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Volumn 13, Issue 8, 2004, Pages 2149-2160

Detecting hidden sequence propensity for amyloid fibril formation

Author keywords

Amyloid fibril; H P, SCOP; Hidden strand propensity; Secondary structure; Tertiary contacts

Indexed keywords

ACETYLCHOLINESTERASE; ALPHA SYNUCLEIN; AMYLIN; AMYLOID; AMYLOID BETA PROTEIN; MYOGLOBIN; PEPTIDE FRAGMENT;

EID: 3342963982     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04790604     Document Type: Article
Times cited : (95)

References (41)
  • 1
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid
    • Balbirnie, M., Grothe, R., and Eisenberg, D.S. 2001. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. Proc. Natl. Acad. Sci. 98: 2375-2380.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 2
    • 0038004726 scopus 로고    scopus 로고
    • 2-microglobulin amyloidosis: Insights from conservation analysis and fibril modeling by protein docking techniques
    • 2-Microglobulin amyloidosis: Insights from conservation analysis and fibril modeling by protein docking techniques. J. Mol. Biol. 330: 159-174.
    • (2003) J. Mol. Biol. , vol.330 , pp. 159-174
    • Benyamini, H.1    Gunasekaran, K.2    Wolfson, H.3    Nussinov, R.4
  • 3
    • 0344407050 scopus 로고    scopus 로고
    • Convervation and amyloid formation: A study of the gelsolin-like family
    • -. 2003b. Convervation and amyloid formation: A study of the gelsolin-like family. Proteins 51: 266-282.
    • (2003) Proteins , vol.51 , pp. 266-282
  • 4
    • 0035853276 scopus 로고    scopus 로고
    • Van der Waals locks: Loop-n-lock structure of globular proteins
    • Berezovsky, I.N. and Trifonov, E.N. 2001. Van der Waals locks: Loop-n-lock structure of globular proteins. J. Mol. Biol. 307: 1419-1426.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1419-1426
    • Berezovsky, I.N.1    Trifonov, E.N.2
  • 5
    • 0034922671 scopus 로고    scopus 로고
    • Identification of the region of non-Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity
    • Bodles, A.M., Guthrie, D.J., Greeg, B., and Irvine, G.B. 2001. Identification of the region of non-Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity. J. Neurochem. 78: 334-395.
    • (2001) J. Neurochem. , vol.78 , pp. 334-395
    • Bodles, A.M.1    Guthrie, D.J.2    Greeg, B.3    Irvine, G.B.4
  • 6
    • 0033977581 scopus 로고    scopus 로고
    • The ASTRAL compendium for protein structure and sequence analysis
    • Brenner, S.E., Koehl, P., and Levitt, M. 2000. The ASTRAL compendium for protein structure and sequence analysis. Nucleic Acids Res. 28: 254-256.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 254-256
    • Brenner, S.E.1    Koehl, P.2    Levitt, M.3
  • 9
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti, F., Stefani, M., Taddei, N., Ramponi, G., and Dobson, C.M. 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
  • 10
    • 0036828769 scopus 로고    scopus 로고
    • Alzheimer's disease: Treatments in discovery and development
    • Citron, M. 2002. Alzheimer's disease: Treatments in discovery and development. Nat. Neurosci. 5: 1055-1057.
    • (2002) Nat. Neurosci. , vol.5 , pp. 1055-1057
    • Citron, M.1
  • 12
    • 0037137221 scopus 로고    scopus 로고
    • Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-β peptide
    • Cottingham, M.G., Hollinshead, M.S., and Vaux, D.J. 2002. Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-β peptide. Biochemistry 41: 13539-13547.
    • (2002) Biochemistry , vol.41 , pp. 13539-13547
    • Cottingham, M.G.1    Hollinshead, M.S.2    Vaux, D.J.3
  • 13
    • 0041817863 scopus 로고    scopus 로고
    • The intact human acetylcholinesterase C-terminal oligomerization domain is α-helical in situ and in isolation, but a shorter fragment forms β-sheet-rich amyloid fibrils and protofibrillar oligomers
