메뉴 건너뛰기




Volumn 51, Issue , 2000, Pages 543-569

The genetics of the amyloidoses

Author keywords

Alzheimer's disease; Amyloidosis; Familial Mediterranean fever; Serum amyloid A; Transthyretin

Indexed keywords

AMYLOID; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; PREALBUMIN; PRESENILIN 1; PRESENILIN 2; SERUM AMYLOID A;

EID: 0034088778     PISSN: 00664219     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.med.51.1.543     Document Type: Review
Times cited : (145)

References (138)
  • 1
    • 0033616575 scopus 로고    scopus 로고
    • Designing conditions for in vitro formation of amyloid protofilaments and fibrils
    • 1. Chiti F, Webster P, Taddei N, et al. 1999. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. USA 96:3590-94
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3590-3594
    • Chiti, F.1    Webster, P.2    Taddei, N.3
  • 2
    • 0027512354 scopus 로고
    • Disruption of the transthyretin gene results in mice with depressed levels of plasma retinol and thyroid hormone
    • 2. Episkopou V, Maeda S, Nishiguchi S, et al. 1993. Disruption of the transthyretin gene results in mice with depressed levels of plasma retinol and thyroid hormone. Proc. Natl. Acad. Sci. USA 90:2375-79
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2375-2379
    • Episkopou, V.1    Maeda, S.2    Nishiguchi, S.3
  • 4
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8A
    • 4. Blake CCF, Geisow MJ, Oatley SJ. 1978. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8A. J. Mol. Biol. 121:339-56
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.2    Oatley, S.J.3
  • 5
    • 0029062667 scopus 로고
    • Structure of a complex of two plasma proteins: Transthyretin and retinol-binding protein
    • 5. Monaco HL, Rizzi M, Coda A. 1995. Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein. Science 268:1039-41
    • (1995) Science , vol.268 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 6
    • 0021572408 scopus 로고
    • Cloning of human prealbumin complementary DNA. Localization of the gene to chromosome 18 and detection of a variant prealbumin allele in a family with familial amyloid polyneuropathy
    • 6. Whitehead AS, Skinner M, Bruns GAP, et al. 1984. Cloning of human prealbumin complementary DNA. Localization of the gene to chromosome 18 and detection of a variant prealbumin allele in a family with familial amyloid polyneuropathy. Mol. Biol. Med. 2:411-23
    • (1984) Mol. Biol. Med. , vol.2 , pp. 411-423
    • Whitehead, A.S.1    Skinner, M.2    Bruns, G.A.P.3
  • 8
    • 77957180065 scopus 로고
    • A peculiar form of peripheral neuropathy. Familial atypical generalized amyloidosis with special involvement of the peripheral nerves
    • 8. Andrade C. 1952. A peculiar form of peripheral neuropathy. Familial atypical generalized amyloidosis with special involvement of the peripheral nerves. Brain 75:408-27
    • (1952) Brain , vol.75 , pp. 408-427
    • Andrade, C.1
  • 9
    • 0016913418 scopus 로고
    • Familial amyloidosis with polyneuropathy. A clinical study based on patients living in Northern Sweden
    • 9. Andersson R. 1976. Familial amyloidosis with polyneuropathy. A clinical study based on patients living in Northern Sweden. Acta Med. Scand. Suppl. 590:1-64
    • (1976) Acta Med. Scand. Suppl. , vol.590 , pp. 1-64
    • Andersson, R.1
  • 10
    • 0021039138 scopus 로고
    • Genetic studies of familial amyloid polyneuropathy in the Arao district of Japan: 1. The genealogical survey
    • 10. Sakoda S, Suzuki T, Higa S, et al. 1983. Genetic studies of familial amyloid polyneuropathy in the Arao district of Japan: 1. The genealogical survey. Clin. Genet. 24:334-38
    • (1983) Clin. Genet. , vol.24 , pp. 334-338
    • Sakoda, S.1    Suzuki, T.2    Higa, S.3
  • 11
    • 0017610714 scopus 로고
    • Generalized amyloid in a family of Swedish origin. A study of 426 family members in seven generations of a new kinship with neuropathy, nephropathy, and central nervous system involvement
    • 11. Benson MD, Cohen AS. 1977. Generalized amyloid in a family of Swedish origin. A study of 426 family members in seven generations of a new kinship with neuropathy, nephropathy, and central nervous system involvement. Ann. Intern. Med. 86:419-24
    • (1977) Ann. Intern. Med. , vol.86 , pp. 419-424
    • Benson, M.D.1    Cohen, A.S.2
  • 12
    • 0021266985 scopus 로고
    • Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type: Definition of molecular abnormality in transthyretin (prealbumin)
    • 12. Saraiva MJM, Birken S, Costa PP, Goodman DS. 1984. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type: definition of molecular abnormality in transthyretin (prealbumin). J. Clin. Invest. 74:104-19
    • (1984) J. Clin. Invest. , vol.74 , pp. 104-119
    • Saraiva, M.J.M.1    Birken, S.2    Costa, P.P.3    Goodman, D.S.4
  • 13
    • 0021012829 scopus 로고
    • Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type)
    • 13. Tawara S, Nakazato M, Kangawa K, et al. 1983. Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem. Biophys. Res. Commun. 116:880-88
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 880-888
    • Tawara, S.1    Nakazato, M.2    Kangawa, K.3
  • 14
    • 0003351753 scopus 로고
    • Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin
    • 14. Dwulet FE, Benson MD. 1984. Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin. Proc. Natl. Acad. Sci. USA 81:694-98
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 694-698
    • Dwulet, F.E.1    Benson, M.D.2
  • 15
    • 0023939698 scopus 로고
    • Restriction fragment analysis confirms the position 33 mutation in transthyretin from an Israeli patient (SKO) with familial amyloidotic polyneuropathy
    • 15. Jacobson DR, Santiago-Schwarz F, Buxbaum JN. 1988. Restriction fragment analysis confirms the position 33 mutation in transthyretin from an Israeli patient (SKO) with familial amyloidotic polyneuropathy. Biochem. Biophys. Res. Commun. 153:198-202
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 198-202
    • Jacobson, D.R.1    Santiago-Schwarz, F.2    Buxbaum, J.N.3
  • 16
    • 0023947016 scopus 로고
    • Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77, and detection of the gene by DNA analysis
