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Volumn 45, Issue , 2000, Pages 107-137

The systemic amyloidoses: An overview

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID;

EID: 0033630225     PISSN: 00652822     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (110)

References (162)
  • 1
    • 0001611370 scopus 로고
    • Electron microscopic observations on a fibrous component in amyloid of diverse origins
    • Cohen AS CE: Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183:1202-1203, 1959.
    • (1959) Nature , vol.183 , pp. 1202-1203
    • Cohen, A.S.C.E.1
  • 2
    • 0014098295 scopus 로고
    • High resolution electron microscopic analysis of the amyloid fibril
    • Shirahama T CA: High resolution electron microscopic analysis of the amyloid fibril. J Cell Biol 333:679-708, 1967.
    • (1967) J Cell Biol , vol.333 , pp. 679-708
    • Shirahama, T.C.A.1
  • 3
    • 0014578835 scopus 로고
    • Characterization of the amyloid fibril as a cross-beta protein
    • Bonar L, Cohen AS, Skinner MM: Characterization of the amyloid fibril as a cross-beta protein. Proc Soc Exp Biol Med 131(4):1373-1375, 1969.
    • (1969) Proc Soc Exp Biol Med , vol.131 , Issue.4 , pp. 1373-1375
    • Bonar, L.1    Cohen, A.S.2    Skinner, M.M.3
  • 4
    • 0015219685 scopus 로고
    • Amyloid fibril proteins: Proof of homology with immunoglobulin light chains by sequence analysis
    • Glenner GG TW, Harada M, Isersky C, et al: Amyloid fibril proteins: Proof of homology with immunoglobulin light chains by sequence analysis. Science 172:1150-1151, 1971.
    • (1971) Science , vol.172 , pp. 1150-1151
    • Glenner, G.G.T.W.1    Harada, M.2    Isersky, C.3
  • 5
    • 0000375747 scopus 로고
    • The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences
    • Benditt E, Eriksen N, Hermodson M, et al: The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett 19:169-173, 1971.
    • (1971) FEBS Lett , vol.19 , pp. 169-173
    • Benditt, E.1    Eriksen, N.2    Hermodson, M.3
  • 6
    • 0010551538 scopus 로고
    • Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy
    • Costa PP, Figueira AS, Bravo FR: Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy. Proc Natl Acad Sci U S A 75(9):4499-4503, 1978.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , Issue.9 , pp. 4499-4503
    • Costa, P.P.1    Figueira, A.S.2    Bravo, F.R.3
  • 7
    • 0032064203 scopus 로고    scopus 로고
    • The pathogenesis of amyloidosis: Understanding general principles
    • Westermark P: The pathogenesis of amyloidosis: Understanding general principles [comment]. Am J Pathol 152(5):1125-1127, 1998.
    • (1998) Am J Pathol , vol.152 , Issue.5 , pp. 1125-1127
    • Westermark, P.1
  • 8
    • 0019951737 scopus 로고
    • Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL
    • Solomon A, Frangione B, Franklin EC: Bence Jones proteins and light chains of immunoglobulins. Preferential association of the V lambda VI subgroup of human light chains with amyloidosis AL (lambda). J Clin Invest 70(2):453-460, 1982.
    • (1982) J Clin Invest , vol.70 , Issue.2 , pp. 453-460
    • Solomon, A.1    Frangione, B.2    Franklin, E.C.3
  • 9
    • 0032523164 scopus 로고    scopus 로고
    • Evidence that amyloidogenic light chains undergo antigen-driven selection
    • Perfetti V, Ubbiali P, Vignarelli MC, et al: Evidence that amyloidogenic light chains undergo antigen-driven selection. Blood 91(8):2948-2954, 1998.
    • (1998) Blood , vol.91 , Issue.8 , pp. 2948-2954
    • Perfetti, V.1    Ubbiali, P.2    Vignarelli, M.C.3
  • 10
    • 0029094974 scopus 로고
    • A molecular model for self-assembly of amyloid fibrils: Immunoglobulin light chains
    • Stevens FJ, Myatt EA, Chang CH, et al: A molecular model for self-assembly of amyloid fibrils: Immunoglobulin light chains. Biochemistry 34(34):10697-10702, 1995.
    • (1995) Biochemistry , vol.34 , Issue.34 , pp. 10697-10702
    • Stevens, F.J.1    Myatt, E.A.2    Chang, C.H.3
  • 11
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle MR, Helms LR, Li L, et al: A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc Natl Acad Sci U S A 91(12):5446-5450, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.12 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3
  • 12
    • 0000573604 scopus 로고
    • Protein and host factors implicated in the pathogenesis of light chain amyloidosis
    • Solomon A, Weiss DT: Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis) [review]. Amyloid 2(4):269-279, 1995.
    • (1995) Amyloid , vol.2 , Issue.4 , pp. 269-279
    • Solomon, A.1    Weiss, D.T.2
  • 13
    • 0030139339 scopus 로고    scopus 로고
    • Molecular anatomy and the pathological expression of antibody light chains
    • Schiffer M: Molecular anatomy and the pathological expression of antibody light chains [comment]. Am J Pathol 148(5):1339-1344, 1996.
    • (1996) Am J Pathol , vol.148 , Issue.5 , pp. 1339-1344
    • Schiffer, M.1
  • 16
    • 0026555175 scopus 로고
    • The N-terminal segment of protein AA determines its fibrillogenic property
    • Westermark GT, Engstrom U, Westermark P: The N-terminal segment of protein AA determines its fibrillogenic property. Biochem Biophys Res Commun 182(1):27-33, 1992.
    • (1992) Biochem Biophys Res Commun , vol.182 , Issue.1 , pp. 27-33
    • Westermark, G.T.1    Engstrom, U.2    Westermark, P.3
  • 17
    • 0022004144 scopus 로고
    • Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. A histochemical study
    • Snow AD, Kisilevsky R: Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. A histochemical study. Lab Invest 53(1):37-44, 1985.
    • (1985) Lab Invest , vol.53 , Issue.1 , pp. 37-44
    • Snow, A.D.1    Kisilevsky, R.2
  • 18
    • 0032478215 scopus 로고    scopus 로고
    • Acceleration, of amyloid protein a amyloidosis by amyloid-like synthetic fibrils
    • Johan K, Westermark G, Engstrom U, et al: Acceleration, of amyloid protein A amyloidosis by amyloid-like synthetic fibrils. Proc Natl Acad Sci U S A 95(5):2558-2563, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.5 , pp. 2558-2563
    • Johan, K.1    Westermark, G.2    Engstrom, U.3
  • 19
    • 0028260652 scopus 로고
    • Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations
    • Gustavsson A, Engstrom U, Westermark P: Mechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizations. Am J Pathol 144(6):1301-1311, 1994.
    • (1994) Am J Pathol , vol.144 , Issue.6 , pp. 1301-1311
    • Gustavsson, A.1    Engstrom, U.2    Westermark, P.3
  • 20
    • 1842589542 scopus 로고    scopus 로고
    • The edge strand hypothesis: Prediction and test of a mutational hot-spot on the transthyretin molecule associated with Fap amyloidogenesis
    • Serpell LC, Goldsteins G, Dacklin I, et al: The edge strand hypothesis: Prediction and test of a mutational hot-spot on the transthyretin molecule associated with Fap amyloidogenesis. Amyloid 3(2):75-85, 1996.
    • (1996) Amyloid , vol.3 , Issue.2 , pp. 75-85
    • Serpell, L.C.1    Goldsteins, G.2    Dacklin, I.3
  • 21
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation
    • Kelly JW, Lansbury PT: A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation [review]. Amyloid 1(3):186-205, 1994.
    • (1994) Amyloid , vol.1 , Issue.3 , pp. 186-205
    • Kelly, J.W.1    Lansbury, P.T.2
  • 22
    • 0025278448 scopus 로고
    • Fibril in senile systemic amyloidosis is derived from normal transthyretin
    • Westermark P, Sletten K, Johansson B, et al: Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci U S A 87(7):2843-2845, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.7 , pp. 2843-2845
    • Westermark, P.1    Sletten, K.2    Johansson, B.3
  • 23
    • 0032479201 scopus 로고    scopus 로고
    • Apolipoprotein A-I induced amyloidosis
    • Genschel J, Haas R, Propsting MJ, et al: Apolipoprotein A-I induced amyloidosis. FEBS Letters 430(3):145-149, 1998.
    • (1998) FEBS Letters , vol.430 , Issue.3 , pp. 145-149
    • Genschel, J.1    Haas, R.2    Propsting, M.J.3
  • 24
    • 0026642154 scopus 로고
    • In vivo metabolism of a mutant apolipoprotein, apoA-Howa, associated with hypoalphalipoproteinemia and hereditary systemic amyloidosis
    • Rader DJ, Gregg RE, Meng MS, et al: In vivo metabolism of a mutant apolipoprotein, apoA-Howa, associated with hypoalphalipoproteinemia and hereditary systemic amyloidosis. J Lipid Res 33(5):755-763, 1992.
    • (1992) J Lipid Res , vol.33 , Issue.5 , pp. 755-763
    • Rader, D.J.1    Gregg, R.E.2    Meng, M.S.3
  • 25
    • 0032918099 scopus 로고    scopus 로고
    • A novel amyloidogenic variant of apolipoprotein A1: Implications for a conformational change leading to cardiomyopathy
    • Walsh M: A novel amyloidogenic variant of apolipoprotein A1: Implications for a conformational change leading to cardiomyopathy. Am J Pathol 154:11-14, 1999.
