메뉴 건너뛰기




Volumn 2, Issue , 2015, Pages

Functional Amyloid Signaling via the Inflammasome, Necrosome, and Signalosome: New Therapeutic Targets in Heart Failure

Author keywords

functional amyloid; inflammasome; necrosome; pharmacological chaperones; signalosome

Indexed keywords


EID: 84999726077     PISSN: None     EISSN: 2297055X     Source Type: Journal    
DOI: 10.3389/fcvm.2015.00025     Document Type: Article
Times cited : (34)

References (105)
  • 1
    • 84856448913 scopus 로고    scopus 로고
    • Current perspectives on cardiac amyloidosis
    • 22058156
    • Guan J, Mishra S, Falk RH, Liao R. Current perspectives on cardiac amyloidosis. Am J Physiol Heart Circ Physiol (2012) 302:H544–52.10.1152/ajpheart.00815.201122058156
    • (2012) Am J Physiol Heart Circ Physiol , vol.302 , pp. H544-H552
    • Guan, J.1    Mishra, S.2    Falk, R.H.3    Liao, R.4
  • 2
    • 0013882861 scopus 로고
    • [The effect of the nervous system on the sensitivity of rat ovaries to lactogenic hormone]
    • Kirshenblat Ia D, Serbeniuk VN. [The effect of the nervous system on the sensitivity of rat ovaries to lactogenic hormone]. Probl Endokrinol Gormonoter (1966) 12:100–5.
    • (1966) Probl Endokrinol Gormonoter , vol.12 , pp. 100-105
    • Kirshenblat Ia, D.1    Serbeniuk, V.N.2
  • 3
    • 0030954873 scopus 로고    scopus 로고
    • The systemic amyloidoses
    • Falk RH, Comenzo RL, Skinner M. The systemic amyloidoses. N Engl J Med (1997) 337:898–909.10.1056/NEJM199709253371306
    • (1997) N Engl J Med , vol.337 , pp. 898-909
    • Falk, R.H.1    Comenzo, R.L.2    Skinner, M.3
  • 4
    • 0024514827 scopus 로고
    • Doppler characterization of left ventricular diastolic function in cardiac amyloidosis
    • 2647814
    • Klein AL, Hatle LK, Burstow DJ, Seward JB, Kyle RA, Bailey KR, et al. Doppler characterization of left ventricular diastolic function in cardiac amyloidosis. J Am Coll Cardiol (1989) 13:1017–26.10.1016/0735-1097(89)90254-42647814
    • (1989) J Am Coll Cardiol , vol.13 , pp. 1017-1026
    • Klein, A.L.1    Hatle, L.K.2    Burstow, D.J.3    Seward, J.B.4    Kyle, R.A.5    Bailey, K.R.6
  • 5
    • 0030744403 scopus 로고    scopus 로고
    • Familial and primary (AL) cardiac amyloidosis: echocardiographically similar diseases with distinctly different clinical outcomes
    • 9290406
    • Dubrey SW, Cha K, Skinner M, LaValley M, Falk RH. Familial and primary (AL) cardiac amyloidosis: echocardiographically similar diseases with distinctly different clinical outcomes. Heart (1997) 78:74–82.10.1136/hrt.78.1.749290406
    • (1997) Heart , vol.78 , pp. 74-82
    • Dubrey, S.W.1    Cha, K.2    Skinner, M.3    LaValley, M.4    Falk, R.H.5
  • 6
    • 2342525940 scopus 로고    scopus 로고
    • Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress
    • 15044325
    • Brenner DA, Jain M, Pimentel DR, Wang B, Connors LH, Skinner M, et al. Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress. Circ Res (2004) 94:1008–10.10.1161/01.RES.0000126569.75419.7415044325
    • (2004) Circ Res , vol.94 , pp. 1008-1010
    • Brenner, D.A.1    Jain, M.2    Pimentel, D.R.3    Wang, B.4    Connors, L.H.5    Skinner, M.6
  • 7
    • 78049467563 scopus 로고    scopus 로고
    • Systemic and microvascular oxidative stress induced by light chain amyloidosis
    • 19446898
    • Migrino RQ, Hari P, Gutterman DD, Bright M, Truran S, Schlundt B, et al. Systemic and microvascular oxidative stress induced by light chain amyloidosis. Int J Cardiol (2010) 145:67–8.10.1016/j.ijcard.2009.04.04419446898
    • (2010) Int J Cardiol , vol.145 , pp. 67-68
    • Migrino, R.Q.1    Hari, P.2    Gutterman, D.D.3    Bright, M.4    Truran, S.5    Schlundt, B.6
  • 8
    • 82855181178 scopus 로고    scopus 로고
    • Human microvascular dysfunction and apoptotic injury induced by AL amyloidosis light chain proteins
    • 21963839
    • Migrino RQ, Truran S, Gutterman DD, Franco DA, Bright M, Schlundt B, et al. Human microvascular dysfunction and apoptotic injury induced by AL amyloidosis light chain proteins. Am J Physiol Heart Circ Physiol (2011) 301:H2305–12.10.1152/ajpheart.00503.201121963839
    • (2011) Am J Physiol Heart Circ Physiol , vol.301 , pp. H2305-H2312
    • Migrino, R.Q.1    Truran, S.2    Gutterman, D.D.3    Franco, D.A.4    Bright, M.5    Schlundt, B.6
  • 9
    • 79958709932 scopus 로고    scopus 로고
    • Cytotoxicity of amyloidogenic immunoglobulin light chains in cell culture
    • 21368874
    • Sikkink LA, Ramirez-Alvarado M. Cytotoxicity of amyloidogenic immunoglobulin light chains in cell culture. Cell Death Dis (2010) 1:e98.10.1038/cddis.2010.7521368874
    • (2010) Cell Death Dis , vol.1 , pp. e98
    • Sikkink, L.A.1    Ramirez-Alvarado, M.2
  • 10
    • 77950467036 scopus 로고    scopus 로고
    • Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy
    • 20194882
    • Gianni D, Li A, Tesco G, McKay KM, Moore J, Raygor K, et al. Protein aggregates and novel presenilin gene variants in idiopathic dilated cardiomyopathy. Circulation (2010) 121:1216–26.10.1161/CIRCULATIONAHA.109.87951020194882
    • (2010) Circulation , vol.121 , pp. 1216-1226
