메뉴 건너뛰기




Volumn 8, Issue 3, 2014, Pages 233-239

When amyloids become prions

Author keywords

Alzheimer's disease; Amyloid; Amyloid cytotoxicity; Amyloid transmission; Creutzfeldt Jakob disease; Prion; Transmissible spongiform encephalopathy

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; PRION PROTEIN; PRION;

EID: 84919708564     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/19336896.2014.968464     Document Type: Review
Times cited : (13)

References (97)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • PMID: 16756495
    • Chiti F, Dobson CM Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75:333-66; PMID: 16756495; http://dx.doi.org/10.1146/annurev.biochem.75.101304.123901
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 79958234542 scopus 로고    scopus 로고
    • Depression and risk of developing dementia
    • PMID: 21537355
    • Byers AL, Yaffe K. Depression and risk of developing dementia. Nat Rev Neurol 2011; 7:323-31; PMID: 21537355; http://dx.doi.org/10.1038/nrneurol.2011.60
    • (2011) Nat Rev Neurol , vol.7 , pp. 323-331
    • Byers, A.L.1    Yaffe, K.2
  • 3
    • 84877146722 scopus 로고    scopus 로고
    • Application of yeast to study the tau and amyloid-beta abnormalities of alzheimer's disease
    • PMID: 23396350
    • Porzoor A, Macreadie IG Application of Yeast to Study the Tau and Amyloid-beta Abnormalities of Alzheimer's Disease. J Alzheimers Dis 2013; 35:217-25; PMID: 23396350
    • (2013) J Alzheimers Dis , vol.35 , pp. 217-225
    • Porzoor, A.1    Macreadie, I.G.2
  • 4
    • 79952574501 scopus 로고    scopus 로고
    • Epidemiology of alzheimer disease
    • PMID: 21304480
    • Reitz C, Brayne C, Mayeux R. Epidemiology of Alzheimer disease. Nat Rev Neurol 2011; 7:137-52; PMID: 21304480; http://dx.doi.org/10.1038/nrneurol.2011.2
    • (2011) Nat Rev Neurol , vol.7 , pp. 137-152
    • Reitz, C.1    Brayne, C.2    Mayeux, R.3
  • 6
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • PMID: 17251001
    • Kodali R, Wetzel R. Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struct Biol 2007; 17:48-57; PMID: 17251001; http://dx.doi.org/10.1016/j.sbi.2007.01.007
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 7
    • 68249086335 scopus 로고    scopus 로고
    • Amyloids in bacterial inclusion bodies
    • PMID: 19647433
    • de Groot NS, Sabate R, Ventura S. Amyloids in bacterial inclusion bodies. Trends Biochem Sci 2009; 34:408-16; PMID: 19647433; http://dx.doi.org/10.1016/j.tibs.2009.03.009
    • (2009) Trends Biochem Sci , vol.34 , pp. 408-416
    • De Groot, N.S.1    Sabate, R.2    Ventura, S.3
  • 8
    • 50249144570 scopus 로고    scopus 로고
    • Bacterial inclusion bodies contain amyloid-like structure
    • PMID: 18684013
    • Wang L, Maji SK, Sawaya MR, Eisenberg D., Riek R. Bacterial inclusion bodies contain amyloid-like structure. PLoS Biol 2008; 6:e195; PMID: 18684013; http://dx.doi.org/10.1371/journal.pbio.0060195
    • (2008) PLoS Biol , vol.6
    • Wang, L.1    Maji, S.K.2    Sawaya, M.R.3    Eisenberg, D.4    Riek, R.5
  • 10
    • 32344448608 scopus 로고    scopus 로고
    • Protein aggregation and amyloidosis: Confusion of the kinds?