    • (1999) Am J Pathol , vol.154 , pp. 11-14
    • Walsh, M.1
  • 26
    • 0010287190 scopus 로고    scopus 로고
    • Hereditary amyloid cardiomyopathy caused by a variant apolipoprotein A1
    • Asl LH, Liepnieks JJ, AsI KH, et al: Hereditary amyloid cardiomyopathy caused by a variant apolipoprotein A1 [see comments]. Am J Pathol 154(1):221-227, 1999.
    • (1999) Am J Pathol , vol.154 , Issue.1 , pp. 221-227
    • Asl, L.H.1    Liepnieks, J.J.2    Asi, K.H.3
  • 27
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth DR, Sunde M, Bellotti V, et al: Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis [see comments]. Nature 385(6619):787-793, 1997.
    • (1997) Nature , vol.385 , Issue.6619 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3
  • 28
    • 0028935156 scopus 로고
    • The putative role of alpha-1-antitrypsin in the disaggregation of amyloid lambda fibrils
    • Eriksson S, Janciauskiene S, Merlini G: The putative role of alpha-1-antitrypsin in the disaggregation of amyloid lambda fibrils. J Intern Med 237(2):143-149, 1995.
    • (1995) J Intern Med , vol.237 , Issue.2 , pp. 143-149
    • Eriksson, S.1    Janciauskiene, S.2    Merlini, G.3
  • 29
    • 0032573082 scopus 로고    scopus 로고
    • Inhibiting transthyretin conformational changes that lead to amyloid fibril formation
    • Peterson SA, Klabunde T, Lashuel HA, et al: Inhibiting transthyretin conformational changes that lead to amyloid fibril formation. Proc Natl Acad Sci U S A 95(22):12956-12960, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.22 , pp. 12956-12960
    • Peterson, S.A.1    Klabunde, T.2    Lashuel, H.A.3
  • 30
    • 0030954873 scopus 로고    scopus 로고
    • The systemic amyloidoses
    • Falk RH, Comenzo RL, Skinner M: The systemic amyloidoses [see comments]. N Engl J Med 337(13):898-909, 1997.
    • (1997) N Engl J Med , vol.337 , Issue.13 , pp. 898-909
    • Falk, R.H.1    Comenzo, R.L.2    Skinner, M.3
  • 31
    • 0026519157 scopus 로고
    • Incidence and natural history of primary systemic amyloidosis in Olmsted County, Minnesota, 1950 through 1989
    • Kyle RA, Linos A, Beard CM, et al: Incidence and natural history of primary systemic amyloidosis in Olmsted County, Minnesota, 1950 through 1989 [see comments]. Blood 79(7):1817-1822, 1992.
    • (1992) Blood , vol.79 , Issue.7 , pp. 1817-1822
    • Kyle, R.A.1    Linos, A.2    Beard, C.M.3
  • 32
    • 0029946836 scopus 로고    scopus 로고
    • Revised transthyretin Ile 122 allele frequency in African-Americans
    • Jacobson DR, Pastore R, Pool S, et al: Revised transthyretin Ile 122 allele frequency in African-Americans. Hum Genet 98(2):236-238, 1996.
    • (1996) Hum Genet , vol.98 , Issue.2 , pp. 236-238
    • Jacobson, D.R.1    Pastore, R.2    Pool, S.3
  • 33
    • 0031028712 scopus 로고    scopus 로고
    • Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans
    • Jacobson DR, Pastore RD, Yaghoubian R, et al: Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans [see comments]. N Engl J Med 336(7):466-473, 1997.
    • (1997) N Engl J Med , vol.336 , Issue.7 , pp. 466-473
    • Jacobson, D.R.1    Pastore, R.D.2    Yaghoubian, R.3
  • 34
    • 0031012126 scopus 로고    scopus 로고
    • Transthyretin ILE20, a new variant associated with late-onset cardiac amyloidosis
    • Jacobson DR, Pan T, Kyle RA, et al: Transthyretin ILE20, a new variant associated with late-onset cardiac amyloidosis. Hum Mutat 9(1):83-85, 1997.
    • (1997) Hum Mutat , vol.9 , Issue.1 , pp. 83-85
    • Jacobson, D.R.1    Pan, T.2    Kyle, R.A.3
  • 35
    • 0030615175 scopus 로고    scopus 로고
    • Transthyretin Ile 122 and cardiac amyloidosis in African-Americans: 2 case reports
    • Jacobson DR, Ittmann M, Buxbaum JN, et al: Transthyretin Ile 122 and cardiac amyloidosis in African-Americans: 2 case reports. Tex Heart Inst J 24(1):45-52, 1997.
    • (1997) Tex Heart Inst J , vol.24 , Issue.1 , pp. 45-52
    • Jacobson, D.R.1    Ittmann, M.2    Buxbaum, J.N.3
  • 36
    • 0031869745 scopus 로고    scopus 로고
    • Scintigraphic imaging and turnover studies with iodine-131 labelled serum amyloid P component in systemic amyloidosis
    • Hawkins PN, Aprile C, Capri G, et al: Scintigraphic imaging and turnover studies with iodine-131 labelled serum amyloid P component in systemic amyloidosis. Eur J Nucl Med 25(7):701-708, 1998.
    • (1998) Eur J Nucl Med , vol.25 , Issue.7 , pp. 701-708
    • Hawkins, P.N.1    Aprile, C.2    Capri, G.3
  • 37
  • 39
    • 0030895545 scopus 로고    scopus 로고
    • A trial of three regimens for primary amyloidosis: Colchicine alone, melphalan and prednisone, and melphalan, prednisone, and colchicine
    • Kyle RA, Gertz MA, Greipp PR, et al: A trial of three regimens for primary amyloidosis: Colchicine alone, melphalan and prednisone, and melphalan, prednisone, and colchicine [see comments]. N Engl J Med 336(17):1202-1207, 1997.
    • (1997) N Engl J Med , vol.336 , Issue.17 , pp. 1202-1207
    • Kyle, R.A.1    Gertz, M.A.2    Greipp, P.R.3
  • 40
    • 0030752482 scopus 로고    scopus 로고
    • Histomorphological patterns of renal amyloidosis: A correlation between histology and chemical type of amyloidosis
    • Looi LM, Cheah PL: Histomorphological patterns of renal amyloidosis: A correlation between histology and chemical type of amyloidosis. Hum Pathol 28(7):847-849, 1997.
    • (1997) Hum Pathol , vol.28 , Issue.7 , pp. 847-849
    • Looi, L.M.1    Cheah, P.L.2
  • 41
    • 0029939944 scopus 로고    scopus 로고
    • Treatment of 100 patients with primary amyloidosis: A randomized trial of melphalan, prednisone, and colchicine versus colchicine only
    • Skinner M, Anderson J, Simms R, et al: Treatment of 100 patients with primary amyloidosis: A randomized trial of melphalan, prednisone, and colchicine versus colchicine only. Am J Med 100(3):290-298, 1996.
    • (1996) Am J Med , vol.100 , Issue.3 , pp. 290-298
    • Skinner, M.1    Anderson, J.2    Simms, R.3
  • 42
    • 0030199312 scopus 로고    scopus 로고
    • Prospective and serial study of primary amyloidosis with serum amyloid P component scintigraphy: From diagnosis to prognosis
    • Hachulla E, Maulin L, Deveaux M, et al: Prospective and serial study of primary amyloidosis with serum amyloid P component scintigraphy: From diagnosis to prognosis. Am J Med 101(1):77-87, 1996.
    • (1996) Am J Med , vol.101 , Issue.1 , pp. 77-87
    • Hachulla, E.1    Maulin, L.2    Deveaux, M.3
  • 43
    • 0027565086 scopus 로고
    • Renal involvement in plasma cell dyscrasias
    • Sanders PW: Renal involvement in plasma cell dyscrasias. Curr Opin Nephrol Hypertens 2(2):246-252, 1993.
    • (1993) Curr Opin Nephrol Hypertens , vol.2 , Issue.2 , pp. 246-252
    • Sanders, P.W.1
  • 44
    • 0027518596 scopus 로고
    • Iodine-123-labelled serum amyloid P component scintigraphy in amyloidosis
    • Saile R, Deveaux M, Hachulla E, et al: Iodine-123-labelled serum amyloid P component scintigraphy in amyloidosis. Eur J Nucl Med 20(2):130-137, 1993.
    • (1993) Eur J Nucl Med , vol.20 , Issue.2 , pp. 130-137
    • Saile, R.1    Deveaux, M.2    Hachulla, E.3
  • 45
    • 0031913337 scopus 로고    scopus 로고
    • The clinical features of immunoglobulin light-chain (AL) amyloidosis with heart involvement
    • Dubrey SW, Cha K, Anderson J, et al: The clinical features of immunoglobulin light-chain (AL) amyloidosis with heart involvement. QJM 91(2):141-157, 1998.
    • (1998) QJM , vol.91 , Issue.2 , pp. 141-157
    • Dubrey, S.W.1    Cha, K.2    Anderson, J.3
  • 46
    • 0030865311 scopus 로고    scopus 로고
    • Electrophysiologic abnormalities in AL (primary) amyloidosis with cardiac involvement
    • Reisinger J, Dubrey SW, Lavalley M, et al: Electrophysiologic abnormalities in AL (primary) amyloidosis with cardiac involvement. J Am Coll Cardiol 30(4):1046-1051, 1997.
