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Volumn 5, Issue , 2005, Pages

Prediction of "hot spots" of aggregation in disease-linked polypeptides

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42];

EID: 26844546357     PISSN: 14726807     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-5-18     Document Type: Article
Times cited : (181)

References (77)
  • 1
    • 0347987854 scopus 로고    scopus 로고
    • Protein misfolding
    • Smith A: protein misfolding. Nature 2003, 426:883-883.
    • (2003) Nature , vol.426 , pp. 883-883
    • Smith, A.1
  • 3
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky VN, Fink AL: Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 2004, 1698:131-153.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 4
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly JW: The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 1998, 8:101-106.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 6
    • 3242735504 scopus 로고    scopus 로고
    • An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril
    • Ivanova MI, Sawaya MR, Gingery M, Attinger A, Eisenberg D: An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci U S A 2004, 101:10584-10589.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10584-10589
    • Ivanova, M.I.1    Sawaya, M.R.2    Gingery, M.3    Attinger, A.4    Eisenberg, D.5
  • 7
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM: Protein misfolding, evolution and disease. Trends Biochem Sci 1999, 24:329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 8
    • 4143133235 scopus 로고    scopus 로고
    • A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins
    • Linding R, Schymkowitz J, Rousseau F, Diella F, Serrano L: A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. J Mol Biol 2004, 342:345-353.
    • (2004) J Mol Biol , vol.342 , pp. 345-353
    • Linding, R.1    Schymkowitz, J.2    Rousseau, F.3    Diella, F.4    Serrano, L.5
  • 9
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L: Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 2004, 22:1302-1306.
    • (2004) Nat Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 11
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization
    • Bitan G, Vollers SS, Teplow DB: Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization. J Biol Chem 2003, 278:34882-34889.
    • (2003) J Biol Chem , vol.278 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 12
    • 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, Dobson CM: Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003, 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
  • 13
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL: Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des 1998, 3:R9-23.
    • (1998) Fold Des , vol.3
    • Fink, A.L.1
  • 14
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "Aggregation-prone" and "Aggregation- susceptible" Regions in Proteins Associated with Neurodegenerative Diseases
    • Pawar AP, Dubay KF, Zurdo J, Chiti F, Vendruscolo M, Dobson CM: Prediction of "Aggregation-prone" and "Aggregation- susceptible" Regions in Proteins Associated with Neurodegenerative Diseases. J Mol Biol 2005, 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
  • 15
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ: Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 20
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling
    • Torok M, Milton S, Kayed R, Wu P, McIntire T, Glabe CG, Langen R: Structural and dynamic features of Alzheimer's Abeta peptide in amyloid fibrils studied by site-directed spin labeling. J Biol Chem 2002, 277:40810-40815.
    • (2002) J Biol Chem , vol.277 , pp. 40810-40815
    • Torok, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5    Glabe, C.G.6    Langen, R.7
  • 21
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by a beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR
    • Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R: Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR. Biochemistry 2000, 39:13748-13759.
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5    Dyda, F.6    Reed, J.7    Tycko, R.8
  • 23
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, Lansbury PT Jr: The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 24
    • 3042770433 scopus 로고    scopus 로고
    • Environment- and mutation-dependent aggregation behavior of Alzheimer amyloid beta-protein
    • Yamamoto N, Hasegawa K, Matsuzaki K, Naiki H, Yanagisawa K: Environment- and mutation-dependent aggregation behavior of Alzheimer amyloid beta-protein. J Neurochem 2004, 90:62-9.
    • (2004) J Neurochem , vol.90 , pp. 62-69
    • Yamamoto, N.1    Hasegawa, K.2    Matsuzaki, K.3    Naiki, H.4    Yanagisawa, K.5
  • 25
    • 0036308719 scopus 로고    scopus 로고
    • Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: An unbiased search for the sequence determinants of Abeta amyloidogenesis
    • Wurth C, Guimard NK, Hecht MH: Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. J Mol Biol 2002, 319:1279-1290.
