메뉴 건너뛰기




Volumn 408, Issue 1, 2007, Pages 131-138

Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: Relevance in drug design

Author keywords

Aggregation; Amyloid; Anti amyloidogenic drug; Iododiflunisal; Transthyretin

Indexed keywords

AMYLOIDS; ANTI-AMYLOIDOGENIC DRUGS; IODODIFLUNISAL; TRANSTHYRETIN;

EID: 36348960658     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070689     Document Type: Article
Times cited : (30)

References (29)
  • 1
    • 4344714361 scopus 로고    scopus 로고
    • Familial amyloidotic polyneuropathy: Protein aggregation in the peripheral nervous system
    • Saraiva, M. J., Sousa, M. M., Cardoso, I. and Fernandes, R. (2004) Familial amyloidotic polyneuropathy: protein aggregation in the peripheral nervous system. J. Mol. Neurosci. 23, 35-40
    • (2004) J. Mol. Neurosci , vol.23 , pp. 35-40
    • Saraiva, M.J.1    Sousa, M.M.2    Cardoso, I.3    Fernandes, R.4
  • 3
    • 0032945924 scopus 로고    scopus 로고
    • Synthesis and evaluation of anthranilic acid-based transthyretin amyloid fibril inhibitors
    • Oza, V. B., Petrassi, H. M., Purkey, H. E. and Kelly, J. W. (1999) Synthesis and evaluation of anthranilic acid-based transthyretin amyloid fibril inhibitors. Bioorg. Med. Chem. Lett. 9, 1-6
    • (1999) Bioorg. Med. Chem. Lett , vol.9 , pp. 1-6
    • Oza, V.B.1    Petrassi, H.M.2    Purkey, H.E.3    Kelly, J.W.4
  • 4
    • 0031684499 scopus 로고    scopus 로고
    • Discoveriog transthyretin amyloid fibril inhibitors by limited screening
    • Baures, P. W., Peterson, S. A. and Kelly, J. W. (1998) Discoveriog transthyretin amyloid fibril inhibitors by limited screening. Bioorg. Med. Chem. 6, 1389-1401
    • (1998) Bioorg. Med. Chem , vol.6 , pp. 1389-1401
    • Baures, P.W.1    Peterson, S.A.2    Kelly, J.W.3
  • 5
    • 0032970177 scopus 로고    scopus 로고
    • Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid
    • Baures, P. W., Oza, V. B., Peterson, S. A. and Kelly, J. W. (1999) Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid. Bioorg. Med. Chem. 7, 1339-1347
    • (1999) Bioorg. Med. Chem , vol.7 , pp. 1339-1347
    • Baures, P.W.1    Oza, V.B.2    Peterson, S.A.3    Kelly, J.W.4
  • 7
    • 0036841818 scopus 로고    scopus 로고
    • Evidence lor early cytotoxic aggregates in transgenic mice for human transthyretin
    • Sousa, M. M., Fernandes, R., Palha, J. A., Taboada, A., Vieira, P. and Saraiva, M. J. (2002) Evidence lor early cytotoxic aggregates in transgenic mice for human transthyretin. Am. J. Pathol. 161, 1935-1948
    • (2002) Am. J. Pathol , vol.161 , pp. 1935-1948
    • Sousa, M.M.1    Fernandes, R.2    Palha, J.A.3    Taboada, A.4    Vieira, P.5    Saraiva, M.J.6
  • 9
    • 0033976870 scopus 로고    scopus 로고
    • Transthyretin in high density lipoproteins: Association with apolipoprotein A-I
    • Sousa, M. M., Berglund, L. and Saraiva, M. J. (2000) Transthyretin in high density lipoproteins: association with apolipoprotein A-I. J. Lipid Res. 41, 58-65
    • (2000) J. Lipid Res , vol.41 , pp. 58-65
    • Sousa, M.M.1    Berglund, L.2    Saraiva, M.J.3
  • 10
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel, W. J., Billeci, T. M., Stults, J. T., Wond, S. C. Grimley, C. and Watanabe, C. (1993) Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. U.S.A. 90, 5011-5015
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wond, S.C.4    Grimley, C.5    Watanabe, C.6
  • 11
    • 0025825160 scopus 로고
    • Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyoeuropathy (FAP)
    • Furuya, H., Saraiva, M. J. M., Gawinowicz, M. A., Alves, I. L., Costa, P. P., Sasaki, H., Goto, I. and Sakaki, Y. (1991) Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyoeuropathy (FAP). Biochemistry 30, 2415-2421
    • (1991) Biochemistry , vol.30 , pp. 2415-2421
    • Furuya, H.1    Saraiva, M.J.M.2    Gawinowicz, M.A.3    Alves, I.L.4    Costa, P.P.5    Sasaki, H.6    Goto, I.7    Sakaki, Y.8
  • 12
    • 0030885583 scopus 로고    scopus 로고
    • Thyroxine binding to transthyretin Met119. Comparative studies of different heterozygotic carriers and structural analysis
    • Almeida, M. R., Damas, A. M., Lans, M. C., Brower, A. and Saraiva, M. J. (1997) Thyroxine binding to transthyretin Met119. Comparative studies of different heterozygotic carriers and structural analysis. Endocrine 6, 309-315
    • (1997) Endocrine , vol.6 , pp. 309-315
    • Almeida, M.R.1    Damas, A.M.2    Lans, M.C.3    Brower, A.4    Saraiva, M.J.5
  • 14
    • 84988113204 scopus 로고
    • Demonstration of human prealbumin by double one-dimensional slab gel electrophoresis
    • Altland, K., Rauh, S. and Hacker, R. (1981) Demonstration of human prealbumin by double one-dimensional slab gel electrophoresis. Electrophoresis 2, 148-155
    • (1981) Electrophoresis , vol.2 , pp. 148-155
    • Altland, K.1    Rauh, S.2    Hacker, R.3
  • 15
    • 3242807241 scopus 로고    scopus 로고
    • Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative
    • Almeida, M. R., Macedo, B., Cardoso, I., Alves, I., Valencia, G., Arsequell, G., Planas, A. and Saraiva, M. J. (2004) Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative. Biochem. J. 381, 351-356
    • (2004) Biochem. J , vol.381 , pp. 351-356
    • Almeida, M.R.1    Macedo, B.2    Cardoso, I.3    Alves, I.4    Valencia, G.5    Arsequell, G.6    Planas, A.7    Saraiva, M.J.8
  • 16
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: Evidence for toxicity of nonfibrillar aggregates
    • Sousa, M. M., Cardoso, I., Fernandes, R., Guimaraes, A. and Saraiva, M. J. (2001) Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am. J. Pathol. 159, 1993-2000
    • (2001) Am. J. Pathol , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 17
    • 0030751036 scopus 로고    scopus 로고
    • An in vitro cellular system for generation of AA amyloid
    • Palm, M., Nielsen, E. H. and Svehag, S. E. (1997) An in vitro cellular system for generation of AA amyloid. APMIS 105, 603-608
    • (1997) APMIS , vol.105 , pp. 603-608
    • Palm, M.1    Nielsen, E.H.2    Svehag, S.E.3
  • 18
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenile 2 in transfected cells
    • Kim, T. W., Pettingell, W. H., Hallmark, O. G., Moir, R. D., Wasco, W. and Tanzi, R. E. (1997) Endoproteolytic cleavage and proteasomal degradation of presenile 2 in transfected cells. J. Biol. Chem. 272, 11006-11010
    • (1997) J. Biol. Chem , vol.272 , pp. 11006-11010
    • Kim, T.W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 19
    • 31044450074 scopus 로고    scopus 로고
    • Overexpression of amyloid precursor protein induces susceptibility to oxidative stress in human neuroblastoma SH-SY5Y cells
    • Matsumoto, K., Akao, Y., Yi, H., Shamoto-Nagai, M., Maruyama, W. and Naoi, M. (2006) Overexpression of amyloid precursor protein induces susceptibility to oxidative stress in human neuroblastoma SH-SY5Y cells. J. Neural Transm. 113, 125-135
    • (2006) J. Neural Transm , vol.113 , pp. 125-135