    • (1997) J Am Coll Cardiol , vol.30 , Issue.4 , pp. 1046-1051
    • Reisinger, J.1    Dubrey, S.W.2    Lavalley, M.3
  • 47
    • 0023107169 scopus 로고
    • Sensitivity and specificity of the echocardiographic features of cardiac amyloidosis
    • Falk RH, Plehn JF, Deering T, et al: Sensitivity and specificity of the echocardiographic features of cardiac amyloidosis. Am J Cardiol 59(5):418-422, 1987.
    • (1987) Am J Cardiol , vol.59 , Issue.5 , pp. 418-422
    • Falk, R.H.1    Plehn, J.F.2    Deering, T.3
  • 48
    • 0031445804 scopus 로고    scopus 로고
    • Signal-averaged electrocardiography in patients with AL (primary) amyloidosis
    • Dubrey SW, Bilazarian S, LaValley M, et al: Signal-averaged electrocardiography in patients with AL (primary) amyloidosis. Am Heart J 134(6):994-1001, 1997.
    • (1997) Am Heart J , vol.134 , Issue.6 , pp. 994-1001
    • Dubrey, S.W.1    Bilazarian, S.2    Lavalley, M.3
  • 49
    • 0020576017 scopus 로고
    • Use of abdominal fat tissue aspirate in the diagnosis of systemic amyloidosis
    • Libbey CA, Skinner M, Cohen AS: Use of abdominal fat tissue aspirate in the diagnosis of systemic amyloidosis. Arch Inten Med 143(8):1549-1552, 1983.
    • (1983) Arch Inten Med , vol.143 , Issue.8 , pp. 1549-1552
    • Libbey, C.A.1    Skinner, M.2    Cohen, A.S.3
  • 50
    • 0023639134 scopus 로고
    • Diagnosis of amyloidosis by abdominal fat aspiration. Analysis of four years' experience
    • Duston MA, Skinner M, Shirahama T, et al: Diagnosis of amyloidosis by abdominal fat aspiration. Analysis of four years' experience. Am J Med 82(3):412-414, 1987.
    • (1987) Am J Med , vol.82 , Issue.3 , pp. 412-414
    • Duston, M.A.1    Skinner, M.2    Shirahama, T.3
  • 51
    • 0023904685 scopus 로고
    • Utility of subcutaneous fat aspiration for the diagnosis of systemic amyloidosis (immunoglobulin light chain)
    • Gertz MA, Li CY, Shirahama T, et al: Utility of subcutaneous fat aspiration for the diagnosis of systemic amyloidosis (immunoglobulin light chain). Arch Intern Med 148(4):929-933, 1988.
    • (1988) Arch Intern Med , vol.148 , Issue.4 , pp. 929-933
    • Gertz, M.A.1    Li, C.Y.2    Shirahama, T.3
  • 52
    • 0031020081 scopus 로고    scopus 로고
    • Diagnostic screening of systemic amyloidosis by abdominal fat aspiration: An analysis of 100 cases
    • Masouye I: Diagnostic screening of systemic amyloidosis by abdominal fat aspiration: An analysis of 100 cases. Am J Dermatopathol 19(1):41-45, 1997.
    • (1997) Am J Dermatopathol , vol.19 , Issue.1 , pp. 41-45
    • Masouye, I.1
  • 53
    • 0032574901 scopus 로고    scopus 로고
    • Current concepts: Neuropathies associated with paraproteinemia
    • Ropper A, Gorson K: Current concepts: Neuropathies associated with paraproteinemia. N Engl J Med 338:1601-1607, 1998.
    • (1998) N Engl J Med , vol.338 , pp. 1601-1607
    • Ropper, A.1    Gorson, K.2
  • 54
    • 0032033026 scopus 로고    scopus 로고
    • Prognosis of patients with primary systemic amyloidosis who present with dominant neuropathy
    • 1998
    • Rajkumar SV, Gertz MA, Kyle RA. Prognosis of patients with primary systemic amyloidosis who present with dominant neuropathy. Am J Med. 1998;104(3):232-237, 1998.
    • (1998) Am J Med. , vol.104 , Issue.3 , pp. 232-237
    • Rajkumar, S.V.1    Gertz, M.A.2    Kyle, R.A.3
  • 55
    • 0011979228 scopus 로고    scopus 로고
    • Functional study of autonomic neuropathy in primary (AL) amyloidosis
    • Gemmi F, Miliani A, Bergesio F, et al: Functional study of autonomic neuropathy in primary (AL) amyloidosis. Amyloid 3(3):167-172, 1996.
    • (1996) Amyloid , vol.3 , Issue.3 , pp. 167-172
    • Gemmi, F.1    Miliani, A.2    Bergesio, F.3
  • 56
    • 0032153516 scopus 로고    scopus 로고
    • The assessment of autonomic function in patients with systemic amyloidosis: Methodological considerations
    • Reyners AK, Hazenberg BP, Haagsma EB, et al: The assessment of autonomic function in patients with systemic amyloidosis: methodological considerations. Amyloid 5(3):193-199, 1998.
    • (1998) Amyloid , vol.5 , Issue.3 , pp. 193-199
    • Reyners, A.K.1    Hazenberg, B.P.2    Haagsma, E.B.3
  • 57
    • 0030004744 scopus 로고    scopus 로고
    • Myopathy in primary systemic amyloidosis
    • Gertz MA, Kyle RA: Myopathy in primary systemic amyloidosis. J Neurol Neurosurg Psychiatry 60(6):655-660, 1996.
    • (1996) J Neurol Neurosurg Psychiatry , vol.60 , Issue.6 , pp. 655-660
    • Gertz, M.A.1    Kyle, R.A.2
  • 58
    • 0021256934 scopus 로고
    • Systemic amyloid myopathy - Light-microscopic and fine-structural study of the skeletal muscles with histochemical and immunohistochemical study of amyloid
    • Ii K, Hizawa K, Nunomura S, et al: Systemic amyloid myopathy - light-microscopic and fine-structural study of the skeletal muscles with histochemical and immunohistochemical study of amyloid. Acta Neuropathol 64(2):114-121, 1984.
    • (1984) Acta Neuropathol , vol.64 , Issue.2 , pp. 114-121
    • Ii, K.1    Hizawa, K.2    Nunomura, S.3
  • 59
    • 0023230083 scopus 로고
    • Proximal weakness of the extremities as main feature of amyloid myopathy
    • Jennekens FG, Wokke JH: Proximal weakness of the extremities as main feature of amyloid myopathy. J Neurol Neurosurg Psychiatry 50(10):1353-1358, 1987.
    • (1987) J Neurol Neurosurg Psychiatry , vol.50 , Issue.10 , pp. 1353-1358
    • Jennekens, F.G.1    Wokke, J.H.2
  • 60
    • 0031900944 scopus 로고    scopus 로고
    • Amyloid myopathy: Clinicopathologic study of 16 cases
    • Prayson RA: Amyloid myopathy: Clinicopathologic study of 16 cases. Hum Pathol 29(5):463-468, 1998.
    • (1998) Hum Pathol , vol.29 , Issue.5 , pp. 463-468
    • Prayson, R.A.1
  • 61
    • 0025804559 scopus 로고
    • Cranial neuropathy associated with primary amyloidosis
    • Traynor AE, Gertz MA, Kyle RA: Cranial neuropathy associated with primary amyloidosis. Ann Neurol 29(4):451-454, 1991.
    • (1991) Ann Neurol , vol.29 , Issue.4 , pp. 451-454
    • Traynor, A.E.1    Gertz, M.A.2    Kyle, R.A.3
  • 62
    • 0030022521 scopus 로고    scopus 로고
    • Pulmonary amyloidosis. The Mayo Clinic experience from 1980 to 1993
    • Utz JP, Swensen SJ, Gertz MA: Pulmonary amyloidosis. The Mayo Clinic experience from 1980 to 1993. Ann Intern Med 124(4):407-413, 1996.
    • (1996) Ann Intern Med , vol.124 , Issue.4 , pp. 407-413
    • Utz, J.P.1    Swensen, S.J.2    Gertz, M.A.3
  • 63
    • 0018159080 scopus 로고
    • Patterns of pulmonary involvement in systemic amyloidosis
    • Celli BR, Rubinow A, Cohen AS, et al: Patterns of pulmonary involvement in systemic amyloidosis. Chest 74(5):543-547, 1978.
    • (1978) Chest , vol.74 , Issue.5 , pp. 543-547
    • Celli, B.R.1    Rubinow, A.2    Cohen, A.S.3
  • 64
    • 0027328843 scopus 로고
    • Symptomatic gastric amyloidosis in patients with primary systemic amyloidosis
    • Menke DM, Kyle RA, Fleming CR, et al: Symptomatic gastric amyloidosis in patients with primary systemic amyloidosis. Mayo Clin Proc 68(8):763-767, 1993.
    • (1993) Mayo Clin Proc , vol.68 , Issue.8 , pp. 763-767
    • Menke, D.M.1    Kyle, R.A.2    Fleming, C.R.3
  • 65
    • 0027487913 scopus 로고
    • Intestinal pseudo-obstruction in patients with amyloidosis: Clinicopathologic differences between chemical types of amyloid protein
    • Tada S, Iida M, Yao T, et al: Intestinal pseudo-obstruction in patients with amyloidosis: Clinicopathologic differences between chemical types of amyloid protein [see comments]. Gut 34(10):1412-1417, 1993.
