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Volumn 207, Issue , 2015, Pages 127-135

Predicting the aggregation propensity of prion sequences

Author keywords

Amyloid algorithm; Amyloid prediction; Hot spot; Prion prediction; Sheet prediction

Indexed keywords

AMYLOID; PRION PROTEIN; PRION; PROTEIN AGGREGATE;

EID: 84938740330     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2015.03.001     Document Type: Article
Times cited : (6)

References (85)
  • 1
    • 70349705441 scopus 로고    scopus 로고
    • Prions: protein aggregation and infectious diseases
    • Aguzzi A., Calella A.M. Prions: protein aggregation and infectious diseases. Physiol. Rev. 2009, 89(4):1105-1152.
    • (2009) Physiol. Rev. , vol.89 , Issue.4 , pp. 1105-1152
    • Aguzzi, A.1    Calella, A.M.2
  • 2
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S., Halfmann R., King O., Kapila A., Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009, 137(1):146-158.
    • (2009) Cell , vol.137 , Issue.1 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 3
    • 84874638938 scopus 로고    scopus 로고
    • Prions, prionoids and pathogenic proteins in Alzheimer disease
    • Ashe K.H., Aguzzi A. Prions, prionoids and pathogenic proteins in Alzheimer disease. Prion 2013, 7(1):55-59.
    • (2013) Prion , vol.7 , Issue.1 , pp. 55-59
    • Ashe, K.H.1    Aguzzi, A.2
  • 4
    • 79960005237 scopus 로고    scopus 로고
    • Prediction of amyloid aggregation in vivo
    • Belli M., Ramazzotti M., Chiti F. Prediction of amyloid aggregation in vivo. EMBO Rep. 2011, 12(7):657-663.
    • (2011) EMBO Rep. , vol.12 , Issue.7 , pp. 657-663
    • Belli, M.1    Ramazzotti, M.2    Chiti, F.3
  • 5
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson J.F., Theos A.C., Harper D.C., Tenza D., Raposo G., Marks M.S. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol. 2003, 161(3):521-533.
    • (2003) J. Cell Biol. , vol.161 , Issue.3 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 6
    • 63549101789 scopus 로고    scopus 로고
    • BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis
    • Bryan A.W., Menke M., Cowen L.J., Lindquist S.L., Berger B. BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis. PLoS Comput. Biol. 2009, 5(3):e1000333.
    • (2009) PLoS Comput. Biol. , vol.5 , Issue.3 , pp. e1000333
    • Bryan, A.W.1    Menke, M.2    Cowen, L.J.3    Lindquist, S.L.4    Berger, B.5
  • 7
    • 84855674302 scopus 로고    scopus 로고
    • STITCHER: dynamic assembly of likely amyloid and prion beta-structures from secondary structure predictions
    • Bryan A.W., O'Donnell C.W., Menke M., Cowen L.J., Lindquist S., Berger B. STITCHER: dynamic assembly of likely amyloid and prion beta-structures from secondary structure predictions. Proteins 2012, 80(2):410-420.
    • (2012) Proteins , vol.80 , Issue.2 , pp. 410-420
    • Bryan, A.W.1    O'Donnell, C.W.2    Menke, M.3    Cowen, L.J.4    Lindquist, S.5    Berger, B.6
  • 8
    • 79957809655 scopus 로고    scopus 로고
    • Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes
    • Castillo V., Grana-Montes R., Sabate R., Ventura S. Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes. Biotechnol. J. 2011, 6(6):674-685.
    • (2011) Biotechnol. J. , vol.6 , Issue.6 , pp. 674-685
    • Castillo, V.1    Grana-Montes, R.2    Sabate, R.3    Ventura, S.4
  • 9
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey B., Baron G.S. Prions and their partners in crime. Nature 2006, 443(7113):803-810.
    • (2006) Nature , vol.443 , Issue.7113 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 12
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P., Weissman J.S., DePace A.H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 2004, 73:617-656.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 13
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 14
    • 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 C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003, 424(6950):805-808.
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 15
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou P.Y., Fasman G.D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 1974, 13(2):211-222.