    • Gianni, D.1    Li, A.2    Tesco, G.3    McKay, K.M.4    Moore, J.5    Raygor, K.6
  • 11
    • 84925358628 scopus 로고    scopus 로고
    • Cofilin-2 phosphorylation and sequestration in myocardial aggregates: novel pathogenetic mechanisms for idiopathic dilated cardiomyopathy
    • 25814227
    • Subramanian K, Gianni D, Balla C, Assenza GE, Joshi M, Semigran MJ, et al. Cofilin-2 phosphorylation and sequestration in myocardial aggregates: novel pathogenetic mechanisms for idiopathic dilated cardiomyopathy. J Am Coll Cardiol (2015) 65:1199–214.10.1016/j.jacc.2015.01.03125814227
    • (2015) J Am Coll Cardiol , vol.65 , pp. 1199-1214
    • Subramanian, K.1    Gianni, D.2    Balla, C.3    Assenza, G.E.4    Joshi, M.5    Semigran, M.J.6
  • 12
    • 34347347236 scopus 로고    scopus 로고
    • Cofilin-mediated neurodegeneration in Alzheimer’s disease and other amyloidopathies
    • 17519504
    • Maloney MT, Bamburg JR. Cofilin-mediated neurodegeneration in Alzheimer’s disease and other amyloidopathies. Mol Neurobiol (2007) 35:21–44.10.1007/BF0270062217519504
    • (2007) Mol Neurobiol , vol.35 , pp. 21-44
    • Maloney, M.T.1    Bamburg, J.R.2
  • 13
    • 84886084984 scopus 로고    scopus 로고
    • The role of the cofilin-actin rod stress response in neurodegenerative diseases uncovers potential new drug targets
    • 23267414
    • Munsie LN, Truant R. The role of the cofilin-actin rod stress response in neurodegenerative diseases uncovers potential new drug targets. Bioarchitecture (2012) 2:204–8.10.4161/bioa.2254923267414
    • (2012) Bioarchitecture , vol.2 , pp. 204-208
    • Munsie, L.N.1    Truant, R.2
  • 14
    • 84904469376 scopus 로고    scopus 로고
    • Chaperones and cardiac misfolding protein diseases
    • 24694370
    • Christians ES, Mustafi SB, Benjamin IJ. Chaperones and cardiac misfolding protein diseases. Curr Protein Pept Sci (2014) 15:189–204.10.2174/138920371566614033111151824694370
    • (2014) Curr Protein Pept Sci , vol.15 , pp. 189-204
    • Christians, E.S.1    Mustafi, S.B.2    Benjamin, I.J.3
  • 15
    • 84901452339 scopus 로고    scopus 로고
    • Re-trafficking of hERG reverses long QT syndrome 2 phenotype in human iPS-derived cardiomyocytes
    • 24623279
    • Mehta A, Sequiera GL, Ramachandra CJ, Sudibyo Y, Chung Y, Sheng J, et al. Re-trafficking of hERG reverses long QT syndrome 2 phenotype in human iPS-derived cardiomyocytes. Cardiovasc Res (2014) 102:497–506.10.1093/cvr/cvu06024623279
    • (2014) Cardiovasc Res , vol.102 , pp. 497-506
    • Mehta, A.1    Sequiera, G.L.2    Ramachandra, C.J.3    Sudibyo, Y.4    Chung, Y.5    Sheng, J.6
  • 16
    • 33644851751 scopus 로고    scopus 로고
    • Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism
    • 16432067
    • Anderson CL, Delisle BP, Anson BD, Kilby JA, Will ML, Tester DJ, et al. Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism. Circulation (2006) 113:365–73.10.1161/CIRCULATIONAHA.105.57020016432067
    • (2006) Circulation , vol.113 , pp. 365-373
    • Anderson, C.L.1    Delisle, B.P.2    Anson, B.D.3    Kilby, J.A.4    Will, M.L.5    Tester, D.J.6
  • 17
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • 21495850
    • Braakman I, Bulleid NJ. Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem (2011) 80:71–99.10.1146/annurev-biochem-062209-09383621495850
    • (2011) Annu Rev Biochem , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 18
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • 16756495
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem (2006) 75:333–66.10.1146/annurev.biochem.75.101304.12390116756495
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 20
    • 84874905513 scopus 로고    scopus 로고
    • Protein misfolding in disease and small molecule therapies
    • 23339300
    • Gomes CM. Protein misfolding in disease and small molecule therapies. Curr Top Med Chem (2012) 12:2460–9.10.2174/156802661121222000223339300
    • (2012) Curr Top Med Chem , vol.12 , pp. 2460-2469
    • Gomes, C.M.1
  • 21
    • 71349087420 scopus 로고    scopus 로고
    • The generic nature of protein folding and misfolding
    • Uversky V.N., Fink A.L., (eds), New York, Springer, In:, editors., :, p
    • Dobson CM. The generic nature of protein folding and misfolding. In: Uversky VN, Fink AL, editors. Protein Misfolding, Aggregation, and Conformational Diseases. New York: Springer (2006). p. 21–41.
    • (2006) Protein Misfolding, Aggregation, and Conformational Diseases , pp. 21-41
    • Dobson, C.M.1
  • 22
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • 8989315
    • Dill KA, Chan HS. From Levinthal to pathways to funnels. Nat Struct Biol (1997) 4:10–9.10.1038/nsb0197-108989315
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 26
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • 15272267
    • Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med (2004) 10(Suppl):S10–7.10.1038/nm106615272267
    • (2004) Nat Med , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 27
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: what is the role of protein aggregation in neurodegeneration?