    • (2002) J Mol Biol , vol.319 , pp. 1279-1290
    • Wurth, C.1    Guimard, N.K.2    Hecht, M.H.3
  • 28
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin
    • Kajava AV, Aebi U, Steven AC: The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. J Mol Biol 2005, 348:247-252.
    • (2005) J Mol Biol , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 29
    • 0037341842 scopus 로고    scopus 로고
    • Identification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis
    • Scrocchi LA, Ha K, Chen Y, Wu L, Wang F, Fraser PE: Identification of minimal peptide sequences in the (8-20) domain of human islet amyloid polypeptide involved in fibrillogenesis. J Struct Biol 2003, 141:218-27.
    • (2003) J Struct Biol , vol.141 , pp. 218-227
    • Scrocchi, L.A.1    Ha, K.2    Chen, Y.3    Wu, L.4    Wang, F.5    Fraser, P.E.6
  • 30
    • 10844254749 scopus 로고    scopus 로고
    • Role of aromatic interactions in amyloid formation by peptides derived from human Amylin
    • Tracz SM, Abedini A, Driscoll M, Raleigh DP: Role of aromatic interactions in amyloid formation by peptides derived from human Amylin. Biochemistry 2004, 43:15901-15908.
    • (2004) Biochemistry , vol.43 , pp. 15901-15908
    • Tracz, S.M.1    Abedini, A.2    Driscoll, M.3    Raleigh, D.P.4
  • 31
    • 0032972592 scopus 로고    scopus 로고
    • Effects of sequential proline substitutions on amyloid formation by human amylin 20-29
    • Moriarty DF, Raleigh DP: Effects of sequential proline substitutions on amyloid formation by human amylin 20-29. Biochemistry 1999, 38:1811-1818.
    • (1999) Biochemistry , vol.38 , pp. 1811-1818
    • Moriarty, D.F.1    Raleigh, D.P.2
  • 32
    • 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, 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 2001, 276:34156-34161.
    • (2001) J Biol Chem , vol.276 , pp. 34156-34161
    • Azriel, R.1    Gazit, E.2
  • 33
    • 0037470589 scopus 로고    scopus 로고
    • Full-length rat amylin forms fibrils following substitution of single residues from human amylin
    • Green J, Goldsbury C, Mini T, Sunderji S, Frey P, Kistler J, Cooper G, Aebi U: Full-length rat amylin forms fibrils following substitution of single residues from human amylin. J Mol Biol 2003, 326:1147-1156.
    • (2003) J Mol Biol , vol.326 , pp. 1147-1156
    • Green, J.1    Goldsbury, C.2    Mini, T.3    Sunderji, S.4    Frey, P.5    Kistler, J.6    Cooper, G.7    Aebi, U.8
  • 35
    • 0024463227 scopus 로고
    • Hyperproinsulinemia and amyloid in NIDDM. Clues to etiology of islet beta-cell dysfunction?
    • Porte D Jr, Kahn SE: Hyperproinsulinemia and amyloid in NIDDM. Clues to etiology of islet beta-cell dysfunction? Diabetes 1989, 38:1333-1336.
    • (1989) Diabetes , vol.38 , pp. 1333-1336
    • Porte Jr., D.1    Kahn, S.E.2
  • 37
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert M: Alpha-synuclein and neurodegenerative diseases. Nat Rev Neurosci 2001, 2:492-501.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 38
    • 0034922671 scopus 로고    scopus 로고
    • Identification of the region of non-Abeta component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity
    • Bodles AM, Guthrie DJ, Greer B, Irvine GB: Identification of the region of non-Abeta component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity. J Neurochem 2001, 78:384-395.
    • (2001) J Neurochem , vol.78 , pp. 384-395
    • Bodles, A.M.1    Guthrie, D.J.2    Greer, B.3    Irvine, G.B.4
  • 39
    • 0035951869 scopus 로고    scopus 로고
    • A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly
    • Giasson BI, Murray IV, Trojanowski JQ, Lee VM: A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J Biol Chem 2001, 276:2380-2386.
