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Volumn 110, Issue 24, 2013, Pages 9992-9997

AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin

Author keywords

Crystal structure; Drug design

Indexed keywords

AG 10; PREALBUMIN; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 84878956207     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1300761110     Document Type: Article
Times cited : (124)

References (40)
  • 1
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ (2003) Folding proteins in fatal ways. Nature 426(6968):900-904.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 900-904
    • Selkoe, D.J.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • Johnson SM, et al. (2005) Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses. Acc Chem Res 38(12):911-921.
    • (2005) Acc Chem Res , vol.38 , Issue.12 , pp. 911-921
    • Johnson, S.M.1
  • 5
    • 0242407579 scopus 로고    scopus 로고
    • Tabulation of human transthyretin (TTR) variants, 2003
    • Connors LH, Lim A, Prokaeva T, Roskens VA, Costello CE (2003) Tabulation of human transthyretin (TTR) variants, 2003. Amyloid 10(3):160-184. (Pubitemid 37372400)
    • (2003) Amyloid , vol.10 , Issue.3 , pp. 160-184
    • Connors, L.H.1    Lim, A.2    Prokaeva, T.3    Roskens, V.A.4    Costello, C.E.5
  • 6
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by fourier refinement at 1.8 A
    • Blake CC, Geisow MJ, Oatley SJ, Rérat B, Rérat C (1978) Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J Mol Biol 121(3):339-356. (Pubitemid 8361803)
    • (1978) Journal of Molecular Biology , vol.121 , Issue.3 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.2    Oatley, S.J.3
  • 7
    • 0029062667 scopus 로고
    • Structure of a complex of two plasma proteins: Transthyretin and retinol-binding protein
    • Monaco HL, Rizzi M, Coda A (1995) Structure of a complex of two plasma proteins: Transthyretin and retinol-binding protein. Science 268(5213):1039-1041.
    • (1995) Science , vol.268 , Issue.5213 , pp. 1039-1041
    • Monaco, H.L.1    Rizzi, M.2    Coda, A.3
  • 8
    • 28244486084 scopus 로고    scopus 로고
    • The pathway by which the tetrameric protein transthyretin dissociates
    • DOI 10.1021/bi051608t
    • Foss TR, Wiseman RL, Kelly JW (2005) The pathway by which the tetrameric protein transthyretin dissociates. Biochemistry 44(47):15525-15533. (Pubitemid 41706136)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15525-15533
    • Foss, T.R.1    Wiseman, R.L.2    Kelly, J.W.3
  • 10
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin arnyloid disease by changing protein misfolding energetics
    • DOI 10.1126/science.1079589
    • Hammarström P, Wiseman RL, Powers ET, Kelly JW (2003) Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299(5607):713-716. (Pubitemid 36159487)
    • (2003) Science , vol.299 , Issue.5607 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 11
    • 17044402604 scopus 로고    scopus 로고
    • The biological and chemical basis for tissue-selective amyloid disease
    • Sekijima Y, et al. (2005) The biological and chemical basis for tissue-selective amyloid disease. Cell 121(1):73-85.
    • (2005) Cell , vol.121 , Issue.1 , pp. 73-85
    • Sekijima, Y.1
  • 12
    • 0032242706 scopus 로고    scopus 로고
    • Autonomic dysfunction in familial amyloidotic polyneuropathy (FAP)
    • Ando Y, Suhr OB (1998) Autonomic dysfunction in familial amyloidotic polyneuropathy (FAP). Amyloid 5(4):288-300. (Pubitemid 128690769)
    • (1998) Amyloid , vol.5 , Issue.4 , pp. 288-300
    • Ando, Y.1    Suhr, O.B.2
  • 13
    • 0024503518 scopus 로고
    • Familial amyloidotic polyneuropathy
    • Benson MD (1989) Familial amyloidotic polyneuropathy. Trends Neurosci 12(3):88-92.
    • (1989) Trends Neurosci , vol.12 , Issue.3 , pp. 88-92
    • Benson, M.D.1
  • 14
    • 70349210200 scopus 로고    scopus 로고
    • Cardiac amyloidosis in African Americans: Comparison of clinical and laboratory features of transthyretin V122I amyloidosis and immunoglobulin light chain amyloidosis
    • Connors LH, et al. (2009) Cardiac amyloidosis in African Americans: Comparison of clinical and laboratory features of transthyretin V122I amyloidosis and immunoglobulin light chain amyloidosis. Am Heart J 158(4):607-614.
