메뉴 건너뛰기




Volumn 7, Issue 4, 2000, Pages 312-321

Rational design of potent human transthyretin amyloid disease inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

2 TRIFLUORMETHYLPHENYL ANTHRANILIC ACID; AMYLOID; DIBENZOFURAN 4,6 DICARBOXYLIC ACID; DICARBOXYLIC ACID DERIVATIVE; DICLOFENAC; DIFLUNISAL; FENOPROFEN; FLUFENAMIC ACID; FLURBIPROFEN; INDOMETACIN; M ANTHRANILIC ACID DERIVATIVE; MECLOFENAMIC ACID; MEFENAMIC ACID; N (3 TRIFLUOROMETHYLPHENYL)PHENOXAZINE 4,6 DICARBOXYLIC ACID; NONSTEROID ANTIINFLAMMATORY AGENT; PREALBUMIN; PROTEIN INHIBITOR; RESVERATROL; UNCLASSIFIED DRUG;

EID: 0034127176     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/74082     Document Type: Article
Times cited : (373)

References (37)
  • 1
    • 0002696182 scopus 로고
    • Amyloidosis
    • Scrirer, C. R., Beaudet. A. Z.. Sly, W. S., Velk, D. eds, New York: McGraw Hill.
    • Benson, M. D., Wallace, M. R. " Amyloidosis" In The Metabolic Basis of Inherited Disease (Scrirer, C. R., Beaudet. A. Z.. Sly, W. S., Velk, D. eds, New York: McGraw Hill. 2439-2460, 1989).
    • (1989) The Metabolic Basis of Inherited Disease , pp. 2439-2460
    • Benson, M.D.1    Wallace, M.R.2
  • 2
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon, W. & Kelly, J.W. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31, 8654-8660 (1992).
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 3
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly, J.W. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6, 11-17 (1996).
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 4
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate which can self-assemble into amyloid
    • Lai, Z.. Colon, W. & Kelly, J.W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate which can self-assemble into amyloid. Biochemistry 35, 6470-6482 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 5
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 6
    • 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. S Colon. W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 34, 13527-36 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • McCutchen, S.L.1    Lai, Z.2    Miroy, G.J.3    Kelly, J.W.S.4    Colon, W.5
  • 10
    • 0006283728 scopus 로고
    • Age-related cardiovascular changes and mechanically induced endocardial pathology
    • nd ed. New York: Churchill Livingstone.
    • nd ed. New York: Churchill Livingstone. 155-162, 1991).
    • (1991) Cardiovascular Pathology , pp. 155-162
    • Pomerance, A.1
  • 11
    • 0017711275 scopus 로고
    • The clinical significance of senile cardiac amyloidosis: A prospective clinico-pathological study
    • Hodkinson, H.M., Pomerance, A. The clinical significance of senile cardiac amyloidosis: a prospective clinico-pathological study. O. J. Med. 46, 381-387 (1977).
    • (1977) O. J. Med. , vol.46 , pp. 381-387
    • Hodkinson, H.M.1    Pomerance, A.2
  • 12
    • 0031028712 scopus 로고    scopus 로고
    • Variant-sequence transthyretin (isoleucin 122) in late-onset cardiac amyloidosis in black americans
    • Jacobson, D.R. et al. Variant-sequence transthyretin (isoleucin 122) in late-onset cardiac amyloidosis in black americans. N. Engl. J. Med. 336, 466-473 (1997).
    • (1997) N. Engl. J. Med. , vol.336 , pp. 466-473
    • Jacobson, D.R.1
  • 13
    • 0029062667 scopus 로고
    • Structure of a complex of two plasma proteins: Transthyretin and retinol-binding protein
    • Monaco, H.L, Rizzi, M. & Coda, A. Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein Science 268, 1039-1041 (1995).
    • (1995) Science , vol.268 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 14
    • 0016830196 scopus 로고
    • Studies of thyroid hormone binding proteins
    • Nilsson, S. F., Rack, L., Peterson, P. Studies of thyroid hormone binding proteins. J. Biol. Chem. 250, 8554-8563 (1975).
    • (1975) J. Biol. Chem. , vol.250 , pp. 8554-8563
    • Nilsson, S.F.1    Rack, L.2    Peterson, P.3