    • 16. Wallace MR, Dwulet FE, Williams EC, et al. 1988. Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77, and detection of the gene by DNA analysis. J. Clin. Invest. 81:189-93
    • (1988) J. Clin. Invest. , vol.81 , pp. 189-193
    • Wallace, M.R.1    Dwulet, F.E.2    Williams, E.C.3
  • 17
    • 0024745055 scopus 로고
    • Direct sequencing of the gene for Maryland/German familial amyloidotic polyneuropathy type II genotyping by allele specific enzymatic amplification
    • 17. Nichols WC, Liepnieks JJ, McKusick VA, Benson MD. 1989. Direct sequencing of the gene for Maryland/German familial amyloidotic polyneuropathy type II genotyping by allele specific enzymatic amplification. Genomics 5: 535-540
    • (1989) Genomics , vol.5 , pp. 535-540
    • Nichols, W.C.1    Liepnieks, J.J.2    McKusick, V.A.3    Benson, M.D.4
  • 19
    • 0028910933 scopus 로고
    • Transthyretin Ser 6 gene frequency in individuals without amyloidosis
    • 19. Jacobson DR, Alves IL, Saraiva MJ, et al. 1995. Transthyretin Ser 6 gene frequency in individuals without amyloidosis. Hum. Genet. 95:308-12
    • (1995) Hum. Genet. , vol.95 , pp. 308-312
    • Jacobson, D.R.1    Alves, I.L.2    Saraiva, M.J.3
  • 20
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation
    • 20. Kelly JW, Lansbury PT Jr. 1994. A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation. Amyloid: Int. J. Exp. Clin. Invest. 1:186-205
    • (1994) Amyloid: Int. J. Exp. Clin. Invest. , vol.1 , pp. 186-205
    • Kelly, J.W.1    Lansbury P.T., Jr.2
  • 21
    • 0027389112 scopus 로고
    • Modifications of transthyretin in amyloid fibrils: Analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation
    • 21. Thylen C, Wahlqvist J, Haettner E, et al. 1993. Modifications of transthyretin in amyloid fibrils: analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation. EMBO J. 12:743-48
    • (1993) EMBO J. , vol.12 , pp. 743-748
    • Thylen, C.1    Wahlqvist, J.2    Haettner, E.3
  • 22
    • 0027769702 scopus 로고
    • Intermolecular disulfide linkages are not required for transthyretin amyloid fibril formation in vitro
    • 22. McCutchen SL, Kelly J. 1993. Intermolecular disulfide linkages are not required for transthyretin amyloid fibril formation in vitro. Biochem. Biophys. Res. Commun. 197:415-21
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 415-421
    • McCutchen, S.L.1    Kelly, J.2
  • 23
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to disease
    • 23. McCutchen SL, Lai Z, Miroy GJ, et al. 1995. Comparison of lethal and nonlethal transthyretin variants and their relationship to disease. Biochemistry 34:13527-36
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.J.3
  • 24
    • 0028281999 scopus 로고
    • A study of 159 Portuguese patients with familial amyloidotic polyneuropathy (FAP) whose parents were both unaffected
    • 24. Coelho T, Sousa A, Lourenco E, Ramalheira J. 1994. A study of 159 Portuguese patients with familial amyloidotic polyneuropathy (FAP) whose parents were both unaffected. J. Med. Genet. 31:293-99
    • (1994) J. Med. Genet. , vol.31 , pp. 293-299
    • Coelho, T.1    Sousa, A.2    Lourenco, E.3    Ramalheira, J.4
  • 25
    • 0013681818 scopus 로고    scopus 로고
    • Anticipation of age-at-onset in Portuguese patients with familial amyloid polyneuropathy-type I (FAP-Met30)
    • ed. MA Gertz, RA Kyle. New York/London: Parthenon. In press
    • 25. Sousa A, Coelho T, Lobato L, Sequeiros J. 1999. Anticipation of age-at-onset in Portuguese patients with familial amyloid polyneuropathy-type I (FAP-Met30). In Amyloidosis, ed. MA Gertz, RA Kyle. New York/London: Parthenon. In press
    • (1999) Amyloidosis
    • Sousa, A.1    Coelho, T.2    Lobato, L.3    Sequeiros, J.4
  • 26
    • 0032788532 scopus 로고    scopus 로고
    • Genetic anticipation in portuguese kindreds with familial amyloidotic polyneuropathy is unlikely to be caused by triplet repeat expansions
    • 26. Soares M, Buxbaum J, Sousa A, et al. 1999. Genetic anticipation in Portuguese kindreds with familial amyloidotic polyneuropathy is unlikely to be caused by triplet repeat expansions. Hum. Genet. 104:480-85
    • (1999) Hum. Genet. , vol.104 , pp. 480-485
    • Soares, M.1    Buxbaum, J.2    Sousa, A.3
  • 27
    • 0002184993 scopus 로고
    • Parental transmission and age-of-onset in familial amyloidotic polyneuropathy (Portuguese type)
    • ed. JB Navtig, Ø Førre, G Husby, et al, Dordrecht, Netherlands/Norwell, MA: Kluwer
    • 27. Sousa A, Coelho T, Sequeiros J. 1990. Parental transmission and age-of-onset in familial amyloidotic polyneuropathy (Portuguese type). In Amyloid and Amyloidosis, ed. JB Navtig, Ø Førre, G Husby, et al, pp. 691-93. Dordrecht, Netherlands/Norwell, MA: Kluwer
    • (1990) Amyloid and Amyloidosis , pp. 691-693
    • Sousa, A.1    Coelho, T.2    Sequeiros, J.3
  • 28
    • 0013676287 scopus 로고
    • Reevaluation of 134 patients with familial amyloidotic polyneuropathy (FAP) type I in Japan, Kumamoto focus
    • ed. JB Navtig, Ø Førre, G Husby, et al, Dordrecht, Netherlands/Norwell, MA: Kluwer
    • 28. Ikegawa S, Yi S, Araki S, et al. 1990. Reevaluation of 134 patients with familial amyloidotic polyneuropathy (FAP) type I in Japan, Kumamoto focus. In Amyloid and Amyloidosis, ed. JB Navtig, Ø Førre, G Husby, et al, pp. 675-78. Dordrecht, Netherlands/Norwell, MA: Kluwer
    • (1990) Amyloid and Amyloidosis , pp. 675-678
    • Ikegawa, S.1    Yi, S.2    Araki, S.3
  • 29
    • 0023823790 scopus 로고
    • Homozygosity for the transthyretin-met 30 gene in two Swedish sibs with familial amyloidotic polyneuropathy
    • 29. Holmgren G, Haettner E, Nordenson I, et al. 1988. Homozygosity for the transthyretin-met 30 gene in two Swedish sibs with familial amyloidotic polyneuropathy. Clin. Genet. 34:333-38
    • (1988) Clin. Genet. , vol.34 , pp. 333-338
    • Holmgren, G.1    Haettner, E.2    Nordenson, I.3
  • 30
    • 0024538761 scopus 로고
    • Haplotype analysis of familial amyloidotic polyneuropathy. Evidence for multiple origins of the Val-Met mutation most common to the disease
    • 30. K Yoshioka, H Furuya, H Sasaki, et al. 1989. Haplotype analysis of familial amyloidotic polyneuropathy. Evidence for multiple origins of the Val-Met mutation most common to the disease. Hum. Genet. 82:9-13
    • (1989) Hum. Genet. , vol.82 , pp. 9-13
    • Yoshioka, K.1    Furuya, H.2    Sasaki, H.3
  • 31
    • 0028894911 scopus 로고