    • (1993) Gut , vol.34 , Issue.10 , pp. 1412-1417
    • Tada, S.1    Iida, M.2    Yao, T.3
  • 66
    • 0014864577 scopus 로고
    • Roentgenologic appearance of systemic amyloidosis involving gastrointestinal tract
    • Legge DA, Carlson HC, Wollaeger EE: Roentgenologic appearance of systemic amyloidosis involving gastrointestinal tract. Am J Roentgenol Radium Ther Nucl Med 110(2):406-412, 1970.
    • (1970) Am J Roentgenol Radium Ther Nucl Med , vol.110 , Issue.2 , pp. 406-412
    • Legge, D.A.1    Carlson, H.C.2    Wollaeger, E.E.3
  • 67
    • 0022702636 scopus 로고
    • Amyloidosis and plasma cell dyscrasias: Gastrointestinal involvement
    • Carlson HC, Breen JF: Amyloidosis and plasma cell dyscrasias: Gastrointestinal involvement. Sem Roentgenol 21(2):128-138, 1986.
    • (1986) Sem Roentgenol , vol.21 , Issue.2 , pp. 128-138
    • Carlson, H.C.1    Breen, J.F.2
  • 68
    • 0031011856 scopus 로고    scopus 로고
    • Diffuse mesenteric amyloidosis
    • Mohan V, Kemp JA, Lewine HE, et al: Diffuse mesenteric amyloidosis. Dig Dis Sci 42(5):1079-1082, 1997.
    • (1997) Dig Dis Sci , vol.42 , Issue.5 , pp. 1079-1082
    • Mohan, V.1    Kemp, J.A.2    Lewine, H.E.3
  • 69
    • 0021332046 scopus 로고
    • Hepatic amyloidosis. A histopathologic analysis of primary (AL) and secondary (AA) forms
    • Chopra S, Rubinow A, Koff RS, et al: Hepatic amyloidosis. A histopathologic analysis of primary (AL) and secondary (AA) forms. Am J Pathol 115(2):186-193, 1984.
    • (1984) Am J Pathol , vol.115 , Issue.2 , pp. 186-193
    • Chopra, S.1    Rubinow, A.2    Koff, R.S.3
  • 70
    • 0031810645 scopus 로고    scopus 로고
    • The liver in systemic amyloidosis: Insights from 1231 serum amyloid P component scintigraphy in 484 patients
    • Lovat LB, Persey MR, Madhoo S, et al: The liver in systemic amyloidosis: Insights from 1231 serum amyloid P component scintigraphy in 484 patients. Gut 42(5):727-734, 1998.
    • (1998) Gut , vol.42 , Issue.5 , pp. 727-734
    • Lovat, L.B.1    Persey, M.R.2    Madhoo, S.3
  • 71
    • 0031022077 scopus 로고    scopus 로고
    • Hepatic amyloidosis: Clinical appraisal in 77 patients
    • Gertz MA, Kyle RA: Hepatic amyloidosis: Clinical appraisal in 77 patients. Hepatology 25(1):118-121, 1997.
    • (1997) Hepatology , vol.25 , Issue.1 , pp. 118-121
    • Gertz, M.A.1    Kyle, R.A.2
  • 72
    • 0024564054 scopus 로고
    • Spontaneous rupture of the liver associated with amyloidosis
    • Ades CJ, Strutton GM, Walker NI, et al: Spontaneous rupture of the liver associated with amyloidosis. J Clin Gastroenterol 11(1):85-87, 1989.
    • (1989) J Clin Gastroenterol , vol.11 , Issue.1 , pp. 85-87
    • Ades, C.J.1    Strutton, G.M.2    Walker, N.I.3
  • 74
    • 84944969547 scopus 로고
    • Bleeding manifestations in 100 patients with amyloidosis
    • Yood RA, Skinner M, Rubinow A, et al: Bleeding manifestations in 100 patients with amyloidosis. JAMA 249(10):1322-1324, 1983.
    • (1983) JAMA , vol.249 , Issue.10 , pp. 1322-1324
    • Yood, R.A.1    Skinner, M.2    Rubinow, A.3
  • 75
    • 0028867184 scopus 로고
    • Primary amyloidosis co-presenting with cervical and massive intra-abdominal lymphadenopathy
    • Segalov E, Gibson J, Joshua DE, et al: Primary amyloidosis co-presenting with cervical and massive intra-abdominal lymphadenopathy. Leuk Lymphoma 19(5-6):519-520, 1995.
    • (1995) Leuk Lymphoma , vol.19 , Issue.5-6 , pp. 519-520
    • Segalov, E.1    Gibson, J.2    Joshua, D.E.3
  • 76
    • 0022298540 scopus 로고
    • Primary amyloidosis causing macroglossia and respiratory symptoms
    • Hammersley N, Moos KF: Primary amyloidosis causing macroglossia and respiratory symptoms. Br J Oral Maxillofac Surg 23(6):445-449, 1985.
    • (1985) Br J Oral Maxillofac Surg , vol.23 , Issue.6 , pp. 445-449
    • Hammersley, N.1    Moos, K.F.2
  • 78
    • 0025902344 scopus 로고
    • Primary systemic amyloidosis causing diffuse alopecia by telogen arrest
    • Hunt SJ, Caserio RJ, Abell E: Primary systemic amyloidosis causing diffuse alopecia by telogen arrest (letter). Arch Dermatol 127(7):1067-1068, 1991.
    • (1991) Arch Dermatol , vol.127 , Issue.7 , pp. 1067-1068
    • Hunt, S.J.1    Caserio, R.J.2    Abell, E.3
  • 79
    • 0019740481 scopus 로고
    • Alopecia universalis. a manifestation of occult amyloidosis and multiple myeloma
    • Wheeler GE, Barrows GH: Alopecia universalis. A manifestation of occult amyloidosis and multiple myeloma. Arch Dermatol 117(12):815-816, 1981.
    • (1981) Arch Dermatol , vol.117 , Issue.12 , pp. 815-816
    • Wheeler, G.E.1    Barrows, G.H.2
  • 80
    • 0028360629 scopus 로고
    • Primary nodular cutaneous amyloidosis - Long-term follow-up and treatment
    • Vestey JP, Tidman MJ, McLaren KM: Primary nodular cutaneous amyloidosis - long-term follow-up and treatment. Clin Exp Dermatol 19(2):159-162, 1994.
    • (1994) Clin Exp Dermatol , vol.19 , Issue.2 , pp. 159-162
    • Vestey, J.P.1    Tidman, M.J.2    McLaren, K.M.3
  • 81
    • 0029826864 scopus 로고    scopus 로고
    • Nodular localized cutaneous amyloidosis: Detection of monoclonality of infiltrating plasma cells by polymerase chain reaction
    • Hagari Y, Mihara M, Hagari S: Nodular localized cutaneous amyloidosis: Detection of monoclonality of infiltrating plasma cells by polymerase chain reaction. Br J Dermatol 135(4):630-633, 1996.
    • (1996) Br J Dermatol , vol.135 , Issue.4 , pp. 630-633
    • Hagari, Y.1    Mihara, M.2    Hagari, S.3
  • 82
    • 0028020454 scopus 로고
    • Endocrine abnormalities in patients with amyloidosis
    • el-Reshaid KA, Hakim AA, Hourani HA, et al: Endocrine abnormalities in patients with amyloidosis. Ren Fail 16(6):725-730, 1994.
    • (1994) Ren Fail , vol.16 , Issue.6 , pp. 725-730
    • El-Reshaid, K.A.1    Hakim, A.A.2    Hourani, H.A.3
  • 83
    • 0029033105 scopus 로고
    • Hypothyroidism in association with systemic amyloidosis
    • Rich MW: Hypothyroidism in association with systemic amyloidosis. Head Neck 17(4):343-345, 1995.
    • (1995) Head Neck , vol.17 , Issue.4 , pp. 343-345
    • Rich, M.W.1
  • 84
    • 0029087112 scopus 로고
    • Occult adrenal insufficiency secondary to amyloidosis in the context of chronic renal failure
    • Harvey CJ, Gower PE, Hawkins PN, et al: Occult adrenal insufficiency secondary to amyloidosis in the context of chronic renal failure. Nephrol Dial Transplant 10(7):1237-1239, 1995.
    • (1995) Nephrol Dial Transplant , vol.10 , Issue.7 , pp. 1237-1239
    • Harvey, C.J.1    Gower, P.E.2    Hawkins, P.N.3
  • 85
    • 0025169118 scopus 로고
    • Subclinical adrenocortical insufficiency in renal amyloidosis
    • Arik N, Tasdemir I, Karaaslan Y, et al: Subclinical adrenocortical insufficiency in renal amyloidosis. Nephron 56(3):246-248, 1990.
    • (1990) Nephron , vol.56 , Issue.3 , pp. 246-248
    • Arik, N.1    Tasdemir, I.2    Karaaslan, Y.3
  • 86
    • 0025079444 scopus 로고
    • Adrenal dysfunction in patients with renal amyloid
    • Danby P, Harris KP, Williams B, et al: Adrenal dysfunction in patients with renal amyloid. Q J Med 76(281):915-922, 1990.