    • PMID: 16434184
    • Rousseau F, Schymkowitz J, Serrano L. Protein aggregation and amyloidosis: confusion of the kinds? Curr Opin Struct Biol 2006; 16:118-26; PMID: 16434184; http://dx.doi.org/10.1016/j.sbi.2006.01.011
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 118-126
    • Rousseau, F.1    Schymkowitz, J.2    Serrano, L.3
  • 11
    • 70349705441 scopus 로고    scopus 로고
    • Prions: Protein aggregation and infectious diseases
    • PMID: 19789378
    • Aguzzi A, Calella AM Prions: protein aggregation and infectious diseases. Physiol Rev 2009; 89:1105-52; PMID: 19789378; http://dx.doi.org/10.1152/physrev.00006.2009
    • (2009) Physiol Rev , vol.89 , pp. 1105-1152
    • Aguzzi, A.1    Calella, A.M.2
  • 12
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • PMID: 15189155
    • Chien P, Weissman JS, DePace AH Emerging principles of conformation-based prion inheritance. Annu Rev Biochem 2004; 73:617-56; PMID: 15189155; http://dx.doi.org/10.1146/annurev.biochem.72.121801.161837
    • (2004) Annu Rev Biochem , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 13
    • 84861559058 scopus 로고    scopus 로고
    • Transmissible proteins: Expanding the prion heresy
    • PMID: 22632966
    • Soto C. Transmissible proteins: expanding the prion heresy. Cell 2012; 149:968-77; PMID: 22632966; http://dx.doi.org/10.1016/j.cell.2012.05.007
    • (2012) Cell , vol.149 , pp. 968-977
    • Soto, C.1
  • 14
    • 80054745655 scopus 로고    scopus 로고
    • De novo generation of prion strains
    • PMID:21947062
    • Colby DW, Prusiner SB De novo generation of prion strains. Nat Rev Microbiol 2011; 9:771-7; PMID:21947062; http://dx.doi.org/10.1038/nrmicro2650
    • (2011) Nat Rev Microbiol , vol.9 , pp. 771-777
    • Colby, D.W.1    Prusiner, S.B.2
  • 17
    • 67650747654 scopus 로고    scopus 로고
    • Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions
    • PMID: 19231987
    • Caughey B, Baron GS, Chesebro B, Jeffrey M. Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem 2009; 78:177-204; PMID: 19231987; http://dx.doi.org/10.1146/annurev.biochem.78.082907.145410
    • (2009) Annu Rev Biochem , vol.78 , pp. 177-204
    • Caughey, B.1    Baron, G.S.2    Chesebro, B.3    Jeffrey, M.4
  • 18
    • 78649907008 scopus 로고    scopus 로고
    • Cell-to-cell transmission of non-prion protein aggregates
    • PMID: 21045796
    • Lee SJ, Desplats P, Sigurdson C., Tsigelny I, Masliah E. Cell-to-cell transmission of non-prion protein aggregates. Nat Rev Neurol 2010; 6:702-6; PMID: 21045796; http://dx.doi.org/10.1038/nrneurol.2010.145
    • (2010) Nat Rev Neurol , vol.6 , pp. 702-706
    • Lee, S.J.1    Desplats, P.2    Sigurdson, C.3    Tsigelny, I.4    Masliah, E.5
  • 19
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • PMID: 20308987
    • Brundin P, Melki R, Kopito R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 2010; 11:301-7; PMID: 20308987; http://dx.doi.org/10.1038/nrm2873
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 20
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in alzheimer disease and other neurodegenerative disorders
    • PMID: 22028219
    • Jucker M, Walker LC Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 2011; 70:532-40; PMID: 22028219; http://dx.doi.org/10.1002/ana.22615
    • (2011) Ann Neurol , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 22
    • 0034724227 scopus 로고    scopus 로고
    • New studies on the heat resistance of hamster-adapted scrapie agent: Threshold survival after ashing at 600 degrees C suggests an inorganic template of replication
    • PMID: 10716712
    • Brown P, Rau EH, Johnson BK, Bacote AE, Gibbs CJ, Jr., Gajdusek DC. New studies on the heat resistance of hamster-adapted scrapie agent: threshold survival after ashing at 600 degrees C suggests an inorganic template of replication. Proc Natl Acad Sci U S A 2000; 97:3418-21; PMID: 10716712
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3418-3421
    • Brown, P.1    Rau, E.H.2    Johnson, B.K.3    Bacote, A.E.4    Gibbs, C.J.5    Gajdusek, D.C.6
  • 23
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • PMID: 6414721
    • McKinley MP, Bolton DC, Prusiner SB A protease-resistant protein is a structural component of the scrapie prion. Cell 1983; 35:57-62; PMID: 6414721; http://dx.doi.org/10.1016/0092-8674(83)90207-6
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 24
    • 79952449094 scopus 로고    scopus 로고
    • Prion hypothesis: The end of the controversy?