    • (1974) Biochemistry , vol.13 , Issue.2 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 17
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • Coustou V., Deleu C., Saupe S., Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. U. S. A. 1997, 94(18):9773-9778.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.18 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 18
    • 79551595773 scopus 로고    scopus 로고
    • Bacterial inclusion bodies of Alzheimer's disease beta-amyloid peptides can be employed to study native-like aggregation intermediate states
    • Dasari M., Espargaro A., Sabate R., Lopez Del Amo J.M., Fink U., Grelle G., Bieschke J., Ventura S., Reif B. Bacterial inclusion bodies of Alzheimer's disease beta-amyloid peptides can be employed to study native-like aggregation intermediate states. Chembiochem 2011, 12(3):407-423.
    • (2011) Chembiochem , vol.12 , Issue.3 , pp. 407-423
    • Dasari, M.1    Espargaro, A.2    Sabate, R.3    Lopez Del Amo, J.M.4    Fink, U.5    Grelle, G.6    Bieschke, J.7    Ventura, S.8    Reif, B.9
  • 20
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 2003, 426(6968):884-890.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 21
    • 3242785264 scopus 로고    scopus 로고
    • Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
    • DuBay K.F., Pawar A.P., Chiti F., Zurdo J., Dobson C.M., Vendruscolo M. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J. Mol. Biol. 2004, 341(5):1317-1326.
    • (2004) J. Mol. Biol. , vol.341 , Issue.5 , pp. 1317-1326
    • DuBay, K.F.1    Pawar, A.P.2    Chiti, F.3    Zurdo, J.4    Dobson, C.M.5    Vendruscolo, M.6
  • 22
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: join the crowd
    • Ellis R.J., Minton A.P. Cell biology: join the crowd. Nature 2003, 425(6953):27-28.
    • (2003) Nature , vol.425 , Issue.6953 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 24
    • 84877834389 scopus 로고    scopus 로고
    • Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains
    • Espinosa Angarica V., Ventura S., Sancho J. Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. BMC Genomics 2013, 14:316.
    • (2013) BMC Genomics , vol.14 , pp. 316
    • Espinosa Angarica, V.1    Ventura, S.2    Sancho, J.3
  • 25
    • 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. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22(10):1302-1306.
    • (2004) Nat. Biotechnol. , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 28
    • 33845990277 scopus 로고    scopus 로고
    • Prediction of amyloidogenic and disordered regions in protein chains
    • Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Y. Prediction of amyloidogenic and disordered regions in protein chains. PLoS Comput. Biol. 2006, 2(12):e177.
    • (2006) PLoS Comput. Biol. , vol.2 , Issue.12 , pp. e177
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 30
    • 0024110035 scopus 로고
    • A protein secondary structure prediction scheme for the IBM PC and compatibles
    • Hamodrakas S.J. A protein secondary structure prediction scheme for the IBM PC and compatibles. Comput. Appl. Biosci. 1988, 4(4):473-477.
    • (1988) Comput. Appl. Biosci. , vol.4 , Issue.4 , pp. 473-477
    • Hamodrakas, S.J.1
  • 31
    • 34250793865 scopus 로고    scopus 로고
    • Consensus prediction of amyloidogenic determinants in amyloid fibril-forming proteins
    • Hamodrakas S.J., Liappa C., Iconomidou V.A. Consensus prediction of amyloidogenic determinants in amyloid fibril-forming proteins. Int. J. Biol. Macromol. 2007, 41(3):295-300.
    • (2007) Int. J. Biol. Macromol. , vol.41 , Issue.3 , pp. 295-300
    • Hamodrakas, S.J.1    Liappa, C.2    Iconomidou, V.A.3
  • 32
    • 3242735504 scopus 로고    scopus 로고
    • An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril
    • Ivanova M.I., Sawaya M.R., 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(29):10584-10589.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.29 , pp. 10584-10589
    • Ivanova, M.I.1    Sawaya, M.R.2    Gingery, M.3    Attinger, A.4    Eisenberg, D.5
  • 33
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: polypeptide conformations on competing pathways
    • Jahn T.R., Radford S.E. Folding versus aggregation: polypeptide conformations on competing pathways. Arch. Biochem. Biophys. 2008, 469(1):100-117.
    • (2008) Arch. Biochem. Biophys. , vol.469 , Issue.1 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 34
    • 0343621535 scopus 로고    scopus 로고
    • AAindex: amino acid index database
    • Kawashima S., Kanehisa M. AAindex: amino acid index database. Nucleic Acids Res. 2000, 28(1):374.