    • Haplotype analysis of French, British and other European patients with familial amyloid polyneuropathy (Met 30 and Tyr 77)
    • 31. Reilly MM, Adams D, Davis MB, et al. 1995. Haplotype analysis of French, British and other European patients with familial amyloid polyneuropathy (Met 30 and Tyr 77). J. Neurol. 242:664-68
    • (1995) J. Neurol. , vol.242 , pp. 664-668
    • Reilly, M.M.1    Adams, D.2    Davis, M.B.3
  • 33
    • 0027275791 scopus 로고
    • Familial amyloidotic polyneuropathy in Sweden: Geographical distribution, age of onset, and prevalence
    • 33. Sousa A, Andersson R, Drugge U, et al. 1993. Familial amyloidotic polyneuropathy in Sweden: geographical distribution, age of onset, and prevalence. Hum. Hered. 43:288-94
    • (1993) Hum. Hered. , vol.43 , pp. 288-294
    • Sousa, A.1    Andersson, R.2    Drugge, U.3
  • 34
    • 0028200952 scopus 로고
    • Geographical distribution of TTR met30 carriers in northern Sweden: Discrepancy between carrier frequency and prevalence rate
    • 34. Holmgren G, Costa PM, Andersson C, et al. 1994. Geographical distribution of TTR met30 carriers in northern Sweden: discrepancy between carrier frequency and prevalence rate. J. Med. Genet. 31:351-54
    • (1994) J. Med. Genet. , vol.31 , pp. 351-354
    • Holmgren, G.1    Costa, P.M.2    Andersson, C.3
  • 35
    • 0000649466 scopus 로고    scopus 로고
    • Discordant symptoms in monozygotic twins with familial amyloidotic polyneuropathy (FAP)(TTR Met 30)
    • 35. Holmgren G, Ando Y, Wikström L, et al. 1997. Discordant symptoms in monozygotic twins with familial amyloidotic polyneuropathy (FAP)(TTR Met 30). Amyloid: Int. J. Exp. Clin. Invest. 4:178-80
    • (1997) Amyloid: Int. J. Exp. Clin. Invest. , vol.4 , pp. 178-180
    • Holmgren, G.1    Ando, Y.2    Wikström, L.3
  • 36
    • 0013637002 scopus 로고
    • Ueber amyloide degeneration
    • 36. Soyka J. 1876. Ueber amyloide degeneration. Prag. Med. Wochenschr. 9:165-71
    • (1876) Prag. Med. Wochenschr. , vol.9 , pp. 165-171
    • Soyka, J.1
  • 37
    • 0013635818 scopus 로고
    • Ein fall von lokaler amyloidose des herzens
    • 37. Beneke R, Bönning F. 1908. Ein fall von lokaler amyloidose des herzens. Beitr. Pathol. Anat. 44:362-85
    • (1908) Beitr. Pathol. Anat. , vol.44 , pp. 362-385
    • Beneke, R.1    Bönning, F.2
  • 39
    • 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
    • 39. Gorevic PD, Prelli FC, Wright J, et al. 1989. 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. 83:836-43
    • (1989) J. Clin. Invest. , vol.83 , pp. 836-843
    • Gorevic, P.D.1    Prelli, F.C.2    Wright, J.3
  • 40
    • 0025335359 scopus 로고
    • A homozygous transthyretin variant associated with senile systemic amyloidosis: Evidence for a late-onset disease of genetic etiology
    • 40. Jacobson DR, Gorevic PD, Buxbaum JN. 1990. A homozygous transthyretin variant associated with senile systemic amyloidosis: evidence for a late-onset disease of genetic etiology. Am. J. Hum. Genet. 47:127-36
    • (1990) Am. J. Hum. Genet. , vol.47 , pp. 127-136
    • Jacobson, D.R.1    Gorevic, P.D.2    Buxbaum, J.N.3
  • 41
    • 44949277138 scopus 로고
    • Senile cardiac amyloidosis associated with homozygosity for a transthyretin variant (Ile-122)
    • 41. Nichols WC, Liepnieks JJ, Snyder EL, Benson MD. 1991. Senile cardiac amyloidosis associated with homozygosity for a transthyretin variant (Ile-122). J. Lab. Clin. Med. 117:175-80
    • (1991) J. Lab. Clin. Med. , vol.117 , pp. 175-180
    • Nichols, W.C.1    Liepnieks, J.J.2    Snyder, E.L.3    Benson, M.D.4
  • 42
    • 0025169627 scopus 로고
    • Cardiac amyloidosis: Report of a patient heterozygous for the transthyretin-isoleucine 122 variant
    • 42. Saraiva MJM, Sherman W, Marboe C, et al. 1990. Cardiac amyloidosis: report of a patient heterozygous for the transthyretin-isoleucine 122 variant. Scand. J. Immunol. 32:341-46
    • (1990) Scand. J. Immunol. , vol.32 , pp. 341-346
    • Saraiva, M.J.M.1    Sherman, W.2    Marboe, C.3
  • 43
    • 0000185477 scopus 로고
    • Direct evidence for hereditary nature of senile cardiac (systemic) amyloidosis
    • Abstr.
    • 43. Snyder EC, Nichols WC, Liepnicks JJ, Benson MD. 1991. Direct evidence for hereditary nature of senile cardiac (systemic) amyloidosis. Am. J. Hum. Genet. 45:A220 (Abstr.)
    • (1991) Am. J. Hum. Genet. , vol.45
    • Snyder, E.C.1    Nichols, W.C.2    Liepnicks, J.J.3    Benson, M.D.4
  • 44
    • 0029946836 scopus 로고    scopus 로고
    • Revised transthyretin Ile 122 allele prevalence in African-Americans
    • 44. Jacobson DR, Pastore R, Pool S, et al. 1996. Revised transthyretin Ile 122 allele prevalence in African-Americans. Hum. Genet. 98:236-38
    • (1996) Hum. Genet. , vol.98 , pp. 236-238
    • Jacobson, D.R.1    Pastore, R.2    Pool, S.3
  • 45
    • 0013677989 scopus 로고    scopus 로고
    • TTR mutations in patients with senile cardiac amyloidosis
    • ed. MA Gertz, RA Kyle, New York, London: Parthenon
    • 45. Booth DR, Gillmore JD, Persey MR, et al. 1999. TTR mutations in patients with senile cardiac amyloidosis. In Amyloidosis, ed. MA Gertz, RA Kyle, pp. 554-55. New York, London: Parthenon
    • (1999) Amyloidosis , pp. 554-555
    • Booth, D.R.1    Gillmore, J.D.2    Persey, M.R.3
  • 46
    • 0031028712 scopus 로고    scopus 로고
    • Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans
    • 46. Jacobson DR, Pastore RD, Yaghoubian R, et al. 1997. Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans. N. Engl. J. Med. 336:466-73
    • (1997) N. Engl. J. Med. , vol.336 , pp. 466-473
    • Jacobson, D.R.1    Pastore, R.D.2    Yaghoubian, R.3
  • 47
    • 0030971508 scopus 로고    scopus 로고
    • Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy
    • 47. Kohno K, Palha JA, Miyakawa K, et al. 1997. Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy. Am. J. Pathol. 150:1497-508
    • (1997) Am. J. Pathol. , vol.150 , pp. 1497-1508
    • Kohno, K.1    Palha, J.A.2    Miyakawa, K.3
  • 49
    • 4243358582 scopus 로고    scopus 로고
    • Age and sex-dependent amyloid fibril formation in mice transgenic for wild type human transthyretin
    • Abstr.
    • 49. Teng M, Yin J, Vidal R, et al. 1998. Age and sex-dependent amyloid fibril formation in mice transgenic for wild type human transthyretin. J. Invest. Med. 46:192A (Abstr.)
