메뉴 건너뛰기




Volumn , Issue , 2009, Pages 171-180

Are amyloids infectious?

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84900231735     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-87995-6_14     Document Type: Chapter
Times cited : (2)

References (56)
  • 1
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • Soto C (2001) Protein misfolding and disease; protein refolding and therapy. FEBS Lett 498: 204-207
    • (2001) FEBS Lett , vol.498 , pp. 204-207
    • Soto, C.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F and Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 27744542188 scopus 로고    scopus 로고
    • Cell toxicity and conformational disease
    • Carrell RW (2005) Cell toxicity and conformational disease. Trends Cell Biol 15: 574-580
    • (2005) Trends Cell Biol , vol.15 , pp. 574-580
    • Carrell, R.W.1
  • 4
    • 33644816759 scopus 로고    scopus 로고
    • Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
    • Soto C, Estrada L, Castilla J (2006) Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem Sci 31: 150-155
    • (2006) Trends Biochem Sci , vol.31 , pp. 150-155
    • Soto, C.1    Estrada, L.2    Castilla, J.3
  • 6
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nature Rev Neurosci 4: 49-60
    • (2003) Nature Rev Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 7
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts)
    • Glenner GG (1980) Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts). N Engl J Med 302: 1283-1292
    • (1980) N Engl J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 9
    • 0032491408 scopus 로고    scopus 로고
    • Genetic classification of primary neurodegenerative disease
    • Hardy J, Gwinn-Hardy K (1998) Genetic classification of primary neurodegenerative disease. Science 282: 1075-1079
    • (1998) Science , vol.282 , pp. 1075-1079
    • Hardy, J.1    Gwinn-Hardy, K.2
  • 10
    • 35348932113 scopus 로고    scopus 로고
    • Transgenic animal models of neurodegenerative diseases and their application to treatment development
    • Rockenstein E, Crews L, Masliah E (2007) Transgenic animal models of neurodegenerative diseases and their application to treatment development. Adv Drug Deliv Rev 59: 1093-1102
    • (2007) Adv Drug Deliv Rev , vol.59 , pp. 1093-1102
    • Rockenstein, E.1    Crews, L.2    Masliah, E.3
  • 11
    • 1542377619 scopus 로고    scopus 로고
    • Toxicity of amyloid beta peptide: Tales of calcium, mitochondria, and oxidative stress
    • Canevari L, Abramov AY, Duchen MR (2004) Toxicity of amyloid beta peptide: Tales of calcium, mitochondria, and oxidative stress. Neurochem Res 29: 637-650
    • (2004) Neurochem Res , vol.29 , pp. 637-650
    • Canevari, L.1    Abramov, A.Y.2    Duchen, M.R.3
  • 12
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8: 101-112
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 13
    • 33344463679 scopus 로고    scopus 로고
    • Common mechanisms of amyloid oligomer pathogenesis in degenerative disease
    • Glabe CG (2006) Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol Aging 27: 570-557
    • (2006) Neurobiol Aging , vol.27 , pp. 570-557
    • Glabe, C.G.1
  • 14
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26: 267-298
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 15
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge J (2001) Prion diseases of humans and animals: Their causes and molecular basis. Annu Rev Neurosci 24: 519-550
    • (2001) Annu Rev Neurosci , vol.24 , pp. 519-550
    • Collinge, J.1
  • 17
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: One century of evolving concepts
    • Aguzzi A, Polymenidou M (2004) Mammalian prion biology: One century of evolving concepts. Cell 116: 313-327
    • (2004) Cell , vol.116 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 18
    • 3142547067 scopus 로고    scopus 로고
    • The controversial protein-only hypothesis of prion propagation
    • Soto C, Castilla J (2004) The controversial protein-only hypothesis of prion propagation. Nat Med 10: S63-S67
    • (2004) Nat Med , vol.10
    • Soto, C.1    Castilla, J.2
  • 20
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 21
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • Bueler H, Aguzzi A, Sailer A,. et al. (1993) Mice devoid of PrP are resistant to scrapie. Cell 73: 1339-1347
    • (1993) Cell , vol.73 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3
  • 22
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer M, Rülicke T, Raeber A,. et al. (1996) Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 15: 1255-1264
    • (1996) EMBO J , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rülicke, T.2    Raeber, A.3
  • 23
    • 50049085479 scopus 로고    scopus 로고
    • Rodent models for prion diseases
    • Groschup MH, Buschmann A (2008) Rodent models for prion diseases. Vet Res 39: 32.
