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Volumn 7, Issue , 2016, Pages

Author Correction: Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity (Nature Communications, (2016), 7, 1, (10787), 10.1038/ncomms10787);Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity

Author keywords

[No Author keywords available]

Indexed keywords

PREALBUMIN; TAFAMIDIS; TETRAMER; TOLCAPONE; BENZOPHENONE DERIVATIVE; CATECHOL METHYLTRANSFERASE INHIBITOR; NITROPHENOL;

EID: 84959087061     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/s41467-023-36239-z     Document Type: Erratum
Times cited : (137)

References (64)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0023696119 scopus 로고
    • Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin
    • Cornwell, 3rd G. G., Sletten, K., Johansson, B. & Westermark, P. Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin. Biochem. Biophys. Res. Commun. 154, 648-653 (1988).
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 648-653
    • Cornwell, G.G.1    Sletten, K.2    Johansson, B.3    Westermark, P.4
  • 3
  • 4
    • 77954177629 scopus 로고    scopus 로고
    • Transthyretin-related amyloidoses and the heart: A clinical overview
    • Rapezzi, C. et al. Transthyretin-related amyloidoses and the heart: a clinical overview. Nat. Rev. Cardiol. 7, 398-408 (2010).
    • (2010) Nat. Rev. Cardiol. , vol.7 , pp. 398-408
    • Rapezzi, C.1
  • 5
    • 33947245436 scopus 로고    scopus 로고
    • Transthyretin and familial amyloidotic polyneuropathy. Recent progress in understanding the molecular mechanism of neurodegeneration
    • Hou, X., Aguilar, M. I. & Small, D. H. Transthyretin and familial amyloidotic polyneuropathy. Recent progress in understanding the molecular mechanism of neurodegeneration. FEBS J. 274, 1637-1650 (2007).
    • (2007) FEBS J , vol.274 , pp. 1637-1650
    • Hou, X.1    Aguilar, M.I.2    Small, D.H.3
  • 6
    • 84861421529 scopus 로고    scopus 로고
    • The transthyretin amyloidoses: From delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug
    • Johnson, S. M., Connelly, S., Fearns, C., Powers, E. T. & Kelly, J. W. The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. J. Mol. Biol. 421, 185-203 (2012).
    • (2012) J. Mol. Biol. , vol.421 , pp. 185-203
    • Johnson, S.M.1    Connelly, S.2    Fearns, C.3    Powers, E.T.4    Kelly, J.W.5
  • 7
    • 0018952424 scopus 로고
    • Familial oculoleptomeningeal amyloidosis
    • Goren, H., Steinberg, M. C. & Farboody, G. H. Familial oculoleptomeningeal amyloidosis. Brain 103, 473-495 (1980).
    • (1980) Brain , vol.103 , pp. 473-495
    • Goren, H.1    Steinberg, M.C.2    Farboody, G.H.3
  • 8
    • 0037344272 scopus 로고    scopus 로고
    • Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology
    • Sekijima, Y. et al. Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology. Lab. Invest. 83, 409-417 (2003).
    • (2003) Lab. Invest. , vol.83 , pp. 409-417
    • Sekijima, Y.1
  • 9
    • 84055184424 scopus 로고    scopus 로고
    • Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: Identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
    • Azevedo, E. P. et al. Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis: identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid. Biochemistry 50, 11070-11083 (2011).
    • (2011) Biochemistry , vol.50 , pp. 11070-11083
    • Azevedo, E.P.1
  • 10
    • 0027326488 scopus 로고
    • Thyroid hormone transport proteins
    • Bartalena, L. & Robbins, J. Thyroid hormone transport proteins. Clin. Lab. Med. 13, 583-598 (1993).
    • (1993) Clin. Lab. Med. , vol.13 , pp. 583-598
    • Bartalena, L.1    Robbins, J.2
  • 11
    • 0034703380 scopus 로고    scopus 로고
    • A comparative analysis of 23 structures of the amyloidogenic protein transthyretin
    • Hornberg, A., Eneqvist, T., Olofsson, A., Lundgren, E. & Sauer-Eriksson, A. E. A comparative analysis of 23 structures of the amyloidogenic protein transthyretin. J. Mol. Biol. 302, 649-669 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 649-669
    • Hornberg, A.1    Eneqvist, T.2    Olofsson, A.3    Lundgren, E.4    Sauer-Eriksson, A.E.5
  • 12
    • 0034799733 scopus 로고    scopus 로고
    • Transthyretin: A review from a structural perspective
    • Hamilton, J. A. & Benson, M. D. Transthyretin: a review from a structural perspective. Cell. Mol. Life. Sci. 58, 1491-1521 (2001).