    • (1998) J. Invest. Med. , vol.46
    • Teng, M.1    Yin, J.2    Vidal, R.3
  • 50
    • 0013635277 scopus 로고    scopus 로고
    • The amyloidoses
    • ed. JH Klippel, PA Dieppe, 1-10. London: Mosby-Wolfe
    • 50. Buxbaum JN. 1997. The amyloidoses. In Rheumatology, ed. JH Klippel, PA Dieppe, pp. 27.1-10. London: Mosby-Wolfe
    • (1997) Rheumatology , pp. 27
    • Buxbaum, J.N.1
  • 52
    • 0013636078 scopus 로고
    • SAA2 deposition in the spleen of the mouse
    • ed. T Isobe, S Araki, F Uchino, et al., London/New York: Plenum
    • 52. Shiroo M, Kawahara E, Nakanishi I, Migita S. 1988. SAA2 deposition in the spleen of the mouse. In Amyloid and Amyloidosis, ed. T Isobe, S Araki, F Uchino, et al., pp. 63-68. London/New York: Plenum
    • (1988) Amyloid and Amyloidosis , pp. 63-68
    • Shiroo, M.1    Kawahara, E.2    Nakanishi, I.3    Migita, S.4
  • 53
    • 0018074981 scopus 로고
    • Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes
    • 53. Lavie G, Zucker-Franklin D, Franklin EC. 1978. Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes. J. Exp. Med. 148:1020-31
    • (1978) J. Exp. Med. , vol.148 , pp. 1020-1031
    • Lavie, G.1    Zucker-Franklin, D.2    Franklin, E.C.3
  • 54
    • 0033045614 scopus 로고    scopus 로고
    • Revised nomenclature for serum amyloid A (SAA)
    • 54. Nomenclature Committee of the International Society of Amyloidosis. 1999. Revised nomenclature for serum amyloid A (SAA). Amyloid: Int. J. Exp. Clin. Invest. 6:67-70
    • (1999) Amyloid: Int. J. Exp. Clin. Invest. , vol.6 , pp. 67-70
  • 55
    • 0028833148 scopus 로고
    • Characterization of amyloid A protein in human secondary amyloidosis: The predominant deposition of serum amyloid A1
    • 55. Liepnieks JJ, Kluve-Beckerman B, Benson MD. 1995. Characterization of amyloid A protein in human secondary amyloidosis: the predominant deposition of serum amyloid A1. Biochim. Biophys. Acta 1270:81-86
    • (1995) Biochim. Biophys. Acta , vol.1270 , pp. 81-86
    • Liepnieks, J.J.1    Kluve-Beckerman, B.2    Benson, M.D.3
  • 57
    • 0001907053 scopus 로고    scopus 로고
    • Do alleles at the serum amyloid A locus influence susceptibility to reactive amyloidosis in systemic onset juvenile chronic arthritis?
    • 57. Faulkes DJ, Woo P. 1997. Do alleles at the serum amyloid A locus influence susceptibility to reactive amyloidosis in systemic onset juvenile chronic arthritis? Amyloid: Int. J. Exp. Clin. Invest. 4:75-79
    • (1997) Amyloid: Int. J. Exp. Clin. Invest. , vol.4 , pp. 75-79
    • Faulkes, D.J.1    Woo, P.2
  • 58
    • 0032151748 scopus 로고    scopus 로고
    • The frequency of serum amyloid A2 alleles in the Japanese population
    • 58. Yamada T, Okuda Y, Itoh Y. 1998. The frequency of serum amyloid A2 alleles in the Japanese population. Amyloid: Int. J. Exp. Clin. Invest. 5:208-11
    • (1998) Amyloid: Int. J. Exp. Clin. Invest. , vol.5 , pp. 208-211
    • Yamada, T.1    Okuda, Y.2    Itoh, Y.3
  • 59
    • 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
    • 59. Samuels J, Aksentijevich I, Torosyan Y, et al. 1998. Familial Mediterranean fever at the millennium. Clinical spectrum, ancient mutations, and a survey of 100 American referrals to the National Institutes of Health. Medicine 77:268-97
    • (1998) Medicine , vol.77 , pp. 268-297
    • Samuels, J.1    Aksentijevich, I.2    Torosyan, Y.3
  • 60
    • 0022570984 scopus 로고
    • Colchicine in the prevention and treatment of the amyloidosis of familial Mediterranean fever
    • 60. Zemer D, Pras M, Sohar E, et al. 1986. Colchicine in the prevention and treatment of the amyloidosis of familial Mediterranean fever. N. Engl. J. Med. 314:1001-5
    • (1986) N. Engl. J. Med. , vol.314 , pp. 1001-1005
    • Zemer, D.1    Pras, M.2    Sohar, E.3
  • 61
    • 0016223474 scopus 로고
    • A controlled trial of colchicine in preventing attacks of familial mediterranean fever
    • 61. Zemer D, Revach M, Pras M, et al. 1974. A controlled trial of colchicine in preventing attacks of familial Mediterranean fever. N. Engl. J. Med. 291:932-37
    • (1974) N. Engl. J. Med. , vol.291 , pp. 932-937
    • Zemer, D.1    Revach, M.2    Pras, M.3
  • 62
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • 62. The French FMF Consortium. 1997. A candidate gene for familial Mediterranean fever. Nature Genet. 17:25-30
    • (1997) Nature Genet. , vol.17 , pp. 25-30
  • 63
    • 0030745449 scopus 로고    scopus 로고
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever
    • 63. The International FMF Consortium. 1997. Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. Cell 90:797-807
    • (1997) Cell , vol.90 , pp. 797-807
  • 64
    • 0033008274 scopus 로고    scopus 로고
    • MEFV mutation analysis in patients suffering from amyloidosis of familial Mediterranean fever
    • 64. Livneh A, Langevitz P, Shinar Y, et al. 1999. MEFV mutation analysis in patients suffering from amyloidosis of familial Mediterranean fever. Amyloid: Int. J. Exp. Clin. Invest. 6:1-6
    • (1999) Amyloid: Int. J. Exp. Clin. Invest. , vol.6 , pp. 1-6
    • Livneh, A.1    Langevitz, P.2    Shinar, Y.3
  • 66
    • 0024317904 scopus 로고
    • Prevalence of Alzheimer's disease in a community population of older persons. Higher than previously reported
    • 66. Evans DA, Funkenstein HH, Albert MS, et al. 1989. Prevalence of Alzheimer's disease in a community population of older persons. Higher than previously reported. J. Am. Med. Assoc. 262:2551-56
    • (1989) J. Am. Med. Assoc. , vol.262 , pp. 2551-2556
    • Evans, D.A.1    Funkenstein, H.H.2    Albert, M.S.3
  • 67
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • 67. Glenner GG, Wong CW. 1984. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120:885-90
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 68
    • 0027288860 scopus 로고
    • Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth
    • 68. Koo EH, Park L, Selkoe DJ. 1993. Amyloid beta-protein as a substrate interacts with extracellular matrix to promote neurite outgrowth. Proc. Natl. Acad. Sci. USA 90:4748-52
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4748-4752
    • Koo, E.H.1    Park, L.2    Selkoe, D.J.3
  • 69
    • 0026600598 scopus 로고
    • Detection of distinct isoform patterns of the beta-amyloid precursor protein in human platelets and lymphocytes
    • 69. Schlossmacher MG, Ostaszewski BL, Hecker LI, et al. 1992. Detection of distinct isoform patterns of the beta-amyloid precursor protein in human platelets and lymphocytes. Neurobiol. Aging 13:421-34
    • (1992) Neurobiol. Aging , vol.13 , pp. 421-434
    • Schlossmacher, M.G.1    Ostaszewski, B.L.2    Hecker, L.I.3