  • 15
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • Blake, C.C., Geisow, M.J., Oatley, S.J., Rerat B. & Rerat, C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J. Mol. Biol. 121, 339-356 (1978).
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 16
    • 0016140360 scopus 로고
    • Structure of human plasma prealbumin at 2.5 Å resolution. a preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding
    • Blake, C.C.F, Geisow, M.J., Swan, I.D., Rerat, C. & Rerat, B. Structure of human plasma prealbumin at 2.5 Å resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding. J. Mol. Biol. 88, 1-12 (1974).
    • (1974) J. Mol. Biol. , vol.88 , pp. 1-12
    • Blake, C.C.F.1    Geisow, M.J.2    Swan, I.D.3    Rerat, C.4    Rerat, B.5
  • 17
    • 0030447882 scopus 로고    scopus 로고
    • Inhibiting transthyretin amyloid fibril formation via protein stabilization
    • Miroy, G.J. et al. Inhibiting transthyretin amyloid fibril formation via protein stabilization. Proc. Natl. Acad. Sci. USA 93, 15051-15056 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15051-15056
    • Miroy, G.J.1
  • 18
    • 0030484635 scopus 로고    scopus 로고
    • Structures of human transthyretin complexed with thyroxine at 2.0 Å Resolution and 3'-5'-Dinitro-N-acetyl-L-thyroxine at 2.2 Å Resolution
    • Wojtczak, A., Cody, V., Luft J.R. & Pangborn W. Structures of human transthyretin complexed with thyroxine at 2.0 Å Resolution and 3'-5'-Dinitro-N-acetyl-L-thyroxine at 2.2 Å Resolution. Acta Crystallogr. D 52, 758-765 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 758-765
    • Wojtczak, A.1    Cody, V.2    Luft, J.R.3    Pangborn, W.4
  • 19
    • 0032573082 scopus 로고    scopus 로고
    • Inhibiting transthyretin conformational changes that lead to amyloid fibril formation
    • Peterson, S.A. et al. Inhibiting transthyretin conformational changes that lead to amyloid fibril formation. Proc. Natl. Acad. Sci. USA 95, 12956-12960 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12956-12960
    • Peterson, S.A.1
  • 20
    • 0029859731 scopus 로고    scopus 로고
    • Familial amyloid polyneuropathy: New developments in genetics and treatment
    • Coelho, T. Familial amyloid polyneuropathy: new developments in genetics and treatment. Cuir. Opin. Neurol. 9, 355-359 (1996).
    • (1996) Cuir. Opin. Neurol. , vol.9 , pp. 355-359
    • Coelho, T.1
  • 21
    • 0024311332 scopus 로고
    • Drug Competition for thyroxine binding to transthyretin (prealbumin): Comparison with effects on thyroxine-binding globulin
    • Munro, S.L. et al. Drug Competition for thyroxine binding to transthyretin (prealbumin): comparison with effects on thyroxine-binding globulin. J. Clin. Endorinol. Metab. 68, 1141-7 (1989).
    • (1989) J. Clin. Endorinol. Metab. , vol.68 , pp. 1141-1147
    • Munro, S.L.1
  • 22
    • 0031684499 scopus 로고    scopus 로고
    • Discovering transthyretin amyloid fibril inhibitors by limited screening
    • Baures, P.W., Peterson, S.A., Kelly, J.W. Discovering transthyretin amyloid fibril inhibitors by limited screening. Bioorg. Med. Chem. 6, 1389-1401 (1998).
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 1389-1401
    • Baures, P.W.1    Peterson, S.A.2    Kelly, J.W.3
  • 23
    • 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. & Kelly, J.W. 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).
    • (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
  • 24
    • 0028929457 scopus 로고
    • Administration of wine and grape juice inhibits in vivo platelet activity and thrombosis in stenosed canine coronary arteries
    • Demrow, H.S., Slane, P.R., Folts, J.D. Administration of wine and grape juice inhibits in vivo platelet activity and thrombosis in stenosed canine coronary arteries. Circulation 91, 1182-88 (1995)
    • (1995) Circulation , vol.91 , pp. 1182-1188
    • Demrow, H.S.1    Slane, P.R.2    Folts, J.D.3
  • 25
    • 0029129124 scopus 로고
