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Volumn 8, Issue 2, 1996, Pages 75-83

Anti-amyloid drugs: Potential in the treatment of diseases associated with aging

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID PRECURSOR PROTEIN; COLCHICINE; DIMETHYL SULFOXIDE; DOXORUBICIN DERIVATIVE; ETHIONINE; HEPARAN SULFATE; SULFATE; SULFONIC ACID; UNCLASSIFIED DRUG;

EID: 0030046401     PISSN: 1170229X     EISSN: None     Source Type: Journal    
DOI: 10.2165/00002512-199608020-00001     Document Type: Review
Times cited : (36)

References (70)
  • 1
    • 0027458857 scopus 로고
    • Nomenclature of amyloid and amyloidosis - WHO-IUIS Nomenclature SubCommittee
    • Kazatchkine MD, Husby G, Araki S, et al. Nomenclature of amyloid and amyloidosis - WHO-IUIS Nomenclature SubCommittee. Bull World Health Organ 1993; 71: 105-8
    • (1993) Bull World Health Organ , vol.71 , pp. 105-108
    • Kazatchkine, M.D.1    Husby, G.2    Araki, S.3
  • 2
    • 0026647903 scopus 로고
    • Serum amyloid A changes high density lipoprotein's cellular affinity: A clue to serum amyloid A's principal function
    • Kisilevsky R, Subrahmanyan L. Serum amyloid A changes high density lipoprotein's cellular affinity: a clue to serum amyloid A's principal function. Lab Invest 1992; 66: 778-85
    • (1992) Lab Invest , vol.66 , pp. 778-785
    • Kisilevsky, R.1    Subrahmanyan, L.2
  • 3
    • 0029049806 scopus 로고
    • Serum amyloid A(SAA): Influence on HDL-mediated cellular cholesterol efflux
    • Banka CL, Yuan T, De Beer MC, et al. Serum amyloid A(SAA): influence on HDL-mediated cellular cholesterol efflux. J Lipid Res 1995; 36: 1058-65
    • (1995) J Lipid Res , vol.36 , pp. 1058-1065
    • Banka, C.L.1    Yuan, T.2    De Beer, M.C.3
  • 4
    • 0025341743 scopus 로고
    • Microangiopathy, the vascular basement membrane and Alzheimers Disease - A review
    • Perlmutter LS, Chui HC. Microangiopathy, the vascular basement membrane and Alzheimers Disease - a review. Brain Res Bull 1990; 24: 677-86
    • (1990) Brain Res Bull , vol.24 , pp. 677-686
    • Perlmutter, L.S.1    Chui, H.C.2
  • 5
    • 0025038826 scopus 로고
    • Antibodies to fibronectin bind to plaques and other structures in Alzheimer's Disease and control brain
    • Howard J, Pilkington GJ. Antibodies to fibronectin bind to plaques and other structures in Alzheimer's Disease and control brain. Neurosci Lett 1990; 118: 71-6
    • (1990) Neurosci Lett , vol.118 , pp. 71-76
    • Howard, J.1    Pilkington, G.J.2
  • 6
    • 0028284580 scopus 로고
    • Vascular basement membrane components and the lesions of Alzheimer's disease: Light and electron microscopic analyses
    • Perlmutter LS, Myers MA, Barron E. Vascular basement membrane components and the lesions of Alzheimer's disease: light and electron microscopic analyses. Microsc Res Tech 1994; 28: 204-15
    • (1994) Microsc Res Tech , vol.28 , pp. 204-215
    • Perlmutter, L.S.1    Myers, M.A.2    Barron, E.3
  • 7
    • 0028491538 scopus 로고
    • Microvascular pathology and vascular basement membrane components in Alzheimer's disease
    • Perlmutter LS. Microvascular pathology and vascular basement membrane components in Alzheimer's disease. Mol Neurobiol 1994; 9: 33-40
    • (1994) Mol Neurobiol , vol.9 , pp. 33-40
    • Perlmutter, L.S.1
  • 9
    • 0018187709 scopus 로고
    • Changes in human serum amyloid-A and C-reactive protein after etiocholanolone-induced inflammation
    • McAdam KPWJ, Elin RJ, Sipe JD, et al. Changes in human serum amyloid-A and C-reactive protein after etiocholanolone-induced inflammation. J Clin Invest 1978; 61: 390-4
    • (1978) J Clin Invest , vol.61 , pp. 390-394
    • McAdam, K.P.W.J.1    Elin, R.J.2    Sipe, J.D.3
  • 10
    • 0001632706 scopus 로고
    • Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity?
