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Volumn 21, Issue 6-7, 2005, Pages 627-633

Amyloidosis: A model of misfolded protein disorder;Les amyloses, un modèle de maladie du repliement des protéines

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; GLYCOSAMINOGLYCAN; PROTEOGLYCAN; SERUM AMYLOID P;

EID: 22144475152     PISSN: 07670974     EISSN: None     Source Type: Journal    
DOI: 10.1051/medsci/2005216-7627     Document Type: Review
Times cited : (13)

References (35)
  • 3
    • 0002539419 scopus 로고    scopus 로고
    • Amyloses
    • Kahn MF, Peltier O, Meyer O, Piette JC, eds. Paris: Flammarion Médecine-Sciences
    • Grateau G. Amyloses. In: Kahn MF, Peltier O, Meyer O, Piette JC, eds. Les maladies systémiques. Paris: Flammarion Médecine-Sciences, 2000: 1279-308.
    • (2000) Les Maladies Systémiques , pp. 1279-1308
    • Grateau, G.1
  • 4
    • 0031960745 scopus 로고    scopus 로고
    • A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils
    • Carter DB, Chou KC. A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils. Neurobiol Aging 1998; 19: 37-40.
    • (1998) Neurobiol Aging , vol.19 , pp. 37-40
    • Carter, D.B.1    Chou, K.C.2
  • 5
    • 0037313614 scopus 로고    scopus 로고
    • Micropurification techniques in the analysis of amyloid proteins
    • Kaplan B, Shtrasburg S, Pras M. Micropurification techniques in the analysis of amyloid proteins. J Clin Pathol 2003; 56: 86-90.
    • (2003) J Clin Pathol , vol.56 , pp. 86-90
    • Kaplan, B.1    Shtrasburg, S.2    Pras, M.3
  • 6
    • 0023013825 scopus 로고
    • Circulating serum amyloid P component is the precursor of amyloid P component in tissue amyloid deposits
    • Baltz ML, Caspi D, Evans DJ, et al. Circulating serum amyloid P component is the precursor of amyloid P component in tissue amyloid deposits. Clin Exp Immunol 1986; 66: 691-700.
    • (1986) Clin Exp Immunol , vol.66 , pp. 691-700
    • Baltz, M.L.1    Caspi, D.2    Evans, D.J.3
  • 7
    • 0036860278 scopus 로고    scopus 로고
    • Serum amyloid P component scintigraphy for diagnosis and monitoring amyloidosis
    • Hawkins PN. Serum amyloid P component scintigraphy for diagnosis and monitoring amyloidosis. Curr Opin Nephrol Hypertens 2002; 11: 649-55.
    • (2002) Curr Opin Nephrol Hypertens , vol.11 , pp. 649-655
    • Hawkins, P.N.1
  • 9
    • 0033580657 scopus 로고    scopus 로고
    • Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
    • Canet D, Sunde M, Last AM, et al. Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants. Biochemistry 1999; 38 : 6419-27.
    • (1999) Biochemistry , vol.38 , pp. 6419-6427
    • Canet, D.1    Sunde, M.2    Last, A.M.3
  • 10
    • 0034799733 scopus 로고    scopus 로고
    • Transthyretin: A review from a structural perspective
    • Hamilton JA, Benson MD. Transthyretin: A review from a structural perspective. Cell Mol Life Sci 2001; 58 : 1-31.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1-31
    • Hamilton, J.A.1    Benson, M.D.2
  • 11
    • 0016369152 scopus 로고
    • Kinetics and mechanism of deoxyhemoglobin S gelation: A new approach to understanding sickle cell disease
    • Hofrichter J, Ross PD, Eaton WA. Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease. Proc Natl Acad Sci USA 1974; 71: 4864-8.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4864-4868
    • Hofrichter, J.1    Ross, P.D.2    Eaton, W.A.3
  • 12
    • 2342444028 scopus 로고    scopus 로고
    • Seeding specificity in amyloid growth induced by heterologous fibrils
    • O'Nuallain B, Williams AD, Westermark P, Wetzel R. Seeding specificity in amyloid growth induced by heterologous fibrils. J Biol Chem 2004; 279: 17490-9.
    • (2004) J Biol Chem , vol.279 , pp. 17490-17499
    • O'Nuallain, B.1    Williams, A.D.2    Westermark, P.3    Wetzel, R.4
  • 13
    • 2942593931 scopus 로고    scopus 로고
    • Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
    • Hurshman AR, White JT, Powers ET, Kelly JW. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 2004; 43: 7365-81.