    • 16167052
    • Ross CA, Poirier MA. Opinion: what is the role of protein aggregation in neurodegeneration? Nat Rev Mol Cell Biol (2005) 6:891–8.10.1038/nrm174216167052
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 28
    • 3042711961 scopus 로고    scopus 로고
    • Desmin-related cardiomyopathy in transgenic mice: a cardiac amyloidosis
    • 15220483
    • Sanbe A, Osinska H, Saffitz JE, Glabe CG, Kayed R, Maloyan A, et al. Desmin-related cardiomyopathy in transgenic mice: a cardiac amyloidosis. Proc Natl Acad Sci USA (2004) 101:10132–6.10.1073/pnas.040190010115220483
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10132-10136
    • Sanbe, A.1    Osinska, H.2    Saffitz, J.E.3    Glabe, C.G.4    Kayed, R.5    Maloyan, A.6
  • 29
    • 0037453585 scopus 로고    scopus 로고
    • Myocytes die by multiple mechanisms in failing human hearts
    • 12649263
    • Kostin S, Pool L, Elsasser A, Hein S, Drexler HC, Arnon E, et al. Myocytes die by multiple mechanisms in failing human hearts. Circ Res (2003) 92:715–24.10.1161/01.RES.0000067471.95890.5C12649263
    • (2003) Circ Res , vol.92 , pp. 715-724
    • Kostin, S.1    Pool, L.2    Elsasser, A.3    Hein, S.4    Drexler, H.C.5    Arnon, E.6
  • 30
    • 47749105267 scopus 로고    scopus 로고
    • Intracellular protein aggregation is a proximal trigger of cardiomyocyte autophagy
    • 18541737
    • Tannous P, Zhu H, Nemchenko A, Berry JM, Johnstone JL, Shelton JM, et al. Intracellular protein aggregation is a proximal trigger of cardiomyocyte autophagy. Circulation (2008) 117:3070–8.10.1161/CIRCULATIONAHA.107.76387018541737
    • (2008) Circulation , vol.117 , pp. 3070-3078
    • Tannous, P.1    Zhu, H.2    Nemchenko, A.3    Berry, J.M.4    Johnstone, J.L.5    Shelton, J.M.6
  • 31
    • 44449104300 scopus 로고    scopus 로고
    • Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure
    • 18490523
    • Pattison JS, Sanbe A, Maloyan A, Osinska H, Klevitsky R, Robbins J. Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure. Circulation (2008) 117:2743–51.10.1161/CIRCULATIONAHA.107.75023218490523
    • (2008) Circulation , vol.117 , pp. 2743-2751
    • Pattison, J.S.1    Sanbe, A.2    Maloyan, A.3    Osinska, H.4    Klevitsky, R.5    Robbins, J.6
  • 32
    • 0035839573 scopus 로고    scopus 로고
    • Oxidative modification and inactivation of the proteasome during coronary occlusion/reperfusion
    • 11375979
    • Bulteau AL, Lundberg KC, Humphries KM, Sadek HA, Szweda PA, Friguet B, et al. Oxidative modification and inactivation of the proteasome during coronary occlusion/reperfusion. J Biol Chem (2001) 276:30057–63.10.1074/jbc.M10014220011375979
    • (2001) J Biol Chem , vol.276 , pp. 30057-30063
    • Bulteau, A.L.1    Lundberg, K.C.2    Humphries, K.M.3    Sadek, H.A.4    Szweda, P.A.5    Friguet, B.6
  • 33
    • 84865497050 scopus 로고    scopus 로고
    • Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocardial ischemia-reperfusion injury in mice
    • 22740087
    • Tian Z, Zheng H, Li J, Li Y, Su H, Wang X. Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocardial ischemia-reperfusion injury in mice. Circ Res (2012) 111:532–42.10.1161/CIRCRESAHA.112.27098322740087
    • (2012) Circ Res , vol.111 , pp. 532-542
    • Tian, Z.1    Zheng, H.2    Li, J.3    Li, Y.4    Su, H.5    Wang, X.6
  • 34
    • 78149244970 scopus 로고    scopus 로고
    • Hold me tight: role of the heat shock protein family of chaperones in cardiac disease
    • Willis MS, Patterson C. Hold me tight: role of the heat shock protein family of chaperones in cardiac disease. Circulation (2010) 122:1740–51.10.1161/CIRCULATIONAHA.110.942250
    • (2010) Circulation , vol.122 , pp. 1740-1751
    • Willis, M.S.1    Patterson, C.2
  • 35
    • 78149416783 scopus 로고    scopus 로고
    • Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways
    • 20863832
    • Zhang H, Rajasekaran NS, Orosz A, Xiao X, Rechsteiner M, Benjamin IJ. Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways. J Mol Cell Cardiol (2010) 49:918–30.10.1016/j.yjmcc.2010.09.00420863832
    • (2010) J Mol Cell Cardiol , vol.49 , pp. 918-930
    • Zhang, H.1    Rajasekaran, N.S.2    Orosz, A.3    Xiao, X.4    Rechsteiner, M.5    Benjamin, I.J.6
  • 36
    • 65449170415 scopus 로고    scopus 로고
    • Protective effect of geranylgeranylacetone via enhancement of HSPB8 induction in desmin-related cardiomyopathy
    • 19399179
    • Sanbe A, Daicho T, Mizutani R, Endo T, Miyauchi N, Yamauchi J, et al. Protective effect of geranylgeranylacetone via enhancement of HSPB8 induction in desmin-related cardiomyopathy. PLoS One (2009) 4:e5351.10.1371/journal.pone.000535119399179
    • (2009) PLoS One , vol.4 , pp. e5351
    • Sanbe, A.1    Daicho, T.2    Mizutani, R.3    Endo, T.4    Miyauchi, N.5    Yamauchi, J.6
  • 37
    • 0034421921 scopus 로고    scopus 로고
    • Pharmacological chaperones: a new twist on receptor folding
    • 11121835
    • Morello JP, Petaja-Repo UE, Bichet DG, Bouvier M. Pharmacological chaperones: a new twist on receptor folding. Trends Pharmacol Sci (2000) 21:466–9.10.1016/S0165-6147(00)01575-311121835
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 466-469
    • Morello, J.P.1    Petaja-Repo, U.E.2    Bichet, D.G.3    Bouvier, M.4
  • 38
    • 0034118221 scopus 로고    scopus 로고
    • Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants
    • 10749568
    • Morello JP, Salahpour A, Laperriere A, Bernier V, Arthus MF, Lonergan M, et al. Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J Clin Invest (2000) 105:887–95.10.1172/JCI868810749568
    • (2000) J Clin Invest , vol.105 , pp. 887-895
    • Morello, J.P.1    Salahpour, A.2    Laperriere, A.3    Bernier, V.4    Arthus, M.F.5    Lonergan, M.6
  • 39
    • 0009689526 scopus 로고    scopus 로고
    • Characterization of SR 121463A, a highly potent and selective, orally active vasopressin V2 receptor antagonist