    • Kisilevsky R, Gruys E, Shirahama T. Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity? Amyloid Int J Exp Clin Invest 1995; 2: 128-33
    • (1995) Amyloid Int J Exp Clin Invest , vol.2 , pp. 128-133
    • Kisilevsky, R.1    Gruys, E.2    Shirahama, T.3
  • 11
    • 0020549270 scopus 로고
    • The kinetics of amyloid deposition. I. The effect of amyloid enhancing factor and splenectomy
    • Kisilevsky R, Boudreau L. The kinetics of amyloid deposition. I. The effect of amyloid enhancing factor and splenectomy. Lab Invest 1983; 48: 53-9
    • (1983) Lab Invest , vol.48 , pp. 53-59
    • Kisilevsky, R.1    Boudreau, L.2
  • 12
    • 0018308853 scopus 로고
    • The effect of a liver protein synthesis inhibitor on plasma SAA levels in a model of accelerated amyloid deposition
    • Kisilevsky R, Benson MD, Axelrad MA, et al. The effect of a liver protein synthesis inhibitor on plasma SAA levels in a model of accelerated amyloid deposition. Lab Invest 1979; 41: 206-10
    • (1979) Lab Invest , vol.41 , pp. 206-210
    • Kisilevsky, R.1    Benson, M.D.2    Axelrad, M.A.3
  • 13
    • 0022965337 scopus 로고
    • Ethionine carcinogenesis in CD-1, BALB/c, and C3H mice
    • Jul
    • Hoover KL, Hyde CL, Wenk ML, et al. Ethionine carcinogenesis in CD-1, BALB/c, and C3H mice. Carcinogenesis 1986 Jul; 7 (7): 1143-8
    • (1986) Carcinogenesis , vol.7 , Issue.7 , pp. 1143-1148
    • Hoover, K.L.1    Hyde, C.L.2    Wenk, M.L.3
  • 14
    • 0025372021 scopus 로고
    • Inhibition of the initiation of hepatic-protein synthesis during ethionine mediated ATP depletion in vivo: Modification to ribosomal subunits, evidence of impaired ternary complex formation and a subcellular redistribution of eIF-2-Alpha
    • Lyon AW, Kisilevsky R. Inhibition of the initiation of hepatic-protein synthesis during ethionine mediated ATP depletion in vivo: modification to ribosomal subunits, evidence of impaired ternary complex formation and a subcellular redistribution of eIF-2-Alpha. Biochim Biophys Acta 1990; 1049: 158-70
    • (1990) Biochim Biophys Acta , vol.1049 , pp. 158-170
    • Lyon, A.W.1    Kisilevsky, R.2
  • 15
    • 0006193979 scopus 로고
    • Transthyretin and apoA-I amyloidosis
    • Kisilevsky R, Benson MD, Frangione B, et al., editors. Park Ridge (NJ): The Parthenon Publishing Group
    • Araki S, Ikegawa S. Transthyretin and apoA-I amyloidosis. In: Kisilevsky R, Benson MD, Frangione B, et al., editors. Amyloid and amyloidosis 1993. Park Ridge (NJ): The Parthenon Publishing Group, 1994: 422-7
    • (1994) Amyloid and Amyloidosis 1993 , pp. 422-427
    • Araki, S.1    Ikegawa, S.2
  • 16
    • 0027312398 scopus 로고
    • Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis
    • Holmgren G, Ericzon BG, Groth CG, et al. Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis. Lancet 1993; 341: 1113-6
    • (1993) Lancet , vol.341 , pp. 1113-1116
    • Holmgren, G.1    Ericzon, B.G.2    Groth, C.G.3
  • 17
    • 0022351610 scopus 로고
    • Primary systemic amyloidosis. Comparison of melphalan/prednisone versus colchicine
    • Kyle RA, Greipp PR, Garton JP, et al. Primary systemic amyloidosis. Comparison of melphalan/prednisone versus colchicine. Am J Med 1985; 79: 708-16
    • (1985) Am J Med , vol.79 , pp. 708-716