    • (1990) Q J Med , vol.76 , Issue.281 , pp. 915-922
    • Danby, P.1    Harris, K.P.2    Williams, B.3
  • 88
    • 0020611171 scopus 로고
    • Hypogonadism and massive testicular infiltration due to amyloidosis
    • Handelsman DJ, Yue DK, Turtle JR: Hypogonadism and massive testicular infiltration due to amyloidosis. J Urol 129(3):610-612, 1983.
    • (1983) J Urol , vol.129 , Issue.3 , pp. 610-612
    • Handelsman, D.J.1    Yue, D.K.2    Turtle, J.R.3
  • 89
    • 1842527698 scopus 로고    scopus 로고
    • Transthyretin amyloidosis
    • Benson MD, Uemichi T: Transthyretin amyloidosis [review]. Amyloid 3(1):44-56, 1996.
    • (1996) Amyloid , vol.3 , Issue.1 , pp. 44-56
    • Benson, M.D.1    Uemichi, T.2
  • 90
    • 0026323364 scopus 로고
    • Irish (Donegal) amyloidosis is associated with the transthyretin ALA60 (Appalachian) variant
    • Staunton H, Davis MB, Guiloff RJ, et al: Irish (Donegal) amyloidosis is associated with the transthyretin ALA60 (Appalachian) variant. Brain 114(Pt 6):2675-2679, 1991.
    • (1991) Brain , vol.114 , Issue.6 PART , pp. 2675-2679
    • Staunton, H.1    Davis, M.B.2    Guiloff, R.J.3
  • 91
    • 0023222657 scopus 로고
    • Hereditary amyloidosis: Description of a new American kindred with late onset cardiomyopathy. Appalachian amyloid
    • Benson MD, Wallace MR, Tejada E, et al: Hereditary amyloidosis: Description of a new American kindred with late onset cardiomyopathy. Appalachian amyloid. Arthritis Rheum 30(2):195-200, 1987.
    • (1987) Arthritis Rheum , vol.30 , Issue.2 , pp. 195-200
    • Benson, M.D.1    Wallace, M.R.2    Tejada, E.3
  • 92
    • 0030744403 scopus 로고    scopus 로고
    • Familial and primary (AL) cardiac amyloidosis: Echocardiographically similar diseases with distinctly different clinical outcomes
    • Dubrey SW, Cha K, Skinner M, et al: Familial and primary (AL) cardiac amyloidosis: Echocardiographically similar diseases with distinctly different clinical outcomes [see comments]. Heart 78(1):74-82, 1997.
    • (1997) Heart , vol.78 , Issue.1 , pp. 74-82
    • Dubrey, S.W.1    Cha, K.2    Skinner, M.3
  • 93
    • 0024560416 scopus 로고
    • Systemic senile amyloidosis. Identification of a new prealbumin (transthyretin) variant in cardiac tissue: Immunologic and biochemical similarity to one form of familial amyloidotic polyneuropathy
    • Gorevic PD, Prelli FC, Wright J, et al: Systemic senile amyloidosis. Identification of a new prealbumin (transthyretin) variant in cardiac tissue: Immunologic and biochemical similarity to one form of familial amyloidotic polyneuropathy. J Clin Invest 83(3):836-843, 1989.
    • (1989) J Clin Invest , vol.83 , Issue.3 , pp. 836-843
    • Gorevic, P.D.1    Prelli, F.C.2    Wright, J.3
  • 94
    • 44949277138 scopus 로고
    • Senile cardiac amyloidosis associated with homozygosity for a transthyretin variant (ILE-122)
    • Nichols WC, Liepnieks JJ, Snyder EL, et al: Senile cardiac amyloidosis associated with homozygosity for a transthyretin variant (ILE-122). J Lab Clin Med 117(3):175-180, 1991.
    • (1991) J Lab Clin Med , vol.117 , Issue.3 , pp. 175-180
    • Nichols, W.C.1    Liepnieks, J.J.2    Snyder, E.L.3
  • 95
    • 0025335359 scopus 로고
    • A homozygous transthyretin variant associated with senile systemic amyloidosis: Evidence for a late-onset disease of genetic etiology
    • Jacobson DR, Gorevic PD, Buxbaum JN: A homozygous transthyretin variant associated with senile systemic amyloidosis: Evidence for a late-onset disease of genetic etiology. Am J Hum Gen 47(1):127-136, 1990.
    • (1990) Am J Hum Gen , vol.47 , Issue.1 , pp. 127-136
    • Jacobson, D.R.1    Gorevic, P.D.2    Buxbaum, J.N.3
  • 96
    • 0025169627 scopus 로고
    • Cardiac amyloidosis: Report of a patient heterozygous for the transthyretin isoleucine 122 variant
    • Saraiva MJ, Sherman W, Marboe C, et al: Cardiac amyloidosis: Report of a patient heterozygous for the transthyretin isoleucine 122 variant. Scand J Immunol 32(4):341-346, 1990.
    • (1990) Scand J Immunol , vol.32 , Issue.4 , pp. 341-346
    • Saraiva, M.J.1    Sherman, W.2    Marboe, C.3
  • 97
    • 0031928747 scopus 로고    scopus 로고
    • A review of the amyloidoses that infiltrate the heart
    • McCarthy RE 3rd, Kasper EK: A review of the amyloidoses that infiltrate the heart. Clin Cardiol 21(8):547-552, 1998.
    • (1998) Clin Cardiol , vol.21 , Issue.8 , pp. 547-552
    • McCarthy III, R.E.1    Kasper, E.K.2
  • 98
    • 0032012657 scopus 로고    scopus 로고
    • Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide
    • Kiuru S: Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide [review]. Amyloid 5(1):55-66, 1998.
    • (1998) Amyloid , vol.5 , Issue.1 , pp. 55-66
    • Kiuru, S.1
  • 99
    • 0025779730 scopus 로고
    • Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin
    • Maury CP: Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin. J Clin Invest 87(4):1195-1199, 1991.
    • (1991) J Clin Invest , vol.87 , Issue.4 , pp. 1195-1199
    • Maury, C.P.1
  • 100
    • 0029948966 scopus 로고    scopus 로고
    • Hereditary hepatic and systemic amyloidosis caused by a new deletion/insertion mutation in the apolipoprotein AI gene
    • Booth DR, Tan SY, Booth SE, et al: Hereditary hepatic and systemic amyloidosis caused by a new deletion/insertion mutation in the apolipoprotein AI gene. J Clin Invest 97(12):2714-2721, 1996.
    • (1996) J Clin Invest , vol.97 , Issue.12 , pp. 2714-2721
    • Booth, D.R.1    Tan, S.Y.2    Booth, S.E.3
  • 101
    • 0028803995 scopus 로고
    • A new apolipoprotein Al variant, Trp50Arg, causes hereditary amyloidosis
    • Booth DR, Tan SY, Booth SE, et al: A new apolipoprotein Al variant, Trp50Arg, causes hereditary amyloidosis. QJM 88(10):695-702, 1995.
    • (1995) QJM , vol.88 , Issue.10 , pp. 695-702
    • Booth, D.R.1    Tan, S.Y.2    Booth, S.E.3
  • 102
    • 0032153493 scopus 로고    scopus 로고
    • Fibrinogen a alpha chain Leu 554: An African-American kindred with late onset renal amyloidosis
    • Uemichi T, Liepnieks JJ, Gertz MA, et al: Fibrinogen A alpha chain Leu 554: An African-American kindred with late onset renal amyloidosis. Amyloid 5(3):188-192, 1998.
    • (1998) Amyloid , vol.5 , Issue.3 , pp. 188-192
    • Uemichi, T.1    Liepnieks, J.J.2    Gertz, M.A.3
  • 103
    • 0028211154 scopus 로고
    • Hereditary renal amyloidosis with a novel variant fibrinogen
    • Uemichi T, Liepnieks JJ, Benson MD: Hereditary renal amyloidosis with a novel variant fibrinogen. J Clin Invest 93(2):731-736, 1994.
    • (1994) J Clin Invest , vol.93 , Issue.2 , pp. 731-736
    • Uemichi, T.1    Liepnieks, J.J.2    Benson, M.D.3
  • 104
    • 0027465319 scopus 로고
    • Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain
    • Benson MD, Liepnieks J, Uemichi T, et al: Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain [see comments]. Nat Genet 3(3):252-255, 1993.
    • (1993) Nat Genet , vol.3 , Issue.3 , pp. 252-255
    • Benson, M.D.1    Liepnieks, J.2    Uemichi, T.3
  • 105
    • 0030032783 scopus 로고    scopus 로고
    • "Fragile" liver and massive hepatic haemorrhage due to hereditary amyloidosis
    • Harrison RF, Hawkins PN, Roche WR, et al: "Fragile" liver and massive hepatic haemorrhage due to hereditary amyloidosis. Gut 38(1):151-152, 1996.
    • (1996) Gut , vol.38 , Issue.1 , pp. 151-152
    • Harrison, R.F.1    Hawkins, P.N.2    Roche, W.R.3
  • 106
    • 0027506498 scopus 로고
    • Human lysozyme gene mutations cause hereditary systemic amyloidosis
    • Pepys MB, Hawkins PN, Booth DR, et al: Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362(6420):553-557, 1993.