  • 70
    • 0028988801 scopus 로고
    • Beta-amyloid precursor protein-deficient mice show gliosis and decreased locomotor activity
    • 70. Zheng H, Jiang M, Trumbauer ME, et al. 1995. Beta-amyloid precursor protein-deficient mice show gliosis and decreased locomotor activity. Cell 81: 525-31
    • (1995) Cell , vol.81 , pp. 525-531
    • Zheng, H.1    Jiang, M.2    Trumbauer, M.E.3
  • 71
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • 71. Kang J, Lemaire H, Unterbeck A, et al. 1987. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 325:733-36
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.2    Unterbeck, A.3
  • 72
    • 0029970325 scopus 로고    scopus 로고
    • APP gene family. Alternative splicing generates functionally related isoforms
    • 72. Sandbrink R, Masters CL, Beyreuther K. 1996. APP gene family. Alternative splicing generates functionally related isoforms. Ann. NY Acad. Sci. 777:281-87
    • (1996) Ann. NY Acad. Sci. , vol.777 , pp. 281-287
    • Sandbrink, R.1    Masters, C.L.2    Beyreuther, K.3
  • 73
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain
    • 73. De Strooper B, Annaert W, Cupers P, et al. 1999. A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature 398:518-22
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1    Annaert, W.2    Cupers, P.3
  • 74
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43)-positive and A beta 40-positive senile plaques with end-specific A beta-monoclonal antibodies: Evidence that an initially deposited A beta species is A beta 1-42(43)
    • 74. Iwatsubo T, Odaka A, Suzuki N, et al. 1994. Visualization of A beta 42(43)-positive and A beta 40-positive senile plaques with end-specific A beta-monoclonal antibodies: evidence that an initially deposited A beta species is A beta 1-42(43). Neuron 13:45-53
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3
  • 75
    • 0026745610 scopus 로고
    • Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production
    • 75. Citron M, Oltersdorf T, Haass C, et al. 1992. Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production. Nature 360:672-74
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3
  • 76
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • 76. Sherrington R, Rogaev EI, Liang Y, et al. 1995. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375:754-60
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 77
    • 0029087026 scopus 로고
    • Candidate gene for the chromosome 1 familial Alzheimer's disease locus
    • 77. Levy-Lahad E, Wasco W, Poorkaj P, et al. 1995. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269:973-77
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 78
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants
    • 78. Suzuki N, Cheung TT, Cai XD, et al. 1994. An increased percentage of long amyloid beta protein secreted by familial amyloid beta protein precursor (beta APP717) mutants. Science 264:1336-40
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3
  • 79
    • 0028176062 scopus 로고
    • Differences in beta-amyloid (beta/A4) deposition in human patients with Down's syndrome and sporadic Alzheimer's disease
    • 79. Armstrong RA. 1994. Differences in beta-amyloid (beta/A4) deposition in human patients with Down's syndrome and sporadic Alzheimer's disease. Neurosci. Lett. 169:133-36
    • (1994) Neurosci. Lett. , vol.169 , pp. 133-136
    • Armstrong, R.A.1
  • 80
    • 0028981717 scopus 로고
    • The Alzheimer's A beta peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • 80. LaFerla FM, Tinkle BT, Bieberich CJ, et al. 1995. The Alzheimer's A beta peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nature Genet. 9:21-30
    • (1995) Nature Genet. , vol.9 , pp. 21-30
    • LaFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3
  • 81
    • 0029873575 scopus 로고    scopus 로고
    • Amyloid beta-protein induces the cerebrovascular cellular pathology of Alzheimer's disease and related disorders
    • 81. Van Nostrand WE, Davis-Salinas J, Saporito-Irwin SM. 1996. Amyloid beta-protein induces the cerebrovascular cellular pathology of Alzheimer's disease and related disorders. Ann. NY Acad. Sci. 777:297-302
    • (1996) Ann. NY Acad. Sci. , vol.777 , pp. 297-302
    • Van Nostrand, W.E.1    Davis-Salinas, J.2    Saporito-Irwin, S.M.3
  • 82
    • 0031918785 scopus 로고    scopus 로고
    • The genetics of Alzheimer disease: Current status and future prospects
    • 82. Blacker D, Tanzi RE. 1998. The genetics of Alzheimer disease: current status and future prospects. Arch. Neurol. 55:294-96
    • (1998) Arch. Neurol. , vol.55 , pp. 294-296
    • Blacker, D.1    Tanzi, R.E.2
  • 83
    • 0030499031 scopus 로고    scopus 로고
    • Wide range in age of onset for chromosome 1-related familial Alzheimer's disease
    • 83. Bird TD, Levy-Lahad E, Poorkaj P, et al. 1996. Wide range in age of onset for chromosome 1-related familial Alzheimer's disease. Ann. Neurol. 40:932-36
    • (1996) Ann. Neurol. , vol.40 , pp. 932-936
    • Bird, T.D.1    Levy-Lahad, E.2    Poorkaj, P.3
  • 84
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • 84. Goate A, Chartier-Harlin M-C, Mullan M, et al. 1991. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349:704-6
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.-C.2    Mullan, M.3
  • 85
    • 0026833684 scopus 로고
    • Molecular biology of Alzheimer's amyloid-Dutch variant
    • 85. Wisniewski T, Frangione B 1992. Molecular biology of Alzheimer's amyloid-Dutch variant. Mol. Neurobiol. 6:75-86
    • (1992) Mol. Neurobiol. , vol.6 , pp. 75-86
    • Wisniewski, T.1    Frangione, B.2
  • 86
    • 0026907151 scopus 로고
    • A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid
    • 86. Mullan M, Crawford F, Axelman K, et al. 1992. A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid. Nature Genet. 1:345-47
    • (1992) Nature Genet. , vol.1 , pp. 345-347
    • Mullan, M.1    Crawford, F.2    Axelman, K.3
  • 87
    • 0025296269 scopus 로고
    • Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type
    • 87. Levy E, Carman MD, Fernandez-Madrid IJ, et al. 1990. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 248:1124-26
    • (1990) Science , vol.248 , pp. 1124-1126
    • Levy, E.1    Carman, M.D.2    Fernandez-Madrid, I.J.3
  • 88
    • 0026471656 scopus 로고
    • Genetic linkage evidence for a familial Alzheimer's disease locus on chromosome 14
    • 88. Schellenberg GD, Bird TD, Wijsman EM, et al. 1992. Genetic linkage evidence for a familial Alzheimer's disease locus on chromosome 14. Science 258: 668-71
    • (1992) Science , vol.258 , pp. 668-671