    • Kyle, R.A.1    Greipp, P.R.2    Garton, J.P.3
  • 18
    • 0023113698 scopus 로고
    • Resolution of acquired factor X deficiency and amyloidosis with melphalan and prednisone therapy
    • Camoriano JK, Greipp PR, Bayer GK, et al. Resolution of acquired factor X deficiency and amyloidosis with melphalan and prednisone therapy. N Engl J Med 1987; 316: 1133-5
    • (1987) N Engl J Med , vol.316 , pp. 1133-1135
    • Camoriano, J.K.1    Greipp, P.R.2    Bayer, G.K.3
  • 19
    • 0025269483 scopus 로고
    • Acute leukemia and cytogenetic abnormalities complicating melphalan treatment of primary systemic amyloidosis
    • Gertz MA, Kyle RA. Acute leukemia and cytogenetic abnormalities complicating melphalan treatment of primary systemic amyloidosis. Arch Intern Med 1990; 150: 629-33
    • (1990) Arch Intern Med , vol.150 , pp. 629-633
    • Gertz, M.A.1    Kyle, R.A.2
  • 20
    • 0028936196 scopus 로고
    • Treatment of primary amyloidosis
    • Merlini G. Treatment of primary amyloidosis. Semin Hematol 1995; 32: 60-79
    • (1995) Semin Hematol , vol.32 , pp. 60-79
    • Merlini, G.1
  • 21
    • 0027367764 scopus 로고
    • Physiological production of the beta-amyloid protein and the mechanism of alzheimer's disease
    • Selkoe DJ. Physiological production of the beta-amyloid protein and the mechanism of alzheimer's disease. Trends Neurosci 1993; 16: 403-9
    • (1993) Trends Neurosci , vol.16 , pp. 403-409
    • Selkoe, D.J.1
  • 22
    • 0028201821 scopus 로고
    • APP processing, Aβ-amyloidogenesis, and the pathogenesis of Alzheimers disease
    • Gandy S, Caporaso G, Buxbaum J, et al. APP processing, Aβ-amyloidogenesis, and the pathogenesis of Alzheimers disease. Neurobiol Aging 1994; 15: 253-6
    • (1994) Neurobiol Aging , vol.15 , pp. 253-256
    • Gandy, S.1    Caporaso, G.2    Buxbaum, J.3
  • 23
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • Selkoe DJ. Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu Rev Cell Biol 1994; 10: 373-403
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 24
    • 0028247930 scopus 로고
    • Alzheimer's disease amyloid precursor protein (AβPP): Proteolytic processing, secretases, and βA4 amyloid production
    • Evin G, Beyreuther K, Master CL. Alzheimer's disease amyloid precursor protein (AβPP): proteolytic processing, secretases, and βA4 amyloid production. Amyloid Int J Exp Clin Invest 1994; 1: 263-80
    • (1994) Amyloid Int J Exp Clin Invest , vol.1 , pp. 263-280
    • Evin, G.1    Beyreuther, K.2    Master, C.L.3
  • 25
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A, Yankner BA. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc Natl Acad Sci USA 1994; 91: 12243-7
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 26
    • 0028883252 scopus 로고
    • Molecular genetics of Alzheimer disease: Identification of genes and gene mutations
    • van Broeckhoven CL. Molecular genetics of Alzheimer disease: identification of genes and gene mutations. Eur Neurol 1995; 35: 8-19
    • (1995) Eur Neurol , vol.35 , pp. 8-19
    • Van Broeckhoven, C.L.1
  • 27
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event - Studies of an amyloidogenic sequence from the bacterial protein OsmB