    • PMID: 21130657
    • Soto C. Prion hypothesis: the end of the controversy? Trends Biochem Sci 2011; 36:151-8; PMID: 21130657; http://dx.doi.org/10.1016/j.tibs.2010.11.001
    • (2011) Trends Biochem Sci , vol.36 , pp. 151-158
    • Soto, C.1
  • 25
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • PMID: 12142498
    • Uptain SM, Lindquist S. Prions as protein-based genetic elements. Annu Rev Microbiol 2002; 56:703-41; PMID: 12142498; http://dx.doi.org/10.1146/annurev.micro.56.013002.100603
    • (2002) Annu Rev Microbiol , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.2
  • 26
    • 34447530804 scopus 로고    scopus 로고
    • Prions of fungi: Inherited structures and biological roles
    • PMID: 17632572
    • Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T. Prions of fungi: inherited structures and biological roles. Nat Rev Microbiol 2007; 5:611-8; PMID: 17632572; http://dx.doi.org/10.1038/nrmicro1708
    • (2007) Nat Rev Microbiol , vol.5 , pp. 611-618
    • Wickner, R.B.1    Edskes, H.K.2    Shewmaker, F.3    Nakayashiki, T.4
  • 27
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • PMID: 16810177
    • Tanaka M, Collins SR, Toyama BH, Weissman JS The physical basis of how prion conformations determine strain phenotypes. Nature 2006; 442:585-9; PMID: 16810177; http://dx.doi.org/10.1038/nature04922
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 28
    • 37049025592 scopus 로고    scopus 로고
    • Role of hsp104 in the propagation and inheritance of the; het-s prion
    • PMID: 17881723
    • Malato L, Dos Reis S, Benkemoun L, Sabate R., Saupe SJ Role of Hsp104 in the propagation and inheritance of the; Het-s prion. Mol Biol Cell 2007; 18:4803-12; PMID: 17881723; http://dx.doi.org/10.1091/mbc.E07-07-0657
    • (2007) Mol Biol Cell , vol.18 , pp. 4803-4812
    • Malato, L.1    Dos Reis, S.2    Benkemoun, L.3    Sabate, R.4    Saupe, S.J.5
  • 29
    • 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
    • PMID: 9275200
    • 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; 94:9773-8; PMID: 9275200; http://dx.doi.org/10.1073/pnas.94.18.9773
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 31
    • 0041345995 scopus 로고    scopus 로고
    • Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry
    • PMID: 12873146
    • Nazabal A, Dos Reis S, Bonneu M, Saupe SJ, Schmitter JM Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry. Biochemistry 2003; 42:8852-61; PMID: 12873146; http://dx.doi.org/10.1021/bi0344275
    • (2003) Biochemistry , vol.42 , pp. 8852-8861
    • Nazabal, A.1    Dos Reis, S.2    Bonneu, M.3    Saupe, S.J.4    Schmitter, J.M.5
  • 32
    • 84856790302 scopus 로고    scopus 로고
    • Localization of HET-S to the cell periphery, not to; het-s aggregates, is associated with; het-s-HET-S toxicity
    • PMID: 22037764
    • Mathur V, Seuring C, Riek R., Saupe SJ, Liebman SW Localization of HET-S to the cell periphery, not to; het-s aggregates, is associated with; het-s-HET-S toxicity. Mol Cell Biol 2012; 32:139-53; PMID: 22037764; http://dx.doi.org/10.1128/MCB.06125-11
    • (2012) Mol Cell Biol , vol.32 , pp. 139-153
    • Mathur, V.1    Seuring, C.2    Riek, R.3    Saupe, S.J.4    Liebman, S.W.5
  • 35
    • 84871682946 scopus 로고    scopus 로고
    • The mechanism of toxicity in HET-S/HET-s prion incompatibility
    • PMID: 23300377
    • Seuring C, Greenwald J, Wasmer C., Wepf R, Saupe SJ, Meier BH, Riek R. The mechanism of toxicity in HET-S/HET-s prion incompatibility. PLoS Biol 2012; 10:e1001451; PMID: 23300377; http://dx.doi.org/10.1371/journal.pbio.1001451
    • (2012) PLoS Biol , vol.10
    • Seuring, C.1    Greenwald, J.2    Wasmer, C.3    Wepf, R.4    Saupe, S.J.5    Meier, B.H.6    Riek, R.7
  • 36
    • 84871181408 scopus 로고    scopus 로고
    • Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure
    • PMID: 23251478
    • Dueholm MS, Albertsen M, Otzen D., Nielsen PH Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure. PLoS One 2012; 7:e51274; PMID: 23251478; http://dx.doi.org/10.1371/journal.pone.0051274
    • (2012) PLoS One , vol.7
    • Dueholm, M.S.1    Albertsen, M.2    Otzen, D.3    Nielsen, P.H.4
  • 37
    • 79955452211 scopus 로고    scopus 로고
    • The assembly of individual chaplin peptides from streptomyces coelicolor into functional amyloid fibrils