    • (2004) Biochemistry , vol.43 , pp. 7365-7381
    • Hurshman, A.R.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 14
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 2002; 27: 527-33.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 15
    • 1642488929 scopus 로고    scopus 로고
    • Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils
    • Niraula TN, Konno T, Li H, et al. Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils. Proc NatlAcad SciUSA 2004; 101: 4089-93.
    • (2004) Proc NatlAcad SciUSA , vol.101 , pp. 4089-4093
    • Niraula, T.N.1    Konno, T.2    Li, H.3
  • 16
    • 11144355853 scopus 로고    scopus 로고
    • Tissue distribution, biochemical properties, and transmission of mouse Type a AApoAII amyloid fibrils
    • Korenaga T, Fu X, Xing Y, et al. Tissue distribution, biochemical properties, and transmission of mouse Type A AApoAII amyloid fibrils. Am J Pathol 2004; 164: 1597-606.
    • (2004) Am J Pathol , vol.164 , pp. 1597-1606
    • Korenaga, T.1    Fu, X.2    Xing, Y.3
  • 17
    • 0037076355 scopus 로고    scopus 로고
    • Transmissibility of systemic amyloidosis by a prion-like mechanism
    • Lundmark K, Westermark GT, Nystrom S, et al. Transmissibility of systemic amyloidosis by a prion-like mechanism. Proc Natl Acad Sci USA 2002; 99: 6979-84.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6979-6984
    • Lundmark, K.1    Westermark, G.T.2    Nystrom, S.3
  • 18
    • 0036150827 scopus 로고    scopus 로고
    • Alzheimer's disease: Do tauists and baptists finally shake hands?
    • Mudher A, Lovestone S. Alzheimer's disease: do tauists and baptists finally shake hands? Trends Neurosci 2002; 25: 22-6.
    • (2002) Trends Neurosci , vol.25 , pp. 22-26
    • Mudher, A.1    Lovestone, S.2
  • 19
    • 3242737470 scopus 로고    scopus 로고
    • Challenging the amyloid cascade hypothesis: Senile plaques and amyloid-beta as protective adaptations to Alzheimer disease
    • Lee HG, Casadesus G, Zhu X, et al. Challenging the amyloid cascade hypothesis: senile plaques and amyloid-beta as protective adaptations to Alzheimer disease. Ann NY Acad Sci 2004; 1019: 1-4.
    • (2004) Ann NY Acad Sci , vol.1019 , pp. 1-4
    • Lee, H.G.1    Casadesus, G.2    Zhu, X.3
  • 20
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300: 486-9.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 21
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R, Sokolov Y, Edmonds B, et al. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 2004; 279: 46363-6.
    • (2004) J Biol Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3
  • 22
    • 2342525940 scopus 로고    scopus 로고
    • Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress
    • Brenner DA, Jain M, Pimentel DR, et al. Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress. Circ Res 2004; 94: 1008-10.
    • (2004) Circ Res , vol.94 , pp. 1008-1010
    • Brenner, D.A.1    Jain, M.2    Pimentel, D.R.3
  • 23
    • 9144269708 scopus 로고    scopus 로고
    • High-dose melphalan and autologous stem-cell transplantation in patients with AL amyloidosis: An 8-year study
    • Skinner M, Sanchorawala V, Seldin DC, et al. High-dose melphalan and autologous stem-cell transplantation in patients with AL amyloidosis: an 8-year study. Ann Intern Med 2004; 140: 85-93.
    • (2004) Ann Intern Med , vol.140 , pp. 85-93
    • Skinner, M.1    Sanchorawala, V.2    Seldin, D.C.3
  • 24
    • 6944240027 scopus 로고    scopus 로고
    • Liver transplantation in transthyretin-related familial amyloid polyneuropathy
    • Stangou AJ, Hawkins PN. Liver transplantation in transthyretin-related familial amyloid polyneuropathy. Curr Opin Neurol 2004; 17: 615-20.
    • (2004) Curr Opin Neurol , vol.17 , pp. 615-620
    • Stangou, A.J.1    Hawkins, P.N.2
  • 25
    • 0346333094 scopus 로고    scopus 로고
    • Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis
    • Adamski-Werner SL, Palaninathan SK, Sacchettini JC, Kelly JW. Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis. J Med Chem 2004; 47: 355-74.