    • Jarrett JT, Lansbury PT. Amyloid fibril formation requires a chemically discriminating nucleation event - studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 1992; 31: 12345-52
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 28
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases - Importance of seeding
    • Come JH, Fraser PE, Lansbury PT. A kinetic model for amyloid formation in the prion diseases - importance of seeding. Proc Natl Acad Sci USA 1993; 90: 5959-63
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 29
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation
    • Kelly JW, Lansbury PT. A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation. Amyloid Int J Exp Clin Invest 1994; 1: 186-205
    • (1994) Amyloid Int J Exp Clin Invest , vol.1 , pp. 186-205
    • Kelly, J.W.1    Lansbury, P.T.2
  • 30
    • 0029058734 scopus 로고
    • The molecular mechanism of amyloid formation in Alzheimer's disease
    • Lansbury PT. The molecular mechanism of amyloid formation in Alzheimer's disease. Eur J Med Chem 1995; 30 Suppl.: S621-S63
    • (1995) Eur J Med Chem , vol.30 , Issue.SUPPL.
    • Lansbury, P.T.1
  • 31
    • 0025896711 scopus 로고
    • Familial Mediterranean fever - Diagnosis and treatment
    • Better OS, Zerner D. Familial Mediterranean fever - diagnosis and treatment. Dtsch Med Wochenschr 1991; 116: 548-52
    • (1991) Dtsch Med Wochenschr , vol.116 , pp. 548-552
    • Better, O.S.1    Zerner, D.2
  • 32
    • 0026660966 scopus 로고
    • Familial Mediterranean lever - Analysis of inheritance and current linkage data
    • Shohat M, Danon YL, Rotter JI. Familial Mediterranean lever - analysis of inheritance and current linkage data. Am J Med Genet 1992; 44: 183-8
    • (1992) Am J Med Genet , vol.44 , pp. 183-188
    • Shohat, M.1    Danon, Y.L.2    Rotter, J.I.3
  • 33
    • 0028821355 scopus 로고
    • Familial Mediterranean fever: High gene frequency among the non-Ashkenazic and Ashkenazic Jewish populations in Israel
    • Daniels M, Shohat T, Brenner-Ullman A, et al. Familial Mediterranean fever: high gene frequency among the non-Ashkenazic and Ashkenazic Jewish populations in Israel. Am J Med Genet 1995; 55: 311-4
    • (1995) Am J Med Genet , vol.55 , pp. 311-314
    • Daniels, M.1    Shohat, T.2    Brenner-Ullman, A.3
  • 34
    • 0027405593 scopus 로고
    • Familial Mediterranean fever in the colehicine era - The late of one family
    • Zemer D, Livneh A, Pras M, et al. Familial Mediterranean fever in the colehicine era - the late of one family. Am J Med Genet 1993; 45: 340-4
    • (1993) Am J Med Genet , vol.45 , pp. 340-344
    • Zemer, D.1    Livneh, A.2    Pras, M.3
  • 35
    • 0028096627 scopus 로고
    • Colehicine treatment of AA amyloidosis of familial Mediterranean fever: An analysis of factors affecting outcome
    • Livneh A, Zemer D, Langevitz P, et al. Colehicine treatment of AA amyloidosis of familial Mediterranean fever: an analysis of factors affecting outcome. Arthritis Rheum 1994; 37: 1804-11
    • (1994) Arthritis Rheum , vol.37 , pp. 1804-1811
    • Livneh, A.1    Zemer, D.2    Langevitz, P.3
  • 36
    • 0021913276 scopus 로고
    • Effect of colehicine on experimental amyloidosis in two CBA/J mouse models: Chronic inflammatory stimulation and administration of amyloid-enhancing factor during acute inflammation