    • Cottingham, M.G., Voskuil, J.L., and Vaux, D.J. 2003. The intact human acetylcholinesterase C-terminal oligomerization domain is α-helical in situ and in isolation, but a shorter fragment forms β-sheet-rich amyloid fibrils and protofibrillar oligomers. Biochemistry 42: 10863-10873.
    • (2003) Biochemistry , vol.42 , pp. 10863-10873
    • Cottingham, M.G.1    Voskuil, J.L.2    Vaux, D.J.3
  • 14
    • 0037023299 scopus 로고    scopus 로고
    • Harmless proteins twist into troublemakers
    • Couzin, J. 2002. Harmless proteins twist into troublemakers. Science 296: 28-29.
    • (2002) Science , vol.296 , pp. 28-29
    • Couzin, J.1
  • 15
    • 0032573597 scopus 로고    scopus 로고
    • Aggregates from mutant and wild-type a-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments
    • El-Agnaf, O.M., Jakes, R., Currar, M.D., Middleton, D., Ingenito, R., Bianchi, E., Pesse, A., Neill, D., and Wallace, A. 1998. Aggregates from mutant and wild-type a-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments. FEBS Lett. 440: 71-75.
    • (1998) FEBS Lett. , vol.440 , pp. 71-75
    • El-Agnaf, O.M.1    Jakes, R.2    Currar, M.D.3    Middleton, D.4    Ingenito, R.5    Bianchi, E.6    Pesse, A.7    Neill, D.8    Wallace, A.9
  • 16
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich, M., Fletcher, M.A., and Dobson, C.M. 2001. Amyloid fibrils from muscle myoglobin. Nature 410: 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 18
    • 0036547110 scopus 로고    scopus 로고
    • Peptide inhibitors of β-amyloid aggregation
    • Findeis, M.A. 2002. Peptide inhibitors of β-amyloid aggregation. Curr. Top. Med. Chem. 2: 417-423.
    • (2002) Curr. Top. Med. Chem. , vol.2 , pp. 417-423
    • Findeis, M.A.1
  • 19
    • 0034703375 scopus 로고    scopus 로고
    • A rapid test for identification of autonomous folding units in proteins
    • Fischer, K.F. and Marqusee, S. 2000. A rapid test for identification of autonomous folding units in proteins. J. Mol. Biol. 302: 701-712.
    • (2000) J. Mol. Biol. , vol.302 , pp. 701-712
    • Fischer, K.F.1    Marqusee, S.2
  • 20
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of a-synuclein is essential for filament assembly
    • Giasson, B.I., Murray, I.V., Trojanowski, J.Q., and Lee, V.M. 2001. A hydrophobic stretch of 12 amino acid residues in the middle of a-synuclein is essential for filament assembly. J. Biol. Chem. 276: 2380-2386.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray, I.V.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 21
    • 0034632806 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes mellitus
    • Hoppener, J.W., Ahren, B., and Lips, C.J.M. 2000. Islet amyloid and type 2 diabetes mellitus. N. Engl. J. Med. 343: 411-419.
    • (2000) N. Engl. J. Med. , vol.343 , pp. 411-419
    • Hoppener, J.W.1    Ahren, B.2    Lips, C.J.M.3
  • 22
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez, J.L., Guijarro, J.I., Orlova, E., Zurdo, J., Dobson, C.M., Sunde, M., and Saibil, H.R. 1999. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18: 815-821.
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 23
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 26
    • 0036414287 scopus 로고    scopus 로고
    • Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide
    • Mazor, Y., Gilead, S., Benhar, I., and Gazit, E. 2002. Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide. J. Mol. Biol. 322: 1013-1024.
    • (2002) J. Mol. Biol. , vol.322 , pp. 1013-1024
    • Mazor, Y.1    Gilead, S.2    Benhar, I.3    Gazit, E.4
  • 27
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor Jr., D.L. and Kim, P.S. 1996. Context-dependent secondary structure formation of a designed protein sequence. Nature 380: 730-734.
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor Jr., D.L.1    Kim, P.S.2
  • 28
    • 53149142471 scopus 로고    scopus 로고