    • (2004) J Med Chem , vol.47 , pp. 355-374
    • Adamski-Werner, S.L.1    Palaninathan, S.K.2    Sacchettini, J.C.3    Kelly, J.W.4
  • 26
    • 0036130774 scopus 로고    scopus 로고
    • A multicenter phase II trial of 4′-iodo-4′deoxydoxorubicin (IDOX) in primary amyloidosis (AL)
    • Gertz MA, Lacy MQ, Dispenzieri A, et al. A multicenter phase II trial of 4′-iodo-4′deoxydoxorubicin (IDOX) in primary amyloidosis (AL). Amyloid 2002; 9: 24-30.
    • (2002) Amyloid , vol.9 , pp. 24-30
    • Gertz, M.A.1    Lacy, M.Q.2    Dispenzieri, A.3
  • 27
    • 0038375018 scopus 로고    scopus 로고
    • 4′-Iodo-4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: Screening for TTR fibril disrupters
    • Cardoso I, Merlini G, Saraiva MJ. 4′-iodo-4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters. FASEB J 2003; 17: 803-9.
    • (2003) FASEB J , vol.17 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 28
    • 0034650634 scopus 로고    scopus 로고
    • Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides
    • Soto C, Kascsak RJ, Saborio GP, et al. Reversion of prion protein conformational changes by synthetic beta-sheet breaker peptides. Lancet 2000; 355: 192-7.
    • (2000) Lancet , vol.355 , pp. 192-197
    • Soto, C.1    Kascsak, R.J.2    Saborio, G.P.3
  • 29
    • 7444221875 scopus 로고    scopus 로고
    • Harnessing chaperones to generate small-molecule inhibitors of amyloid beta aggregation
    • Gestwicki JE, Crabtree GR, Graef IA. Harnessing chaperones to generate small-molecule inhibitors of amyloid beta aggregation. Science 2004; 306: 865-9.
    • (2004) Science , vol.306 , pp. 865-869
    • Gestwicki, J.E.1    Crabtree, G.R.2    Graef, I.A.3
  • 30
    • 0028913416 scopus 로고
    • Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease
    • Kisilevsky R, Lemieux LJ, Fraser PE, et al. Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nat Med 1995; 1: 143-8.
    • (1995) Nat Med , vol.1 , pp. 143-148
    • Kisilevsky, R.1    Lemieux, L.J.2    Fraser, P.E.3
  • 31
    • 2442675503 scopus 로고    scopus 로고
    • Inhibition of amyloid a amyloidogenesis in vivo and in tissue culture by 4-deoxy analogues of peracetylated 2-acetamido-2-deoxy-alpha- and beta-d-glucose: Implications for the treatment of various amyloidoses
    • Kisilevsky R, Szarek WA, Ancsin JB, et al. Inhibition of amyloid A amyloidogenesis in vivo and in tissue culture by 4-deoxy analogues of peracetylated 2-acetamido-2-deoxy-alpha- and beta-d-glucose: implications for the treatment of various amyloidoses. Am J Pathol 2004; 164: 2127-37.
    • (2004) Am J Pathol , vol.164 , pp. 2127-2137
    • Kisilevsky, R.1    Szarek, W.A.2    Ancsin, J.B.3
  • 32
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • Pepys MB, Herbert J, Hutchinson WL. Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 2002; 417: 254-9.
    • (2002) Nature , vol.417 , pp. 254-259
    • Pepys, M.B.1    Herbert, J.2    Hutchinson, W.L.3
  • 33
    • 8844257296 scopus 로고    scopus 로고
    • Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
    • Dumoulin M, Dobson CM. Probing the origins, diagnosis and treatment of amyloid diseases using antibodies. Biochimie 2004; 86: 589-600.
    • (2004) Biochimie , vol.86 , pp. 589-600
    • Dumoulin, M.1    Dobson, C.M.2
  • 34
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B, Wetzel R. Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci USA 2002; 99: 1485-90.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 35
    • 0033810109 scopus 로고    scopus 로고
    • Antibody-mediated resolution of light chain-associated amyloid deposits
    • Hrncic R, Wall J, Wolfenbarger DA, et al. Antibody-mediated resolution of light chain-associated amyloid deposits. Am J Pathol 2000; 157: 1239-46.
    • (2000) Am J Pathol , vol.157 , pp. 1239-1246
    • Hrncic, R.1    Wall, J.2    Wolfenbarger, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.