    • (2009) Am Heart J , vol.158 , Issue.4 , pp. 607-614
    • Connors, L.H.1
  • 15
    • 77951551396 scopus 로고    scopus 로고
    • Significance of the amyloidogenic transthyretin Val 122 Ile allele in African Americans in the Arteriosclerosis Risk in Communities (ARIC) and Cardiovascular Health (CHS) Studies
    • Buxbaum J, et al. (2010) Significance of the amyloidogenic transthyretin Val 122 Ile allele in African Americans in the Arteriosclerosis Risk in Communities (ARIC) and Cardiovascular Health (CHS) Studies. Am Heart J 159(5):864-870.
    • (2010) Am Heart J , vol.159 , Issue.5 , pp. 864-870
    • Buxbaum, J.1
  • 17
    • 0035909981 scopus 로고    scopus 로고
    • The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
    • DOI 10.1073/pnas.261419998
    • Jiang X, Buxbaum JN, Kelly JW (2001) The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc Natl Acad Sci USA 98(26):14943-14948. (Pubitemid 34013949)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.26 , pp. 14943-14948
    • Jiang, X.1    Buxbaum, J.N.2    Kelly, J.W.3
  • 18
    • 84865849112 scopus 로고    scopus 로고
    • Transthyretin (TTR) cardiac amyloidosis
    • Ruberg FL, Berk JL (2012) Transthyretin (TTR) cardiac amyloidosis. Circulation 126(10):1286-1300.
    • (2012) Circulation , vol.126 , Issue.10 , pp. 1286-1300
    • Ruberg, F.L.1    Berk, J.L.2
  • 19
    • 80052286754 scopus 로고    scopus 로고
    • Cardiac amyloidosis: A treatable disease, often overlooked
    • Falk RH (2011) Cardiac amyloidosis: A treatable disease, often overlooked. Circulation 124(9):1079-1085.
    • (2011) Circulation , vol.124 , Issue.9 , pp. 1079-1085
    • Falk, R.H.1
  • 21
    • 77954177629 scopus 로고    scopus 로고
    • Transthyretin-related amyloidoses and the heart: A clinical overview
    • Rapezzi C, et al. (2010) Transthyretin-related amyloidoses and the heart: A clinical overview. Nat Rev Cardiol 7(7):398-408.
    • (2010) Nat Rev Cardiol , vol.7 , Issue.7 , pp. 398-408
    • Rapezzi, C.1
  • 22
    • 0035964955 scopus 로고    scopus 로고
    • Trans-suppression of misfolding in an amyloid disease
    • DOI 10.1126/science.1062245
    • Hammarström P, Schneider F, Kelly JW (2001) Trans-suppression of misfolding in an amyloid disease. Science 293(5539):2459-2462. (Pubitemid 32917328)
    • (2001) Science , vol.293 , Issue.5539 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 23
    • 80052071085 scopus 로고    scopus 로고
    • Potent kinetic stabilizers that prevent transthyretin-mediated cardiomyocyte proteotoxicity
    • Alhamadsheh MM, et al. (2011) Potent kinetic stabilizers that prevent transthyretin-mediated cardiomyocyte proteotoxicity. Sci Transl Med 3(97):97ra81.
    • (2011) Sci Transl Med , vol.3 , Issue.97
    • Alhamadsheh, M.M.1
  • 24
    • 84862234023 scopus 로고    scopus 로고
    • Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade
    • Bulawa CE, et al. (2012) Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade. Proc Natl Acad Sci USA 109(24):9629-9634.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.24 , pp. 9629-9634
    • Bulawa, C.E.1
  • 25
    • 84862222705 scopus 로고    scopus 로고
    • Tafamidis for transthyretin familial amyloid polyneuropathy: A randomized, controlled trial
    • Coelho T, et al. (2012) Tafamidis for transthyretin familial amyloid polyneuropathy: A randomized, controlled trial. Neurology 79(8):785-792.
    • (2012) Neurology , vol.79 , Issue.8 , pp. 785-792
    • Coelho, T.1
  • 26
    • 33751082387 scopus 로고    scopus 로고
    • Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis
    • DOI 10.1080/13506120600960882, PII U1K50W114874R4JR
    • Sekijima Y, Dendle MA, Kelly JW (2006) Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis. Amyloid 13(4):236-249. (Pubitemid 44764463)
    • (2006) Amyloid , vol.13 , Issue.4 , pp. 236-249
    • Sekijima, Y.1    Dendle, M.A.2    Kelly, J.W.3
  • 27
    • 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 (2000) Consumption of NSAIDs and the development of congestive heart failure in elderly patients: An underrecognized public health problem. Arch Intern Med 160(6):777-784. (Pubitemid 30165238)