    • (1993) Nature , vol.362 , Issue.6420 , pp. 553-557
    • Pepys, M.B.1    Hawkins, P.N.2    Booth, D.R.3
  • 107
    • 0030245783 scopus 로고    scopus 로고
    • Progressive dementia and leucoencephalopathy as the initial presentation of late onset hereditary cystatin-C amyloidosis. Clinicopathological presentation of two cases
    • Sveinbjornsdottir S, Blondal H, Gudmundsson G, et al: Progressive dementia and leucoencephalopathy as the initial presentation of late onset hereditary cystatin-C amyloidosis. Clinicopathological presentation of two cases. J Neurol Sci 140(1-2):101-108, 1996.
    • (1996) J Neurol Sci , vol.140 , Issue.1-2 , pp. 101-108
    • Sveinbjornsdottir, S.1    Blondal, H.2    Gudmundsson, G.3
  • 108
    • 0026378765 scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis - Dutch type: A congophilic angiopathy. An overview
    • Roos RA, Haan J, Van Broeckhoven C: Hereditary cerebral hemorrhage with amyloidosis - Dutch type: A congophilic angiopathy. An overview. Ann N Y Acad Sci 640:155-160, 1991.
    • (1991) Ann N Y Acad Sci , vol.640 , pp. 155-160
    • Roos, R.A.1    Haan, J.2    Van Broeckhoven, C.3
  • 109
    • 0032412970 scopus 로고    scopus 로고
    • A simple screening test for variant transthyretins associated with familial transthyretin amyloidosis using isoelectric focusing
    • Connors LH, Ericsson T, Skare J, et al: A simple screening test for variant transthyretins associated with familial transthyretin amyloidosis using isoelectric focusing. Biochim Biophys Acta 1407(3):185-192, 1998.
    • (1998) Biochim Biophys Acta , vol.1407 , Issue.3 , pp. 185-192
    • Connors, L.H.1    Ericsson, T.2    Skare, J.3
  • 110
    • 0025997625 scopus 로고
    • Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide-like immunoreactivity
    • Pucci A, Wharton J, Arbustini E, et al: Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide-like immunoreactivity. J Pathol 165(3):235-241, 1991.
    • (1991) J Pathol , vol.165 , Issue.3 , pp. 235-241
    • Pucci, A.1    Wharton, J.2    Arbustini, E.3
  • 111
    • 0027161613 scopus 로고
    • Isolated atrial amyloidosis: A clinicopathologic study indicating increased prevalence in chronic heart disease
    • Looi LM: Isolated atrial amyloidosis: A clinicopathologic study indicating increased prevalence in chronic heart disease. Hum Pathol 24(6):602-607, 1993.
    • (1993) Hum Pathol , vol.24 , Issue.6 , pp. 602-607
    • Looi, L.M.1
  • 112
    • 0032520388 scopus 로고    scopus 로고
    • Expression of atrial and brain natriuretic peptides and their genes in hearts of patients with cardiac amyloidosis
    • Takemura G, Takatsu Y, Doyama K, et al: Expression of atrial and brain natriuretic peptides and their genes in hearts of patients with cardiac amyloidosis. J Am Coll Cardiol 31(4):754-765, 1998.
    • (1998) J Am Coll Cardiol , vol.31 , Issue.4 , pp. 754-765
    • Takemura, G.1    Takatsu, Y.2    Doyama, K.3
  • 113
    • 0032010958 scopus 로고    scopus 로고
    • Ultrastructural evidence for the formation of amyloid fibrils within cardiomyocytes in isolated atrial amyloid
    • Takahashi M, Hoshii Y, Kawano H, et al: Ultrastructural evidence for the formation of amyloid fibrils within cardiomyocytes in isolated atrial amyloid. Amyloid 5(1):35-42, 1998.
    • (1998) Amyloid , vol.5 , Issue.1 , pp. 35-42
    • Takahashi, M.1    Hoshii, Y.2    Kawano, H.3
  • 114
    • 0020519870 scopus 로고
    • Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation
    • Cornwell GG, Murdoch WL, Kyle RA, et al: Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation. Am J Med 75(4):618-623, 1983.
    • (1983) Am J Med , vol.75 , Issue.4 , pp. 618-623
    • Cornwell, G.G.1    Murdoch, W.L.2    Kyle, R.A.3
  • 115
    • 0020308777 scopus 로고
    • Immunohistochemical identification and cross reactions of amyloid fibril proteins in senile heart and amyloid in familial polyneuropathy. Lack of reactivity with cerebral amyloid in Alzheimer's disease
    • Linke RP: Immunohistochemical identification and cross reactions of amyloid fibril proteins in senile heart and amyloid in familial polyneuropathy. Lack of reactivity with cerebral amyloid in Alzheimer's disease. Clin Neuropathol 1(4):172-182, 1982.
    • (1982) Clin Neuropathol , vol.1 , Issue.4 , pp. 172-182
    • Linke, R.P.1
  • 116
    • 0019825401 scopus 로고
    • Senile cardiac amyloid: Evidence that fibrils contain a protein immunologically related to prealbumin
    • Cornwell GG, Westermark P, Natvig JB, et al: Senile cardiac amyloid: Evidence that fibrils contain a protein immunologically related to prealbumin. Immunology 44(3):447-452, 1981.
    • (1981) Immunology , vol.44 , Issue.3 , pp. 447-452
    • Cornwell, G.G.1    Westermark, P.2    Natvig, J.B.3
  • 117
    • 0030272240 scopus 로고    scopus 로고
    • The premortem recognition of systemic senile amyloidosis with cardiac involvement
    • Kyle RA, Spittell PC, Gertz MA, et al: The premortem recognition of systemic senile amyloidosis with cardiac involvement. Am J Med 101(4):395-400, 1996.
    • (1996) Am J Med , vol.101 , Issue.4 , pp. 395-400
    • Kyle, R.A.1    Spittell, P.C.2    Ma, G.3
  • 118
    • 0025936525 scopus 로고
    • Secondary systemic amyloidosis: Response and survival in 64 patients
    • Gertz MA, Kyle RA: Secondary systemic amyloidosis: Response and survival in 64 patients. Medicine 70(4):246-256, 1991.
    • (1991) Medicine , vol.70 , Issue.4 , pp. 246-256
    • Gertz, M.A.1    Kyle, R.A.2
  • 119
    • 0031837483 scopus 로고    scopus 로고
    • Renal transplantation in secondary systemic amyloidosis
    • Heering P, Hetzel R, Grabensee B, et al: Renal transplantation in secondary systemic amyloidosis. Clin Transpl 12(3):159-164, 1998.
    • (1998) Clin Transpl , vol.12 , Issue.3 , pp. 159-164
    • Heering, P.1    Hetzel, R.2    Grabensee, B.3
  • 120
    • 0030918593 scopus 로고    scopus 로고
    • Secondary amyloidosis in ankylosing spondylitis. a systematic survey of 137 patients using abdominal fat aspiration
    • Gratacos J, Orellana C, Sanmarti R, et al: Secondary amyloidosis in ankylosing spondylitis. A systematic survey of 137 patients using abdominal fat aspiration. J Rheumatol 24(5):912-915, 1997.
    • (1997) J Rheumatol , vol.24 , Issue.5 , pp. 912-915
    • Gratacos, J.1    Orellana, C.2    Sanmarti, R.3
  • 121
    • 0030693617 scopus 로고    scopus 로고
    • Secondary amyloidosis in the course of idiopathic myelofibrosis
    • Ferhanoglu B, Erzin Y, Baslar Z, et al: Secondary amyloidosis in the course of idiopathic myelofibrosis. Leukemia Res 21(9):897-898, 1997.
    • (1997) Leukemia Res , vol.21 , Issue.9 , pp. 897-898
    • Ferhanoglu, B.1    Erzin, Y.2    Baslar, Z.3
  • 122
    • 0029879139 scopus 로고    scopus 로고
    • Secondary amyloidosis following juvenile chronic arthritis
    • Sarkar B, Singh S, Suri M, et al: Secondary amyloidosis following juvenile chronic arthritis. Indian Pediatr 33(2):125-127, 1996.
    • (1996) Indian Pediatr , vol.33 , Issue.2 , pp. 125-127
    • Sarkar, B.1    Singh, S.2    Suri, M.3
  • 123
    • 0029892828 scopus 로고    scopus 로고
    • Secondary amyloidosis complicating arthropathic psoriasis
    • Tsuda S, Maeyama Y, Yamamoto N, et al: Secondary amyloidosis complicating arthropathic psoriasis. Clin Exp Dermatol 21(2):141-144, 1996.
    • (1996) Clin Exp Dermatol , vol.21 , Issue.2 , pp. 141-144
    • Tsuda, S.1    Maeyama, Y.2    Yamamoto, N.3
  • 124
    • 0025764944 scopus 로고
    • Secondary amyloidosis in chronic osteomyelitis
    • Alabi ZO, Ojo OS, Odesanmi WO: Secondary amyloidosis in chronic osteomyelitis. Int Orthop 15(1):21-22, 1991.
    • (1991) Int Orthop , vol.15 , Issue.1 , pp. 21-22
    • Alabi, Z.O.1    Ojo, O.S.2    Odesanmi, W.O.3
  • 125
    • 0025854580 scopus 로고
    • Colchicine prophylaxis in familial Mediterranean fever: Reappraisal after 15 years
    • Ben-Chetrit E, Levy M: Colchicine prophylaxis in familial Mediterranean fever: Reappraisal after 15 years. Sem Arthritis Rheum 20(4):241-246, 1991.