    • (2000) Nucleic Acids Res. , vol.28 , Issue.1 , pp. 374
    • Kawashima, S.1    Kanehisa, M.2
  • 37
    • 0038612852 scopus 로고    scopus 로고
    • Amyloid as a natural product
    • Kelly J.W., Balch W.E. Amyloid as a natural product. J. Cell Biol. 2003, 161(3):461-462.
    • (2003) J. Cell Biol. , vol.161 , Issue.3 , pp. 461-462
    • Kelly, J.W.1    Balch, W.E.2
  • 38
    • 67849110003 scopus 로고    scopus 로고
    • NetCSSP: web application for predicting chameleon sequences and amyloid fibril formation
    • Kim C., Choi J., Lee S.J., Welsh W.J., Yoon S. NetCSSP: web application for predicting chameleon sequences and amyloid fibril formation. Nucleic Acids Res. 2009, 37(Web Server issue):W469-W473.
    • (2009) Nucleic Acids Res. , vol.37 , Issue.Web Server issue , pp. W469-W473
    • Kim, C.1    Choi, J.2    Lee, S.J.3    Welsh, W.J.4    Yoon, S.5
  • 40
    • 84907029459 scopus 로고    scopus 로고
    • PLAAC: a web and command-line application to identify proteins with prion-like amino acid composition
    • Lancaster A.K., Nutter-Upham A., Lindquist S., King O.D. PLAAC: a web and command-line application to identify proteins with prion-like amino acid composition. Bioinformatics 2014, 30(17):2501-2502.
    • (2014) Bioinformatics , vol.30 , Issue.17 , pp. 2501-2502
    • Lancaster, A.K.1    Nutter-Upham, A.2    Lindquist, S.3    King, O.D.4
  • 41
    • 84892408882 scopus 로고    scopus 로고
    • Discriminant analysis of prion sequences for prediction of susceptibility
    • Lee J.H., Bae S.E., Jung S., Ahn I., Son H.S. Discriminant analysis of prion sequences for prediction of susceptibility. Exp. Mol. Med. 2013, 45:e48.
    • (2013) Exp. Mol. Med. , vol.45 , pp. e48
    • Lee, J.H.1    Bae, S.E.2    Jung, S.3    Ahn, I.4    Son, H.S.5
  • 46
    • 0025264854 scopus 로고
    • The equilibrium partition function and base pair binding probabilities for RNA secondary structure
    • McCaskill J.S. The equilibrium partition function and base pair binding probabilities for RNA secondary structure. Biopolymers 1990, 29(6-7):1105-1119.
    • (1990) Biopolymers , vol.29 , Issue.6-7 , pp. 1105-1119
    • McCaskill, J.S.1
  • 48
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models of amyloid fibril structure
    • Nelson R., Eisenberg D. Recent atomic models of amyloid fibril structure. Curr. Opin. Struct. Biol. 2006, 16(2):260-265.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , Issue.2 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 52
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of aggregation-prone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases
    • Pawar A.P., Dubay K.F., Zurdo J., Chiti F., Vendruscolo M., Dobson C.M. Prediction of aggregation-prone and aggregation-susceptible regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 2005, 350(2):379-392.
    • (2005) J. Mol. Biol. , vol.350 , Issue.2 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 54
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 1982, 216(4542):136-144.
    • (1982) Science , vol.216 , Issue.4542 , pp. 136-144
    • Prusiner, S.B.1
  • 55
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture - neurodegenerative diseases and prions
    • Prusiner S.B. Shattuck lecture - neurodegenerative diseases and prions. N. Engl. J. Med. 2001, 344(20):1516-1526.
    • (2001) N. Engl. J. Med. , vol.344 , Issue.20 , pp. 1516-1526
    • Prusiner, S.B.1
  • 56
    • 77952330147 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the alpha-helix to beta-sheet transition in coiled protein filaments: evidence for a critical filament length scale
    • Qin Z., Buehler M.J. Molecular dynamics simulation of the alpha-helix to beta-sheet transition in coiled protein filaments: evidence for a critical filament length scale. Phys. Rev. Lett. 2010, 104(19):198304.