    • (2000) Archives of Internal Medicine , vol.160 , Issue.6 , pp. 777-784
    • Page, J.1    Henry, D.2
  • 28
    • 0034758114 scopus 로고    scopus 로고
    • Pathogenesis of NSAID-induced gastroduodenal mucosal injury
    • Wallace JL (2001) Pathogenesis of NSAID-induced gastroduodenal mucosal injury. Best Pract Res Clin Gastroenterol 15(5):691-703.
    • (2001) Best Pract Res Clin Gastroenterol , vol.15 , Issue.5 , pp. 691-703
    • Wallace, J.L.1
  • 29
    • 0035091384 scopus 로고    scopus 로고
    • Early liver transplantation is essential for familial amyloidotic polyneuropathy patients' quality of life
    • Jonsén E, Suhr OB, Tashima K, Athlin E (2001) Early liver transplantation is essential for familial amyloidotic polyneuropathy patients' quality of life. Amyloid 8(1):52-57. (Pubitemid 32210180)
    • (2001) Amyloid , vol.8 , Issue.1 , pp. 52-57
    • Jonsen, E.1    Suhr, O.B.2    Tashima, K.3    Athlin, E.4
  • 31
    • 77949272212 scopus 로고    scopus 로고
    • Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses
    • Connelly S, Choi S, Johnson SM, Kelly JW, Wilson IA (2010) Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses. Curr Opin Struct Biol 20(1):54-62.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.1 , pp. 54-62
    • Connelly, S.1    Choi, S.2    Johnson, S.M.3    Kelly, J.W.4    Wilson, I.A.5
  • 32
    • 79960291244 scopus 로고    scopus 로고
    • Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs
    • Bourgault S, et al. (2011) Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs. Biochem Biophys Res Commun 410(4):707-713.
    • (2011) Biochem Biophys Res Commun , vol.410 , Issue.4 , pp. 707-713
    • Bourgault, S.1
  • 33
    • 79951554447 scopus 로고    scopus 로고
    • A competition assay to identify amyloidogenesis inhibitors by monitoring the fluorescence emitted by the covalent attachment of a stilbene derivative to transthyretin
    • Choi S, Kelly JW (2011) A competition assay to identify amyloidogenesis inhibitors by monitoring the fluorescence emitted by the covalent attachment of a stilbene derivative to transthyretin. Bioorg Med Chem 19(4):1505-1514.
    • (2011) Bioorg Med Chem , vol.19 , Issue.4 , pp. 1505-1514
    • Choi, S.1    Kelly, J.W.2
  • 34
    • 33751023007 scopus 로고    scopus 로고
    • Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis
    • DOI 10.1016/j.neures.2006.08.014, PII S0168010206002239
    • Tojo K, Sekijima Y, Kelly JW, Ikeda S (2006) Diflunisal stabilizes familial amyloid polyneuropathy-associated transthyretin variant tetramers in serum against dissociation required for amyloidogenesis. Neurosci Res 56(4):441-449. (Pubitemid 44755449)
    • (2006) Neuroscience Research , vol.56 , Issue.4 , pp. 441-449
    • Tojo, K.1    Sekijima, Y.2    Kelly, J.W.3    Ikeda, S.-i.4
  • 35
    • 84878963521 scopus 로고    scopus 로고
    • European Medicines Agency Committee for Medicinal Products for Human Use EMA/729083/2011. Procedure No. EMEA/H/C/002294
    • European Medicines Agency Committee for Medicinal Products for Human Use (2011) Tafamidis Meglumine (Vyndaqel) assessment report, 22 September 2011. EMA/729083/2011. Procedure No. EMEA/H/C/002294.
    • (2011) Tafamidis Meglumine (Vyndaqel) Assessment Report, 22 September 2011
  • 38
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • Freire E (2008) Do enthalpy and entropy distinguish first in class from best in class? Drug Discov Today 13(19-20):869-874.
    • (2008) Drug Discov Today , vol.13 , Issue.19-20 , pp. 869-874
    • Freire, E.1
  • 39
    • 80052398365 scopus 로고    scopus 로고
    • α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T, Choi JG, Selkoe DJ (2011) α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477(7362):107-110.
    • (2011) Nature , vol.477 , Issue.7362 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 40
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly ML (1983) Solvent-accessible surfaces of proteins and nucleic acids. Science 221(4612):709-713.
    • (1983) Science , vol.221 , Issue.4612 , pp. 709-713
    • Connolly, M.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.