    • (1991) Sem Arthritis Rheum , vol.20 , Issue.4 , pp. 241-246
    • Ben-Chetrit, E.1    Levy, M.2
  • 126
    • 0027356580 scopus 로고
    • The kidney in familial Mediterranean fever
    • Zemer D, Livneh A, Pras M, et al: The kidney in familial Mediterranean fever. Contrib Nephrol 102:187-197, 1993.
    • (1993) Contrib Nephrol , vol.102 , pp. 187-197
    • Zemer, D.1    Livneh, A.2    Pras, M.3
  • 127
    • 0028096627 scopus 로고
    • Colchicine treatment of AA amyloidosis of familial Mediterranean fever. An analysis of factors affecting outcome
    • Livneh A, Zemer D, Langevitz P, et al: Colchicine treatment of AA amyloidosis of familial Mediterranean fever. An analysis of factors affecting outcome. Arthritis Rheum 37(12):1804-1811, 1994.
    • (1994) Arthritis Rheum , vol.37 , Issue.12 , pp. 1804-1811
    • Livneh, A.1    Zemer, D.2    Langevitz, P.3
  • 128
    • 0031814513 scopus 로고    scopus 로고
    • Familial Mediterranean fever at the millennium. Clinical spectrum, ancient mutations, and a survey of 100 American referrals to the National Institutes of Health
    • Samuels J, Aksentijevich I, Torosyan Y, et al: Familial Mediterranean fever at the millennium. Clinical spectrum, ancient mutations, and a survey of 100 American referrals to the National Institutes of Health. Medicine 77(4):268-297, 1998.
    • (1998) Medicine , vol.77 , Issue.4 , pp. 268-297
    • Samuels, J.1    Aksentijevich, I.2    Torosyan, Y.3
  • 129
    • 0028874395 scopus 로고
    • Diagnostic approach to and follow-up of difficult cases of AL amyloidosis
    • Perfetti V, Garini P, Vignarelli MC, et al: Diagnostic approach to and follow-up of difficult cases of AL amyloidosis. Haematologica 80(5):409-415, 1995.
    • (1995) Haematologica , vol.80 , Issue.5 , pp. 409-415
    • Perfetti, V.1    Garini, P.2    Vignarelli, M.C.3
  • 130
    • 0032914224 scopus 로고    scopus 로고
    • Sequence of testing for monoclonal gammopathies - Serum and urine assays
    • Kyle RA: Sequence of testing for monoclonal gammopathies - serum and urine assays. Arch Pathol Lab Med 123(2):114-118, 1999.
    • (1999) Arch Pathol Lab Med , vol.123 , Issue.2 , pp. 114-118
    • Kyle, R.A.1
  • 131
    • 0025824386 scopus 로고
    • Classification of amyloidosis by the detection of clonal excess of plasma cells in the bone marrow
    • Gertz MA, Greipp PR, Kyle RA: Classification of amyloidosis by the detection of clonal excess of plasma cells in the bone marrow. J Lab Clin Med 118(1):33-39, 1991.
    • (1991) J Lab Clin Med , vol.118 , Issue.1 , pp. 33-39
    • Gertz, M.A.1    Greipp, P.R.2    Kyle, R.A.3
  • 132
    • 0026055179 scopus 로고
    • Gene rearrangement studies in the diagnosis of primary systemic and nodular primary localized cutaneous amyloidosis
    • Grunewald K, Sepp N, Weyrer K, et al: Gene rearrangement studies in the diagnosis of primary systemic and nodular primary localized cutaneous amyloidosis. J Invest Dermatol 97(4):693-696, 1991.
    • (1991) J Invest Dermatol , vol.97 , Issue.4 , pp. 693-696
    • Grunewald, K.1    Sepp, N.2    Weyrer, K.3
  • 133
    • 0029831695 scopus 로고    scopus 로고
    • Monoclonal origin of localised orbital amyloidosis detected by molecular analysis
    • Pasternak S, White VA, Gascoyne RD, et al: Monoclonal origin of localised orbital amyloidosis detected by molecular analysis. Br J Ophthalmol 80(11):1013-1017, 1996.
    • (1996) Br J Ophthalmol , vol.80 , Issue.11 , pp. 1013-1017
    • Pasternak, S.1    White, V.A.2    Gascoyne, R.D.3
  • 134
    • 0033556212 scopus 로고    scopus 로고
    • Characterization of transthyretin mutants from serum using immunoprecipitation, HPLC/electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry
    • Theberge R, Connors L, Skinner M, et al: Characterization of transthyretin mutants from serum using immunoprecipitation, HPLC/electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry. Anal Chem 71(2):452-459, 1999.
    • (1999) Anal Chem , vol.71 , Issue.2 , pp. 452-459
    • Theberge, R.1    Connors, L.2    Skinner, M.3
  • 135
    • 0029816662 scopus 로고    scopus 로고
    • The classification of amyloid deposits in clinicopathological practice
    • Rocken C, Schwotzer EB, Linke RP, et al: The classification of amyloid deposits in clinicopathological practice. Histopathology 29(4):325-335, 1996.
    • (1996) Histopathology , vol.29 , Issue.4 , pp. 325-335
    • Rocken, C.1    Schwotzer, E.B.2    Linke, R.P.3
  • 136
    • 0029147345 scopus 로고
    • High-sensitivity diagnosis of AA amyloidosis using Congo red and immunohistochemistry detects missed amyloid deposits
    • Linke RP, Gartner HV, Michels H: High-sensitivity diagnosis of AA amyloidosis using Congo red and immunohistochemistry detects missed amyloid deposits. J Histochem Cytochem 43(9):863-869, 1995.
    • (1995) J Histochem Cytochem , vol.43 , Issue.9 , pp. 863-869
    • Linke, R.P.1    Gartner, H.V.2    Michels, H.3
  • 137
    • 0020661450 scopus 로고
    • Sensitivity of technetium-99m-pyrophosphate scintigraphy in diagnosing cardiac amyloidosis
    • Falk RH, Lee VW, Rubinow A, et al: Sensitivity of technetium-99m-pyrophosphate scintigraphy in diagnosing cardiac amyloidosis. Am J Cardiol 51(5):826-830, 1983.
    • (1983) Am J Cardiol , vol.51 , Issue.5 , pp. 826-830
    • Falk, R.H.1    Lee, V.W.2    Rubinow, A.3
  • 138
    • 0021750397 scopus 로고
    • Cardiac technetium-99m pyrophosphate scintigraphy in familial amyloidosis
    • Falk RH, Lee VW, Rubinow A, et al: Cardiac technetium-99m pyrophosphate scintigraphy in familial amyloidosis. Am J Cardiol 54(8):1150-1151, 1984.
    • (1984) Am J Cardiol , vol.54 , Issue.8 , pp. 1150-1151
    • Falk, R.H.1    Lee, V.W.2    Rubinow, A.3
  • 139
    • 0029560611 scopus 로고
    • Cardiac and pleuropulmonary AL amyloid imaging with technetium-99m labelled aprotinin
    • Aprile C, Marinone G, Saponaro R, et al: Cardiac and pleuropulmonary AL amyloid imaging with technetium-99m labelled aprotinin. Eur J Nucl Med 22(12):1393-1401, 1995.
    • (1995) Eur J Nucl Med , vol.22 , Issue.12 , pp. 1393-1401
    • Aprile, C.1    Marinone, G.2    Saponaro, R.3
  • 140
    • 0023926566 scopus 로고
    • Diagnostic radionuclide imaging of amyloid: Biological targeting by circulating human serum amyloid P component
    • Hawkins PN, Myers MJ, Lavender JP, et al: Diagnostic radionuclide imaging of amyloid: biological targeting by circulating human serum amyloid P component. Lancet 1(8600):1413-1418, 1988.
    • (1988) Lancet , vol.1 , Issue.8600 , pp. 1413-1418
    • Hawkins, P.N.1    Myers, M.J.2    Lavender, J.P.3
  • 141
    • 0028129229 scopus 로고
    • Studies with radiolabelled serum amyloid P component provide evidence for turnover and regression of amyloid deposits in vivo
    • Hawkins PN: Studies with radiolabelled serum amyloid P component provide evidence for turnover and regression of amyloid deposits in vivo. Clin Sci 87(3):289-295, 1994.
    • (1994) Clin Sci , vol.87 , Issue.3 , pp. 289-295
    • Hawkins, P.N.1
  • 142
    • 0029031935 scopus 로고
    • Imaging amyloidosis with radiolabelled SAP
    • Hawkins PN, Pepys MB: Imaging amyloidosis with radiolabelled SAP (editorial). Eur J Nucl Med 1995;22(7):595-599.
    • (1995) Eur J Nucl Med , vol.22 , Issue.7 , pp. 595-599
    • Hawkins, P.N.1    Pepys, M.B.2
  • 143
    • 0021844895 scopus 로고
    • Worsening of congestive heart failure in amyloid heart disease treated by calcium channel-blocking agents
    • Gertz MA, Falk RH, Skinner M, et al: Worsening of congestive heart failure in amyloid heart disease treated by calcium channel-blocking agents. Am J Cardiol 55(13 Pt 1):1645, 1985.
    • (1985) Am J Cardiol , vol.55 , Issue.1 PART , pp. 1645
    • Gertz, M.A.1    Falk, R.H.2    Skinner, M.3
  • 144
    • 0021873337 scopus 로고
    • Selective binding of nifedipine to amyloid fibrils
    • Gertz MA, Skinner M, Connors LH, et al: Selective binding of nifedipine to amyloid fibrils. Am J Cardiol 55(13 Pt 1):1646, 1985.