    • (2001) Cell. Mol. Life. Sci. , vol.58 , pp. 1491-1521
    • Hamilton, J.A.1    Benson, M.D.2
  • 13
    • 0035949432 scopus 로고    scopus 로고
    • An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured
    • Jiang, X. et al. An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured. Biochemistry 40, 11442-11452 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11442-11452
    • Jiang, X.1
  • 14
    • 0035920156 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. 276, 27207-27213 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.4    Brito, R.M.5
  • 15
    • 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. USA 99(Suppl 4): 16427-16432 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 16
    • 17044402604 scopus 로고    scopus 로고
    • The biological and chemical basis for tissue-selective amyloid disease
    • Sekijima, Y. et al. The biological and chemical basis for tissue-selective amyloid disease. Cell 121, 73-85 (2005).
    • (2005) Cell , vol.121 , pp. 73-85
    • Sekijima, Y.1
  • 17
    • 1642566049 scopus 로고    scopus 로고
    • Familial amyloidotic polyneuropathy world transplant R. Ten years of international experience with liver transplantation for familial amyloidotic polyneuropathy: Results from the Familial Amyloidotic Polyneuropathy World Transplant Registry
    • Herlenius, G., Wilczek, H. E., Larsson, M. & Ericzon, B. G. Familial amyloidotic polyneuropathy world transplant R. Ten years of international experience with liver transplantation for familial amyloidotic polyneuropathy: results from the Familial Amyloidotic Polyneuropathy World Transplant Registry. Transplantation 77, 64-71 (2004).
    • (2004) Transplantation , vol.77 , pp. 64-71
    • Herlenius, G.1    Wilczek, H.E.2    Larsson, M.3    Ericzon, B.G.4
  • 18
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • Johnson, S. M. et al. Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc. Chem. Res. 38, 911-921 (2005).
    • (2005) Acc. Chem. Res. , vol.38 , pp. 911-921
    • Johnson, S.M.1
  • 19
    • 2942599707 scopus 로고    scopus 로고
    • Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants
    • Miller, S. R., Sekijima, Y. & Kelly, J. W. Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants. Lab. Invest. 84, 545-552 (2004).
    • (2004) Lab. Invest. , vol.84 , pp. 545-552
    • Miller, S.R.1    Sekijima, Y.2    Kelly, J.W.3
  • 20
    • 33751023007 scopus 로고    scopus 로고
    • Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis
    • Tojo, K., Sekijima, Y., Kelly, J. W. & Ikeda, S. Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis. Neurosci. Res. 56, 441-449 (2006).
    • (2006) Neurosci. Res. , vol.56 , pp. 441-449
    • Tojo, K.1    Sekijima, Y.2    Kelly, J.W.3    Ikeda, S.4
  • 21
    • 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
  • 22
    • 0034127176 scopus 로고    scopus 로고
    • Rational design of potent human transthyretin amyloid disease inhibitors
    • Klabunde, T. et al. Rational design of potent human transthyretin amyloid disease inhibitors. Nat. Struct. Biol. 7, 312-321 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 312-321
    • Klabunde, T.1
  • 23
    • 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. 17, 803-809 (2003).
    • (2003) FASEB J , vol.17 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 24
    • 14944376972 scopus 로고    scopus 로고
    • Kinetic stabilization of an oligomeric protein by a single ligand binding event
    • Wiseman, R. L. et al. Kinetic stabilization of an oligomeric protein by a single ligand binding event. J. Am. Chem. Soc. 127, 5540-5551 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5540-5551
    • Wiseman, R.L.1
  • 25
    • 54549114463 scopus 로고    scopus 로고
    • Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies
    • Johnson, S. M., Connelly, S., Wilson, I. A. & Kelly, J. W. Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies. J. Med. Chem. 51, 6348-6358 (2008).
    • (2008) J. Med. Chem. , vol.51 , pp. 6348-6358
    • Johnson, S.M.1    Connelly, S.2    Wilson, I.A.3    Kelly, J.W.4
  • 26
    • 0037122698 scopus 로고    scopus 로고
    • Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors
    • Oza, V. B. et al. Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors. J. Med. Chem. 45, 321-332 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 321-332
    • Oza, V.B.1
  • 27
    • 16244396730 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of oxazole transthyretin amyloidogenesis inhibitors
    • Razavi, H. et al. Design, synthesis, and evaluation of oxazole transthyretin amyloidogenesis inhibitors. Bioorg. Med. Chem. Lett. 15, 1075-1078 (2005).
