메뉴 건너뛰기




Volumn 35, Issue 4, 2010, Pages 325-332

Transthyretin amyloidoses: New strategies for therapeutic intervention

Author keywords

[No Author keywords available]

Indexed keywords

4' IODOESORUBICIN; AMYLOID; APTAMER; DIFLUNISAL; DOXYCYCLINE; EPRODISATE; METHIONINE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 11 1F4; PREALBUMIN; PROTEIN INHIBITOR; RO 63 8695; SERUM AMYLOID P; SMALL INTERFERING RNA; STABILIZING AGENT; TAFAMIDIS MEGLUMINE; TETRAMER; UNCLASSIFIED DRUG; URSODEOXYCHOLIC ACID; VALINE;

EID: 77954612014     PISSN: 03778282     EISSN: None     Source Type: Journal    
DOI: 10.1358/dof.2010.035.04.1452076     Document Type: Review
Times cited : (2)

References (83)
  • 1
    • 0037058942 scopus 로고    scopus 로고
    • Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
    • Hammarstrom, P., Jiang, X., Hurshman, A.R., Powers, E.T., Kelly, J.W. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proc Natl Acad Sci U S A 2002, 99(Suppl. 4): 16427-32.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.SUPPL. 4 , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 2
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
    • McCutchen, S.L., Lai, Z., Miroy, G.J., Kelly, J.W., Colon, W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 1995, 34(41): 13527-36.
    • (1995) Biochemistry , vol.34 , Issue.41 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.J.3    Kelly, J.W.4    Colon, W.5
  • 3
    • 0028277396 scopus 로고
    • Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure
    • Pepys, M.B., Rademacher, T.W., Amatayakul-Chantler, S. et al. Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. Proc Natl Acad Sci U S A 1994, 91(12): 5602-6.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.12 , pp. 5602-5606
    • Pepys, M.B.1    Rademacher, T.W.2    Amatayakul-Chantler, S.3
  • 4
    • 0028988187 scopus 로고
    • Ca(2+)-dependent binding of human serum amyloid P component to Alzheimer's beta-amyloid peptide
    • Hamazaki, H. Ca(2+)-dependent binding of human serum amyloid P component to Alzheimer's beta-amyloid peptide. J Biol Chem 1995, 270(18): 10392-4.
    • (1995) J Biol Chem , vol.270 , Issue.18 , pp. 10392-10394
    • Hamazaki, H.1
  • 5
    • 0028802246 scopus 로고
    • Inhibition of Alzheimer beta-peptide fibril formation by serum amyloid P component
    • Janciauskiene, S., Garcia de Frutos, P., Carlemalm, E., Dahlback, B., Eriksson, S. Inhibition of Alzheimer beta-peptide fibril formation by serum amyloid P component. J Biol Chem 1995, 270(44): 26041-4.
    • (1995) J Biol Chem , vol.270 , Issue.44 , pp. 26041-26044
    • Janciauskiene, S.1    Garcia De Frutos, P.2    Carlemalm, E.3    Dahlback, B.4    Eriksson, S.5
  • 6
    • 0029758030 scopus 로고    scopus 로고
    • Relative efficacies of amyloid beta peptide (A beta) binding proteins in a beta aggregation
    • Webster, S., Rogers, J. Relative efficacies of amyloid beta peptide (A beta) binding proteins in A beta aggregation. J Neurosci Res 1996, 46(1): 58-66.
    • (1996) J Neurosci Res , vol.46 , Issue.1 , pp. 58-66
    • Webster, S.1    Rogers, J.2
  • 7
    • 0026744136 scopus 로고
    • Effect of serum amyloid P component level on transthyretin-derived amyloid deposition in a transgenic mouse model of familial amyloidotic polyneuropathy
    • Murakami, T., Yi, S., Maeda, S. et al. Effect of serum amyloid P component level on transthyretin-derived amyloid deposition in a transgenic mouse model of familial amyloidotic polyneuropathy. Am J Pathol 1992, 141(2): 451-6.
    • (1992) Am J Pathol , vol.141 , Issue.2 , pp. 451-456
    • Murakami, T.1    Yi, S.2    Maeda, S.3
  • 8
    • 0030757182 scopus 로고    scopus 로고
    • Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
    • Botto, M., Hawkins, P.N., Bickerstaff, M.C. et al. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nat Med 1997, 3(8): 855-9.
    • (1997) Nat Med , vol.3 , Issue.8 , pp. 855-859
    • Botto, M.1    Hawkins, P.N.2    Bickerstaff, M.C.3
  • 9
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • Pepys, M.B., Herbert, J., Hutchinson, W.L. et al. Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 2002, 417(6886): 254-9.