    • Schellenberg, G.D.1    Bird, T.D.2    Wijsman, E.M.3
  • 89
    • 12644258498 scopus 로고    scopus 로고
    • The presenilin-2 mutation (N1411) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue
    • 89. Tomita T, Maruyama K, Saido TC, et al. 1997. The presenilin-2 mutation (N1411) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue. Proc. Natl. Acad. Sci. USA 94:2025-30
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2025-2030
    • Tomita, T.1    Maruyama, K.2    Saido, T.C.3
  • 90
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • 90. Wolfe MS, Xia W, Ostaszewski BL, et al. 1999. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 398:513-17
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3
  • 91
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • 91. De Strooper B, Saftig P, Craessaerts K, et al. 1998. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391:387-90
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1    Saftig, P.2    Craessaerts, K.3
  • 92
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
    • 92. Levitan D, Greenwald I. 1995. Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature 377: 351-54
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 93
    • 0031108103 scopus 로고    scopus 로고
    • Human presenilin 1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signaling independently of proteolytic processing
    • 93. Baumeister R, Leimer U, Zweckbronner I, et al. 1997. Human presenilin 1, but not familial Alzheimer's disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signaling independently of proteolytic processing. Genes Funct. 1:149-59
    • (1997) Genes Funct. , vol.1 , pp. 149-159
    • Baumeister, R.1    Leimer, U.2    Zweckbronner, I.3
  • 94
    • 0032905727 scopus 로고    scopus 로고
    • Presenilin mutations associated with Alzheimer disease cause defective intracellular trafficking of beta-catenin, a component of the presenilin protein complex
    • 94. Nishimura M, Yu G, Levesque G, et al. 1999. Presenilin mutations associated with Alzheimer disease cause defective intracellular trafficking of beta-catenin, a component of the presenilin protein complex. Nature Med. 5:164-69
    • (1999) Nature Med. , vol.5 , pp. 164-169
    • Nishimura, M.1    Yu, G.2    Levesque, G.3
  • 95
    • 0031054505 scopus 로고    scopus 로고
    • Formation of stable complexes between two Alzheimer's diseases gene products: Presenilin-2 and beta-amyloid precursor protein
    • 95. Weidemann A, Paliga K, Durrwang U, et al. 1997. Formation of stable complexes between two Alzheimer's diseases gene products: presenilin-2 and beta-amyloid precursor protein. Nature Med. 3:328-32
    • (1997) Nature Med. , vol.3 , pp. 328-332
    • Weidemann, A.1    Paliga, K.2    Durrwang, U.3
  • 96
    • 0029101491 scopus 로고
    • Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene
    • 96. Rogaev EI, Sherrington R, Rogaeva EA, et al. 1995. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376:775-78
    • (1995) Nature , vol.376 , pp. 775-778
    • Rogaev, E.I.1    Sherrington, R.2    Rogaeva, E.A.3
  • 97
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overproducing V717F beta-amyloid precursor protein
    • 97. Games D, Adams D, Alessandrini R, et al. 1995. Alzheimer-type neuropathology in transgenic mice overproducing V717F beta-amyloid precursor protein. Nature 373:523-27
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 98
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, A beta elevation and amyloid plaques in transgenic mice
    • 98. Hsiao K, Chapman P, Nilsen S, et al. 1996. Correlative memory deficits, A beta elevation and amyloid plaques in transgenic mice. Science 274:99-102
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 99
    • 0031914718 scopus 로고    scopus 로고
    • Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes
    • 99. Holcomb L, Gordon MN, McGowan E, et al. 1998. Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nature Med. 4:97-100
    • (1998) Nature Med. , vol.4 , pp. 97-100
    • Holcomb, L.1    Gordon, M.N.2    McGowan, E.3
  • 100
    • 0011444914 scopus 로고    scopus 로고
    • Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
    • 100. Sturchler-Pierrat C, Abramowski D, Duke M, et al. 1997. Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology. Proc. Natl. Acad. Sci. USA 94:13287-92
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13287-13292
    • Sturchler-Pierrat, C.1    Abramowski, D.2    Duke, M.3
  • 101
    • 0040177065 scopus 로고
    • Low density lipoprotein receptor-related protein mediates uptake of cholesterol esters derived from apoprotein E-enriched lipoproteins
    • 101. Kowal RC, Herz J, Goldstein JL, et al. 1989. Low density lipoprotein receptor-related protein mediates uptake of cholesterol esters derived from apoprotein E-enriched lipoproteins. Proc. Natl. Acad. Sci. USA 86:5810-14
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5810-5814
    • Kowal, R.C.1    Herz, J.2    Goldstein, J.L.3
  • 102
    • 0024449363 scopus 로고
    • The LDL-receptor-related protein, LRP, is an apolipoprotein E-binding protein
    • 102. Beisiegel U, Weber W, Ihrke G, et al. 1989. The LDL-receptor-related protein, LRP, is an apolipoprotein E-binding protein. Nature 341:162-64
    • (1989) Nature , vol.341 , pp. 162-164
    • Beisiegel, U.1    Weber, W.2    Ihrke, G.3
  • 103
    • 0028122892 scopus 로고
    • Potential role of apolipoprotein-E in fibrillogenesis
    • 103. Gallo G, Wisniewski T, Choi-Miura N-H, et al. 1994. Potential role of apolipoprotein-E in fibrillogenesis. Am. J. Pathol. 145:526-30
    • (1994) Am. J. Pathol. , vol.145 , pp. 526-530
    • Gallo, G.1    Wisniewski, T.2    Choi-Miura, N.-H.3
  • 104
    • 0028092997 scopus 로고
    • Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms
    • 104. Dong LM, Wilson C, Wardell MR, et al. 1994. Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms. J. Biol. Chem. 269:22358-65
    • (1994) J. Biol. Chem. , vol.269 , pp. 22358-22365
    • Dong, L.M.1    Wilson, C.2    Wardell, M.R.3
  • 105
    • 0029820675 scopus 로고    scopus 로고
    • Apolipoprotein function in health and disease: Insights from natural mutations
    • 105. Franceschini G. 1996. Apolipoprotein function in health and disease: insights from natural mutations. Eur. J. Clin. Invest. 26:733-46
    • (1996) Eur. J. Clin. Invest. , vol.26 , pp. 733-746
    • Franceschini, G.1
  • 106
    • 0024561665 scopus 로고
    • Genetic studies of human apolipoproteins. VI. Common polymorphism of apolipoprotein E in blacks