    • (2010) Phys. Rev. Lett. , vol.104 , Issue.19 , pp. 198304
    • Qin, Z.1    Buehler, M.J.2
  • 57
    • 77955629284 scopus 로고    scopus 로고
    • The effects of amino acid composition on yeast prion formation and prion domain interactions
    • Ross E.D., Toombs J.A. The effects of amino acid composition on yeast prion formation and prion domain interactions. Prion 2010, 4(2):60-65.
    • (2010) Prion , vol.4 , Issue.2 , pp. 60-65
    • Ross, E.D.1    Toombs, J.A.2
  • 58
    • 29444444251 scopus 로고    scopus 로고
    • How evolutionary pressure against protein aggregation shaped chaperone specificity
    • Rousseau F., Serrano L., Schymkowitz J.W. How evolutionary pressure against protein aggregation shaped chaperone specificity. J. Mol. Biol. 2006, 355(5):1037-1047.
    • (2006) J. Mol. Biol. , vol.355 , Issue.5 , pp. 1037-1047
    • Rousseau, F.1    Serrano, L.2    Schymkowitz, J.W.3
  • 59
    • 84919708564 scopus 로고    scopus 로고
    • When amyloids become prions
    • Sabate R. When amyloids become prions. Prion 2014, 8(3):233-239.
    • (2014) Prion , vol.8 , Issue.3 , pp. 233-239
    • Sabate, R.1
  • 62
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe D.J. Folding proteins in fatal ways. Nature 2003, 426(6968):900-904.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 65
    • 84861559058 scopus 로고    scopus 로고
    • Transmissible proteins: expanding the prion heresy
    • Soto C. Transmissible proteins: expanding the prion heresy. Cell 2012, 149(5):968-977.
    • (2012) Cell , vol.149 , Issue.5 , pp. 968-977
    • Soto, C.1
  • 66
    • 3042584515 scopus 로고    scopus 로고
    • The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
    • Tartaglia G.G., Cavalli A., Pellarin R., Caflisch A. The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates. Protein Sci. 2004, 13(7):1939-1941.
    • (2004) Protein Sci. , vol.13 , Issue.7 , pp. 1939-1941
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 67
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator method for predicting protein aggregation propensities
    • Tartaglia G.G., Vendruscolo M. The Zyggregator method for predicting protein aggregation propensities. Chem. Soc. Rev. 2008, 37(7):1395-1401.
    • (2008) Chem. Soc. Rev. , vol.37 , Issue.7 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 69
    • 60849089613 scopus 로고    scopus 로고
    • Prediction of amyloid fibril-forming segments based on a support vector machine
    • Tian J., Wu N., Guo J., Fan Y. Prediction of amyloid fibril-forming segments based on a support vector machine. BMC Bioinform. 2009, 10(Suppl. 1):S45.
    • (2009) BMC Bioinform. , vol.10 , pp. S45
    • Tian, J.1    Wu, N.2    Guo, J.3    Fan, Y.4
  • 70
    • 73549115633 scopus 로고    scopus 로고
    • Compositional determinants of prion formation in yeast
    • Toombs J.A., McCarty B.R., Ross E.D. Compositional determinants of prion formation in yeast. Mol. Cell. Biol. 2010, 30(1):319-332.
    • (2010) Mol. Cell. Biol. , vol.30 , Issue.1 , pp. 319-332
    • Toombs, J.A.1    McCarty, B.R.2    Ross, E.D.3
  • 72
    • 36248964819 scopus 로고    scopus 로고
    • The PASTA server for protein aggregation prediction
    • Trovato A., Seno F., Tosatto S.C. The PASTA server for protein aggregation prediction. Protein Eng. Des. Sel. 2007, 20(10):521-523.
    • (2007) Protein Eng. Des. Sel. , vol.20 , Issue.10 , pp. 521-523
    • Trovato, A.1    Seno, F.2    Tosatto, S.C.3
  • 73
    • 84872223302 scopus 로고    scopus 로고
    • A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins
    • Tsolis A.C., Papandreou N.C., Iconomidou V.A., Hamodrakas S.J. A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins. PLoS ONE 2013, 8(1):e54175.