    • (2002) Nature , vol.417 , Issue.6886 , pp. 254-259
    • Pepys, M.B.1    Herbert, J.2    Hutchinson, W.L.3
  • 10
    • 0023128689 scopus 로고
    • Sulfated glycosaminoglycans: A common constituent of all amyloids?
    • Snow, A.D., Willmer, J., Kisilevsky, R. Sulfated glycosaminoglycans: A common constituent of all amyloids? Lab Invest 1987, 56(1): 120-3.
    • (1987) Lab Invest , vol.56 , Issue.1 , pp. 120-123
    • Snow, A.D.1    Willmer, J.2    Kisilevsky, R.3
  • 11
    • 0028278477 scopus 로고
    • Binding of heparan sulfate glycosaminoglycan to beta-amyloid peptide: Inhibition by potentially therapeutic polysulfated compounds
    • Leveugle, B., Scanameo, A., Ding, W., Fillit, H. Binding of heparan sulfate glycosaminoglycan to beta-amyloid peptide: Inhibition by potentially therapeutic polysulfated compounds. Neuroreport 1994, 5(11): 1389-92.
    • (1994) Neuroreport , vol.5 , Issue.11 , pp. 1389-1392
    • Leveugle, B.1    Scanameo, A.2    Ding, W.3    Fillit, H.4
  • 12
    • 18144377807 scopus 로고    scopus 로고
    • In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis
    • Li, J.P., Galvis, M.L., Gong, F. et al. In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis. Proc Natl Acad Sci U S A 2005, 102(18): 6473-7.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.18 , pp. 6473-6477
    • Li, J.P.1    Galvis, M.L.2    Gong, F.3
  • 13
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease
    • Yan, S.D., Chen, X., Fu, J. et al. RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease. Nature 1996, 382(6593): 685-91.
    • (1996) Nature , vol.382 , Issue.6593 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3
  • 14
    • 0001358519 scopus 로고    scopus 로고
    • Receptor-dependent cell stress and amyloid accumulation in systemic amyloidosis
    • Yan, S.D., Zhu, H., Zhu, A. et al. Receptor-dependent cell stress and amyloid accumulation in systemic amyloidosis. Nat Med 2000, 6(6): 643-51.
    • (2000) Nat Med , vol.6 , Issue.6 , pp. 643-651
    • Yan, S.D.1    Zhu, H.2    Zhu, A.3
  • 15
    • 0035478665 scopus 로고    scopus 로고
    • Familial amyloid polyneuropathy: Receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways
    • Sousa, M.M., Du Yan, S., Fernandes, R., Guimaraes, A., Stern, D., Saraiva, M.J. Familial amyloid polyneuropathy: Receptor for advanced glycation end products-dependent triggering of neuronal inflammatory and apoptotic pathways. J Neurosci 2001, 21(19): 7576-86.
    • (2001) J Neurosci , vol.21 , Issue.19 , pp. 7576-7586
    • Sousa, M.M.1    Du Yan, S.2    Fernandes, R.3    Guimaraes, A.4    Stern, D.5    Saraiva, M.J.6
  • 16
    • 0342646984 scopus 로고    scopus 로고
    • Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor kB (NF-kB) activation
    • Sousa, M.M., Yan, S.D., Stern, D., Saraiva, M.J. Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor kB (NF-kB) activation. Lab Invest 2000, 80(7): 1101-10.
    • (2000) Lab Invest , vol.80 , Issue.7 , pp. 1101-1110
    • Sousa, M.M.1    Yan, S.D.2    Stern, D.3    Saraiva, M.J.4
  • 17
    • 0036934382 scopus 로고    scopus 로고
    • Advanced glycation end products (AGE) and the receptor for AGE are present in gastrointestinal tract of familial amyloidotic polyneuropathy patients but do not induce NF-kappaB activation
    • Matsunaga, N., Anan, I., Forsgren, S. et al. Advanced glycation end products (AGE) and the receptor for AGE are present in gastrointestinal tract of familial amyloidotic polyneuropathy patients but do not induce NF-kappaB activation. Acta Neuropathol 2002, 104(5): 441-7.
    • (2002) Acta Neuropathol , vol.104 , Issue.5 , pp. 441-447
    • Matsunaga, N.1    Anan, I.2    Forsgren, S.3
  • 18
    • 0034017171 scopus 로고    scopus 로고
    • Advanced glycation end product in familial amyloidotic polyneuropathy (FAP)
    • Nyhlin, N., Ando, Y., Nagai, R. et al. Advanced glycation end product in familial amyloidotic polyneuropathy (FAP). J Intern Med 2000, 247(4): 485-92.