    • 8981918
    • Serradeil-Le Gal C, Lacour C, Valette G, Garcia G, Foulon L, Galindo G, et al. Characterization of SR 121463A, a highly potent and selective, orally active vasopressin V2 receptor antagonist. J Clin Invest (1996) 98:2729–38.10.1172/JCI1190988981918
    • (1996) J Clin Invest , vol.98 , pp. 2729-2738
    • Serradeil-Le Gal, C.1    Lacour, C.2    Valette, G.3    Garcia, G.4    Foulon, L.5    Galindo, G.6
  • 40
    • 50149112642 scopus 로고    scopus 로고
    • Protein misfolding in conformational disorders: rescue of folding defects and chemical chaperoning
    • 18691147
    • Leandro P, Gomes CM. Protein misfolding in conformational disorders: rescue of folding defects and chemical chaperoning. Mini Rev Med Chem (2008) 8:901–11.10.2174/13895570878513278318691147
    • (2008) Mini Rev Med Chem , vol.8 , pp. 901-911
    • Leandro, P.1    Gomes, C.M.2
  • 41
    • 84860663436 scopus 로고    scopus 로고
    • Transthyretin deposition in familial amyloidotic polyneuropathy
    • 22471982
    • Saraiva MJ, Magalhaes J, Ferreira N, Almeida MR. Transthyretin deposition in familial amyloidotic polyneuropathy. Curr Med Chem (2012) 19:2304–11.10.2174/09298671280026923622471982
    • (2012) Curr Med Chem , vol.19 , pp. 2304-2311
    • Saraiva, M.J.1    Magalhaes, J.2    Ferreira, N.3    Almeida, M.R.4
  • 42
    • 84906048507 scopus 로고    scopus 로고
    • An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis
    • 25003808
    • Obici L, Merlini G. An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis. Expert Opin Investig Drugs (2014) 23:1239–51.10.1517/13543784.2014.92254125003808
    • (2014) Expert Opin Investig Drugs , vol.23 , pp. 1239-1251
    • Obici, L.1    Merlini, G.2
  • 43
    • 84861421529 scopus 로고    scopus 로고
    • The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug
    • 22244854
    • Johnson SM, Connelly S, Fearns C, Powers ET, Kelly JW. The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. J Mol Biol (2012) 421:185–203.10.1016/j.jmb.2011.12.06022244854
    • (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
  • 44
    • 38349124133 scopus 로고    scopus 로고
    • Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors
    • 18095641
    • Johnson SM, Connelly S, Wilson IA, Kelly JW. Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors. J Med Chem (2008) 51:260–70.10.1021/jm070873518095641
    • (2008) J Med Chem , vol.51 , pp. 260-270
    • Johnson, S.M.1    Connelly, S.2    Wilson, I.A.3    Kelly, J.W.4
  • 46
    • 84889238225 scopus 로고    scopus 로고
    • Long-term effects of tafamidis for the treatment of transthyretin familial amyloid polyneuropathy
    • 23974642
    • Coelho T, Maia LF, da Silva AM, Cruz MW, Plante-Bordeneuve V, Suhr OB, et al. Long-term effects of tafamidis for the treatment of transthyretin familial amyloid polyneuropathy. J Neurol (2013) 260:2802–14.10.1007/s00415-013-7051-723974642
    • (2013) J Neurol , vol.260 , pp. 2802-2814
    • Coelho, T.1    Maia, L.F.2    da Silva, A.M.3    Cruz, M.W.4    Plante-Bordeneuve, V.5    Suhr, O.B.6
  • 47
    • 84862222705 scopus 로고    scopus 로고
    • Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trial
    • 22843282
    • Coelho T, Maia LF, Martins da Silva A, Waddington Cruz M, Plante-Bordeneuve V, Lozeron P, et al. Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trial. Neurology (2012) 79:785–92.10.1212/WNL.0b013e3182661eb122843282
    • (2012) Neurology , vol.79 , pp. 785-792
    • Coelho, T.1    Maia, L.F.2    Martins da Silva, A.3    Waddington Cruz, M.4    Plante-Bordeneuve, V.5    Lozeron, P.6
  • 48
    • 84906727945 scopus 로고    scopus 로고
    • Tafamidis: a review of its use in familial amyloid polyneuropathy
    • 25022953
    • Scott LJ. Tafamidis: a review of its use in familial amyloid polyneuropathy. Drugs (2014) 74:1371–8.10.1007/s40265-014-0260-225022953
    • (2014) Drugs , vol.74 , pp. 1371-1378
    • Scott, L.J.1
  • 50
    • 80052071085 scopus 로고    scopus 로고
    • Potent kinetic stabilizers that prevent transthyretin-mediated cardiomyocyte proteotoxicity
    • Alhamadsheh MM, Connelly S, Cho A, Reixach N, Powers ET, Pan DW, et al. Potent kinetic stabilizers that prevent transthyretin-mediated cardiomyocyte proteotoxicity. Sci Transl Med (2011) 3:97ra81.10.1126/scitranslmed.3002473
    • (2011) Sci Transl Med , vol.3 , pp. 97ra81
    • Alhamadsheh, M.M.1    Connelly, S.2    Cho, A.3    Reixach, N.4    Powers, E.T.5    Pan, D.W.6
  • 51
    • 0029094670 scopus 로고
    • New drug therapy of amyloidoses: resorption of AL-type deposits with 4’-iodo-4’-deoxydoxorubicin
    • 7620181
    • Gianni L, Bellotti V, Gianni AM, Merlini G. New drug therapy of amyloidoses: resorption of AL-type deposits with 4’-iodo-4’-deoxydoxorubicin. Blood (1995) 86:855–61.7620181
    • (1995) Blood , vol.86 , pp. 855-861
    • Gianni, L.1    Bellotti, V.2    Gianni, A.M.3    Merlini, G.4
  • 52
    • 0028914019 scopus 로고
    • Interaction of the anthracycline 4’-iodo-4’-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis
    • 7708755
    • Merlini G, Ascari E, Amboldi N, Bellotti V, Arbustini E, Perfetti V, et al. Interaction of the anthracycline 4’-iodo-4’-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis. Proc Natl Acad Sci USA (1995) 92:2959–63.10.1073/pnas.92.7.29597708755
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2959-2963
    • Merlini, G.1    Ascari, E.2    Amboldi, N.3    Bellotti, V.4    Arbustini, E.5    Perfetti, V.6
  • 53
    • 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
    • 12724338
    • Cardoso I, Merlini G, Saraiva MJ. 4’-iodo-4’-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters. FASEB J (2003) 17:803–9.10.1096/fj.02-0764com12724338
    • (2003) FASEB J , vol.17 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 54