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 1075-1078
    • Razavi, H.1
  • 28
    • 38349124133 scopus 로고    scopus 로고
    • Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors
    • Johnson, S. M., Connelly, S., Wilson, I. A. & Kelly, J. W. Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors. J. Med. Chem. 51, 260-270 (2008).
    • (2008) J. Med. Chem. , vol.51 , pp. 260-270
    • Johnson, S.M.1    Connelly, S.2    Wilson, I.A.3    Kelly, J.W.4
  • 29
    • 84862234023 scopus 로고    scopus 로고
    • Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade
    • Bulawa, C. E. et al. Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade. Proc. Natl Acad. Sci. USA 109, 9629-9634 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 9629-9634
    • Bulawa, C.E.1
  • 30
    • 84878370455 scopus 로고    scopus 로고
    • Tafamidis for transthyretin familial amyloid polyneuropathy: A randomized, controlled trial
    • Merkies, I. S. Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trial. Neurology 80, 1444-1445 (2013).
    • (2013) Neurology , vol.80 , pp. 1444-1445
    • Merkies, I.S.1
  • 31
    • 84887402882 scopus 로고    scopus 로고
    • Effect on disability and safety of Tafamidis in late onset of Met30 transthyretin familial amyloid polyneuropathy
    • Lozeron, P. et al. Effect on disability and safety of Tafamidis in late onset of Met30 transthyretin familial amyloid polyneuropathy. Eur. J. Neurol. 20, 1539-1545 (2013).
    • (2013) Eur. J. Neurol. , vol.20 , pp. 1539-1545
    • Lozeron, P.1
  • 32
    • 84858978535 scopus 로고    scopus 로고
    • Drug repositioning for personalized medicine
    • Li, Y. Y. & Jones, S. J. Drug repositioning for personalized medicine. Genome Med. 4, 27 (2012).
    • (2012) Genome Med. , vol.4 , pp. 27
    • Li, Y.Y.1    Jones, S.J.2
  • 33
    • 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 13, 236-249 (2006).
    • (2006) Amyloid , vol.13 , pp. 236-249
    • Sekijima, Y.1    Dendle, M.A.2    Kelly, J.W.3
  • 34
    • 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. & Kelly, J. W. Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis. J. Med. Chem. 47, 355-374 (2004).
    • (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
  • 35
    • 84890954073 scopus 로고    scopus 로고
    • Repurposing diflunisal for familial amyloid polyneuropathy: A randomized clinical trial
    • Berk, J. L. et al. Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial. JAMA 310, 2658-2667 (2013).
    • (2013) JAMA , vol.310 , pp. 2658-2667
    • Berk, J.L.1
  • 36
    • 17144421562 scopus 로고    scopus 로고
    • Kinetic assay for high-throughput screening of in vitro transthyretin amyloid fibrillogenesis inhibitors
    • Dolado, I. et al. Kinetic assay for high-throughput screening of in vitro transthyretin amyloid fibrillogenesis inhibitors. J. Comb. Chem. 7, 246-252 (2005).
    • (2005) J. Comb. Chem. , vol.7 , pp. 246-252
    • Dolado, I.1
  • 37
    • 0035909981 scopus 로고    scopus 로고
    • The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
    • Jiang, X., Buxbaum, J. N. & Kelly, J. W. The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc. Natl Acad. Sci. USA 98, 14943-14948 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14943-14948
    • Jiang, X.1    Buxbaum, J.N.2    Kelly, J.W.3
  • 38
    • 84875426278 scopus 로고    scopus 로고
    • Age-related oxidative modifications of transthyretin modulate its amyloidogenicity
    • Zhao, L., Buxbaum, J. N. & Reixach, N. Age-related oxidative modifications of transthyretin modulate its amyloidogenicity. Biochemistry 52, 1913-1926 (2013).
    • (2013) Biochemistry , vol.52 , pp. 1913-1926
    • Zhao, L.1    Buxbaum, J.N.2    Reixach, N.3
  • 39
    • 84908216706 scopus 로고    scopus 로고
    • Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: The transthyretin case
    • Robinson, L. Z. & Reixach, N. Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case. Biochemistry 53, 6496-6510 (2014).