    • (2000) J Intern Med , vol.247 , Issue.4 , pp. 485-492
    • Nyhlin, N.1    Ando, Y.2    Nagai, R.3
  • 19
    • 0031575827 scopus 로고    scopus 로고
    • Oxidative stress is found in amyloid deposits in systemic amyloidosis
    • Ando, Y., Nyhlin, N., Suhr, O. et al. Oxidative stress is found in amyloid deposits in systemic amyloidosis. Biochem Biophys Res Comm 1997, 232(2): 497-502.
    • (1997) Biochem Biophys Res Comm , vol.232 , Issue.2 , pp. 497-502
    • Ando, Y.1    Nyhlin, N.2    Suhr, O.3
  • 20
    • 58849148616 scopus 로고    scopus 로고
    • Mitochondrial haplogroup is associated with the phenotype of familial amyloidosis with polyneuropathy in Swedish and French patients
    • Olsson, M., Hellman, U., Plante-Bordeneuve, V., Jonasson, J., Lang, K., Suhr, O.B. Mitochondrial haplogroup is associated with the phenotype of familial amyloidosis with polyneuropathy in Swedish and French patients. Clin Genet 2009, 75(2): 163-8.
    • (2009) Clin Genet , vol.75 , Issue.2 , pp. 163-168
    • Olsson, M.1    Hellman, U.2    Plante-Bordeneuve, V.3    Jonasson, J.4    Lang, K.5    Suhr, O.B.6
  • 21
    • 0034126224 scopus 로고    scopus 로고
    • Liver transplantation for hereditary transthyretin amyloidosis
    • Suhr, O.B., Herlenius, G., Friman, S., Ericzon, B.G. Liver transplantation for hereditary transthyretin amyloidosis. Liver Transpl 2000, 6(3): 263-76.
    • (2000) Liver Transpl , vol.6 , Issue.3 , pp. 263-276
    • Suhr, O.B.1    Herlenius, G.2    Friman, S.3    Ericzon, B.G.4
  • 22
    • 0032558120 scopus 로고    scopus 로고
    • Progressive cardiac amyloidosis following liver transplantation for familial amyloid polyneuropathy: Implications for amyloid fibrillogenesis
    • Stangou, A.J., Hawkins, P.N., Heaton, N.D. et al. Progressive cardiac amyloidosis following liver transplantation for familial amyloid polyneuropathy: Implications for amyloid fibrillogenesis. Transplantation 1998, 66(2): 229-33.
    • (1998) Transplantation , vol.66 , Issue.2 , pp. 229-233
    • Stangou, A.J.1    Hawkins, P.N.2    Heaton, N.D.3
  • 23
    • 20244385523 scopus 로고    scopus 로고
    • Targeted conversion of the transthyretin gene in vitro and in vivo
    • Nakamura, M., Ando, Y., Nagahara, S. et al. Targeted conversion of the transthyretin gene in vitro and in vivo. Gene Ther 2004, 11(10): 838-46.
    • (2004) Gene Ther , vol.11 , Issue.10 , pp. 838-846
    • Nakamura, M.1    Ando, Y.2    Nagahara, S.3
  • 25
    • 0025278448 scopus 로고
    • Fibril in senile systemic amyloidosis is derived from normal transthyretin
    • Westermark, P., Sletten, K., Johansson, B., Cornwell, G.Gd. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci U S A 1990, 87(7): 2843-5.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.7 , pp. 2843-2845
    • Westermark, P.1    Sletten, K.2    Johansson, B.3    Cornwell, G.G.4
  • 26
    • 19944365557 scopus 로고    scopus 로고
    • Amyloid deposits in transthyretin-derived amyloidosis: Cleaved transthyretin is associated with distinct amyloid morphology
    • Bergstrom, J., Gustavsson, A., Hellman, U. et al. Amyloid deposits in transthyretin-derived amyloidosis: Cleaved transthyretin is associated with distinct amyloid morphology. J Pathol 2005, 206(2): 224-32.
    • (2005) J Pathol , vol.206 , Issue.2 , pp. 224-232
    • Bergstrom, J.1    Gustavsson, A.2    Hellman, U.3
  • 27
    • 53149119909 scopus 로고    scopus 로고
    • Amyloid fibril composition is related to the phenotype of hereditary transthyretin V30M amyloidosis
    • Ihse, E., Ybo, A., Suhr, O.B., Lindqvist, P., Backman, C., Westermark, P. Amyloid fibril composition is related to the phenotype of hereditary transthyretin V30M amyloidosis. J Pathol 2008, 216(2): 253-61.