    • 33644919388 scopus 로고    scopus 로고
    • Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model
    • 16449795
    • Cardoso I, Saraiva MJ. Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model. FASEB J (2006) 20:234–9.10.1096/fj.05-4509com16449795
    • (2006) FASEB J , vol.20 , pp. 234-239
    • Cardoso, I.1    Saraiva, M.J.2
  • 55
    • 49349097870 scopus 로고    scopus 로고
    • Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of familial amyloidotic polyneuropathy
    • 18572024
    • Macedo B, Batista AR, Ferreira N, Almeida MR, Saraiva MJ. Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of familial amyloidotic polyneuropathy. Biochim Biophys Acta (2008) 1782:517–22.10.1016/j.bbadis.2008.05.00518572024
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 517-522
    • Macedo, B.1    Batista, A.R.2    Ferreira, N.3    Almeida, M.R.4    Saraiva, M.J.5
  • 56
    • 84874609836 scopus 로고    scopus 로고
    • Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-beta species
    • 23426629
    • Hyung SJ, DeToma AS, Brender JR, Lee S, Vivekanandan S, Kochi A, et al. Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-beta species. Proc Natl Acad Sci USA (2013) 110:3743–8.10.1073/pnas.122032611023426629
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 3743-3748
    • Hyung, S.J.1    DeToma, A.S.2    Brender, J.R.3    Lee, S.4    Vivekanandan, S.5    Kochi, A.6
  • 57
    • 84864281808 scopus 로고    scopus 로고
    • Structural properties of EGCG-induced, nontoxic Alzheimer’s disease abeta oligomers
    • 22300765
    • Lopez del Amo JM, Fink U, Dasari M, Grelle G, Wanker EE, Bieschke J, et al. Structural properties of EGCG-induced, nontoxic Alzheimer’s disease abeta oligomers. J Mol Biol (2012) 421:517–24.10.1016/j.jmb.2012.01.01322300765
    • (2012) J Mol Biol , vol.421 , pp. 517-524
    • Lopez del Amo, J.M.1    Fink, U.2    Dasari, M.3    Grelle, G.4    Wanker, E.E.5    Bieschke, J.6
  • 58
    • 84869109959 scopus 로고    scopus 로고
    • Green tea halts progression of cardiac transthyretin amyloidosis: an observational report
    • 22584381
    • Kristen AV, Lehrke S, Buss S, Mereles D, Steen H, Ehlermann P, et al. Green tea halts progression of cardiac transthyretin amyloidosis: an observational report. Clin Res Cardiol (2012) 101:805–13.10.1007/s00392-012-0463-z22584381
    • (2012) Clin Res Cardiol , vol.101 , pp. 805-813
    • Kristen, A.V.1    Lehrke, S.2    Buss, S.3    Mereles, D.4    Steen, H.5    Ehlermann, P.6
  • 59
    • 77955841265 scopus 로고    scopus 로고
    • Chitosan nanoparticles enhance the intestinal absorption of the green tea catechins (+)-catechin and (-)-epigallocatechin gallate
    • Dube A, Nicolazzo JA, Larson I. Chitosan nanoparticles enhance the intestinal absorption of the green tea catechins (+)-catechin and (-)-epigallocatechin gallate. Eur J Pharm Sci (2010) 41:219–25.10.1016/j.ejps.2010.06.010
    • (2010) Eur J Pharm Sci , vol.41 , pp. 219-225
    • Dube, A.1    Nicolazzo, J.A.2    Larson, I.3
  • 61
    • 67349111321 scopus 로고    scopus 로고
    • Binding and stabilization of transthyretin by curcumin
    • 19268650
    • Pullakhandam R, Srinivas PN, Nair MK, Reddy GB. Binding and stabilization of transthyretin by curcumin. Arch Biochem Biophys (2009) 485:115–9.10.1016/j.abb.2009.02.01319268650
    • (2009) Arch Biochem Biophys , vol.485 , pp. 115-119
    • Pullakhandam, R.1    Srinivas, P.N.2    Nair, M.K.3    Reddy, G.B.4
  • 62
    • 79960910835 scopus 로고    scopus 로고
    • Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation
    • 21740906
    • Ferreira N, Saraiva MJ, Almeida MR. Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS Lett (2011) 585:2424–30.10.1016/j.febslet.2011.06.03021740906
    • (2011) FEBS Lett , vol.585 , pp. 2424-2430
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 63
    • 84868592337 scopus 로고    scopus 로고
    • Dietary curcumin counteracts extracellular transthyretin deposition: insights on the mechanism of amyloid inhibition
    • 23069388
    • Ferreira N, Santos SA, Domingues MR, Saraiva MJ, Almeida MR. Dietary curcumin counteracts extracellular transthyretin deposition: insights on the mechanism of amyloid inhibition. Biochim Biophys Acta (2013) 1832:39–45.10.1016/j.bbadis.2012.10.00723069388
    • (2013) Biochim Biophys Acta , vol.1832 , pp. 39-45
    • Ferreira, N.1    Santos, S.A.2    Domingues, M.R.3    Saraiva, M.J.4    Almeida, M.R.5
  • 65
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • Latz E, Xiao TS, Stutz A. Activation and regulation of the inflammasomes. Nat Rev Immunol (2013) 13:397–411.10.1038/nri3452
    • (2013) Nat Rev Immunol , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 66
    • 84884332722 scopus 로고    scopus 로고
    • Mechanisms of NOD-like receptor-associated inflammasome activation
    • 24054327
    • Wen H, Miao EA, Ting JP. Mechanisms of NOD-like receptor-associated inflammasome activation. Immunity (2013) 39:432–41.10.1016/j.immuni.2013.08.03724054327
    • (2013) Immunity , vol.39 , pp. 432-441
    • Wen, H.1    Miao, E.A.2    Ting, J.P.3
  • 67
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • 24630723
    • Cai X, Chen J, Xu H, Liu S, Jiang QX, Halfmann R, et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell (2014) 156:1207–22.10.1016/j.cell.2014.01.06324630723
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1    Chen, J.2    Xu, H.3    Liu, S.4    Jiang, Q.X.5    Halfmann, R.6
  • 68
    • 84904692363 scopus 로고    scopus 로고
    • The adaptor ASC has extracellular and ‘prionoid’ activities that propagate inflammation
    • 24952505
    • Franklin BS, Bossaller L, De Nardo D, Ratter JM, Stutz A, Engels G, et al. The adaptor ASC has extracellular and ‘prionoid’ activities that propagate inflammation. Nat Immunol (2014) 15:727–37.10.1038/ni.291324952505
    • (2014) Nat Immunol , vol.15 , pp. 727-737
