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Volumn 32, Issue 5, 2007, Pages 217-224

Functional amyloid - from bacteria to humans

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; MELANIN;

EID: 34247899121     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2007.03.003     Document Type: Review
Times cited : (909)

References (77)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang X., et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127 (2006) 803-815
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1
  • 3
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink A.L. Natively unfolded proteins. Curr. Opin. Struct. Biol. 15 (2005) 35-41
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 4
    • 33845648118 scopus 로고    scopus 로고
    • Natural triple β-stranded fibrous folds
    • Mitraki A., et al. Natural triple β-stranded fibrous folds. Adv. Protein Chem. 73 (2006) 97-124
    • (2006) Adv. Protein Chem. , vol.73 , pp. 97-124
    • Mitraki, A.1
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen F.E., and Kelly J.W. Therapeutic approaches to protein-misfolding diseases. Nature 426 (2003) 905-909
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 7
    • 0032855076 scopus 로고    scopus 로고
    • Staining methods for identification of amyloid in tissue
    • Westermark G.T., et al. Staining methods for identification of amyloid in tissue. Methods Enzymol. 309 (1999) 3-25
    • (1999) Methods Enzymol. , vol.309 , pp. 3-25
    • Westermark, G.T.1
  • 8
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel H.A., and Lansbury P.T. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?. Q. Rev. Biophys. 39 (2006) 167-201
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, P.T.2
  • 9
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V., et al. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 281 (2006) 13828-13836
    • (2006) J. Biol. Chem. , vol.281 , pp. 13828-13836
    • Novitskaya, V.1
  • 10
    • 8844238368 scopus 로고    scopus 로고
    • Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition?
    • Chernoff Y.O. Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition?. Curr. Opin. Chem. Biol. 8 (2004) 665-671
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 665-671
    • Chernoff, Y.O.1
  • 11
    • 0035089501 scopus 로고    scopus 로고
    • The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures
    • Mackay J.P., et al. The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures. Structure 9 (2001) 83-91
    • (2001) Structure , vol.9 , pp. 83-91
    • Mackay, J.P.1
  • 12
    • 31144460030 scopus 로고    scopus 로고
    • Functional amyloid formation within mammalian tissue
    • Fowler D.M., et al. Functional amyloid formation within mammalian tissue. PLoS Biol. 4 (2006) e6
    • (2006) PLoS Biol. , vol.4
    • Fowler, D.M.1
  • 13
    • 0036468673 scopus 로고    scopus 로고
    • Role of Escherichia coli curli operons in directing amyloid fiber formation
    • Chapman M.R., et al. Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295 (2002) 851-855
    • (2002) Science , vol.295 , pp. 851-855
    • Chapman, M.R.1
  • 14
    • 0038004458 scopus 로고    scopus 로고
    • A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils
    • Claessen D., et al. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev. 17 (2003) 1714-1726
    • (2003) Genes Dev. , vol.17 , pp. 1714-1726
    • Claessen, D.1
  • 15
    • 0034683126 scopus 로고    scopus 로고
    • Amyloids protect the silkmoth oocyte and embryo
    • Iconomidou V.A., et al. Amyloids protect the silkmoth oocyte and embryo. FEBS Lett. 479 (2000) 141-145
    • (2000) FEBS Lett. , vol.479 , pp. 141-145
    • Iconomidou, V.A.1
  • 16
    • 0036403732 scopus 로고    scopus 로고
    • Prions as protein-based genetic elements
    • Uptain S.M., and Lindquist S. Prions as protein-based genetic elements. Annu. Rev. Microbiol. 56 (2002) 703-741
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 703-741
    • Uptain, S.M.1    Lindquist, S.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., et al. 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. 94 (1997) 9773-9778
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9773-9778
    • Coustou, V.1
  • 18
    • 0034816786 scopus 로고    scopus 로고
    • Spectroscopic evidence for amyloid-like interfacial self-assembly of hydrophobin Sc3
    • Butko P., et al. Spectroscopic evidence for amyloid-like interfacial self-assembly of hydrophobin Sc3. Biochem. Biophys. Res. Commun. 280 (2001) 212-215