    • (2014) Biochemistry , vol.53 , pp. 6496-6510
    • Robinson, L.Z.1    Reixach, N.2
  • 40
    • 0030876269 scopus 로고    scopus 로고
    • Optimizing levodopa pharmacokinetics with multiple tolcapone doses in the elderly
    • Jorga, K. M. et al. Optimizing levodopa pharmacokinetics with multiple tolcapone doses in the elderly. Clin. Pharmacol. Ther. 62, 300-310 (1997).
    • (1997) Clin. Pharmacol. Ther. , vol.62 , pp. 300-310
    • Jorga, K.M.1
  • 41
    • 2942593931 scopus 로고    scopus 로고
    • Transthyretin aggregation under partially denaturing conditions is a downhill polymerization
    • Hurshman, A. R., White, J. T., Powers, E. T. & Kelly, J. W. Transthyretin aggregation under partially denaturing conditions is a downhill polymerization. Biochemistry 43, 7365-7381 (2004).
    • (2004) Biochemistry , vol.43 , pp. 7365-7381
    • Hurshman, A.R.1    White, J.T.2    Powers, E.T.3    Kelly, J.W.4
  • 42
    • 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. et al. 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).
    • (2004) Biochem. J , vol.381 , pp. 351-356
    • Almeida, M.R.1
  • 43
    • 61849095281 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: General formalism using binding polynomials
    • Freire, E., Schon, A. & Velazquez-Campoy, A. Isothermal titration calorimetry: general formalism using binding polynomials. Methods Enzymol. 455, 127-155 (2009).
    • (2009) Methods Enzymol. , vol.455 , pp. 127-155
    • Freire, E.1    Schon, A.2    Velazquez-Campoy, A.3
  • 44
    • 84925436890 scopus 로고    scopus 로고
    • A unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry
    • Vega, S., Abian, O. & Velazquez-Campoy, A. A unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry. Methods 76, 99-115 (2015).
    • (2015) Methods , vol.76 , pp. 99-115
    • Vega, S.1    Abian, O.2    Velazquez-Campoy, A.3
  • 45
    • 84878956207 scopus 로고    scopus 로고
    • AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin
    • Penchala, S. C. et al. AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin. Proc. Natl Acad. Sci. USA 110, 9992-9997 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9992-9997
    • Penchala, S.C.1
  • 46
    • 20644456260 scopus 로고    scopus 로고
    • Novel cell lines derived from adult human ventricular cardiomyocytes
    • Davidson, M. M. et al. Novel cell lines derived from adult human ventricular cardiomyocytes. J. Mol. Cell. Cardiol. 39, 133-147 (2005).
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 133-147
    • Davidson, M.M.1
  • 47
    • 79960291244 scopus 로고    scopus 로고
    • Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs
    • Bourgault, S. et al. Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs. Biochem. Biophys. Res. Co. 410, 707-713 (2011).
    • (2011) Biochem. Biophys. Res. Co. , vol.410 , pp. 707-713
    • Bourgault, S.1
  • 48
    • 84921673359 scopus 로고    scopus 로고
    • Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: Insights into early events of non-fibrillar tissue damage
    • Manral, P. & Reixach, N. Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage. Biosci. Rep. 35, e00172 (2015).
    • (2015) Biosci. Rep. , vol.35
    • Manral, P.1    Reixach, N.2
  • 49
    • 79960910835 scopus 로고    scopus 로고
    • Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation
    • Ferreira, N., Saraiva, M. J. & Almeida, M. R. Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS Lett. 585, 2424-2430 (2011).
    • (2011) FEBS Lett. , vol.585 , pp. 2424-2430
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 50
    • 0033550075 scopus 로고    scopus 로고
    • The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
    • Lashuel, H. A., Wurth, C., Woo, L. & Kelly, J. W. The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. Biochemistry 38, 13560-13573 (1999).
    • (1999) Biochemistry , vol.38 , pp. 13560-13573
    • Lashuel, H.A.1    Wurth, C.2    Woo, L.3    Kelly, J.W.4
  • 51
    • 36348960658 scopus 로고    scopus 로고
    • Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: Relevance in drug design
    • Cardoso, I. et al. Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design. Biochem. J. 408, 131-138 (2007).
    • (2007) Biochem. J , vol.408 , pp. 131-138
    • Cardoso, I.1
  • 52
    • 0028858966 scopus 로고
    • A 6-kb upstream region of the human transthyretin gene can direct developmental, tissue-specific, and quantitatively normal expression in transgenic mouse
    • Nagata, Y. et al. A 6-kb upstream region of the human transthyretin gene can direct developmental, tissue-specific, and quantitatively normal expression in transgenic mouse. J. Biochem. 117, 169-175 (1995).