    • Franklin, B.S.1    Bossaller, L.2    De Nardo, D.3    Ratter, J.M.4    Stutz, A.5    Engels, G.6
  • 69
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • 24630722
    • Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos MR, et al. Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell (2014) 156:1193–206.10.1016/j.cell.2014.02.00824630722
    • (2014) Cell , vol.156 , pp. 1193-1206
    • Lu, A.1    Magupalli, V.G.2    Ruan, J.3    Yin, Q.4    Atianand, M.K.5    Vos, M.R.6
  • 70
    • 33746876396 scopus 로고    scopus 로고
    • Neonatal-onset multisystem inflammatory disease responsive to interleukin-1beta inhibition
    • 16899778
    • Goldbach-Mansky R, Dailey NJ, Canna SW, Gelabert A, Jones J, Rubin BI, et al. Neonatal-onset multisystem inflammatory disease responsive to interleukin-1beta inhibition. N Engl J Med (2006) 355:581–92.10.1056/NEJMoa05513716899778
    • (2006) N Engl J Med , vol.355 , pp. 581-592
    • Goldbach-Mansky, R.1    Dailey, N.J.2    Canna, S.W.3    Gelabert, A.4    Jones, J.5    Rubin, B.I.6
  • 72
    • 84864958598 scopus 로고    scopus 로고
    • Pro-inflammatory interleukin-18 increases Alzheimer’s disease-associated amyloid-beta production in human neuron-like cells
    • 22898493
    • Sutinen EM, Pirttila T, Anderson G, Salminen A, Ojala JO. Pro-inflammatory interleukin-18 increases Alzheimer’s disease-associated amyloid-beta production in human neuron-like cells. J Neuroinflammation (2012) 9:199.10.1186/1742-2094-9-19922898493
    • (2012) J Neuroinflammation , vol.9 , pp. 199
    • Sutinen, E.M.1    Pirttila, T.2    Anderson, G.3    Salminen, A.4    Ojala, J.O.5
  • 73
    • 27744602338 scopus 로고    scopus 로고
    • Hereditary periodic fever and reactive amyloidosis
    • van der Hilst JC, Simon A, Drenth JP. Hereditary periodic fever and reactive amyloidosis. Clin Exp Med (2005) 5:87–98.10.1007/s10238-005-0071-6
    • (2005) Clin Exp Med , vol.5 , pp. 87-98
    • van der Hilst, J.C.1    Simon, A.2    Drenth, J.P.3
  • 74
    • 67349254827 scopus 로고    scopus 로고
    • A case of systemic amyloidosis following ankylosing spondylitis associated with congestive heart failure
    • Ha SJ, Kim WS, Hwang SJ, Woo JS, Shon IS, Bae JH, et al. A case of systemic amyloidosis following ankylosing spondylitis associated with congestive heart failure. J Am Soc Echocardiogr (2009) 22(542):e545–7.10.1016/j.echo.2009.01.022
    • (2009) J Am Soc Echocardiogr , vol.22 , Issue.542 , pp. e545-e547
    • Ha, S.J.1    Kim, W.S.2    Hwang, S.J.3    Woo, J.S.4    Shon, I.S.5    Bae, J.H.6
  • 75
    • 84887145196 scopus 로고    scopus 로고
    • [Cardiac amyloidosis: a case series of 14 patients, description and prognosis]
    • 24090573
    • Isabel C, Georgin-Lavialle S, Aouba A, Delarue R, Nochy D, Karras A, et al. [Cardiac amyloidosis: a case series of 14 patients, description and prognosis]. Rev Med Interne (2013) 34:671–8.10.1016/j.revmed.2013.05.00324090573
    • (2013) Rev Med Interne , vol.34 , pp. 671-678
    • Isabel, C.1    Georgin-Lavialle, S.2    Aouba, A.3    Delarue, R.4    Nochy, D.5    Karras, A.6
  • 76
    • 84938929627 scopus 로고    scopus 로고
    • Therapeutic benefits of tocilizumab vary in different organs of a patient with AA amyloidosis
    • 25197587
    • Matsui M, Okayama S, Tsushima H, Samejima K, Kanki T, Hasegawa A, et al. Therapeutic benefits of tocilizumab vary in different organs of a patient with AA amyloidosis. Case Rep Nephrol (2014) 2014:823093.10.1155/2014/82309325197587
    • (2014) Case Rep Nephrol , vol.2014 , pp. 823093
    • Matsui, M.1    Okayama, S.2    Tsushima, H.3    Samejima, K.4    Kanki, T.5    Hasegawa, A.6
  • 78
    • 57449092930 scopus 로고    scopus 로고
    • Amyloidosis is frequently undetected in patients with rheumatoid arthritis
    • 19065298
    • Koivuniemi R, Paimela L, Suomalainen R, Tornroth T, Leirisalo-Repo M. Amyloidosis is frequently undetected in patients with rheumatoid arthritis. Amyloid (2008) 15:262–8.10.1080/1350612080252467619065298
    • (2008) Amyloid , vol.15 , pp. 262-268
    • Koivuniemi, R.1    Paimela, L.2    Suomalainen, R.3    Tornroth, T.4    Leirisalo-Repo, M.5
  • 79
    • 84857220265 scopus 로고    scopus 로고
    • Tocilizumab improves cardiac disease in a hemodialysis patient with AA amyloidosis secondary to rheumatoid arthritis
    • 22260742
    • Hattori Y, Ubara Y, Sumida K, Hiramatsu R, Hasegawa E, Yamanouchi M, et al. Tocilizumab improves cardiac disease in a hemodialysis patient with AA amyloidosis secondary to rheumatoid arthritis. Amyloid (2012) 19:37–40.10.3109/13506129.2011.63646022260742
    • (2012) Amyloid , vol.19 , pp. 37-40
    • Hattori, Y.1    Ubara, Y.2    Sumida, K.3    Hiramatsu, R.4    Hasegawa, E.5    Yamanouchi, M.6
  • 80
    • 80053403444 scopus 로고    scopus 로고
    • Cardiac AA amyloidosis in a patient with rheumatoid arthritis and systemic sclerosis: the therapeutic potential of biological reagents
    • Wada Y, Kobayashi D, Murakami S, Oda M, Hanawa H, Kuroda T, et al. Cardiac AA amyloidosis in a patient with rheumatoid arthritis and systemic sclerosis: the therapeutic potential of biological reagents. Scand J Rheumatol (2011) 40:402–4.10.3109/03009742.2011.569754
    • (2011) Scand J Rheumatol , vol.40 , pp. 402-404
    • Wada, Y.1    Kobayashi, D.2    Murakami, S.3    Oda, M.4    Hanawa, H.5    Kuroda, T.6
  • 81
    • 79960386345 scopus 로고    scopus 로고
    • Serum amyloid A activates the NLRP3 inflammasome and promotes Th17 allergic asthma in mice
    • 21622869
    • Ather JL, Ckless K, Martin R, Foley KL, Suratt BT, Boyson JE, et al. Serum amyloid A activates the NLRP3 inflammasome and promotes Th17 allergic asthma in mice. J Immunol (2011) 187:64–73.10.4049/jimmunol.110050021622869
    • (2011) J Immunol , vol.187 , pp. 64-73
    • Ather, J.L.1    Ckless, K.2    Martin, R.3    Foley, K.L.4    Suratt, B.T.5    Boyson, J.E.6