    • (2008) J Pathol , vol.216 , Issue.2 , pp. 253-261
    • Ihse, E.1    Ybo, A.2    Suhr, O.B.3    Lindqvist, P.4    Backman, C.5    Westermark, P.6
  • 28
    • 0014188325 scopus 로고
    • The adoptive transfer of experimental mouse amyloidosis by intravenous injections of spleen cell extracts from casein-treated syngeneic donor mice
    • Ranlov, P. The adoptive transfer of experimental mouse amyloidosis by intravenous injections of spleen cell extracts from casein-treated syngeneic donor mice. Acta Pathol Microbiol Scand 1967, 70(3): 321-35.
    • (1967) Acta Pathol Microbiol Scand , vol.70 , Issue.3 , pp. 321-335
    • Ranlov, P.1
  • 30
    • 17844367336 scopus 로고    scopus 로고
    • Protein fibrils in nature can enhance amyloid protein a amyloidosis in mice: Cross-seeding as a disease mechanism
    • Lundmark, K., Westermark, G.T., Olsen, A., Westermark, P. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism. Proc Natl Acad Sci U S A 2005, 102(17): 6098-102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.17 , pp. 6098-6102
    • Lundmark, K.1    Westermark, G.T.2    Olsen, A.3    Westermark, P.4
  • 31
    • 0034193676 scopus 로고    scopus 로고
    • Enhancement of AA-amyloid formation in mice by transthyretin amyloid fragments and polyethylene glycol
    • Mambule, C., Ando, Y., Anan, I. et al. Enhancement of AA-amyloid formation in mice by transthyretin amyloid fragments and polyethylene glycol. Biochim Biophys Acta 2000, 1474(3): 331-6.
    • (2000) Biochim Biophys Acta , vol.1474 , Issue.3 , pp. 331-336
    • Mambule, C.1    Ando, Y.2    Anan, I.3
  • 32
    • 33845608550 scopus 로고    scopus 로고
    • Progressive wild-type transthyretin deposition after liver transplantation preferentially occurs onto myocardium in FAP patients
    • Yazaki, M., Mitsuhashi, S., Tokuda, T. et al. Progressive wild-type transthyretin deposition after liver transplantation preferentially occurs onto myocardium in FAP patients. Am J Transplant 2007, 7(1): 235-42.
    • (2007) Am J Transplant , vol.7 , Issue.1 , pp. 235-242
    • Yazaki, M.1    Mitsuhashi, S.2    Tokuda, T.3
  • 33
    • 21144444931 scopus 로고    scopus 로고
    • Transmission of systemic transthyretin amyloidosis by means of domino liver transplantation
    • Stangou, A.J., Heaton, N.D., Hawkins, P.N. Transmission of systemic transthyretin amyloidosis by means of domino liver transplantation. N Engl J Med 2005, 352(22): 2356.
    • (2005) N Engl J Med , vol.352 , Issue.22 , pp. 2356
    • Stangou, A.J.1    Heaton, N.D.2    Hawkins, P.N.3
  • 34
  • 35
    • 0037030659 scopus 로고    scopus 로고
    • Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis
    • Lachmann, H.J., Booth, D.R., Booth, S.E. et al. Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis. N Engl J Med 2002, 346(23): 1786-91.
    • (2002) N Engl J Med , vol.346 , Issue.23 , pp. 1786-1791
    • Lachmann, H.J.1    Booth, D.R.2    Booth, S.E.3
  • 36
    • 70449746706 scopus 로고    scopus 로고
    • Misclassification of amyloidosis is unwarranted
    • Solomon, A., Murphy, C., Westermark, P. Misclassification of amyloidosis is unwarranted. Blood 2006, 107(9): 3489-91.
    • (2006) Blood , vol.107 , Issue.9 , pp. 3489-3491
    • Solomon, A.1    Murphy, C.2    Westermark, P.3
  • 37
    • 0028200952 scopus 로고
    • Geographical distribution of TTR met30 carriers in northern Sweden: Discrepancy between carrier frequency and prevalence rate
    • Holmgren, G., Costa, P.M., Andersson, C. et al. Geographical distribution of TTR met30 carriers in northern Sweden: Discrepancy between carrier frequency and prevalence rate. J Med Genet 1994, 31(5): 351-4.
    • (1994) J Med Genet , vol.31 , Issue.5 , pp. 351-354
    • Holmgren, G.1    Costa, P.M.2    Andersson, C.3
  • 38
    • 68649090785 scopus 로고    scopus 로고
    • Animal models of human amyloidoses: Are transgenic mice worth the time and trouble?
    • Buxbaum, J.N. Animal models of human amyloidoses: Are transgenic mice worth the time and trouble? FEBS Lett 2009, 583(16): 2663-73.