    • (2008) Vet Res , vol.39 , pp. 32
    • Groschup, M.H.1    Buschmann, A.2
  • 24
    • 0141849856 scopus 로고    scopus 로고
    • Prion protein conversions: Insight into mechanisms, TSE transmission barriers and strains
    • Caughey B (2003) Prion protein conversions: Insight into mechanisms, TSE transmission barriers and strains. Br Med Bull 66: 109-120
    • (2003) Br Med Bull , vol.66 , pp. 109-120
    • Caughey, B.1
  • 25
    • 0036680112 scopus 로고    scopus 로고
    • Cyclic amplification of protein misfolding: Application to prion-related disorders and beyond
    • Soto C, Saborio GP, Anderes L (2002) Cyclic amplification of protein misfolding: Application to prion-related disorders and beyond. Trends Neurosci 25: 390-394
    • (2002) Trends Neurosci , vol.25 , pp. 390-394
    • Soto, C.1    Saborio, G.P.2    Anderes, L.3
  • 27
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio GP, Permanne B, Soto C (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411: 810-813
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 28
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saá P, Hetz C, Soto C (2005) In vitro generation of infectious scrapie prions. Cell 121: 195-206
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saá, P.2    Hetz, C.3    Soto, C.4
  • 29
    • 0027195933 scopus 로고
    • Seeding one-dimensional crystallization of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr (1993) Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73: 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 30
    • 0036386817 scopus 로고    scopus 로고
    • Modeling Alzheimer's disease and other proteopathies in vivo: Is seeding the key?
    • Walker LC, Bian F, Callahan MJ,. et al. (2002) Modeling Alzheimer's disease and other proteopathies in vivo: Is seeding the key? Amino Acids 23: 87-93
    • (2002) Amino Acids , vol.23 , pp. 87-93
    • Walker, L.C.1    Bian, F.2    Callahan, M.J.3
  • 31
    • 0028227756 scopus 로고
    • Nucleation of amyloidogenesis in infectious and noninfectious amyloidoses of brain
    • Gajdusek DC (1994) Nucleation of amyloidogenesis in infectious and noninfectious amyloidoses of brain. Ann NY Acad Sci 724: 173-190
    • (1994) Ann NY Acad Sci , vol.724 , pp. 173-190
    • Gajdusek, D.C.1
  • 32
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, Lansbury PT Jr (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66: 385-407
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 34
    • 0014021742 scopus 로고
    • Experimental transmission of a Kuru-like syndrome to chimpanzees
    • Gajdusek DC, Gibbs CJ, Alpers M (1966) Experimental transmission of a Kuru-like syndrome to chimpanzees. Nature 209: 794-796
    • (1966) Nature , vol.209 , pp. 794-796
    • Gajdusek, D.C.1    Gibbs, C.J.2    Alpers, M.3
  • 36
    • 0028376473 scopus 로고
    • Induction of beta (A4)-Amyloid in primates by injection of Alzheimer's disease brain homogenate. Comparison with transmission of spongiform encephalopathy
    • Baker HF, Ridley RM, Duchen LW, Crow TJ, Bruton CJ (1994) Induction of beta (A4)-Amyloid in primates by injection of Alzheimer's disease brain homogenate. Comparison with transmission of spongiform encephalopathy. Mol Neurobiol 8: 25-39
    • (1994) Mol Neurobiol , vol.8 , pp. 25-39
    • Baker, H.F.1    Ridley, R.M.2    Duchen, L.W.3    Crow, T.J.4    Bruton, C.J.5
  • 37
    • 0018819210 scopus 로고
    • Evidence for and against the transmissibility of Alzheimer disease
    • Goudsmit J, Morrow CH, Asher DM,. et al. (1980) Evidence for and against the transmissibility of Alzheimer disease. Neurology 30: 945-950
    • (1980) Neurology , vol.30 , pp. 945-950
    • Goudsmit, J.1    Morrow, C.H.2    Asher, D.M.3
  • 38
    • 34249993165 scopus 로고    scopus 로고
    • The prion strain phenomenon: Molecular basis and unprecedented features
    • Morales R, Abid K, Soto C (2007) The prion strain phenomenon: Molecular basis and unprecedented features. Biochim Biophys Acta 1772: 681-691
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 681-691
    • Morales, R.1    Abid, K.2    Soto, C.3
  • 39
    • 0035223911 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease: Phenotype and mechanisms of pathogenesis
    • Duff K (2001) Transgenic mouse models of Alzheimer's disease: Phenotype and mechanisms of pathogenesis. Biochem Soc Symp 67: 195-202.