  • 82
    • 84870705290 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation in macrophage cell lines by prion protein fibrils as the source of IL-1beta and neuronal toxicity
    • 22926439
    • Hafner-Bratkovic I, Bencina M, Fitzgerald KA, Golenbock D, Jerala R. NLRP3 inflammasome activation in macrophage cell lines by prion protein fibrils as the source of IL-1beta and neuronal toxicity. Cell Mol Life Sci (2012) 69:4215–28.10.1007/s00018-012-1140-022926439
    • (2012) Cell Mol Life Sci , vol.69 , pp. 4215-4228
    • Hafner-Bratkovic, I.1    Bencina, M.2    Fitzgerald, K.A.3    Golenbock, D.4    Jerala, R.5
  • 83
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • 18604209
    • Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, Reinheckel T, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol (2008) 9:857–65.10.1038/ni.163618604209
    • (2008) Nat Immunol , vol.9 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3    Stewart, C.R.4    Monks, B.G.5    Reinheckel, T.6
  • 84
    • 77956958947 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1beta in type 2 diabetes
    • 20835230
    • Masters SL, Dunne A, Subramanian SL, Hull RL, Tannahill GM, Sharp FA, et al. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1beta in type 2 diabetes. Nat Immunol (2010) 11:897–904.10.1038/ni.193520835230
    • (2010) Nat Immunol , vol.11 , pp. 897-904
    • Masters, S.L.1    Dunne, A.2    Subramanian, S.L.3    Hull, R.L.4    Tannahill, G.M.5    Sharp, F.A.6
  • 85
    • 79958040762 scopus 로고    scopus 로고
    • Serum amyloid A activates the NLRP3 inflammasome via P2X7 receptor and a cathepsin B-sensitive pathway
    • 21508263
    • Niemi K, Teirila L, Lappalainen J, Rajamaki K, Baumann MH, Oorni K, et al. Serum amyloid A activates the NLRP3 inflammasome via P2X7 receptor and a cathepsin B-sensitive pathway. J Immunol (2011) 186:6119–28.10.4049/jimmunol.100284321508263
    • (2011) J Immunol , vol.186 , pp. 6119-6128
    • Niemi, K.1    Teirila, L.2    Lappalainen, J.3    Rajamaki, K.4    Baumann, M.H.5    Oorni, K.6
  • 86
    • 84921340508 scopus 로고    scopus 로고
    • Toll-like receptor 2 and NLRP3 cooperate to recognize a functional bacterial amyloid, curli
    • 25422268
    • Rapsinski GJ, Wynosky-Dolfi MA, Oppong GO, Tursi SA, Wilson RP, Brodsky IE, et al. Toll-like receptor 2 and NLRP3 cooperate to recognize a functional bacterial amyloid, curli. Infect Immun (2015) 83:693–701.10.1128/IAI.02370-1425422268
    • (2015) Infect Immun , vol.83 , pp. 693-701
    • Rapsinski, G.J.1    Wynosky-Dolfi, M.A.2    Oppong, G.O.3    Tursi, S.A.4    Wilson, R.P.5    Brodsky, I.E.6
  • 87
    • 0032540267 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway for cardiac hypertrophy
    • 9568714
    • Molkentin JD, Lu JR, Antos CL, Markham B, Richardson J, Robbins J, et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell (1998) 93:215–28.10.1016/S0092-8674(00)81573-19568714
    • (1998) Cell , vol.93 , pp. 215-228
    • Molkentin, J.D.1    Lu, J.R.2    Antos, C.L.3    Markham, B.4    Richardson, J.5    Robbins, J.6
  • 88
    • 84872696318 scopus 로고    scopus 로고
    • The Nlrp3 inflammasome promotes myocardial dysfunction in structural cardiomyopathy through interleukin-1beta
    • 22848083
    • Bracey NA, Beck PL, Muruve DA, Hirota SA, Guo J, Jabagi H, et al. The Nlrp3 inflammasome promotes myocardial dysfunction in structural cardiomyopathy through interleukin-1beta. Exp Physiol (2013) 98:462–72.10.1113/expphysiol.2012.06833822848083
    • (2013) Exp Physiol , vol.98 , pp. 462-472
    • Bracey, N.A.1    Beck, P.L.2    Muruve, D.A.3    Hirota, S.A.4    Guo, J.5    Jabagi, H.6
  • 89
    • 84882984332 scopus 로고    scopus 로고
    • Association of nucleotide-binding oligomerization domain-like receptor 3 inflammasome and adverse clinical outcomes in patients with idiopathic dilated cardiomyopathy
    • 23382313
    • Luo B, Wang F, Li B, Dong Z, Liu X, Zhang C, et al. Association of nucleotide-binding oligomerization domain-like receptor 3 inflammasome and adverse clinical outcomes in patients with idiopathic dilated cardiomyopathy. Clin Chem Lab Med (2013) 51:1521–8.10.1515/cclm-2012-060023382313
    • (2013) Clin Chem Lab Med , vol.51 , pp. 1521-1528
    • Luo, B.1    Wang, F.2    Li, B.3    Dong, Z.4    Liu, X.5    Zhang, C.6
  • 90
    • 0032805207 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha and interleukin-1beta synergistically depress human myocardial function
    • 10446825
    • Cain BS, Meldrum DR, Dinarello CA, Meng X, Joo KS, Banerjee A, et al. Tumor necrosis factor-alpha and interleukin-1beta synergistically depress human myocardial function. Crit Care Med (1999) 27:1309–18.10.1097/00003246-199907000-0001810446825
    • (1999) Crit Care Med , vol.27 , pp. 1309-1318
    • Cain, B.S.1    Meldrum, D.R.2    Dinarello, C.A.3    Meng, X.4    Joo, K.S.5    Banerjee, A.6
  • 91
    • 47649086507 scopus 로고    scopus 로고
    • Inhibition of interleukin-1 by anakinra improves vascular and left ventricular function in patients with rheumatoid arthritis
    • 18474811
    • Ikonomidis I, Lekakis JP, Nikolaou M, Paraskevaidis I, Andreadou I, Kaplanoglou T, et al. Inhibition of interleukin-1 by anakinra improves vascular and left ventricular function in patients with rheumatoid arthritis. Circulation (2008) 117:2662–9.10.1161/CIRCULATIONAHA.107.73187718474811
    • (2008) Circulation , vol.117 , pp. 2662-2669
    • Ikonomidis, I.1    Lekakis, J.P.2    Nikolaou, M.3    Paraskevaidis, I.4    Andreadou, I.5    Kaplanoglou, T.6
  • 92
    • 80053644777 scopus 로고    scopus 로고
    • Interleukin-1beta inhibition and the prevention of recurrent cardiovascular events: rationale and design of the Canakinumab Anti-inflammatory Thrombosis Outcomes Study (CANTOS)
    • 21982649