    • (2009) FEBS Lett , vol.583 , Issue.16 , pp. 2663-2673
    • Buxbaum, J.N.1
  • 39
    • 0025963347 scopus 로고
    • Systemic amyloidosis in transgenic mice carrying the human mutant transthyretin (Met30) gene. Pathologic similarity to human familial amyloidotic polyneuropathy, type I
    • Yi, S., Takahashi, K., Naito, M. et al. Systemic amyloidosis in transgenic mice carrying the human mutant transthyretin (Met30) gene. Pathologic similarity to human familial amyloidotic polyneuropathy, type I. Am J Pathol 1991, 138(2): 403-12.
    • (1991) Am J Pathol , vol.138 , Issue.2 , pp. 403-412
    • Yi, S.1    Takahashi, K.2    Naito, M.3
  • 40
    • 71349088766 scopus 로고    scopus 로고
    • The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems
    • Santos, S.D., Fernandes, R., Saraiva, M.J. The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems. Neurobiol Aging 2010, 31(2): 280-9.
    • (2010) Neurobiol Aging , vol.31 , Issue.2 , pp. 280-289
    • Santos, S.D.1    Fernandes, R.2    Saraiva, M.J.3
  • 41
    • 0036841818 scopus 로고    scopus 로고
    • Evidence for early cytotoxic aggregates in transgenic mice for human transthyretin Leu55Pro
    • Sousa, M.M., Fernandes, R., Palha, J.A., Taboada, A., Vieira, P., Saraiva, M.J. Evidence for early cytotoxic aggregates in transgenic mice for human transthyretin Leu55Pro. Am J Pathol 2002, 161(5): 1935-48.
    • (2002) Am J Pathol , vol.161 , Issue.5 , pp. 1935-1948
    • Sousa, M.M.1    Fernandes, R.2    Palha, J.A.3    Taboada, A.4    Vieira, P.5    Saraiva, M.J.6
  • 42
    • 0242643752 scopus 로고    scopus 로고
    • The pathogenesis of transthyretin tissue deposition: Lessons from transgenic mice
    • Buxbaum, J., Tagoe, C., Gallo, G., Reixach, N., French, D. The pathogenesis of transthyretin tissue deposition: Lessons from transgenic mice. Amyloid 2003, 10(Suppl. 1): 2-6.
    • (2003) Amyloid , vol.10 , Issue.SUPPL. 1 , pp. 2-6
    • Buxbaum, J.1    Tagoe, C.2    Gallo, G.3    Reixach, N.4    French, D.5
  • 43
    • 34547969339 scopus 로고    scopus 로고
    • Misfolded transthyretin causes behavioral changes in a Drosophila model for transthyretin-associated amyloidosis
    • Pokrzywa, M., Dacklin, I., Hultmark, D., Lundgren, E. Misfolded transthyretin causes behavioral changes in a Drosophila model for transthyretin-associated amyloidosis. Eur J Neurosci 2007, 26(4): 913-24.
    • (2007) Eur J Neurosci , vol.26 , Issue.4 , pp. 913-924
    • Pokrzywa, M.1    Dacklin, I.2    Hultmark, D.3    Lundgren, E.4
  • 45
    • 33751082387 scopus 로고    scopus 로고
    • Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis
    • Sekijima, Y., Dendle, M.A., Kelly, J.W. Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis. Amyloid 2006, 13(4): 236-49.
    • (2006) Amyloid , vol.13 , Issue.4 , pp. 236-249
    • Sekijima, Y.1    Dendle, M.A.2    Kelly, J.W.3
  • 47
    • 30644472492 scopus 로고    scopus 로고
    • Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation
    • Sato, T., Ando, Y., Susuki, S. et al. Chromium(III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation. FEBS Lett 2006, 580(2): 491-6.
    • (2006) FEBS Lett , vol.580 , Issue.2 , pp. 491-496
    • Sato, T.1    Ando, Y.2    Susuki, S.3
  • 48
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation
    • Kelly, J., Lansbury, P. A chemical approach to elucidate the mechanism of transthyretin and β-protein amyloid fibril formation. Amyloid 1994, 1: 186-205.
    • (1994) Amyloid , vol.1 , pp. 186-205
    • Kelly, J.1    Lansbury, P.2
  • 49
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that con self-assemble into amyloid
    • Lai, Z., Colon, W., Kelly, J.W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that con self-assemble into amyloid. Biochemistry 1996, 35(20): 6470-82.
    • (1996) Biochemistry , vol.35 , Issue.20 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 50
    • 77954589603 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • Quintas, A., Vaz, D.C., Cardoso, I., Saraiva, M.J., Brito, R.M. Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J Biol Chem 2001, 16: 16.