    • (2001) J Biol Chem , vol.276 , pp. 2380-2386
    • Giasson, B.I.1    Murray IV2    Trojanowski, J.Q.3    Lee, V.M.4
  • 40
    • 0037166267 scopus 로고    scopus 로고
    • Biochemical characterization of the core structure of alpha-synuclein filaments
    • Miake H, Mizusawa H, Iwatsubo T, Hasegawa M: Biochemical characterization of the core structure of alpha-synuclein filaments. J Biol Chem 2002, 277:19213-10219.
    • (2002) J Biol Chem , vol.277 , pp. 19213-110219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 41
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling
    • Der-Sarkissian A, Jao CC, Chen J, Langen R: Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. J Biol Chem 2003, 278:37530-37535.
    • (2003) J Biol Chem , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 42
    • 6344228684 scopus 로고    scopus 로고
    • Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein
    • Choi W, Zibaee S, Jakes R, Serpell LC, Davletov B, Crowther RA, Goedert M: Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein. FEBS Lett 2004, 576:363-8.
    • (2004) FEBS Lett , vol.576 , pp. 363-368
    • Choi, W.1    Zibaee, S.2    Jakes, R.3    Serpell, L.C.4    Davletov, B.5    Crowther, R.A.6    Goedert, M.7
  • 43
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D: Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305:1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 46
    • 0026561487 scopus 로고
    • Dialysis-related amyloidosis
    • Koch KM: Dialysis-related amyloidosis. Kidney Int 1992, 41:1416-1429.
    • (1992) Kidney Int , vol.41 , pp. 1416-1429
    • Koch, K.M.1
  • 48
    • 0037059764 scopus 로고    scopus 로고
    • Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I
    • Kozhukh GV, Hagihara Y, Kawakami T, Hasegawa K, Naiki H, Goto Y: Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I. J Biol Chem 2002, 277:1310-1315.
    • (2002) J Biol Chem , vol.277 , pp. 1310-1315
    • Kozhukh, G.V.1    Hagihara, Y.2    Kawakami, T.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 50
    • 0037227173 scopus 로고    scopus 로고
    • Amyloid-forming peptides from beta2-microglobulin - Insights into the mechanism of fibril formation in vitro
    • Jones S, Manning J, Kad NM, Radford SE: Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro. J Mol Biol 2003, 325:249-57.
    • (2003) J Mol Biol , vol.325 , pp. 249-257
    • Jones, S.1    Manning, J.2    Kad, N.M.3    Radford, S.E.4
  • 51
    • 0345686434 scopus 로고    scopus 로고
    • Role of the C-terminal 28 residues of beta2-microglobulin in amyloid fibril formation
    • Ivanova MI, Gingery M, Whitson LJ, Eisenberg D: Role of the C-terminal 28 residues of beta2-microglobulin in amyloid fibril formation. Biochemistry 2003, 42:13536-13540.
    • (2003) Biochemistry , vol.42 , pp. 13536-13540
    • Ivanova, M.I.1    Gingery, M.2    Whitson, L.J.3    Eisenberg, D.4
  • 53
    • 3242735504 scopus 로고    scopus 로고
    • An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril
    • Ivanova MI, Sawaya MR, Gingery M, Attinger A, Eisenberg D: An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc Natl Acad Sci U S A 2004, 101:10584-10589.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10584-10589
    • Ivanova, M.I.1    Sawaya, M.R.2    Gingery, M.3    Attinger, A.4    Eisenberg, D.5
  • 54
    • 4644335370 scopus 로고    scopus 로고
    • Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH
    • Yamamoto S, Hasegawa K, Yamaguchi I, Tsutsumi S, Kardos J, Goto Y, Gejyo F, Naiki H: Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry 2004, 43:11075-11082.
    • (2004) Biochemistry , vol.43 , pp. 11075-11082
    • Yamamoto, S.1    Hasegawa, K.2    Yamaguchi, I.3    Tsutsumi, S.4    Kardos, J.5    Goto, Y.6    Gejyo, F.7    Naiki, H.8
  • 55
    • 15744386870 scopus 로고    scopus 로고
    • Seeding-dependent maturation of beta2-microglobulin amyloid fibrils at neutral pH
    • Kihara M, Chatani E, Sakai M, Hasegawa K, Naiki H, Goto Y: Seeding-dependent maturation of beta2-microglobulin amyloid fibrils at neutral pH. J Biol Chem 2005, 280:12012-12018.