    • PMID: 21526199
    • Sawyer EB, Claessen D, Haas M., Hurgobin B, Gras SL The assembly of individual chaplin peptides from Streptomyces coelicolor into functional amyloid fibrils. PLoS One 2011; 6:e18839; PMID: 21526199; http://dx.doi.org/10.1371/journal.pone.0018839
    • (2011) PLoS One , vol.6
    • Sawyer, E.B.1    Claessen, D.2    Haas, M.3    Hurgobin, B.4    Gras, S.L.5
  • 39
    • 84864054380 scopus 로고    scopus 로고
    • Functional amyloids composed of phenol soluble modulins stabilize staphylococcus aureus biofilms
    • PMID: 22685403
    • Schwartz K, Syed AK, Stephenson RE, Rickard AH, Boles BR Functional amyloids composed of phenol soluble modulins stabilize Staphylococcus aureus biofilms. PLoS Pathog 2012; 8:e1002744; PMID: 22685403; http://dx.doi.org/10.1371/journal.ppat.1002744
    • (2012) PLoS Pathog , vol.8
    • Schwartz, K.1    Syed, A.K.2    Stephenson, R.E.3    Rickard, A.H.4    Boles, B.R.5
  • 41
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • PMID: 19345193
    • Alberti S, Halfmann R, King O., Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009; 137:146-58; PMID: 19345193; http://dx.doi.org/10.1016/j.cell.2009.02.044
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 42
    • 0036041641 scopus 로고    scopus 로고
    • Amyloidogenic nature of spider silk
    • PMID: 12180993
    • Kenney JM, Knight D, Wise MJ, Vollrath F. Amyloidogenic nature of spider silk. Eur J Biochem 2002; 269:4159-63; PMID: 12180993; http://dx.doi.org/10.1046/j.1432-1033.2002.03112.x
    • (2002) Eur J Biochem , vol.269 , pp. 4159-4163
    • Kenney, J.M.1    Knight, D.2    Wise, M.J.3    Vollrath, F.4
  • 43
    • 0034683126 scopus 로고    scopus 로고
    • Amyloids protect the silkmoth oocyte and embryo
    • PMID: 10981723
    • Iconomidou VA, Vriend G, Hamodrakas SJ Amyloids protect the silkmoth oocyte and embryo. FEBS Lett 2000; 479:141-5; PMID: 10981723; http://dx.doi.org/10.1016/S0014-5793(00)01888-3
    • (2000) FEBS Lett , vol.479 , pp. 141-145
    • Iconomidou, V.A.1    Vriend, G.2    Hamodrakas, S.J.3
  • 44
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • PMID: 14697205
    • Si K, Lindquist S, Kandel ER A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003; 115:879-91; PMID: 14697205; http://dx.doi.org/10.1016/S0092-8674(03)01020-1
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 46
    • 84860523522 scopus 로고    scopus 로고
    • Nonpathological extracellular amyloid is present during normal epididymal sperm maturation
    • PMID: 22570708
    • Whelly S, Johnson S, Powell J., Borchardt C, Hastert MC, Cornwall GA Nonpathological extracellular amyloid is present during normal epididymal sperm maturation. PLoS One 2012; 7:e36394; PMID: 22570708; http://dx.doi.org/10.1371/journal.pone.0036394
    • (2012) PLoS One , vol.7
    • Whelly, S.1    Johnson, S.2    Powell, J.3    Borchardt, C.4    Hastert, M.C.5    Cornwall, G.A.6
  • 48
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial poreforming toxins?
    • PMID: 16978447
    • Lashuel HA, Lansbury PT, Jr. Are amyloid diseases caused by protein aggregates that mimic bacterial poreforming toxins? Q Rev Biophys 2006; 39:167-201; PMID: 16978447; http://dx.doi.org/10.1017/S0033583506004422
    • (2006) Q Rev Biophys , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, P.T.2
  • 50
    • 33748298650 scopus 로고    scopus 로고
    • Curli biogenesis and function
    • PMID: 16704339
    • Barnhart MM, Chapman MR Curli biogenesis and function. Annu Rev Microbiol 2006; 60:131-47; PMID: 16704339; http://dx.doi.org/10.1146/annurev.micro.60.080805.142106
    • (2006) Annu Rev Microbiol , vol.60 , pp. 131-147
    • Barnhart, M.M.1    Chapman, M.R.2
  • 51
    • 84860363205 scopus 로고    scopus 로고
    • Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors
    • PMID: 22553999
    • Villar-Pique A., Espargaro A, Sabate R., de Groot NS, Ventura S. Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors. Microb Cell Fact 2012; 11:55; PMID: 22553999; http://dx.doi.org/10.1186/1475-2859-11-55
    • (2012) Microb Cell Fact , vol.11 , pp. 55
    • Villar-Pique, A.1    Espargaro, A.2    Sabate, R.3    De Groot, N.S.4    Ventura, S.5
  • 52
    • 79955084272 scopus 로고    scopus 로고
    • Suicidal; PSIC is a lethal yeast prion
    • PMID: 21402947