    • Brandwein SR, Sipe JD, Skinner M, et al. Effect of colehicine on experimental amyloidosis in two CBA/J mouse models: chronic inflammatory stimulation and administration of amyloid-enhancing factor during acute inflammation. Lab Invest 1985; 52: 319-25
    • (1985) Lab Invest , vol.52 , pp. 319-325
    • Brandwein, S.R.1    Sipe, J.D.2    Skinner, M.3
  • 37
    • 0025830613 scopus 로고
    • Co-deposition of basement membrane components during the induction of murine splenic AA amyloid
    • Lyon AW, Narindrasorasak S, Young ID, et al. Co-deposition of basement membrane components during the induction of murine splenic AA amyloid. Lab Invest 1991; 64: 785-90
    • (1991) Lab Invest , vol.64 , pp. 785-790
    • Lyon, A.W.1    Narindrasorasak, S.2    Young, I.D.3
  • 38
    • 0028934953 scopus 로고
    • An interaction between basement membrane and Alzheimer amyloid precursor proteins suggests a role in the pathogenesis of Alzheimer's disease
    • Narindrasorasak S, Altman RA, Gonzalez-DeWhitt P, et al. An interaction between basement membrane and Alzheimer amyloid precursor proteins suggests a role in the pathogenesis of Alzheimer's disease. Lab Invest 1995; 72: 272-82
    • (1995) Lab Invest , vol.72 , pp. 272-282
    • Narindrasorasak, S.1    Altman, R.A.2    Gonzalez-DeWhitt, P.3
  • 39
    • 0024212706 scopus 로고
    • Circular dichroism and fluorescence studies on two murine serum amyloid A proteins
    • McCubbin WD, Kay CM, Narindrasorasak S, et al. Circular dichroism and fluorescence studies on two murine serum amyloid A proteins. Biochem J 1988; 256: 775-83
    • (1988) Biochem J , vol.256 , pp. 775-783
    • McCubbin, W.D.1    Kay, C.M.2    Narindrasorasak, S.3
  • 40
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer-beta/A4 peptide assemblies - Implications for amyloid fibril-proteoglycan interactions
    • Fraser PE, Nguyen JT, Chin DT, et al. Effects of sulfate ions on Alzheimer-beta/A4 peptide assemblies - implications for amyloid fibril-proteoglycan interactions. J Neureichem 1992; 59: 1531-40
    • (1992) J Neureichem , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3
  • 41
    • 9044245133 scopus 로고
    • Binding of sulfated-proleins and alpha-1-antichymotrypsin to Alzheimer Aβ: Different actions of amyloid associated proteins
    • Kisilevsky R, Benson MD, Frangione B, et al. editors. Park Ridge (NJ): The Parthenon Publishing Group
    • Fraser PE, Kirschner DA, Nguven JT, et al. Binding of sulfated-proleins and alpha-1-antichymotrypsin to Alzheimer Aβ: different actions of amyloid associated proteins. In: Kisilevsky R, Benson MD, Frangione B, et al. editors. Amyloid and amyloidosis 1993. Park Ridge (NJ): The Parthenon Publishing Group, 1994: 341-3
    • (1994) Amyloid and Amyloidosis 1993 , pp. 341-343
    • Fraser, P.E.1    Kirschner, D.A.2    Nguven, J.T.3
  • 42
    • 0027165834 scopus 로고
    • Structural prerequisites for serum amyloid A fibril formation
    • De Beer MC, de Beer FC, McCubbin WD, et al. Structural prerequisites for serum amyloid A fibril formation. J Biol Chem 1993; 268: 20606-12
    • (1993) J Biol Chem , vol.268 , pp. 20606-20612
    • De Beer, M.C.1    De Beer, F.C.2    McCubbin, W.D.3