    • (2001) Biochem Soc Symp , vol.67 , pp. 195-202
    • Duff, K.1
  • 40
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of beta-Amyloid by intracerebral infusion of Alzheimer brain extracts in beta-Amyloid precursor proteintransgenic mice
    • Kane MD, Lipinski WJ, Callahan MJ,. et al. (2000) Evidence for seeding of beta-Amyloid by intracerebral infusion of Alzheimer brain extracts in beta-Amyloid precursor proteintransgenic mice. J Neurosci 20: 3606-3611
    • (2000) J Neurosci , vol.20 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3
  • 41
    • 0035997227 scopus 로고    scopus 로고
    • Exogenous induction of cerebral betaamyloidosis in betaAPP-Transgenic mice
    • Walker LC, Callahan MJ, Bian F,. et al. (2002) Exogenous induction of cerebral betaamyloidosis in betaAPP-Transgenic mice. Peptides 23: 1241-1247
    • (2002) Peptides , vol.23 , pp. 1241-1247
    • Walker, L.C.1    Callahan, M.J.2    Bian, F.3
  • 42
    • 33749020837 scopus 로고    scopus 로고
    • Exogenous induction of cerebral beta-Amyloidogenesis is governed by agent and host
    • Meyer-Luehmann M, Coomaraswamy J, Bolmont T,. et al. (2006) Exogenous induction of cerebral beta-Amyloidogenesis is governed by agent and host. Science 313: 1781-1784
    • (2006) Science , vol.313 , pp. 1781-1784
    • Meyer-Luehmann, M.1    Coomaraswamy, J.2    Bolmont, T.3
  • 43
    • 0034028197 scopus 로고    scopus 로고
    • Serum amyloid A: From fibril to function
    • Sipe JD (2000) Serum amyloid A: From fibril to function. Current status. Amyloid 7: 10-12
    • (2000) Current status. Amyloid , vol.7 , pp. 10-12
    • Sipe, J.D.1
  • 44
    • 0346786219 scopus 로고    scopus 로고
    • The systemic amyloidoses
    • Buxbaum JN (2004) The systemic amyloidoses. Curr Opin Rheumatol 16: 67-75
    • (2004) Curr Opin Rheumatol , vol.16 , pp. 67-75
    • Buxbaum, J.N.1
  • 45
    • 0016706386 scopus 로고
    • Isolation and characterization of amyloid-related serum protein SAA as a low molecular weight protein
    • Anders RF, Natvig JB, Michaelsen TE, Husby G (1975) Isolation and characterization of amyloid-related serum protein SAA as a low molecular weight protein. Scand J Immunol 4: 397-401
    • (1975) Scand J Immunol , vol.4 , pp. 397-401
    • Anders, R.F.1    Natvig, J.B.2    Michaelsen, T.E.3    Husby, G.4
  • 46
    • 0019969508 scopus 로고
    • Serum amyloid-A protein concentration in inflammatory diseases and its relationship to the incidence of reactive systemic amyloidosis
    • De Beer FC, Mallya RK, Fagan EA, Lanham JG, Hughes GR, Pepys MB (1982) Serum amyloid-A protein concentration in inflammatory diseases and its relationship to the incidence of reactive systemic amyloidosis. Lancet 2: 231-234
    • (1982) Lancet , vol.2 , pp. 231-234
    • De Beer, F.C.1    Mallya, R.K.2    Fagan, E.A.3    Lanham, J.G.4    Hughes, G.R.5    Pepys, M.B.6
  • 47
    • 0021876805 scopus 로고
    • Human serum amyloid A (SAA): Biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA
    • Sipe JD, Colten HR, Goldberger G,. et al. (1985) Human serum amyloid A (SAA): Biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA. Biochemistry 24: 2931-2936
    • (1985) Biochemistry , vol.24 , pp. 2931-2936
    • Sipe, J.D.1    Colten, H.R.2    Goldberger, G.3
  • 48