    • McGlinchey RP, Kryndushkin D, Wickner RB Suicidal; PSIC is a lethal yeast prion. Proc Natl Acad Sci U S A 2011; 108:5337-41; PMID: 21402947; http://dx.doi.org/10.1073/pnas.1102762108
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 5337-5341
    • McGlinchey, R.P.1    Kryndushkin, D.2    Wickner, R.B.3
  • 53
    • 83755183700 scopus 로고    scopus 로고
    • The yeast prions; PSIC and; URE3 are molecular degenerative diseases
    • PMID: 22052353
    • Wickner RB, Edskes HK, Bateman D, Kelly AC, Gorkovskiy A. The yeast prions; PSIC and; URE3 are molecular degenerative diseases. Prion 2011; 5:258-62; PMID: 22052353; http://dx.doi.org/10.4161/pri.17748
    • (2011) Prion , vol.5 , pp. 258-262
    • Wickner, R.B.1    Edskes, H.K.2    Bateman, D.3    Kelly, A.C.4    Gorkovskiy, A.5
  • 54
    • 84857097463 scopus 로고    scopus 로고
    • Prions are a common mechanism for phenotypic inheritance in wild yeasts
    • PMID: 22337056
    • Halfmann R, Jarosz DF, Jones SK, Chang A., Lancaster AK, Lindquist S. Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 2012; 482:363-8; PMID: 22337056; http://dx.doi.org/10.1038/nature10875
    • (2012) Nature , vol.482 , pp. 363-368
    • Halfmann, R.1    Jarosz, D.F.2    Jones, S.K.3    Chang, A.4    Lancaster, A.K.5    Lindquist, S.6
  • 55
    • 0034760879 scopus 로고    scopus 로고
    • Molecular population genetics and evolution of a prion-like protein in saccharomyces cerevisiae
    • PMID: 11606530
    • Jensen MA, True HL, Chernoff YO, Lindquist S. Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae. Genetics 2001; 159:527-35; PMID: 11606530
    • (2001) Genetics , vol.159 , pp. 527-535
    • Jensen, M.A.1    True, H.L.2    Chernoff, Y.O.3    Lindquist, S.4
  • 56
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • PMID: 10202160
    • Eaglestone SS, Cox BS, Tuite MF Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J 1999; 18:1974-81; PMID: 10202160; http://dx.doi.org/10.1093/emboj/18.7.1974
    • (1999) EMBO J , vol.18 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 57
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • PMID: 15311209
    • True HL, Berlin I, Lindquist SL Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 2004; 431:184-7; PMID: 15311209; http://dx.doi.org/10.1038/nature02885
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1    Berlin, I.2    Lindquist, S.L.3
  • 58
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • PMID: 11028992
    • True HL, Lindquist SL A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000; 407:477-83; PMID: 11028992; http://dx.doi.org/10.1038/35035005
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 59
  • 60
    • 77749271373 scopus 로고    scopus 로고
    • The spontaneous appearance rate of the yeast prion; PSIC and its implications for the evolution of the evolvability properties of the; PSIC system
    • PMID: 19917766
    • Lancaster AK, Bardill JP, True HL, Masel J. The spontaneous appearance rate of the yeast prion; PSIC and its implications for the evolution of the evolvability properties of the; PSIC system. Genetics 2010; 184:393-400; PMID: 19917766; http://dx.doi.org/10.1534/genetics.109.110213
    • (2010) Genetics , vol.184 , pp. 393-400
    • Lancaster, A.K.1    Bardill, J.P.2    True, H.L.3    Masel, J.4
  • 61
    • 34547136725 scopus 로고    scopus 로고
    • Ure2p function is enhanced by its prion domain in saccharomyces cerevisiae
    • PMID: 17507672
    • Shewmaker F, Mull L, Nakayashiki T., Masison DC, Wickner RB Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae. Genetics 2007; 176:1557-65; PMID: 17507672; http://dx.doi.org/10.1534/genetics.107.074153
    • (2007) Genetics , vol.176 , pp. 1557-1565
    • Shewmaker, F.1    Mull, L.2    Nakayashiki, T.3    Masison, D.C.4    Wickner, R.B.5
  • 62
    • 34848929022 scopus 로고    scopus 로고
    • Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • PMID: 17941703
    • Cheon M, Chang I, Mohanty S., Luheshi LM, Dobson CM, Vendruscolo M, Favrin G. Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLoS Comput Biol 2007; 3:1727-38; PMID: 17941703
    • (2007) PLoS Comput Biol , vol.3 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6    Favrin, G.7
  • 63
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • PMID: 17284452