    • (1995) J. Biochem. , vol.117 , pp. 169-175
    • Nagata, Y.1
  • 54
    • 77649234756 scopus 로고    scopus 로고
    • How to improve R&D productivity: The pharmaceutical industry's grand challenge
    • Paul, S. M. et al. How to improve R&D productivity: the pharmaceutical industry's grand challenge. Nat. Rev. Drug Discov. 9, 203-214 (2010).
    • (2010) Nat. Rev. Drug Discov , vol.9 , pp. 203-214
    • Paul, S.M.1
  • 55
    • 0343184105 scopus 로고    scopus 로고
    • Consumption of NSAIDs and the development of congestive heart failure in elderly patients: An underrecognized public health problem
    • Page, J. & Henry, D. Consumption of NSAIDs and the development of congestive heart failure in elderly patients: an underrecognized public health problem. Arch. Intern. Med. 160, 777-784 (2000).
    • (2000) Arch. Intern. Med. , vol.160 , pp. 777-784
    • Page, J.1    Henry, D.2
  • 56
    • 0034758114 scopus 로고    scopus 로고
    • Pathogenesis of NSAID-induced gastroduodenal mucosal injury
    • Wallace, J. L. Pathogenesis of NSAID-induced gastroduodenal mucosal injury. Best Pract. Res. Clin. Gastroenterol. 15, 691-703 (2001).
    • (2001) Best Pract. Res. Clin. Gastroenterol. , vol.15 , pp. 691-703
    • Wallace, J.L.1
  • 57
    • 0026577768 scopus 로고
    • Role of transthyretin in the transport of thyroxine from the blood to the choroid plexus, the cerebrospinal fluid, and the brain
    • Chanoine, J. P. et al. Role of transthyretin in the transport of thyroxine from the blood to the choroid plexus, the cerebrospinal fluid, and the brain. Endocrinology 130, 933-938 (1992).
    • (1992) Endocrinology , vol.130 , pp. 933-938
    • Chanoine, J.P.1
  • 58
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini, M. et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511 (2002).
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1
  • 59
    • 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. USA 101, 2817-2822 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 60
    • 0028969996 scopus 로고
    • Transthyretin mutations in health and disease
    • Saraiva, M. J. Transthyretin mutations in health and disease. Hum. Mutat. 5, 191-196 (1995).
    • (1995) Hum. Mutat , vol.5 , pp. 191-196
    • Saraiva, M.J.1
  • 61
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • Freire, E. Do enthalpy and entropy distinguish first in class from best in class? Drug Discov. Today 13, 869-874 (2008).
    • (2008) Drug Discov. Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 62
    • 71749085436 scopus 로고    scopus 로고
    • Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity
    • Ferreira, N. et al. Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicity. FEBS Lett. 583, 3569-3576 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 3569-3576
    • Ferreira, N.1
  • 63
    • 0032988614 scopus 로고    scopus 로고
    • Determination of the catechol-O-methyltransferase inhibitor tolcapone and three of its metabolites in animal and human plasma and urine by reversed-phase high-performance liquid chromatography with ultraviolet detection
    • Heizmann, P., Schmitt, M., Leube, J., Martin, H. & Saner, A. Determination of the catechol-O-methyltransferase inhibitor tolcapone and three of its metabolites in animal and human plasma and urine by reversed-phase high-performance liquid chromatography with ultraviolet detection. J. Chromatogr. B Biomed. Sci. Appl. 730, 153-160 (1999).
    • (1999) J. Chromatogr. B Biomed. Sci. Appl. , vol.730 , pp. 153-160
    • Heizmann, P.1    Schmitt, M.2    Leube, J.3    Martin, H.4    Saner, A.5
  • 64
    • 67650726440 scopus 로고    scopus 로고
    • Identification of metabolite profiles of the catechol-O-methyl transferase inhibitor tolcapone in rat urine using LC/MS-based metabonomics analysis
    • Sun, J., Von Tungeln, L. S., Hines, W. & Beger, R. D. Identification of metabolite profiles of the catechol-O-methyl transferase inhibitor tolcapone in rat urine using LC/MS-based metabonomics analysis. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 877, 2557-2565 (2009).
    • (2009) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.877 , pp. 2557-2565
    • Sun, J.1    Von Tungeln, L.S.2    Hines, W.3    Beger, R.D.4


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