    • 106. Kamboh MI, Sepehrnia B, Ferrell RE. 1989. Genetic studies of human apolipoproteins. VI. Common polymorphism of apolipoprotein E in blacks. Dis. Markers 7:49-55
    • (1989) Dis. Markers , vol.7 , pp. 49-55
    • Kamboh, M.I.1    Sepehrnia, B.2    Ferrell, R.E.3
  • 107
    • 0028359655 scopus 로고
    • Genetic associations with human longevity at the Apo E and ACE loci
    • 107. Schächter F, Faure-Delanef L, Guénot F, et al. 1994. Genetic associations with human longevity at the Apo E and ACE loci. Nature Genet. 6:29-32
    • (1994) Nature Genet. , vol.6 , pp. 29-32
    • Schächter, F.1    Faure-Delanef, L.2    Guénot, F.3
  • 108
    • 0026611012 scopus 로고
    • Apolipoprotein E4 homozygosity in young men with coronary heart disease
    • 108. Van Bockxmeer FM, Mamotte CDS. 1992. Apolipoprotein E4 homozygosity in young men with coronary heart disease. Lancet 340:879-80
    • (1992) Lancet , vol.340 , pp. 879-880
    • Van Bockxmeer, F.M.1    Mamotte, C.D.S.2
  • 109
    • 1542739152 scopus 로고    scopus 로고
    • Increased risk of dialysis-related amyloidosis in patients with the apolipoprotein E4 allele
    • 109. Gejyo F, Suzuki S, Kimura H, et al. 1997. Increased risk of dialysis-related amyloidosis in patients with the apolipoprotein E4 allele. Amyloid: Int. J. Exp. Clin. Invest. 4:13-17
    • (1997) Amyloid: Int. J. Exp. Clin. Invest. , vol.4 , pp. 13-17
    • Gejyo, F.1    Suzuki, S.2    Kimura, H.3
  • 110
    • 0027327267 scopus 로고
    • Association of apolipoprotein E allele epsilon 4 with late-onset familial and sporadic Alzheimer's disease
    • 110. Saunders AM, Strittmatter WJ, Schmechel D, et al. 1993. Association of apolipoprotein E allele epsilon 4 with late-onset familial and sporadic Alzheimer's disease. Neurology 43:1467-72
    • (1993) Neurology , vol.43 , pp. 1467-1472
    • Saunders, A.M.1    Strittmatter, W.J.2    Schmechel, D.3
  • 111
    • 0028305380 scopus 로고
    • Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease
    • 111. Corder EH, Saunders AM, Risch NJ, et al. 1994. Protective effect of apolipoprotein E type 2 allele for late onset Alzheimer disease. Nature Genet. 7:180-84
    • (1994) Nature Genet. , vol.7 , pp. 180-184
    • Corder, E.H.1    Saunders, A.M.2    Risch, N.J.3
  • 112
    • 0028841027 scopus 로고
    • Apolipoprotein E, dementia, and cortical deposition of beta-amyloid protein
    • 112. Polvikoski T, Sulkava R, Haltia M, et al. 1995. Apolipoprotein E, dementia, and cortical deposition of beta-amyloid protein. N. Engl. J. Med. 333:1242-47
    • (1995) N. Engl. J. Med. , vol.333 , pp. 1242-1247
    • Polvikoski, T.1    Sulkava, R.2    Haltia, M.3
  • 113
    • 17744410836 scopus 로고    scopus 로고
    • Apo E-4 and age at onset of Alzheimer's disease: The NIMH genetics initiative
    • 113. Blacker D, Haines JL, Rodes L, et al. 1997. Apo E-4 and age at onset of Alzheimer's disease: the NIMH genetics initiative. Neurology 48:139-47
    • (1997) Neurology , vol.48 , pp. 139-147
    • Blacker, D.1    Haines, J.L.2    Rodes, L.3
  • 114
    • 0029001744 scopus 로고
    • Epistatic effect of APP717 mutation and apolipoprotein E genotype in familial Alzheimer's disease
    • 114. Sorbi S, Nacmias B, Forleo P, et al. 1995. Epistatic effect of APP717 mutation and apolipoprotein E genotype in familial Alzheimer's disease. Ann. Neurol. 38: 124-27
    • (1995) Ann. Neurol. , vol.38 , pp. 124-127
    • Sorbi, S.1    Nacmias, B.2    Forleo, P.3
  • 115
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • 115. Wisniewski T, Castano EM, Golabek AA, et al. 1994. Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am. J. Pathol. 145:1030-35
    • (1994) Am. J. Pathol. , vol.145 , pp. 1030-1035
    • Wisniewski, T.1    Castano, E.M.2    Golabek, A.A.3
  • 116
    • 0031278270 scopus 로고    scopus 로고
    • Lack of apolipoprotein E dramatically reduces amyloid beta-peptide deposition
    • 116. Bales KR, Verina T, Dodel RC, et al. 1997. Lack of apolipoprotein E dramatically reduces amyloid beta-peptide deposition. Nature Genet. 17:263-64
    • (1997) Nature Genet. , vol.17 , pp. 263-264
    • Bales, K.R.1    Verina, T.2    Dodel, R.C.3
  • 117
    • 0028816355 scopus 로고
    • Apolipoprotein E and Alzheimer's disease: Ethnic variation in genotypic risks
    • 117. Maestre G, Ottman R, Stern Y, et al. 1995. Apolipoprotein E and Alzheimer's disease: ethnic variation in genotypic risks. Ann. Neurol. 37:254-59
    • (1995) Ann. Neurol. , vol.37 , pp. 254-259
    • Maestre, G.1    Ottman, R.2    Stern, Y.3
  • 118
    • 0032545939 scopus 로고    scopus 로고
    • Utility of the apolipoprotein E genotype in the diagnosis of Alzheimer's disease. Alzheimer's disease centers consortium in apolipoprotein E and Alzheimer's disease
    • 118. Mayeux R, Saunders AM, Shea S, et al. 1998. Utility of the apolipoprotein E genotype in the diagnosis of Alzheimer's disease. Alzheimer's disease centers consortium in apolipoprotein E and Alzheimer's disease. N. Engl. J. Med. 338:506-11
    • (1998) N. Engl. J. Med. , vol.338 , pp. 506-511
    • Mayeux, R.1    Saunders, A.M.2    Shea, S.3
  • 119
    • 0030611584 scopus 로고    scopus 로고
    • Alpha2-macroglobulin complexes with and mediates the endocytosis of beta-amyloid peptide via cell surface low-density lipoprotein receptor-related protein
    • 119. Narita M, Holtzman DM, Schwartz AL, Bu G. 1997. Alpha2-macroglobulin complexes with and mediates the endocytosis of beta-amyloid peptide via cell surface low-density lipoprotein receptor-related protein. J. Neurochem. 69:1904-11
    • (1997) J. Neurochem. , vol.69 , pp. 1904-1911
    • Narita, M.1    Holtzman, D.M.2    Schwartz, A.L.3    Bu, G.4
  • 120
    • 17344362232 scopus 로고    scopus 로고
    • Alpha-2 macroglobulin is genetically associated with Alzheimer disease
    • 120. Blacker D, Wilcox MA, Laird NM, et al. 1998. Alpha-2 macroglobulin is genetically associated with Alzheimer disease. Nature Genet. 19:357-60
    • (1998) Nature Genet. , vol.19 , pp. 357-360
    • Blacker, D.1    Wilcox, M.A.2    Laird, N.M.3
  • 121
    • 0032539723 scopus 로고    scopus 로고
    • Alpha 2-macroglobin associates with beta-amyloid peptide and prevents fibril formation
    • 121. Hughes SR, Khorkova O, Goyal S, et al. 1998. Alpha 2-macroglobin associates with beta-amyloid peptide and prevents fibril formation. Proc. Natl. Acad. Sci. USA 95:3275-80
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3275-3280
    • Hughes, S.R.1    Khorkova, O.2    Goyal, S.3
  • 122
    • 7844252287 scopus 로고    scopus 로고
    • Genetic association of an alpha 2-macroglobulin (Val1000Ile) polymorphism and Alzheimer's disease