  • 43
    • 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. Nature Med 1995; 1: 143-8
    • (1995) Nature Med , vol.1 , pp. 143-148
    • Kisilevsky, R.1    Lemieux, L.J.2    Fraser, P.E.3
  • 44
    • 0028588694 scopus 로고
    • Congo Red protects against toxicity of beta-amyloid peptides on rat hippocampal neurones
    • Burgevin MC, Passat M, Daniel N, et al. Congo Red protects against toxicity of beta-amyloid peptides on rat hippocampal neurones. NeuroReport 1994; 5: 2429-32
    • (1994) NeuroReport , vol.5 , pp. 2429-2432
    • Burgevin, M.C.1    Passat, M.2    Daniel, N.3
  • 45
    • 0028870182 scopus 로고
    • Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of beta-amyloid in rat PC12 cells
    • Pollack SJ, Sadler HJ, Hawtin SR, et al. Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of beta-amyloid in rat PC12 cells. Neurosci Lett 1995; 184: 113-6
    • (1995) Neurosci Lett , vol.184 , pp. 113-116
    • Pollack, S.J.1    Sadler, H.J.2    Hawtin, S.R.3
  • 46
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrPaccumulation by Congo Red
    • Caughey B, Race RE. Potent inhibition of scrapie-associated PrPaccumulation by Congo Red. J Neurochem 1992; 59: 768-71
    • (1992) J Neurochem , vol.59 , pp. 768-771
    • Caughey, B.1    Race, R.E.2
  • 47
    • 0028256222 scopus 로고
    • Binding of the protease-sensitive form of PrP(prion protein) to sulfated glycosaminoglycan and congo red
    • Caughey B, Brown K, Raymond GJ, et al. Binding of the protease-sensitive form of PrP(prion protein) to sulfated glycosaminoglycan and congo red. J Virol 1994; 68: 2135-41
    • (1994) J Virol , vol.68 , pp. 2135-2141
    • Caughey, B.1    Brown, K.2    Raymond, G.J.3
  • 48
    • 0028420936 scopus 로고
    • Inhibition of scrapie-associated PrP accumulation - Probing the role of glycosuminoglycans in amyloidogenesis
    • Priola SA, Caughey B. Inhibition of scrapie-associated PrP accumulation - probing the role of glycosuminoglycans in amyloidogenesis. Mol Neurobiol 1994; 8: 113-20
    • (1994) Mol Neurobiol , vol.8 , pp. 113-120
    • Priola, S.A.1    Caughey, B.2
  • 49
    • 0020383508 scopus 로고
    • The resolution of amyloid substance
    • Wegelius O. The resolution of amyloid substance. Acta Med Scand 1982; 212: 273-5
    • (1982) Acta Med Scand , vol.212 , pp. 273-275
    • Wegelius, O.1
  • 50
    • 0024367041 scopus 로고
    • Remission of nephrolic syndrome in amyloidosis associated with a hypernephroma
    • Tang AL, Davies DR, Wing AJ. Remission of nephrolic syndrome in amyloidosis associated with a hypernephroma. Clin Nephrol 1989; 32: 225-8
    • (1989) Clin Nephrol , vol.32 , pp. 225-228
    • Tang, A.L.1    Davies, D.R.2    Wing, A.J.3
  • 51
    • 0028225998 scopus 로고
    • Reversal of nephrotic syndrome due to reactive amyloidosis (AA-type) after excision of localized Castleman's disease
    • Perfetti V, Bellolti V, Maggi A, et al. Reversal of nephrotic syndrome due to reactive amyloidosis (AA-type) after excision of localized Castleman's disease. Am J Hematol 1994; 46: 189-93
    • (1994) Am J Hematol , vol.46 , pp. 189-193
    • Perfetti, V.1    Bellolti, V.2    Maggi, A.3
  • 52
    • 0020405821 scopus 로고