    • Necula M, Kayed R, Milton S., Glabe CG Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 2007; 282:10311-24; PMID: 17284452; http://dx.doi.org/10.1074/jbc.M608207200
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 64
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of abeta oligomers
    • PMID: 20148964
    • Sakono M, Zako T. Amyloid oligomers: formation and toxicity of Abeta oligomers. FEBS J 2010; 277:1348-58; PMID: 20148964; http://dx.doi.org/10.1111/j.1742-4658.2010.07568.x
    • (2010) FEBS J , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 65
    • 0031963428 scopus 로고    scopus 로고
    • Identification of the end stage of scrapie using infected neural grafts
    • PMID: 9458163
    • Brandner S, Isenmann S, Kuhne G., Aguzzi A. Identification of the end stage of scrapie using infected neural grafts. Brain Pathol 1998; 8:19-27; PMID: 9458163; http://dx.doi.org/10.1111/j.1750-3639.1998.tb00130.x
    • (1998) Brain Pathol , vol.8 , pp. 19-27
    • Brandner, S.1    Isenmann, S.2    Kuhne, G.3    Aguzzi, A.4
  • 67
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • PMID: 16554307
    • Novitskaya V, Bocharova OV, Bronstein I, Baskakov IV Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J Biol Chem 2006; 281:13828-36; PMID: 16554307; http://dx.doi.org/10.1074/jbc.M511174200
    • (2006) J Biol Chem , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 70
    • 0032892306 scopus 로고    scopus 로고
    • Protease-resistant prion protein produced in vitro lacks detectable infectivity
    • PMID: 9934677
    • Hill AF, Antoniou M, Collinge J. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J Gen Virol 1999; 80 (Pt 1):11-4; PMID: 9934677
    • (1999) J Gen Virol , vol.80 , pp. 11-14
    • Hill, A.F.1    Antoniou, M.2    Collinge, J.3
  • 71
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • PMID: 21350487
    • Sandberg MK, Al-Doujaily H, Sharps B., Clarke AR, Collinge J. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 2011; 470:540-2; PMID: 21350487; http://dx.doi.org/10.1038/nature09768
    • (2011) Nature , vol.470 , pp. 540-542
    • Sandberg, M.K.1    Al-Doujaily, H.2    Sharps, B.3    Clarke, A.R.4    Collinge, J.5
  • 72
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • PMID: 17991853
    • Collinge J, Clarke AR A general model of prion strains and their pathogenicity. Science 2007; 318:930-6; PMID: 17991853; http://dx.doi.org/10.1126/science.1138718
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 73
    • 84857408200 scopus 로고    scopus 로고
    • Highly neurotoxic monomeric alpha-helical prion protein
    • PMID: 22323583
    • Zhou M, Ottenberg G, Sferrazza GF, Lasmezas CI Highly neurotoxic monomeric alpha-helical prion protein. Proc Natl Acad Sci U S A 2012; 109:3113-8; PMID: 22323583; http://dx.doi.org/10.1073/pnas.1118090109
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 3113-3118
    • Zhou, M.1    Ottenberg, G.2    Sferrazza, G.F.3    Lasmezas, C.I.4
  • 74
    • 44449092737 scopus 로고    scopus 로고
    • Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease
    • PMID: 18474855
    • Zhang B, Une Y, Fu X., Yan J, Ge F, Yao J., Sawashita J, Mori M, Tomozawa H., Kametani F, et al. Fecal transmission of AA amyloidosis in the cheetah contributes to high incidence of disease. Proc Natl Acad Sci U S A 2008; 105:7263-8; PMID: 18474855; http://dx.doi.org/10.1073/pnas.0800367105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7263-7268
    • Zhang, B.1    Une, Y.2    Fu, X.3    Yan, J.4    Ge, F.5    Yao, J.6    Sawashita, J.7    Mori, M.8    Tomozawa, H.9    Kametani, F.10
  • 76
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • PMID: 19651612
    • Desplats P, Lee HJ, Bae EJ, Patrick C., Rockenstein E, Crews L, Spencer B., Masliah E, Lee SJ Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc Natl Acad Sci U S A 2009; 106:13010-5; PMID: 19651612; http://dx.doi.org/10.1073/pnas.0903691106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3    Patrick, C.4    Rockenstein, E.5    Crews, L.6    Spencer, B.7    Masliah, E.8    Lee, S.J.9
  • 78
    • 84892538035 scopus 로고    scopus 로고
    • Alpha-synuclein transfers from neurons to oligodendrocytes
    • PMID: 24382629
    • Reyes JF, Rey NL, Bousset L, Melki R., Brundin P, Angot E. Alpha-synuclein transfers from neurons to oligodendrocytes. Glia 2014; 62:387-98; PMID: 24382629; http://dx.doi.org/10.1002/glia.22611