    • What is the minimum number of residues to determine the secondary structural state?
    • Pan, X.-M., Niu, W.-D., and Wang, Z.-X. 1999. What is the minimum number of residues to determine the secondary structural state? J. Protein Chem. 18: 579-584.
    • (1999) J. Protein Chem. , vol.18 , pp. 579-584
    • Pan, X.-M.1    Niu, W.-D.2    Wang, Z.-X.3
  • 29
    • 0345827608 scopus 로고    scopus 로고
    • Sequence determinants of amyloid fibril formation
    • Paz, M. and Serrano, L. 2004. Sequence determinants of amyloid fibril formation. Proc. Natl. Acad. Sci. 101: 87-92.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 87-92
    • Paz, M.1    Serrano, L.2
  • 30
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a β-sheet breaker peptide
    • Permanne, B., Adessi, C., Saborio, G.P., Fraga, S., Frossard, M.-J., Dorpe, J.V., Dewachter, I., Banks, W.A., Leuven, F.V., and Soto, C. 2002. Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a β-sheet breaker peptide. FASEB J. 8: 860-862.
    • (2002) FASEB J. , vol.8 , pp. 860-862
    • Permanne, B.1    Adessi, C.2    Saborio, G.P.3    Fraga, S.4    Frossard, M.-J.5    Dorpe, J.V.6    Dewachter, I.7    Banks, W.A.8    Leuven, F.V.9    Soto, C.10
  • 31
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K.W., Simons, K.T., and Baker, D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277: 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 32
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B. 1996. PHD: Predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266: 525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 33
    • 0036527699 scopus 로고    scopus 로고
    • Therapeutic strategies for human amyloid diseases
    • Sacchettini, J.C. and Kelly, J.W. 2002. Therapeutic strategies for human amyloid diseases. Nat. Rev. Drug Discovery 1: 267-275.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 267-275
    • Sacchettini, J.C.1    Kelly, J.W.2
  • 34
    • 0000507749 scopus 로고
    • Matrices for detecting distant relationships
    • (ed. M.O. Dayhoff). National Biomedical Research Foundation, Washington, DC
    • Schwartz, R.M. and Dayhoff, M.O. 1978. Matrices for detecting distant relationships. In Atlas of protein sequence and structure (ed. M.O. Dayhoff), pp. 353-358. National Biomedical Research Foundation, Washington, DC.
    • (1978) Atlas of Protein Sequence and Structure , pp. 353-358
    • Schwartz, R.M.1    Dayhoff, M.O.2
  • 35
    • 0031873102 scopus 로고    scopus 로고
    • β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Soto, C., Sigurdsson, E.M., Morelli, L., Kumar, R.A., Castano, E.M., and Frangione, B. 1998. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nat. Med. 4: 822-826.
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 37
    • 0032568534 scopus 로고    scopus 로고
    • α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
    • Spillantini, M.G., Crowther, R.A., Jakes, R., Hasegawa, M., and Goedert, M. 1998. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. 95: 6469-6473.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 40
    • 0036833437 scopus 로고    scopus 로고
    • Therapeutic strategies for Alzheimer's disease
    • Wolfe, M.S. 2002. Therapeutic strategies for Alzheimer's disease. Nat. Rev. Drug Discovery 1: 859-866.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 859-866
    • Wolfe, M.S.1
  • 41
    • 0034333229 scopus 로고    scopus 로고
    • An analysis of the helix-to-strand transition between peptides with identical sequence
    • Zhou, X., Alber, F.A., Folkers, G., Gonnet, G.H., and Chelvanayagam, G. 2000. An analysis of the helix-to-strand transition between peptides with identical sequence. Proteins 41: 248-256.
    • (2000) Proteins , vol.41 , pp. 248-256
    • Zhou, X.1    Alber, F.A.2    Folkers, G.3    Gonnet, G.H.4    Chelvanayagam, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.