    • (2001) J Biol Chem , vol.16 , pp. 16
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.4    Brito, R.M.5
  • 51
    • 33646185371 scopus 로고    scopus 로고
    • RNAI-mediated gene silencing in non-human primates
    • Zimmermann, T.S., Lee, A.C., Akinc, A. et al. RNAI-mediated gene silencing in non-human primates. Nature 2006, 441(7089): 111-4.
    • (2006) Nature , vol.441 , Issue.7089 , pp. 111-114
    • Zimmermann, T.S.1    Lee, A.C.2    Akinc, A.3
  • 53
    • 34249076067 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell
    • Sato, T., Susuki, S., Suico, M.A. et al. Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell. EMBO J 2007, 26(10): 2501-12.
    • (2007) EMBO J , vol.26 , Issue.10 , pp. 2501-2512
    • Sato, T.1    Susuki, S.2    Suico, M.A.3
  • 54
    • 43249124993 scopus 로고    scopus 로고
    • Activation of the heat shock response in familial amyloidotic polyneuropathy
    • Santos, S.D., Magalhaes, J., Saraiva, M.J. Activation of the heat shock response in familial amyloidotic polyneuropathy. J Neuropathol Exp Neurol 2008, 67(5): 449-55.
    • (2008) J Neuropathol Exp Neurol , vol.67 , Issue.5 , pp. 449-455
    • Santos, S.D.1    Magalhaes, J.2    Saraiva, M.J.3
  • 55
  • 56
    • 34447629569 scopus 로고    scopus 로고
    • Therapeutic approaches for prion and Alzheimer's diseases
    • Wisniewski, T., Sigurdsson, E.M. Therapeutic approaches for prion and Alzheimer's diseases. FEBS J 2007, 274(15): 3784-98.
    • (2007) FEBS J , vol.274 , Issue.15 , pp. 3784-3798
    • Wisniewski, T.1    Sigurdsson, E.M.2
  • 57
    • 0015644626 scopus 로고
    • Morphologic, chemical, and immunologic studies of amyloid-like fibrils formed from Bence Jones proteins by proteolysis
    • Linke, R.P., Zucker-Franklin, D., Franklin, E.D. Morphologic, chemical, and immunologic studies of amyloid-like fibrils formed from Bence Jones proteins by proteolysis. J Immunol 1973, 111(1): 10-23.
    • (1973) J Immunol , vol.111 , Issue.1 , pp. 10-23
    • Linke, R.P.1    Zucker-Franklin, D.2    Franklin, E.D.3
  • 58
    • 0033053678 scopus 로고    scopus 로고
    • Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants
    • Goldsteins, G., Persson, H., Andersson, K. et al. Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants. Proc Natl Acad Sci U S A 1999, 96(6): 3108-13.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.6 , pp. 3108-3113
    • Goldsteins, G.1    Persson, H.2    Andersson, K.3
  • 59
    • 32844473029 scopus 로고    scopus 로고
    • Immunization in familial amyloidotic polyneuropathy: Counteracting deposition by immunization with a Y78F TTR mutant
    • Terazaki, H., Ando, Y., Fernandes, R., Yamamura, K.I., Maeda, S., Saraiva, M.J. Immunization in familial amyloidotic polyneuropathy: Counteracting deposition by immunization with a Y78F TTR mutant. Lab Invest 2006, 86(1): 23-31.
    • (2006) Lab Invest , vol.86 , Issue.1 , pp. 23-31
    • Terazaki, H.1    Ando, Y.2    Fernandes, R.3    Yamamura, K.I.4    Maeda, S.5    Saraiva, M.J.6
  • 61
    • 0347569588 scopus 로고    scopus 로고
    • Immunotherapy in systemic primary (AL) amyloidosis using amyloid-reactive monoclonal antibodies
    • Solomon, A., Weiss, D.T., Wall, J.S. Immunotherapy in systemic primary (AL) amyloidosis using amyloid-reactive monoclonal antibodies. Cancer Biother Radiopharm 2003, 18(6): 853-60.
    • (2003) Cancer Biother Radiopharm , vol.18 , Issue.6 , pp. 853-860
    • Solomon, A.1    Weiss, D.T.2    Wall, J.S.3
  • 62
    • 27144437903 scopus 로고    scopus 로고
    • Quantitative high-resolution microradiographic imaging of amyloid deposits in a novel murine model of AA amyloidosis
    • Wall, J.S., Kennel, S.J., Paulus, M.J. et al. Quantitative high-resolution microradiographic imaging of amyloid deposits in a novel murine model of AA amyloidosis. Amyloid 2005, 12: 149-56.