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 212-215
    • Butko, P.1
  • 19
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King C.Y., et al. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 6618-6622
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6618-6622
    • King, C.Y.1
  • 20
    • 0036041641 scopus 로고    scopus 로고
    • Amyloidogenic nature of spider silk
    • Kenney J.M., et al. Amyloidogenic nature of spider silk. Eur. J. Biochem. 269 (2002) 4159-4163
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4159-4163
    • Kenney, J.M.1
  • 21
    • 33748441614 scopus 로고    scopus 로고
    • Calcitonin forms oligomeric pore-like structures in lipid membranes
    • Diociaiuti M., et al. Calcitonin forms oligomeric pore-like structures in lipid membranes. Biophys. J. 91 (2006) 2275-2281
    • (2006) Biophys. J. , vol.91 , pp. 2275-2281
    • Diociaiuti, M.1
  • 22
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • Si K., et al. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 115 (2003) 879-891
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1
  • 23
    • 33750480868 scopus 로고    scopus 로고
    • Characterization of the nanoscale properties of individual amyloid fibrils
    • Smith J.F., et al. Characterization of the nanoscale properties of individual amyloid fibrils. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 15806-15811
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15806-15811
    • Smith, J.F.1
  • 25
    • 23944519950 scopus 로고    scopus 로고
    • The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats
    • Cherny I., et al. The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats. J. Mol. Biol. 352 (2005) 245-252
    • (2005) J. Mol. Biol. , vol.352 , pp. 245-252
    • Cherny, I.1
  • 26
    • 0034665999 scopus 로고    scopus 로고
    • Structural and functional role of the disulfide bridges in the hydrophobin SC3
    • de Vocht M.L., et al. Structural and functional role of the disulfide bridges in the hydrophobin SC3. J. Biol. Chem. 275 (2000) 28428-28432
    • (2000) J. Biol. Chem. , vol.275 , pp. 28428-28432
    • de Vocht, M.L.1
  • 27
    • 15944405779 scopus 로고    scopus 로고
    • Amyloids - a functional coat for microorganisms
    • Gebbink M.F., et al. Amyloids - a functional coat for microorganisms. Nat. Rev. Microbiol. 3 (2005) 333-341
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 333-341
    • Gebbink, M.F.1
  • 28
    • 33644864861 scopus 로고    scopus 로고
    • Structural basis for rodlet assembly in fungal hydrophobins
    • Kwan A.H., et al. Structural basis for rodlet assembly in fungal hydrophobins. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 3621-3626
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 3621-3626
    • Kwan, A.H.1
  • 29
    • 33750994604 scopus 로고    scopus 로고
    • Amyloid fibril formation propensity is inherent into the hexapeptide tandemly repeating sequence of the central domain of silkmoth chorion proteins of the A-family
    • Iconomidou V.A., et al. Amyloid fibril formation propensity is inherent into the hexapeptide tandemly repeating sequence of the central domain of silkmoth chorion proteins of the A-family. J. Struct. Biol. 156 (2006) 480-488
    • (2006) J. Struct. Biol. , vol.156 , pp. 480-488
    • Iconomidou, V.A.1
  • 30
    • 0035005523 scopus 로고    scopus 로고
    • Survival of water stress in annual fish embryos: dehydration avoidance and egg envelope amyloid fibers
    • Podrabsky J.E., et al. Survival of water stress in annual fish embryos: dehydration avoidance and egg envelope amyloid fibers. Am. J. Physiol. Regul. Integr. Comp. Physiol. 280 (2001) R123-R131
    • (2001) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.280
    • Podrabsky, J.E.1
  • 32
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett J.T., and Lansbury Jr. P.T. Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 73 (1993) 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 33
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • True H.L., et al. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature 431 (2004) 184-187
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1
  • 34
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien P., et al. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73 (2004) 617-656
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1
  • 35
    • 20944436593 scopus 로고    scopus 로고