    • (2005) J Biol Chem , vol.280 , pp. 12012-12018
    • Kihara, M.1    Chatani, E.2    Sakai, M.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 63
    • 0021266985 scopus 로고
    • Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin)
    • Saraiva MJ, Birken S, Costa PP, Goodman DS: Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest 1984, 74:104-119.
    • (1984) J Clin Invest , vol.74 , pp. 104-119
    • Saraiva, M.J.1    Birken, S.2    Costa, P.P.3    Goodman, D.S.4
  • 64
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • McCutchen SL, Lai Z, Miroy GJ, Kelly JW, Colon W: Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 1995, 34:13527-13536.
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.J.3    Kelly, J.W.4    Colon, W.5
  • 66
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson JS, Richardson DC: Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A 2002, 99:2754-2759.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 68
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec CP, MacPhee CE, Bajaj VS, McMahon MT, Dobson CM, Griffin RG: High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc Natl Acad Sci U S A 2004, 101:711-716.
    • (2004) Proc Natl Acad Sci U S A , 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
  • 69
    • 0028172158 scopus 로고
    • 1H NMR analysis of fibril-forming peptide fragments of transthyretin
    • Jarvis JA, Kirkpatrick A, Craik DJ: 1H NMR analysis of fibril-forming peptide fragments of transthyretin. Int J Pept Protein Res 1994, 44:388-39.
    • (1994) Int J Pept Protein Res , vol.44 , pp. 388-439
    • Jarvis, J.A.1    Kirkpatrick, A.2    Craik, D.J.3
  • 74
    • 0037127225 scopus 로고    scopus 로고
    • Prion peptide 106-126 modulates the aggregation of cellular prion protein and induces the synthesis of potentially neurotoxic transmembrane PrP
    • Gu Y, Fujioka H, Mishra RS, Li R, Singh N: Prion peptide 106-126 modulates the aggregation of cellular prion protein and induces the synthesis of potentially neurotoxic transmembrane PrP. J Biol Chem 2002, 277:2275-86.
    • (2002) J Biol Chem , vol.277 , pp. 2275-2286
    • Gu, Y.1    Fujioka, H.2    Mishra, R.S.3    Li, R.4    Singh, N.5
  • 75
    • 0037439629 scopus 로고    scopus 로고
    • In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression
    • Chabry J, Ratsimanohatra C, Sponne I, Elena PP, Vincent JP, Pillot T: In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression. J Neurosci 2003, 23:462-469.
    • (2003) J Neurosci , vol.23 , pp. 462-469
    • Chabry, J.1    Ratsimanohatra, C.2    Sponne, I.3    Elena, P.P.4    Vincent, J.P.5    Pillot, T.6
  • 76
    • 3142568651 scopus 로고    scopus 로고
    • Pathway complexity of Alzheimer's beta-amyloid Abeta16-22 peptide assembly
    • Santini S, Wei G, Mousseau N, Derreumaux P: Pathway complexity of Alzheimer's beta-amyloid Abeta16-22 peptide assembly. Structure 2004, 12:1245-1255.
    • (2004) Structure , vol.12 , pp. 1245-1255
    • Santini, S.1    Wei, G.2    Mousseau, N.3    Derreumaux, P.4
  • 77
    • 11844291405 scopus 로고    scopus 로고
    • A comparative study of amyloid fibril formation by residues 15-19 of the human calcitonin hormone: A single beta-sheet model with a small hydrophobic core
    • Haspel N, Zanuy D, Ma B, Wolfson H, Nussinov R: A comparative study of amyloid fibril formation by residues 15-19 of the human calcitonin hormone: a single beta-sheet model with a small hydrophobic core. J Mol Biol 2005, 345:1213-1227.
    • (2005) J Mol Biol , vol.345 , pp. 1213-1227
    • Haspel, N.1    Zanuy, D.2    Ma, B.3    Wolfson, H.4    Nussinov, R.5


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