    • (2013) PLoS ONE , vol.8 , Issue.1 , pp. e54175
    • Tsolis, A.C.1    Papandreou, N.C.2    Iconomidou, V.A.3    Hamodrakas, S.J.4
  • 74
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • UniProt C. The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res. 2010, 38(Database issue):D142-D148.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.Database issue , pp. D142-D148
    • UniProt, C.1
  • 75
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain S.M., Lindquist S. Prions as protein-based genetic elements. Annu. Rev. Microbiol. 2002, 56:703-741.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 77
    • 84904499277 scopus 로고    scopus 로고
    • Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection
    • Villar-Pique A., Espargaro A., Ventura S., Sabate R. Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection. Curr. Protein Pept. Sci. 2014, 15(5):477-489.
    • (2014) Curr. Protein Pept. Sci. , vol.15 , Issue.5 , pp. 477-489
    • Villar-Pique, A.1    Espargaro, A.2    Ventura, S.3    Sabate, R.4
  • 78
    • 84904786762 scopus 로고    scopus 로고
    • PASTA 2.0: an improved server for protein aggregation prediction
    • Walsh I., Seno F., Tosatto S.C., Trovato A. PASTA 2.0: an improved server for protein aggregation prediction. Nucleic Acids Res. 2014, 42(Web Server issue):W301-W307.
    • (2014) Nucleic Acids Res. , vol.42 , Issue.Web Server issue , pp. W301-W307
    • Walsh, I.1    Seno, F.2    Tosatto, S.C.3    Trovato, A.4
  • 79
    • 83755183700 scopus 로고    scopus 로고
    • The yeast prions [PSI+] and [URE3] are molecular degenerative diseases
    • Wickner R.B., Edskes H.K., Bateman D., Kelly A.C., Gorkovskiy A. The yeast prions [PSI+] and [URE3] are molecular degenerative diseases. Prion 2011, 5(4):258-262.
    • (2011) Prion , vol.5 , Issue.4 , pp. 258-262
    • Wickner, R.B.1    Edskes, H.K.2    Bateman, D.3    Kelly, A.C.4    Gorkovskiy, A.5
  • 80
    • 3342963982 scopus 로고    scopus 로고
    • Detecting hidden sequence propensity for amyloid fibril formation
    • Yoon S., Welsh W.J. Detecting hidden sequence propensity for amyloid fibril formation. Protein Sci. 2004, 13(8):2149-2160.
    • (2004) Protein Sci. , vol.13 , Issue.8 , pp. 2149-2160
    • Yoon, S.1    Welsh, W.J.2
  • 81
    • 19544391613 scopus 로고    scopus 로고
    • Rapid assessment of contact-dependent secondary structure propensity: relevance to amyloidogenic sequences
    • Yoon S., Welsh W.J. Rapid assessment of contact-dependent secondary structure propensity: relevance to amyloidogenic sequences. Proteins 2005, 60(1):110-117.
    • (2005) Proteins , vol.60 , Issue.1 , pp. 110-117
    • Yoon, S.1    Welsh, W.J.2
  • 82
    • 35148821507 scopus 로고    scopus 로고
    • CSSP2: an improved method for predicting contact-dependent secondary structure propensity
    • Yoon S., Welsh W.J., Jung H., Yoo Y.D. CSSP2: an improved method for predicting contact-dependent secondary structure propensity. Comput. Biol. Chem. 2007, 31(5-6):373-377.
    • (2007) Comput. Biol. Chem. , vol.31 , Issue.5-6 , pp. 373-377
    • Yoon, S.1    Welsh, W.J.2    Jung, H.3    Yoo, Y.D.4
  • 84
    • 34548756136 scopus 로고    scopus 로고
    • Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential
    • Zhang Z., Chen H., Lai L. Identification of amyloid fibril-forming segments based on structure and residue-based statistical potential. Bioinformatics 2007, 23(17):2218-2225.
    • (2007) Bioinformatics , vol.23 , Issue.17 , pp. 2218-2225
    • Zhang, Z.1    Chen, H.2    Lai, L.3
  • 85
    • 34247591802 scopus 로고    scopus 로고
    • A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone
    • Zibaee S., Makin O.S., Goedert M., Serpell L.C. A simple algorithm locates beta-strands in the amyloid fibril core of alpha-synuclein, Abeta, and tau using the amino acid sequence alone. Protein Sci. 2007, 16(5):906-918.
    • (2007) Protein Sci. , vol.16 , Issue.5 , pp. 906-918
    • Zibaee, S.1    Makin, O.S.2    Goedert, M.3    Serpell, L.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.