    • Matsumoto, K.1    Akao, Y.2    Yi, H.3    Shamoto-Nagai, M.4    Maruyama, W.5    Naoi, M.6
  • 20
    • 33646772566 scopus 로고    scopus 로고
    • The spice sage and its active ingredient rosmarinic acid protect PC12 cells from amyloid-β peptide-induced neurotoxicity
    • Iuvone, T., De Filippis, D., Esposito, G., D'Amico, A. and Izzo, A. A. (2006) The spice sage and its active ingredient rosmarinic acid protect PC12 cells from amyloid-β peptide-induced neurotoxicity. J. Pharmacol. Exp. Ther. 317, 1143-1149
    • (2006) J. Pharmacol. Exp. Ther , vol.317 , pp. 1143-1149
    • Iuvone, T.1    De Filippis, D.2    Esposito, G.3    D'Amico, A.4    Izzo, A.A.5
  • 21
    • 0029057814 scopus 로고
    • Intracellular Aβ1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • Yang, A. J., Knauer, M., Burdick, D. A. and Glabe, C. (1995) Intracellular Aβ1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. J. Biol. Chem. 270, 14786-14792
    • (1995) J. Biol. Chem , vol.270 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 23
    • 0346333094 scopus 로고    scopus 로고
    • Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis
    • Adamski-Werner, S. L., Palaninathan, S. K., Sacchettini, J. C. and Kelly, J. W. (2004) Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis. J. Med. Chem. 47, 355-374
    • (2004) J. Med. Chem , vol.47 , pp. 355-374
    • Adamski-Werner, S.L.1    Palaninathan, S.K.2    Sacchettini, J.C.3    Kelly, J.W.4
  • 24
    • 0242299247 scopus 로고    scopus 로고
    • Synthesis and characterization of potent bivalent inhibitors that bind prior to transthyretin tetramerization
    • Greeen, N. S., Palaninathan, S. K., Sacchettini, J. C. and Kelly, J. W. (2003) Synthesis and characterization of potent bivalent inhibitors that bind prior to transthyretin tetramerization. J. Am. Chem. Soc. 125, 13404-13414
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 13404-13414
    • Greeen, N.S.1    Palaninathan, S.K.2    Sacchettini, J.C.3    Kelly, J.W.4
  • 27
    • 0038375018 scopus 로고    scopus 로고
    • 4′-Iodo- 4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing non-cytotoxic species. Screening for TTR fibril disrupters
    • Cardoso, I., Merlini, G. and Saraiva, M. J. (2003) 4′-Iodo- 4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing non-cytotoxic species. Screening for TTR fibril disrupters. FASEB J. 17, 803-809
    • (2003) FASEB J , vol.17 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 28
    • 11144228259 scopus 로고    scopus 로고
    • The crystal structure of transthyretin in complex with diethylstilbestrol: A promising template for the design of amyloid inhibitors
    • Morais-de-Sa, E., Pereira, P. J., Saraiva, M. J. and Damas, A. M. (2004) The crystal structure of transthyretin in complex with diethylstilbestrol: a promising template for the design of amyloid inhibitors. J. Biol. Chem. 279, 53483-53490
    • (2004) J. Biol. Chem , vol.279 , pp. 53483-53490
    • Morais-de-Sa, E.1    Pereira, P.J.2    Saraiva, M.J.3    Damas, A.M.4
  • 29
    • 26844546899 scopus 로고    scopus 로고
    • Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis
    • Green, N. S., Foss, T. R. and Kelly, J. W. (2005) Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis. Proc. Natl. Acad. Sci. U.S.A. 102, 14545-14550
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 14545-14550
    • Green, N.S.1    Foss, T.R.2    Kelly, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.