequence: Towards controlling the formation of bacterial inclusion bodies
    • Hamodrakas, S. J. (2011). Protein aggregation and amyloid fibril formation prediction software from primary sequence: Towards controlling the formation of bacterial inclusion bodies. FEBS Journal, 278, 2428-2435.
    • (2011) FEBS Journal , vol.278 , pp. 2428-2435
    • Hamodrakas, S.J.1
  • 57
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157, 105-132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 59
    • 77956203411 scopus 로고    scopus 로고
    • A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation
    • Monsellier, E., Ramazzotti, M., Taddei, N., & Chiti, F. (2010). A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation. PLoS One, 5, e11363.
    • (2010) PLoS One , vol.5
    • Monsellier, E.1    Ramazzotti, M.2    Taddei, N.3    Chiti, F.4
  • 61
    • 79851492876 scopus 로고    scopus 로고
    • Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion
    • Bourgault, S., Solomon, J. P., Reixach, N., & Kelly, J. W. (2011). Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion. Biochemistry, 50, 1001-1015.
    • (2011) Biochemistry , vol.50 , pp. 1001-1015
    • Bourgault, S.1    Solomon, J.P.2    Reixach, N.3    Kelly, J.W.4
  • 62
    • 35648975218 scopus 로고    scopus 로고
    • Amyloid formation by pro-islet amyloid polypeptide processing intermediates: Examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes
    • Meng, F., Abedini, A., Song, B., & Raleigh, D. P. (2007). Amyloid formation by pro-islet amyloid polypeptide processing intermediates: Examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. Biochemistry, 46, 12091-12099.
    • (2007) Biochemistry , vol.46 , pp. 12091-12099
    • Meng, F.1    Abedini, A.2    Song, B.3    Raleigh, D.P.4
  • 63
    • 0037018932 scopus 로고    scopus 로고
    • α-helix structure in Alzheimer's disease aggregates of tau-protein
    • Sadqi, M., Hernandez, F., Pan, U. M., Perez, M., Schaeberle, M. D., Avila, J., et al. (2002). α-helix structure in Alzheimer's disease aggregates of tau-protein. Biochemistry, 41, 7150-7155.
    • (2002) Biochemistry , vol.41 , pp. 7150-7155
    • Sadqi, M.1    Hernandez, F.2    Pan, U.M.3    Perez, M.4    Schaeberle, M.D.5    Avila, J.6
  • 64
    • 2942707921 scopus 로고    scopus 로고
    • Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin
    • Paci, E., Gsponer, J., Salvatella, X., & Vendruscolo, M. (2004). Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin. Journal of Molecular Biology, 340, 555-569.
    • (2004) Journal of Molecular Biology , vol.340 , pp. 555-569
    • Paci, E.1    Gsponer, J.2    Salvatella, X.3    Vendruscolo, M.4
  • 65
    • 70349218070 scopus 로고    scopus 로고
    • A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides
    • Abedini, A., & Raleigh, D. P. (2009). A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides. Protein Engineering, Design and Selection, 22, 453-459.
    • (2009) Protein Engineering, Design and Selection , vol.22 , pp. 453-459
    • Abedini, A.1    Raleigh, D.P.2


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