    • (1985) Am J Cardiol , vol.55 , Issue.1 PART , pp. 1646
    • Gertz, M.A.1    Skinner, M.2    Connors, L.H.3
  • 145
    • 0027213967 scopus 로고
    • Left ventricular systolic dysfunction precipitated by verapamil in cardiac amyloidosis
    • Pollak A, Falk RH: Left ventricular systolic dysfunction precipitated by verapamil in cardiac amyloidosis. Chest 104(2):618-620, 1993.
    • (1993) Chest , vol.104 , Issue.2 , pp. 618-620
    • Pollak, A.1    Falk, R.H.2
  • 146
    • 0000497104 scopus 로고
    • Heart transplantation in AL amyloidosis
    • Dubrey S, Falk RH: Heart transplantation in AL amyloidosis. Amyloid 2(4):284-287, 1995.
    • (1995) Amyloid , vol.2 , Issue.4 , pp. 284-287
    • Dubrey, S.1    Falk, R.H.2
  • 147
    • 0028104590 scopus 로고
    • Cardiac transplantation for AL amyloidosis
    • Hall R, Hawkins PN: Cardiac transplantation for AL amyloidosis [clinical conference]. BMJ 309(6962):1135-1137, 1994.
    • (1994) BMJ , vol.309 , Issue.6962 , pp. 1135-1137
    • Hall, R.1    Hawkins, P.N.2
  • 148
    • 0031568563 scopus 로고    scopus 로고
    • Effectiveness of cardiac transplantation for primary (AL) cardiac amyloidosis
    • Pelosi F Jr, Capehart J, Roberts WC: Effectiveness of cardiac transplantation for primary (AL) cardiac amyloidosis. Am J Cardiol 79(4):532-535, 1997.
    • (1997) Am J Cardiol , vol.79 , Issue.4 , pp. 532-535
    • Pelosi Jr., F.1    Capehart, J.2    Roberts, W.C.3
  • 149
    • 0029082773 scopus 로고
    • Recurrence of primary (AL) amyloidosis in a transplanted heart with four-year survival
    • Dubrey S, Simms RW, Skinner M, et al: Recurrence of primary (AL) amyloidosis in a transplanted heart with four-year survival. Am J Cardiol 76(10):739-741, 1995.
    • (1995) Am J Cardiol , vol.76 , Issue.10 , pp. 739-741
    • Dubrey, S.1    Simms, R.W.2    Skinner, M.3
  • 150
    • 0026261681 scopus 로고
    • Progression of systemic disease and reduced long-term survival in patients with cardiac amyloidosis undergoing heart transplantation. Follow-up results of a multicenter survey
    • Hosenpud JD, DeMarco T, Frazier OH, et al: Progression of systemic disease and reduced long-term survival in patients with cardiac amyloidosis undergoing heart transplantation. Follow-up results of a multicenter survey. Circulation 84(5 Suppl):III338-343, 1991.
    • (1991) Circulation , vol.84 , Issue.5 SUPPL.
    • Hosenpud, J.D.1    Demarco, T.2    Frazier, O.H.3
  • 151
    • 0029591203 scopus 로고
    • Regression of the nephrotic syndrome in rheumatoid arthritis and amyloidosis treated with azathioprine. A case report
    • Shapiro DL, Spiera H: Regression of the nephrotic syndrome in rheumatoid arthritis and amyloidosis treated with azathioprine. A case report [see comments]. Arthritis Rheum 38(12):1851-1854, 1995.
    • (1995) Arthritis Rheum , vol.38 , Issue.12 , pp. 1851-1854
    • Shapiro, D.L.1    Spiera, H.2
  • 152
    • 0024519413 scopus 로고
    • Resolution of nephrotic syndrome and lack of progression of heroin-associated renal amyloidosis
    • Crowley S, Feinfeld DA, Janis R: Resolution of nephrotic syndrome and lack of progression of heroin-associated renal amyloidosis. Am J Kidney Dis 13(4):333-335, 1989.
    • (1989) Am J Kidney Dis , vol.13 , Issue.4 , pp. 333-335
    • Crowley, S.1    Feinfeld, D.A.2    Janis, R.3
  • 153
    • 0024374637 scopus 로고
    • Regression of amyloid in Crohn's disease after bowel resection. a 19-year follow-up
    • Mandelstam P, Simmons DE, Mitchell B: Regression of amyloid in Crohn's disease after bowel resection. A 19-year follow-up. J Clin Gastroenterol 11(3):324-326, 1989.
    • (1989) J Clin Gastroenterol , vol.11 , Issue.3 , pp. 324-326
    • Mandelstam, P.1    Simmons, D.E.2    Mitchell, B.3
  • 154
    • 0018580410 scopus 로고
    • Regression of amyloidosis secondary to granulomatous ileitis following surgical resection and colchicine administration
    • Ravid M, Shapira J, Kedar I, et al: Regression of amyloidosis secondary to granulomatous ileitis following surgical resection and colchicine administration. Acta Hepato-Gastroenterol 26(6):513-515, 1979.
    • (1979) Acta Hepato-Gastroenterol , vol.26 , Issue.6 , pp. 513-515
    • Ravid, M.1    Shapira, J.2    Kedar, I.3
  • 155
    • 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 79(6):708-716, 1985.
    • (1985) Am J Med , vol.79 , Issue.6 , pp. 708-716
    • Kyle, R.A.1    Greipp, P.R.2    Garton, J.P.3
  • 156
    • 0032525180 scopus 로고    scopus 로고
    • Dose-intensive melphalan with blood stem-cell support for the treatment of AL (amyloid light-chain) amyloidosis: Survival and responses in 25 patients
    • Comenzo RL, Vosburgh E, Falk RH, et al: Dose-intensive melphalan with blood stem-cell support for the treatment of AL (amyloid light-chain) amyloidosis: Survival and responses in 25 patients. Blood 91(10):3662-3670, 1998.
    • (1998) Blood , vol.91 , Issue.10 , pp. 3662-3670
    • Comenzo, R.L.1    Vosburgh, E.2    Falk, R.H.3
  • 157
    • 10144219963 scopus 로고    scopus 로고
    • Dose-intensive melphalan with blood stem cell support for the treatment of AL amyloidosis: One-year follow-up in five patients
    • Comenzo RL, Vosburgh E, Simms RW, et al: Dose-intensive melphalan with blood stem cell support for the treatment of AL amyloidosis: One-year follow-up in five patients. Blood 88(7):2801-2806, 1996.
    • (1996) Blood , vol.88 , Issue.7 , pp. 2801-2806
    • Comenzo, R.L.1    Vosburgh, E.2    Simms, R.W.3
  • 158
    • 0032986336 scopus 로고    scopus 로고
    • Intermediate-dose intravenous melphalan and blood stem cells mobilized with sequential GM+G-CSF or G-CSF alone to treat AL (amyloid light chain) amyloidosis
    • Comenzo RL, Sanchorawala V, Fisher C, et al: Intermediate-dose intravenous melphalan and blood stem cells mobilized with sequential GM+G-CSF or G-CSF alone to treat AL (amyloid light chain) amyloidosis. Br J Haematol 104(3):553-559, 1999.
    • (1999) Br J Haematol , vol.104 , Issue.3 , pp. 553-559
    • Comenzo, R.L.1    Sanchorawala, V.2    Fisher, C.3
  • 159
    • 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 86(3):855-861, 1995.
    • (1995) Blood , vol.86 , Issue.3 , pp. 855-861
    • Gianni, L.1    Bellotti, V.2    Gianni, A.M.3
  • 160
    • 0032934032 scopus 로고    scopus 로고
    • Treatment of AL amyloidosis with 4′-iodo-4′-deoxydoxorubicin: An update
    • Merlini G, Anesi E, Garihi P, et al: Treatment of AL amyloidosis with 4′-iodo-4′-deoxydoxorubicin: An update (letter). Blood 93(3):1112-1113, 1999.
    • (1999) Blood , vol.93 , Issue.3 , pp. 1112-1113
    • Merlini, G.1    Anesi, E.2    Garihi, P.3
  • 161
    • 0030805834 scopus 로고    scopus 로고
    • Progression of ventricular wall thickening after liver transplantation for familial amyloidosis
    • Dubrey SW, Davidoff R, Skinner M, et al: Progression of ventricular wall thickening after liver transplantation for familial amyloidosis. Transplantation 64(1):74-80, 1997.
    • (1997) Transplantation , vol.64 , Issue.1 , pp. 74-80
    • Dubrey, S.W.1    Davidoff, R.2    Skinner, M.3
  • 162
    • 0032558120 scopus 로고    scopus 로고
    • Progressive cardiac amyloidosis following liver transplantation for familial amyloid polyneuropathy: Implications for amyloid fibrillogenesis
    • Stangou AJ, Hawkins PN, Heaton ND, et al: Progressive cardiac amyloidosis following liver transplantation for familial amyloid polyneuropathy: Implications for amyloid fibrillogenesis. Transplantation 66(2):229-233, 1998.
    • (1998) Transplantation , vol.66 , Issue.2 , pp. 229-233
    • Stangou, A.J.1    Hawkins, P.N.2    Heaton, N.D.3


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