    • (2014) Glia , vol.62 , pp. 387-398
    • Reyes, J.F.1    Rey, N.L.2    Bousset, L.3    Melki, R.4    Brundin, P.5    Angot, E.6
  • 79
  • 80
    • 33947505619 scopus 로고    scopus 로고
    • Aggregated alpha-synuclein mediates dopaminergic neurotoxicity in vivo
    • PMID: 17376994
    • Periquet M, Fulga T, Myllykangas L., Schlossmacher MG, Feany MB Aggregated alpha-synuclein mediates dopaminergic neurotoxicity in vivo. J Neurosci 2007; 27:3338-46; PMID: 17376994; http://dx.doi.org/10.1523/JNEUROSCI.0285-07.2007
    • (2007) J Neurosci , vol.27 , pp. 3338-3346
    • Periquet, M.1    Fulga, T.2    Myllykangas, L.3    Schlossmacher, M.G.4    Feany, M.B.5
  • 81
    • 84862672217 scopus 로고    scopus 로고
    • Aggregation of alphaSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons
    • PMID: 22167382
    • Taschenberger G, Garrido M, Tereshchenko Y., Bahr M, Zweckstetter M, Kugler S. Aggregation of alphaSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons. Acta Neuropathol 2012; 123:671-83; PMID: 22167382; http://dx.doi.org/10.1007/s00401-011-0926-8
    • (2012) Acta Neuropathol , vol.123 , pp. 671-683
    • Taschenberger, G.1    Garrido, M.2    Tereshchenko, Y.3    Bahr, M.4    Zweckstetter, M.5    Kugler, S.6
  • 82
    • 84872458771 scopus 로고    scopus 로고
    • Aggregation and neurotoxicity of recombinant alpha-synuclein aggregates initiated by dimerization
    • PMID: 23339399
    • Roostaee A, Beaudoin S, Staskevicius A., Roucou X. Aggregation and neurotoxicity of recombinant alpha-synuclein aggregates initiated by dimerization. Mol Neurodegener 2013; 8:5; PMID: 23339399; http://dx.doi.org/10.1186/1750-1326-8-5
    • (2013) Mol Neurodegener , vol.8 , pp. 5
    • Roostaee, A.1    Beaudoin, S.2    Staskevicius, A.3    Roucou, X.4
  • 84
    • 0036641242 scopus 로고    scopus 로고
    • Tau neurotoxicity without the lesions: A fly challenges a tangled web
    • PMID: 12079751
    • de Silva R., Farrer M. Tau neurotoxicity without the lesions: a fly challenges a tangled web. Trends Neurosci 2002; 25:327-9; PMID: 12079751; http://dx.doi.org/10.1016/S0166-2236(02)02170-7
    • (2002) Trends Neurosci , vol.25 , pp. 327-329
    • De Silva, R.1    Farrer, M.2
  • 85
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in huntington's disease
    • PMID: 12747895
    • Bates G. Huntingtin aggregation and toxicity in Huntington's disease. Lancet 2003; 361:1642-4; PMID: 12747895; http://dx.doi.org/10.1016/S0140-6736(03)13304-1
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 86
    • 80051717705 scopus 로고    scopus 로고
    • Mechanisms of tau self-aggregation and neurotoxicity
    • PMID: 21605046
    • Farias G, Cornejo A, Jimenez J., Guzman L, Maccioni RB Mechanisms of tau self-aggregation and neurotoxicity. Curr Alzheimer Res 2011; 8:608-14; PMID: 21605046; http://dx.doi.org/10.2174/156720511796717258
    • (2011) Curr Alzheimer Res , vol.8 , pp. 608-614
    • Farias, G.1    Cornejo, A.2    Jimenez, J.3    Guzman, L.4    Maccioni, R.B.5
  • 87
    • 77953675879 scopus 로고    scopus 로고
    • Probing the biology of alzheimer's disease in mice
    • PMID: 20547123
    • Ashe KH, Zahs KR Probing the biology of Alzheimer's disease in mice. Neuron 2010; 66:631-45; PMID: 20547123; http://dx.doi.org/10.1016/j.neuron.2010.04.031
    • (2010) Neuron , vol.66 , pp. 631-645
    • Ashe, K.H.1    Zahs, K.R.2
  • 88
    • 79957913270 scopus 로고    scopus 로고
    • Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
    • PMID: 21645391
    • Lasagna-Reeves CA, Castillo-Carranza DL, Sengupta U., Clos AL, Jackson GR, Kayed R. Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice. Mol Neurodegener 2011; 6:39; PMID: 21645391; http://dx.doi.org/10.1186/1750-1326-6-39
    • (2011) Mol Neurodegener , vol.6 , pp. 39
    • Lasagna-Reeves, C.A.1    Castillo-Carranza, D.L.2    Sengupta, U.3    Clos, A.L.4    Jackson, G.R.5    Kayed, R.6
  • 89
    • 84860879196 scopus 로고    scopus 로고
    • Identification of novel potentially toxic oligomers formed in vitro from mammalian-derived expanded huntingtin exon-1 protein
    • PMID: 22433867