    • Filaments of the Ure2p prion protein have a cross-β core structure
    • Baxa U., et al. Filaments of the Ure2p prion protein have a cross-β core structure. J. Struct. Biol. 150 (2005) 170-179
    • (2005) J. Struct. Biol. , vol.150 , pp. 170-179
    • Baxa, U.1
  • 36
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: an epigenetic modifier of protein function in yeast
    • Sondheimer N., and Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell 5 (2000) 163-172
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 37
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter J., and Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat. Rev. Genet. 6 (2005) 435-450
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 38
    • 33645993282 scopus 로고    scopus 로고
    • The yeast prion protein Ure2: structure, function and folding
    • Lian H.Y., et al. The yeast prion protein Ure2: structure, function and folding. Biochim. Biophys. Acta 1764 (2006) 535-545
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 535-545
    • Lian, H.Y.1
  • 39
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor K.L., et al. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283 (1999) 1339-1343
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1
  • 40
    • 0037155213 scopus 로고    scopus 로고
    • The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils
    • Dos Reis S., et al. The HET-s prion protein of the filamentous fungus Podospora anserina aggregates in vitro into amyloid-like fibrils. J. Biol. Chem. 277 (2002) 5703-5706
    • (2002) J. Biol. Chem. , vol.277 , pp. 5703-5706
    • Dos Reis, S.1
  • 41
    • 0038219626 scopus 로고    scopus 로고
    • Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina
    • Balguerie A., et al. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J. 22 (2003) 2071-2081
    • (2003) EMBO J. , vol.22 , pp. 2071-2081
    • Balguerie, A.1
  • 42
    • 20444458341 scopus 로고    scopus 로고
    • Correlation of structural elements and infectivity of the HET-s prion
    • Ritter C., et al. Correlation of structural elements and infectivity of the HET-s prion. Nature 435 (2005) 844-848
    • (2005) Nature , vol.435 , pp. 844-848
    • Ritter, C.1
  • 43
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True H.L., and Lindquist S.L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407 (2000) 477-483
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 44
    • 24944584730 scopus 로고    scopus 로고
    • Non-mendelian inheritance of the HET-s prion or HET-s prion domains determines the het-S spore killing system in Podospora anserina
    • Dalstra H.J., et al. Non-mendelian inheritance of the HET-s prion or HET-s prion domains determines the het-S spore killing system in Podospora anserina. Fungal Genet. Biol. 42 (2005) 836-847
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 836-847
    • Dalstra, H.J.1
  • 45
    • 0034760879 scopus 로고    scopus 로고
    • Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae
    • Jensen M.A., et al. Molecular population genetics and evolution of a prion-like protein in Saccharomyces cerevisiae. Genetics 159 (2001) 527-535
    • (2001) Genetics , vol.159 , pp. 527-535
    • Jensen, M.A.1
  • 46
    • 0037783482 scopus 로고    scopus 로고
    • Sexual transmission of the [Het-S] prion leads to meiotic drive in Podospora anserina
    • Dalstra H.J., et al. Sexual transmission of the [Het-S] prion leads to meiotic drive in Podospora anserina. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6616-6621
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 6616-6621
    • Dalstra, H.J.1
  • 48
    • 0041968890 scopus 로고    scopus 로고
    • Conservation of the prion properties of Ure2p through evolution
    • Baudin-Baillieu A., et al. Conservation of the prion properties of Ure2p through evolution. Mol. Biol. Cell 14 (2003) 3449-3458
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3449-3458
    • Baudin-Baillieu, A.1
  • 49
    • 26444520003 scopus 로고    scopus 로고
    • The [URE3] prion is not conserved among Saccharomyces species
    • Talarek N., et al. The [URE3] prion is not conserved among Saccharomyces species. Genetics 171 (2005) 23-34
    • (2005) Genetics , vol.171 , pp. 23-34
    • Talarek, N.1
  • 50
    • 0032931038 scopus 로고    scopus 로고
    • Zinc-dependent activation of the plasma kinin-forming cascade by aggregated β amyloid protein