    • (2005) Amyloid , vol.12 , pp. 149-156
    • Wall, J.S.1    Kennel, S.J.2    Paulus, M.J.3
  • 63
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain, B., Wetzel, R. Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci U S A 2002, 99(3): 1485-90.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.3 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 64
    • 33646865770 scopus 로고    scopus 로고
    • Diagnostic and therapeutic potential of amyloid-reactive IgG antibodies contained in human sera
    • O'Nuallain, B., Hrncic, R., Wall, J.S., Weiss, D.T., Solomon, A. Diagnostic and therapeutic potential of amyloid-reactive IgG antibodies contained in human sera. J Immunol 2006, 176(11): 7071-8.
    • (2006) J Immunol , vol.176 , Issue.11 , pp. 7071-7078
    • O'Nuallain, B.1    Hrncic, R.2    Wall, J.S.3    Weiss, D.T.4    Solomon, A.5
  • 65
    • 67849130968 scopus 로고    scopus 로고
    • Developing novel immunogens for a safe and effective Alzheimer's disease vaccine
    • Lemere, C.A. Developing novel immunogens for a safe and effective Alzheimer's disease vaccine. Prog Brain Res 2009, 175: 83-93.
    • (2009) Prog Brain Res , vol.175 , pp. 83-93
    • Lemere, C.A.1
  • 66
    • 73349091534 scopus 로고    scopus 로고
    • A phase 2 multiple ascending dose trial of bapineuzumab in mild to moderate Alzheimer disease
    • Salloway, S., Sperting, R., Gilman, S. et al. A phase 2 multiple ascending dose trial of bapineuzumab in mild to moderate Alzheimer disease. Neurology 2009, 73(24): 2061-70.
    • (2009) Neurology , vol.73 , Issue.24 , pp. 2061-2070
    • Salloway, S.1    Sperting, R.2    Gilman, S.3
  • 67
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed, R., Head, E., Sarsoza, F. et al. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2007, 2: 18.
    • (2007) Mol Neurodegener , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3
  • 68
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J.L., McIntire, T.M., Milton, S.C., Cotman, C.W., Glabe, C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003, 300(5618): 486-9.
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 69
    • 70350324013 scopus 로고    scopus 로고
    • An amyloid-beta protofibril-selective antibody prevents amyloid formation in a mouse model of Alzheimer's disease
    • Lord, A., Gumucio, A., Englund, H. et al. An amyloid-beta protofibril-selective antibody prevents amyloid formation in a mouse model of Alzheimer's disease. Neurobiol Dis 2009, 36(3): 425-34.
    • (2009) Neurobiol Dis , vol.36 , Issue.3 , pp. 425-434
    • Lord, A.1    Gumucio, A.2    Englund, H.3
  • 70
    • 33747164245 scopus 로고    scopus 로고
    • Aptamers come of age - At last
    • Bunka, D.H.J., Stockley, P.G. Aptamers come of age - at last. Nat Rev Microbiol 2006, 4(8): 588-96.
    • (2006) Nat Rev Microbiol , vol.4 , Issue.8 , pp. 588-596
    • Bunka, D.H.J.1    Stockley, P.G.2
  • 71
    • 36348973644 scopus 로고    scopus 로고
    • Production and characterization of RNA aptamers specific for amyloid fibril epitopes
    • Bunka, D.H., Mantle, B.J., Morten, I.J., Tennent, G.A., Radford, S.E., Stockley, P.G. Production and characterization of RNA aptamers specific for amyloid fibril epitopes. J Biol Chem 2007, 282(47): 34500-9.
    • (2007) J Biol Chem , vol.282 , Issue.47 , pp. 34500-34509
    • Bunka, D.H.1    Mantle, B.J.2    Morten, I.J.3    Tennent, G.A.4    Radford, S.E.5    Stockley, P.G.6
  • 72
    • 0036289319 scopus 로고    scopus 로고
    • Selection of RNA aptamers to the Alzheimer's disease amyloid peptide
    • Ylera, F., Lurz, R., Erdmann, V.A., Fürste, J.P. Selection of RNA aptamers to the Alzheimer's disease amyloid peptide. Biochem Biophys Res Commun 2002, 290(5): 1583-8.
    • (2002) Biochem Biophys Res Commun , vol.290 , Issue.5 , pp. 1583-1588
    • Ylera, F.1    Lurz, R.2    Erdmann, V.A.3    Fürste, J.P.4
  • 74
    • 70450159254 scopus 로고    scopus 로고
    • RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity
    • Rahimi, F., Murakami, K., Summers, J.L., Chen, C.H., Bitan, G. RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity. PLoS One 2009, 4(11): e7694.