    • Prolonged dimethylsulphoxide treatment in 13 patients with systemic amyloidosis
    • Ravid M, Shapira J, Lang R, et al. Prolonged dimethylsulphoxide treatment in 13 patients with systemic amyloidosis. Ann Rheum Dis 1982; 41: 587-92
    • (1982) Ann Rheum Dis , vol.41 , pp. 587-592
    • Ravid, M.1    Shapira, J.2    Lang, R.3
  • 53
    • 0017611245 scopus 로고
    • Treatment of experimental murine amyloidosis with dimethyl sulfoxide
    • Kedar I, Greenwald M, Ravid M. Treatment of experimental murine amyloidosis with dimethyl sulfoxide. Eur J Clin Invest 1977; 7: 149-50
    • (1977) Eur J Clin Invest , vol.7 , pp. 149-150
    • Kedar, I.1    Greenwald, M.2    Ravid, M.3
  • 55
    • 0028914019 scopus 로고
    • Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: Inhibition of amyloidogenesis
    • Merlini G, Ascari E, Amboldi N, et al. Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis. Proc Natl Acad Sci USA 1995; 92: 2959-63
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2959-2963
    • Merlini, G.1    Ascari, E.2    Amboldi, N.3
  • 56
    • 0029094670 scopus 로고
    • New drug therapy of amyloidoses: Resorption of AL-type deposits with 4′-iodo-4′-deoxydoxorubicin
    • Gianni L, Bellotti V, Gianni AM, et al. New drug therapy of amyloidoses: resorption of AL-type deposits with 4′-iodo-4′-deoxydoxorubicin. Blood 1995; 86: 855-61
    • (1995) Blood , vol.86 , pp. 855-861
    • Gianni, L.1    Bellotti, V.2    Gianni, A.M.3
  • 57
    • 0029010736 scopus 로고
    • Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis
    • Tennent GA, Lovat LB, Pepys MB. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc Natl Acad Sci USA 1995; 92: 4299-303
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4299-4303
    • Tennent, G.A.1    Lovat, L.B.2    Pepys, M.B.3
  • 58
    • 0028978227 scopus 로고
    • Proteoglycanmediated inhibition of A beta proteolysis - A potential cause of senile plaque accumulation
    • Gupta-Bansal R, Frederickson RCA, Brunden KR. Proteoglycanmediated inhibition of A beta proteolysis - a potential cause of senile plaque accumulation. J Biol Chem 1995; 270: 18666-71
    • (1995) J Biol Chem , vol.270 , pp. 18666-18671
    • Gupta-Bansal, R.1    Frederickson, R.C.A.2    Brunden, K.R.3
  • 59
    • 0028043322 scopus 로고
    • Combined treatment with terbutaline and aminophylline inhibits experimental amyloid-osis in mice
    • Brandwein SR, Sipe JD, Cohen AS. Combined treatment with terbutaline and aminophylline inhibits experimental amyloid-osis in mice. Arthritis Rheum 1994; 37: 1757-60
    • (1994) Arthritis Rheum , vol.37 , pp. 1757-1760
    • Brandwein, S.R.1    Sipe, J.D.2    Cohen, A.S.3
  • 60
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • Lorenzo A, Razzaboni B, Weir GC, et al. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature 1994; 368: 756-60
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Weir, G.C.3
  • 61
    • 0027991946 scopus 로고
    • Chronic exposure of cultured rat pancreatic islets to elevated concentrations of islet amyloid polypeptide (IAPP) causes a decrease in islet DNA content and medium insulin accumulation
    • Sandler S, Stridsberg M. Chronic exposure of cultured rat pancreatic islets to elevated concentrations of islet amyloid polypeptide (IAPP) causes a decrease in islet DNA content and medium insulin accumulation. Regul Pept 1994; 53: 103-9