    • Ridker PM, Thuren T, Zalewski A, Libby P. Interleukin-1beta inhibition and the prevention of recurrent cardiovascular events: rationale and design of the Canakinumab Anti-inflammatory Thrombosis Outcomes Study (CANTOS). Am Heart J (2011) 162:597–605.10.1016/j.ahj.2011.06.01221982649
    • (2011) Am Heart J , vol.162 , pp. 597-605
    • Ridker, P.M.1    Thuren, T.2    Zalewski, A.3    Libby, P.4
  • 93
    • 84877324483 scopus 로고    scopus 로고
    • Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases
    • 23597596
    • Furukawa Y, Nukina N. Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases. Biochim Biophys Acta (2013) 1832:1271–8.10.1016/j.bbadis.2013.04.01123597596
    • (2013) Biochim Biophys Acta , vol.1832 , pp. 1271-1278
    • Furukawa, Y.1    Nukina, N.2
  • 94
    • 84864240409 scopus 로고    scopus 로고
    • The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
    • 22817896
    • Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, et al. The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell (2012) 150:339–50.10.1016/j.cell.2012.06.01922817896
    • (2012) Cell , vol.150 , pp. 339-350
    • Li, J.1    McQuade, T.2    Siemer, A.B.3    Napetschnig, J.4    Moriwaki, K.5    Hsiao, Y.S.6
  • 95
    • 84904322380 scopus 로고    scopus 로고
    • RIP3, a kinase promoting necroptotic cell death, mediates adverse remodelling after myocardial infarction
    • 24920296
    • Luedde M, Lutz M, Carter N, Sosna J, Jacoby C, Vucur M, et al. RIP3, a kinase promoting necroptotic cell death, mediates adverse remodelling after myocardial infarction. Cardiovasc Res (2014) 103:206–16.10.1093/cvr/cvu14624920296
    • (2014) Cardiovasc Res , vol.103 , pp. 206-216
    • Luedde, M.1    Lutz, M.2    Carter, N.3    Sosna, J.4    Jacoby, C.5    Vucur, M.6
  • 96
    • 84860584135 scopus 로고    scopus 로고
    • Inhibition of RIP1-dependent necrosis prevents adverse cardiac remodeling after myocardial ischemia-reperfusion in vivo
    • 22553001
    • Oerlemans MI, Liu J, Arslan F, den Ouden K, van Middelaar BJ, Doevendans PA, et al. Inhibition of RIP1-dependent necrosis prevents adverse cardiac remodeling after myocardial ischemia-reperfusion in vivo. Basic Res Cardiol (2012) 107:270.10.1007/s00395-012-0270-822553001
    • (2012) Basic Res Cardiol , vol.107 , pp. 270
    • Oerlemans, M.I.1    Liu, J.2    Arslan, F.3    den Ouden, K.4    van Middelaar, B.J.5    Doevendans, P.A.6
  • 97
    • 84899062708 scopus 로고    scopus 로고
    • Necrosis-dependent and independent signaling of the RIP kinases in inflammation
    • 24412261
    • Moriwaki K, Chan FK. Necrosis-dependent and independent signaling of the RIP kinases in inflammation. Cytokine Growth Factor Rev (2014) 25:167–74.10.1016/j.cytogfr.2013.12.01324412261
    • (2014) Cytokine Growth Factor Rev , vol.25 , pp. 167-174
    • Moriwaki, K.1    Chan, F.K.2
  • 98
    • 84942244833 scopus 로고    scopus 로고
    • Neddylation and deneddylation in cardiac biology
    • 25628956
    • Kandala S, Kim IM, Su H. Neddylation and deneddylation in cardiac biology. Am J Cardiovasc Dis (2014) 4:140–58.25628956
    • (2014) Am J Cardiovasc Dis , vol.4 , pp. 140-158
    • Kandala, S.1    Kim, I.M.2    Su, H.3
  • 99
    • 0028365625 scopus 로고
    • Arabidopsis COP9 is a component of a novel signaling complex mediating light control of development
    • 8033203
    • Wei N, Chamovitz DA, Deng XW. Arabidopsis COP9 is a component of a novel signaling complex mediating light control of development. Cell (1994) 78:117–24.10.1016/0092-8674(94)90578-98033203
    • (1994) Cell , vol.78 , pp. 117-124
    • Wei, N.1    Chamovitz, D.A.2    Deng, X.W.3
  • 100
    • 0344824691 scopus 로고    scopus 로고
    • The COP9 signalosome
    • Wei N, Deng XW. The COP9 signalosome. Annu Rev Cell Dev Biol (2003) 19:261–86.10.1146/annurev.cellbio.19.111301.112449
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 261-286
    • Wei, N.1    Deng, X.W.2
  • 102
    • 80855148621 scopus 로고    scopus 로고
    • COP9 signalosome regulates autophagosome maturation
    • 21986281
    • Su H, Li F, Ranek MJ, Wei N, Wang X. COP9 signalosome regulates autophagosome maturation. Circulation (2011) 124:2117–28.10.1161/CIRCULATIONAHA.111.04893421986281
    • (2011) Circulation , vol.124 , pp. 2117-2128
    • Su, H.1    Li, F.2    Ranek, M.J.3    Wei, N.4    Wang, X.5
  • 103
    • 84887423435 scopus 로고    scopus 로고
    • The COP9 signalosome is required for autophagy, proteasome-mediated proteolysis, and cardiomyocyte survival in adult mice
    • 23873473
    • Su H, Li J, Osinska H, Li F, Robbins J, Liu J, et al. The COP9 signalosome is required for autophagy, proteasome-mediated proteolysis, and cardiomyocyte survival in adult mice. Circ Heart Fail (2013) 6:1049–57.10.1161/CIRCHEARTFAILURE.113.00033823873473
    • (2013) Circ Heart Fail , vol.6 , pp. 1049-1057
    • Su, H.1    Li, J.2    Osinska, H.3    Li, F.4    Robbins, J.5    Liu, J.6
  • 104
    • 77951639210 scopus 로고    scopus 로고
    • Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3
    • 20399188
    • Enchev RI, Schreiber A, Beuron F, Morris EP. Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3. Structure (2010) 18:518–27.10.1016/j.str.2010.02.00820399188
    • (2010) Structure , vol.18 , pp. 518-527
    • Enchev, R.I.1    Schreiber, A.2    Beuron, F.3    Morris, E.P.4
  • 105
    • 23644447173 scopus 로고    scopus 로고
    • Consequences of COP9 signalosome and 26S proteasome interaction
    • 16045761
    • Huang X, Hetfeld BK, Seifert U, Kähne T, Kloetzel PM, Naumann M, et al. Consequences of COP9 signalosome and 26S proteasome interaction. FEBS J (2005) 272:3909–17.10.1111/j.1742-4658.2005.04807.x16045761
    • (2005) FEBS J , vol.272 , pp. 3909-3917
    • Huang, X.1    Hetfeld, B.K.2    Seifert, U.3    Kähne, T.4    Kloetzel, P.M.5    Naumann, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.