    • 122. Liao A, Nitsch RM, Greenberg SM, et al. 1998. Genetic association of an alpha 2-macroglobulin (Val1000Ile) polymorphism and Alzheimer's disease. Hum. Mol. Genet. 7:1953-56
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1953-1956
    • Liao, A.1    Nitsch, R.M.2    Greenberg, S.M.3
  • 123
    • 0030725311 scopus 로고    scopus 로고
    • Perlecan binds to the beta-amyloid proteins (A beta) of Alzheimer's disease, accelerates A beta fibril formation, and maintains A beta fibril stability
    • 123. Castillo GM, Ngo C, Cummings J, et al. 1997. Perlecan binds to the beta-amyloid proteins (A beta) of Alzheimer's disease, accelerates A beta fibril formation, and maintains A beta fibril stability. J. Neurochem. 69:2452-65
    • (1997) J. Neurochem. , vol.69 , pp. 2452-2465
    • Castillo, G.M.1    Ngo, C.2    Cummings, J.3
  • 124
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • 124. van Leeuwen FW, de Kleijn DP, van den Hurk HH, et al. 1998. Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279:242-47
    • (1998) Science , vol.279 , pp. 242-247
    • Van Leeuwen, F.W.1    De Kleijn, D.P.2    Van Den Hurk, H.H.3
  • 125
    • 0014444934 scopus 로고
    • Inherited predisposition to generalised amyloidosis. Clinical and pathological study of a family with neuropathy, nephropathy and peptic ulcer
    • 125. Van Allen MW, Frohlich JA, Davis JR, et al. 1969. Inherited predisposition to generalised amyloidosis. Clinical and pathological study of a family with neuropathy, nephropathy and peptic ulcer. Neurology 19:10-25
    • (1969) Neurology , vol.19 , pp. 10-25
    • Van Allen, M.W.1    Frohlich, J.A.2    Davis, J.R.3
  • 126
    • 0028267150 scopus 로고
    • Familial nephropathic systemic amyloidosis caused by apolipoprotein AI variant Arg26
    • 126. Vigushin DM, Gough J, Allan D, et al. 1994. Familial nephropathic systemic amyloidosis caused by apolipoprotein AI variant Arg26. Q.J. Med. 87:149-54
    • (1994) Q.J. Med. , vol.87 , pp. 149-154
    • Vigushin, D.M.1    Gough, J.2    Allan, D.3
  • 127
    • 0028866543 scopus 로고
    • Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques
    • 127. Westermark P, Mucchiano G, Marthin T, et al. 1995. Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques. Am. J. Pathol. 147:1186-92
    • (1995) Am. J. Pathol. , vol.147 , pp. 1186-1192
    • Westermark, P.1    Mucchiano, G.2    Marthin, T.3
  • 128
    • 0027384540 scopus 로고
    • Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation. Structure:Function relationships
    • 128. Sorci-Thomas M, Kearns MW, Lee JP, et al. 1993. Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation. Structure:function relationships. J. Biol. Chem. 268: 21403-9
    • (1993) J. Biol. Chem. , vol.268 , pp. 21403-21409
    • Sorci-Thomas, M.1    Kearns, M.W.2    Lee, J.P.3
  • 129
    • 0032567661 scopus 로고    scopus 로고
    • Extensive intimal apolipoprotein A1-derived amyloid deposits in a patient with apolipoprotein A1 mutation
    • 129. Amarzguioui M, Mucchiano G, Häggqvist B, et al. 1998. Extensive intimal apolipoprotein A1-derived amyloid deposits in a patient with apolipoprotein A1 mutation. Biochem. Biophys. Res. Commun. 242:534-39
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 534-539
    • Amarzguioui, M.1    Mucchiano, G.2    Häggqvist, B.3
  • 130
    • 0026642154 scopus 로고
    • In vivo metabolism of a mutant apolipoprotein, apoA-1Iowa, associated with hypoalphalipoproteinemia and hereditary systemic amyloidosis
    • 130. Rader DJ, Gregg RE, Meng MS, et al. 1992. In vivo metabolism of a mutant apolipoprotein, apoA-1Iowa, associated with hypoalphalipoproteinemia and hereditary systemic amyloidosis. J. Lipid Res. 33:755-58
    • (1992) J. Lipid Res. , vol.33 , pp. 755-758
    • Rader, D.J.1    Gregg, R.E.2    Meng, M.S.3
  • 131
    • 0026712979 scopus 로고
    • Apolipoprotein Ai mutation Arg-60 causes autosomal dominant amyloidosis
    • 131. Soutar AK, Hawkins PN, Vigushin DM, et al. 1992. Apolipoprotein AI mutation Arg-60 causes autosomal dominant amyloidosis. Proc. Natl. Acad. Sci. USA 89:7389-93
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7389-7393
    • Soutar, A.K.1    Hawkins, P.N.2    Vigushin, D.M.3
  • 132
    • 0028803995 scopus 로고
    • A new apolipoprotein A1 variant, Trp50Arg, causes hereditary amyloidosis
    • 132. Booth DR, Tan SY, Booth SE, et al. 1995. A new apolipoprotein A1 variant, Trp50Arg, causes hereditary amyloidosis. Q.J. Med. 88:695-702
    • (1995) Q.J. Med. , vol.88 , pp. 695-702
    • Booth, D.R.1    Tan, S.Y.2    Booth, S.E.3
  • 133
    • 0029948966 scopus 로고    scopus 로고
    • Hereditary hepatic and systemic amyloidosis caused by a new deletion/insertion mutation in the apolipoprotein AI gene
    • 133. Booth DR, Yan SY, Booth SE, et al. 1996. Hereditary hepatic and systemic amyloidosis caused by a new deletion/ insertion mutation in the apolipoprotein AI gene. J. Clin. Invest. 97:2714-21
    • (1996) J. Clin. Invest. , vol.97 , pp. 2714-2721
    • Booth, D.R.1    Yan, S.Y.2    Booth, S.E.3
  • 134
    • 0031907376 scopus 로고    scopus 로고
    • Hereditary nephropathic systemic amyloidosis caused by a novel variant apolipoprotein A-1
    • 134. Persey MR, Booth DR, Booth SE, et al. 1998. Hereditary nephropathic systemic amyloidosis caused by a novel variant apolipoprotein A-1. Kidney Int. 53:276-81
    • (1998) Kidney Int. , vol.53 , pp. 276-281
    • Persey, M.R.1    Booth, D.R.2    Booth, S.E.3
  • 135
    • 0038188915 scopus 로고    scopus 로고
    • A novel apolipoprotein A-1 variant, Arg173Pro, associated with cardiac and cutaneous amyloidosis
    • 135. Hamidi Asl K, Liepnieks JJ, Nakamura M, et al. 1999. A novel apolipoprotein A-1 variant, Arg173Pro, associated with cardiac and cutaneous amyloidosis. Biochem. Biophys. Res. Commun. 257: 584-88
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 584-588
    • Hamidi Asl, K.1    Liepnieks, J.J.2    Nakamura, M.3
  • 136
    • 0010287190 scopus 로고    scopus 로고
    • Hereditary amyloid cardiomyopathy caused by a variant apolipoprotein A1
    • 136. Hamidi Asl L, Liepnicks JJ, Hamidi Asl K, et al. 1999. Hereditary amyloid cardiomyopathy caused by a variant apolipoprotein A1. Am. J. Pathol. 154:221-27
    • (1999) Am. J. Pathol. , vol.154 , pp. 221-227
    • Hamidi Asl, L.1    Liepnicks, J.J.2    Hamidi Asl, K.3
  • 137
    • 0028906054 scopus 로고
    • The transmissible spongiform encephalopathies
    • 137. Goldfarb LG, Brown P. 1995. The transmissible spongiform encephalopathies. Annu. Rev. Med. 46:57-65
    • (1995) Annu. Rev. Med. , vol.46 , pp. 57-65
    • Goldfarb, L.G.1    Brown, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.