    • Shibayama Y., et al. Zinc-dependent activation of the plasma kinin-forming cascade by aggregated β amyloid protein. Clin. Immunol. 90 (1999) 89-99
    • (1999) Clin. Immunol. , vol.90 , pp. 89-99
    • Shibayama, Y.1
  • 51
    • 0031127083 scopus 로고    scopus 로고
    • Determination of secondary structure of normal fibrin from human peripheral blood
    • Bramanti E., et al. Determination of secondary structure of normal fibrin from human peripheral blood. Biopolymers 41 (1997) 545-553
    • (1997) Biopolymers , vol.41 , pp. 545-553
    • Bramanti, E.1
  • 52
    • 0037195269 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator is a multiligand cross-β structure receptor
    • Kranenburg O., et al. Tissue-type plasminogen activator is a multiligand cross-β structure receptor. Curr. Biol. 12 (2002) 1833-1839
    • (2002) Curr. Biol. , vol.12 , pp. 1833-1839
    • Kranenburg, O.1
  • 53
    • 0036138245 scopus 로고    scopus 로고
    • Variations in the csgD promoter of Escherichia coli O157:H7 associated with increased virulence in mice and increased invasion of HEp-2 cells
    • Uhlich G.A., et al. Variations in the csgD promoter of Escherichia coli O157:H7 associated with increased virulence in mice and increased invasion of HEp-2 cells. Infect. Immun. 70 (2002) 395-399
    • (2002) Infect. Immun. , vol.70 , pp. 395-399
    • Uhlich, G.A.1
  • 54
    • 25444456658 scopus 로고    scopus 로고
    • The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function
    • Theos A.C., et al. The Silver locus product Pmel17/gp100/Silv/ME20: controversial in name and in function. Pigment Cell Res. 18 (2005) 322-336
    • (2005) Pigment Cell Res. , vol.18 , pp. 322-336
    • Theos, A.C.1
  • 55
    • 0035200704 scopus 로고    scopus 로고
    • Pmel17 initiates premelanosome morphogenesis within multivesicular bodies
    • Berson J.F., et al. Pmel17 initiates premelanosome morphogenesis within multivesicular bodies. Mol. Biol. Cell 12 (2001) 3451-3464
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3451-3464
    • Berson, J.F.1
  • 56
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson J.F., et al. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol. 161 (2003) 521-533
    • (2003) J. Cell Biol. , vol.161 , pp. 521-533
    • Berson, J.F.1
  • 57
    • 0018251759 scopus 로고
    • 5,6-Dihydroxyindole is a melanin precursor showing potent cytotoxicity
    • Pawelek J.M., and Lerner A.B. 5,6-Dihydroxyindole is a melanin precursor showing potent cytotoxicity. Nature 276 (1978) 626-628
    • (1978) Nature , vol.276 , pp. 626-628
    • Pawelek, J.M.1    Lerner, A.B.2
  • 58
    • 19944361828 scopus 로고    scopus 로고
    • The Dominant white, Dun and Smoky color variants in chicken are associated with insertion/deletion polymorphisms in the Pmel17 gene
    • Kerje S., et al. The Dominant white, Dun and Smoky color variants in chicken are associated with insertion/deletion polymorphisms in the Pmel17 gene. Genetics 168 (2004) 1507-1518
    • (2004) Genetics , vol.168 , pp. 1507-1518
    • Kerje, S.1
  • 59
    • 0026494153 scopus 로고
    • Fowl model for vitiligo: genetic regulation on the fate of the melanocytes
    • Bowers R.R., et al. Fowl model for vitiligo: genetic regulation on the fate of the melanocytes. Pigment Cell Res. Suppl. 2 (1992) 242-248
    • (1992) Pigment Cell Res. , Issue.SUPPL. 2 , pp. 242-248
    • Bowers, R.R.1
  • 60
    • 0028702503 scopus 로고
    • Premature avian melanocyte death due to low antioxidant levels of protection: fowl model for vitiligo
    • Bowers R.R., et al. Premature avian melanocyte death due to low antioxidant levels of protection: fowl model for vitiligo. Pigment Cell Res. 7 (1994) 409-418
    • (1994) Pigment Cell Res. , vol.7 , pp. 409-418
    • Bowers, R.R.1
  • 61
    • 17844367336 scopus 로고    scopus 로고
    • Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism
    • Lundmark K., et al. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: cross-seeding as a disease mechanism. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6098-6102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6098-6102
    • Lundmark, K.1
  • 62
    • 33746405081 scopus 로고    scopus 로고
    • Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
    • Shorter J., and Lindquist S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol. Cell 23 (2006) 425-438
    • (2006) Mol. Cell , vol.23 , pp. 425-438
    • Shorter, J.1    Lindquist, S.2
  • 63
    • 17444417025 scopus 로고    scopus 로고
    • Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion
    • Allen K.D., et al. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion. Genetics 169 (2005) 1227-1242
    • (2005) Genetics , vol.169 , pp. 1227-1242
    • Allen, K.D.1
  • 64
    • 0035873740 scopus 로고    scopus 로고
    • +] prion
    • +] prion. EMBO J. 20 (2001) 2435-2442
    • (2001) EMBO J. , vol.20 , pp. 2435-2442
    • Sondheimer, N.1
  • 65
    • 20744441099 scopus 로고    scopus 로고
    • Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model
    • Gokhale K.C., et al. Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J. Biol. Chem. 280 (2005) 22809-22818
    • (2005) J. Biol. Chem. , vol.280 , pp. 22809-22818
    • Gokhale, K.C.1
  • 66
    • 17144379660 scopus 로고    scopus 로고
    • MART-1 is required for the function of the melanosomal matrix protein Pmel17/GP100 and the maturation of melanosomes
    • Hoashi T., et al. MART-1 is required for the function of the melanosomal matrix protein Pmel17/GP100 and the maturation of melanosomes. J. Biol. Chem. 280 (2005) 14006-14016
    • (2005) J. Biol. Chem. , vol.280 , pp. 14006-14016
    • Hoashi, T.1
  • 67
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio T.R., et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289 (2000) 1317-1321
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1
  • 68
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-β (1-42) fibrils
    • Luhrs T., et al. 3D structure of Alzheimer's amyloid-β (1-42) fibrils. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17342-17347
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17342-17347
    • Luhrs, T.1
  • 69
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova A.T., et al. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 16742-16747
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16742-16747
    • Petkova, A.T.1
  • 70
    • 33845334180 scopus 로고    scopus 로고
    • 3D structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR
    • Iwata K., et al. 3D structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 18119-18124
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18119-18124
    • Iwata, K.1
  • 71
    • 33750826280 scopus 로고    scopus 로고
    • General structural motifs of amyloid protofilaments
    • Ferguson N., et al. General structural motifs of amyloid protofilaments. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 16248-16253
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16248-16253
    • Ferguson, N.1
  • 72
    • 33845938549 scopus 로고    scopus 로고
    • Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure
    • Shewmaker F., et al. Amyloid of the prion domain of Sup35p has an in-register parallel β-sheet structure. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 19754-19759
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 19754-19759
    • Shewmaker, F.1
  • 73
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • Nelson R., et al. Structure of the cross-β spine of amyloid-like fibrils. Nature 435 (2005) 773-778
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1
  • 74
    • 13144259646 scopus 로고    scopus 로고
    • Amyloid fibril formation by an SH3 domain
    • Guijarro J.I., et al. Amyloid fibril formation by an SH3 domain. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 4224-4228
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4224-4228
    • Guijarro, J.I.1
  • 75
    • 33749864323 scopus 로고    scopus 로고
    • Sequence and structural determinants of amyloid fibril formation
    • Bemporad F., et al. Sequence and structural determinants of amyloid fibril formation. Acc. Chem. Res. 39 (2006) 620-627
    • (2006) Acc. Chem. Res. , vol.39 , pp. 620-627
    • Bemporad, F.1
  • 76
    • 24144438172 scopus 로고    scopus 로고
    • Structure and morphology of the Alzheimer's amyloid fibril
    • Stromer T., and Serpell L.C. Structure and morphology of the Alzheimer's amyloid fibril. Microsc. Res. Tech. 67 (2005) 210-217
    • (2005) Microsc. Res. Tech. , vol.67 , pp. 210-217
    • Stromer, T.1    Serpell, L.C.2
  • 77
    • 0036219181 scopus 로고    scopus 로고
    • The dark side of lysosome-related organelles: specialization of the endocytic pathway for melanosome biogenesis
    • Raposo G., and Marks M.S. The dark side of lysosome-related organelles: specialization of the endocytic pathway for melanosome biogenesis. Traffic 3 (2002) 237-248
    • (2002) Traffic , vol.3 , pp. 237-248
    • Raposo, G.1    Marks, M.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.