    • (2009) PLoS One , vol.4 , Issue.11
    • Rahimi, F.1    Murakami, K.2    Summers, J.L.3    Chen, C.H.4    Bitan, G.5
  • 75
    • 34249992082 scopus 로고    scopus 로고
    • Eprodisate for the treatment of renal disease in AA amyloidosis
    • Dember, L.M., Hawkins, P.N., Hazenberg, B.P. et al. Eprodisate for the treatment of renal disease in AA amyloidosis. New Engl J Med 2007, 356(23): 2349-60.
    • (2007) New Engl J Med , vol.356 , Issue.23 , pp. 2349-2360
    • Dember, L.M.1    Hawkins, P.N.2    Hazenberg, B.P.3
  • 76
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • Reixach, N., Deechongkit, S., Jiang, X., Kelly, J.W., Buxbaum, J.N. Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc Natl Acad Sci U S A 2004, 101(9): 2817-22.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.9 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 77
    • 0035068510 scopus 로고    scopus 로고
    • Scavenger treatment of free radical injury in familial amyloidotic polyneuropathy: A study on Swedish transplanted and non-transplanted patients
    • Suhr, O.B., Lang, K., Wikstrom, L. et al. Scavenger treatment of free radical injury in familial amyloidotic polyneuropathy: A study on Swedish transplanted and non-transplanted patients. Scand J Clin Lab Invest 2001, 61(1): 11-8.
    • (2001) Scand J Clin Lab Invest , vol.61 , Issue.1 , pp. 11-18
    • Suhr, O.B.1    Lang, K.2    Wikstrom, L.3
  • 78
    • 49349097870 scopus 로고    scopus 로고
    • Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of familial amyloidotic polyneuropathy
    • Macedo, B., Batista, A.R., Ferreira, N., Almeida, M.R., Saraiva, M.J. Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of familial amyloidotic polyneuropathy. Biochim Biophys Acta 2008, 1782(9): 517-22.
    • (2008) Biochim Biophys Acta , vol.1782 , Issue.9 , pp. 517-522
    • Macedo, B.1    Batista, A.R.2    Ferreira, N.3    Almeida, M.R.4    Saraiva, M.J.5
  • 79
    • 0033872046 scopus 로고    scopus 로고
    • 4′-iodo-4′-deoxydoxorubicin disrupts the fibrillar structure of transthyretin amyloid
    • Palha, J.A., Ballinari, D., Amboldi, N. et al. 4′-iodo-4′- deoxydoxorubicin disrupts the fibrillar structure of transthyretin amyloid. Am J Pathol 2000, 156(6): 1919-25.
    • (2000) Am J Pathol , vol.156 , Issue.6 , pp. 1919-1925
    • Palha, J.A.1    Ballinari, D.2    Amboldi, N.3
  • 80
    • 0036130774 scopus 로고    scopus 로고
    • A multicenter phase II trial of 4′-iodo-4′deoxydoxorubicin (IDOX) in primary amyloidosis (AL)
    • Gertz, M.A., Lacy, M.Q., Dispenzieri, A. et al. A multicenter phase II trial of 4′-iodo-4′deoxydoxorubicin (IDOX) in primary amyloidosis (AL). Amyloid 2002, 9(1): 24-30.
    • (2002) Amyloid , vol.9 , Issue.1 , pp. 24-30
    • Gertz, M.A.1    Lacy, M.Q.2    Dispenzieri, A.3
  • 81
    • 0038375018 scopus 로고    scopus 로고
    • 4′-iodo-4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: Screening for TTR fibril disrupters
    • Cardoso, I., Merlini, G., Saraiva, M.J. 4′-iodo-4′- deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: Screening for TTR fibril disrupters. FASEB J 2003, 17(8): 803-9.
    • (2003) FASEB J , vol.17 , Issue.8 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 82
    • 33644919388 scopus 로고    scopus 로고
    • Doxycycline disrupts transthyretin amyloid: Evidence from studies in a FAP transgenic mice model
    • Cardoso, I., Saraiva, M.J. Doxycycline disrupts transthyretin amyloid: Evidence from studies in a FAP transgenic mice model. FASEB J 2006, 20(2): 234-9.
    • (2006) FASEB J , vol.20 , Issue.2 , pp. 234-239
    • Cardoso, I.1    Saraiva, M.J.2
  • 83
    • 70350549746 scopus 로고    scopus 로고
    • Liver transplantation for familial amyloidotic polyneuropathy: Impact on Swedish patients' survival
    • Okamoto, S., Wixner, J., Obayashi, K. et al. Liver transplantation for familial amyloidotic polyneuropathy: Impact on Swedish patients' survival. Liver Transpl 2009, 15(10): 1229-35.
    • (2009) Liver Transpl , vol.15 , Issue.10 , pp. 1229-1235
    • Okamoto, S.1    Wixner, J.2    Obayashi, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.