    • (1994) Regul Pept , vol.53 , pp. 103-109
    • Sandler, S.1    Stridsberg, M.2
  • 62
    • 0026577183 scopus 로고
    • Islet amyloid polypeptide - A novel controversy in diabetes research
    • Westermark P, Johnson KH, O'Brien TD, et al. Islet amyloid polypeptide - a novel controversy in diabetes research. Diabetologia 1992; 35: 297-303
    • (1992) Diabetologia , vol.35 , pp. 297-303
    • Westermark, P.1    Johnson, K.H.2    O'Brien, T.D.3
  • 63
    • 0026654926 scopus 로고
    • Islet amyloid polypeptide - Mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus
    • Johnson KH, O'Brien TD, Betsholtz C, et al. Islet amyloid polypeptide - mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus. Lab Invest 1992; 66: 522-35
    • (1992) Lab Invest , vol.66 , pp. 522-535
    • Johnson, K.H.1    O'Brien, T.D.2    Betsholtz, C.3
  • 64
    • 0027633921 scopus 로고
    • Islet amyloid polypeptide - A review of its biology and potential roles in the pathogenesis of diabetes mellitus
    • O'Brien TD, Butler PC, Westermark P, et al. Islet amyloid polypeptide - a review of its biology and potential roles in the pathogenesis of diabetes mellitus. Vet Pathol 1993; 30: 317-32
    • (1993) Vet Pathol , vol.30 , pp. 317-332
    • O'Brien, T.D.1    Butler, P.C.2    Westermark, P.3
  • 65
    • 0028857285 scopus 로고
    • Areappraisal of current hypotheses concerning the possible roles of amylin in physiology, pathology and therapeutics
    • Cooper GJS. Areappraisal of current hypotheses concerning the possible roles of amylin in physiology, pathology and therapeutics. Clin Sci 1995; 88: 7-12
    • (1995) Clin Sci , vol.88 , pp. 7-12
    • Cooper, G.J.S.1
  • 66
    • 0028906054 scopus 로고
    • The transmissible spongiform encephalopathies
    • Goldfarb LG, Brown P. The transmissible spongiform encephalopathies. Ann Rev Med 1995; 46: 57-65
    • (1995) Ann Rev Med , vol.46 , pp. 57-65
    • Goldfarb, L.G.1    Brown, P.2
  • 68
    • 0029041357 scopus 로고
    • Biochemistry and genetics of prion proteins
    • Prusiner SB. Biochemistry and genetics of prion proteins. Eur J Med Chem 1995; 30 Suppl.: S11-S50
    • (1995) Eur J Med Chem , vol.30 , Issue.SUPPL.
    • Prusiner, S.B.1
  • 69
    • 0028233508 scopus 로고
    • Systemic distribution of beta(2)-microglobulin-derived amyloidosis in patients who undergo long-term hemodialysis - Report of seven cases and review of the literature
    • Gal R, Korzets A, Schwartz A, et al. Systemic distribution of beta(2)-microglobulin-derived amyloidosis in patients who undergo long-term hemodialysis - report of seven cases and review of the literature. Arch Pathol Lab Med 1994; 118: 718-21
    • (1994) Arch Pathol Lab Med , vol.118 , pp. 718-721
    • Gal, R.1    Korzets, A.2    Schwartz, A.3
  • 70
    • 0026195440 scopus 로고
    • Amyloid and amyloidosis: Differences, common themes, and practical considerations
    • Kisilevsky R. Amyloid and amyloidosis: differences, common themes, and practical considerations. Mod Pathol 1991; 4: 514-8
    • (1991) Mod Pathol , vol.4 , pp. 514-518
    • Kisilevsky, R.1


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