    • 0020549270 scopus 로고
    • Kinetics of amyloid deposition I The effects of amyloidenhancing factor and splenectomy
    • Kisilevsky R, Boudreau L (1983) Kinetics of amyloid deposition. I. The effects of amyloidenhancing factor and splenectomy. Lab Invest 48: 53-59
    • (1983) Lab Invest , vol.48 , pp. 53-59
    • Kisilevsky, R.1    Boudreau, L.2
  • 49
    • 0028286663 scopus 로고
    • Fibrils from synthetic amyloid-related peptides enhance development of experimental AA-Amyloidosis in mice
    • Ganowiak K, Hultman P, Engstrom U, Gustavsson A, Westermark P (1994) Fibrils from synthetic amyloid-related peptides enhance development of experimental AA-Amyloidosis in mice. Biochem Biophys Res Commun 199: 306-312
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 306-312
    • Ganowiak, K.1    Hultman, P.2    Engstrom, U.3    Gustavsson, A.4    Westermark, P.5
  • 51
    • 0028836331 scopus 로고
    • Apolipoprotein A-II gene and development of amyloidosis and senescence in a congenic strain of mice carrying amyloidogenic ApoA-II
    • Higuchi K, Naiki H, Kitagawa K,. et al. (1995) Apolipoprotein A-II gene and development of amyloidosis and senescence in a congenic strain of mice carrying amyloidogenic ApoA-II. Lab Invest 72: 75-82
    • (1995) Lab Invest , vol.72 , pp. 75-82
    • Higuchi, K.1    Naiki, H.2    Kitagawa, K.3
  • 52
    • 0025809780 scopus 로고
    • Mouse senile amyloidosis. ASSAM amyloidosis in mice presents universally as a systemic age-Associated amyloidosis
    • Higuchi K, Naiki H, Kitagawa K, Hosokawa M, Takeda T (1991) Mouse senile amyloidosis. ASSAM amyloidosis in mice presents universally as a systemic age-Associated amyloidosis. Virchows Arch B Cell Pathol Incl Mol Pathol 60: 231-238
    • (1991) Virchows Arch B Cell Pathol Incl Mol Pathol , vol.60 , pp. 231-238
    • Higuchi, K.1    Naiki, H.2    Kitagawa, K.3    Hosokawa, M.4    Takeda, T.5
  • 53
    • 0036860193 scopus 로고    scopus 로고
    • Amyloid fibril proteins
    • Xing Y, Higuchi K (2002) Amyloid fibril proteins. Mech Ageing Dev 123: 1625-1636
    • (2002) Mech Ageing Dev , vol.123 , pp. 1625-1636
    • Xing, Y.1    Higuchi, K.2
  • 54
    • 0032422306 scopus 로고    scopus 로고
    • Fibrilization in mouse senile amyloidosis is fibril conformation- dependent
    • Higuchi K, Kogishi K, Wang J,. et al. (1998) Fibrilization in mouse senile amyloidosis is fibril conformation-dependent. Lab Invest 78: 1535-1542
    • (1998) Lab Invest , vol.78 , pp. 1535-1542
    • Higuchi, K.1    Kogishi, K.2    Wang, J.3
  • 55
    • 0035048758 scopus 로고    scopus 로고
    • Transmission of mouse senile amyloidosis
    • Xing Y, Nakamura A, Chiba T,. et al. (2001) Transmission of mouse senile amyloidosis. Lab Invest 81: 493-499
    • (2001) Lab Invest , vol.81 , pp. 493-499
    • Xing, Y.1    Nakamura, A.2    Chiba, T.3
  • 56
    • 0037031915 scopus 로고    scopus 로고
    • Induction of protein conformational change in mouse senile amyloidosis
    • Xing Y, Nakamura A, Korenaga T,. et al. (2002) Induction of protein conformational change in mouse senile amyloidosis. J Biol Chem 277: 33164-33169
    • (2002) J Biol Chem , vol.277 , pp. 33164-33169
    • Xing, Y.1    Nakamura, A.2    Korenaga, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.