    • Nucifora LG, Burke KA, Feng X, Arbez N., Zhu S, Miller J, Yang G., Ratovitski T, Delannoy M, Muchowski PJ, et al. Identification of novel potentially toxic oligomers formed in vitro from mammalian-derived expanded huntingtin exon-1 protein. J Biol Chem 2012; 287:16017-28; PMID: 22433867; http://dx.doi.org/10.1074/jbc.M111.252577
    • (2012) J Biol Chem , vol.287 , pp. 16017-16028
    • Nucifora, L.G.1    Burke, K.A.2    Feng, X.3    Arbez, N.4    Zhu, S.5    Miller, J.6    Yang, G.7    Ratovitski, T.8    Delannoy, M.9    Muchowski, P.J.10
  • 90
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • PMID: 19487684
    • Nekooki-Machida Y., Kurosawa M, Nukina N., Ito K, Oda T, Tanaka M. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc Natl Acad Sci U S A 2009; 106:9679-84; PMID: 19487684; http://dx.doi.org/10.1073/pnas.0812083106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 91
    • 84980053087 scopus 로고    scopus 로고
    • Multiple mechanisms of extracellular tau spreading in a non-transgenic tauopathy model
    • PMID: 23383401
    • Le MN, Kim W, Lee S., McKee AC, Hall GF Multiple mechanisms of extracellular tau spreading in a non-transgenic tauopathy model. Am J Neurodegener Dis 2012; 1:316-33; PMID: 23383401
    • (2012) Am J Neurodegener Dis , vol.1 , pp. 316-333
    • Le, M.N.1    Kim, W.2    Lee, S.3    McKee, A.C.4    Hall, G.F.5
  • 92
    • 80054010366 scopus 로고    scopus 로고
    • Soluble abeta seeds are potent inducers of cerebral beta-amyloid deposition
    • PMID: 21994365
    • Langer F, Eisele YS, Fritschi SK, Staufenbiel M., Walker LC, Jucker M. Soluble Abeta seeds are potent inducers of cerebral beta-amyloid deposition. J Neurosci 2011; 31:14488-95; PMID: 21994365; http://dx.doi.org/10.1523/JNEUROSCI.3088-11.2011
    • (2011) J Neurosci , vol.31 , pp. 14488-14495
    • Langer, F.1    Eisele, Y.S.2    Fritschi, S.K.3    Staufenbiel, M.4    Walker, L.C.5    Jucker, M.6
  • 94
    • 70349295278 scopus 로고    scopus 로고
    • Structure-neurotoxicity relationships of amyloid beta-protein oligomers
    • PMID: 19706468
    • Ono K, Condron MM, Teplow DB Structure-neurotoxicity relationships of amyloid beta-protein oligomers. Proc Natl Acad Sci U S A 2009; 106:14745-50; PMID: 19706468; http://dx.doi.org/10.1073/pnas.0905127106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 95
    • 84902937102 scopus 로고    scopus 로고
    • Neurotoxic amyloid beta oligomeric assemblies recreated in microfluidic platform with interstitial level of slow flow
    • PMID: 23719665
    • Choi YJ, Chae S, Kim JH, Barald KF, Park JY, Lee SH Neurotoxic amyloid beta oligomeric assemblies recreated in microfluidic platform with interstitial level of slow flow. Sci Rep 2013; 3:1921; PMID: 23719665
    • (2013) Sci Rep , vol.3 , pp. 1921
    • Choi, Y.J.1    Chae, S.2    Kim, J.H.3    Barald, K.F.4    Park, J.Y.5    Lee, S.H.6
  • 96
    • 84865577637 scopus 로고    scopus 로고
    • Dispersible amyloid beta-protein oligomers, protofibrils, and fibrils represent diffusible but not soluble aggregates: Their role in neurodegeneration in amyloid precursor protein (APP) transgenic mice
    • PMID: 22305478
    • Rijal Upadhaya A., Capetillo-Zarate E, Kosterin I., Abramowski D, Kumar S, Yamaguchi H., Walter J, Fändrich M, Staufenbiel M., Thal DR. Dispersible amyloid beta-protein oligomers, protofibrils, and fibrils represent diffusible but not soluble aggregates: their role in neurodegeneration in amyloid precursor protein (APP) transgenic mice. Neurobiol Aging 2012; 33:2641-60; PMID: 22305478; http://dx.doi.org/10.1016/j.neurobiolaging.2011.12.032
    • (2012) Neurobiol Aging , vol.33 , pp. 2641-2660
    • Rijal Upadhaya, A.1    Capetillo-Zarate, E.2    Kosterin, I.3    Abramowski, D.4    Kumar, S.5    Yamaguchi, H.6    Walter, J.7    Fändrich, M.8    Staufenbiel, M.9    Thal, D.R.10
  • 97
    • 84862844825 scopus 로고    scopus 로고
    • Effect of the surface charge of artificial model membranes on the aggregation of amyloid beta-peptide
    • PMID: 22542639
    • Sabate R, Espargaro A, Barbosa-Barros L, Ventura S., Estelrich J. Effect of the surface charge of artificial model membranes on the aggregation of amyloid beta-peptide. Biochimie 2012; 94:1730-8; PMID: 22542639; http://dx.doi.org/10.1016/j.biochi.2012.03.027
    • (2012) Biochimie , vol.94 , pp. 1730-1738
    • Sabate, R.1    Espargaro, A.2    Barbosa-Barros, L.3    Ventura, S.4    Estelrich, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.