    • Antiplatelet activity of synthetic and natural resveratrol in red wine
    • Bertelli A.A., et al. Antiplatelet activity of synthetic and natural resveratrol in red wine. Int. J. Tissue React. 17, 1-3 (1995).
    • (1995) Int. J. Tissue React. , vol.17 , pp. 1-3
    • Bertelli, A.A.1
  • 26
    • 0003133991 scopus 로고    scopus 로고
    • Resveratrol prevents apoptosis in K562 cells by inhibiting lipoxygenase and cyclooxygenase activity
    • MacCarrone M., Lorenzon T., Guerrieri P. & Agro A.F. Resveratrol prevents apoptosis in K562 cells by inhibiting lipoxygenase and cyclooxygenase activity, Eur. J. Biochem. 265, 27-34 (1999).
    • (1999) Eur. J. Biochem. , vol.265 , pp. 27-34
    • MacCarrone, M.1    Lorenzon, T.2    Guerrieri, P.3    Agro, A.F.4
  • 27
    • 0032076219 scopus 로고    scopus 로고
    • Cyclooxygenase-1 and cyclooxygenase-2 selectivity of widely used nonsteroidal anti-inflammatory drugs
    • Cryer, B. & Feldman, M. Cyclooxygenase-1 and cyclooxygenase-2 selectivity of widely used nonsteroidal anti-inflammatory drugs. Am J. Med. 104, 413-421 (1998).
    • (1998) Am J. Med. , vol.104 , pp. 413-421
    • Cryer, B.1    Feldman, M.2
  • 28
    • 0030461132 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents
    • Kurumbail R.G. et al. Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents. Nature 384, 644-648 (1996).
    • (1996) Nature , vol.384 , pp. 644-648
    • Kurumbail, R.G.1
  • 29
    • 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. & Kelly, J.W. Synthesis and evaluation of anthranilic acid-based transthyretin amyloid fibril inhibitors. Bioorg. Med. Chem. Lett 9, 1-6 (1999).
    • (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
  • 30
    • 33847531968 scopus 로고
    • Inhibition of prostaglandin synthetase and carrageenaninduced edema by analogs of flufenamic acid. Drugs
    • Horodniak, J.W. et al. Inhibition of prostaglandin synthetase and carrageenaninduced edema by analogs of flufenamic acid. Drugs Exptl. Clin. Res. 2, 35-45 (1977).
    • (1977) Exptl. Clin. Res. , vol.2 , pp. 35-45
    • Horodniak, J.W.1
  • 31
    • 0034654494 scopus 로고    scopus 로고
    • Structure-based design of N-phenyl phenoxazine transthyretin amyloid fibril inhibitors
    • in the press
    • Petrassi, H. M., Klabunde, T., Sacchettini, J., Kelly, J. W. Structure-based design of N-phenyl phenoxazine transthyretin amyloid fibril inhibitors. J. Am. Chem. Soc. 122, in the press (2000).
    • (2000) J. Am. Chem. Soc. , vol.122
    • Petrassi, H.M.1    Klabunde, T.2    Sacchettini, J.3    Kelly, J.W.4
  • 32
  • 33
    • 84936887577 scopus 로고
    • A dibenzofuran-based amino acid designed to nucleate antiparrallel β-sheet structure: Evidence for intramolecular hydrogenbond formation
    • Diaz, H., Espina, J. R., Kelly, J. W. A dibenzofuran-based amino acid designed to nucleate antiparrallel β-sheet structure: evidence for intramolecular hydrogenbond formation. J. Am. Chem. Soc. Am 114, 8316-8318 (1992).
    • (1992) J. Am. Chem. Soc. Am , vol.114 , pp. 8316-8318
    • Diaz, H.1    Espina, J.R.2    Kelly, J.W.3
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data in oscillation mode
    • Otwinowski, J. & Minor, W. Processing of X-ray diffraction data in oscillation mode. Methods Enz. 276, 307-326 (1997).
    • (1997) Methods Enz. , vol.276 , pp. 307-326
    • Otwinowski, J.1    Minor, W.2
  • 35
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System
    • Brunger. A.T. Crystallography & NMR System. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 36
    • 84889120137 scopus 로고
    • Improved method for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved method for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47,110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 37
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S. V. SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11,134-138 (1993).
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.