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Volumn 70, Issue 16, 2013, Pages 2999-3012

Activation of innate immunity by lysozyme fibrils is critically dependent on cross-β sheet structure

Author keywords

Amyloid induced inflammation; Cross structure; NLRP3 inflammasome; Toll like receptors

Indexed keywords

AMYLOID; CRYOPYRIN; INFLAMMASOME; INTERLEUKIN 1BETA; TOLL LIKE RECEPTOR 1; TOLL LIKE RECEPTOR 2;

EID: 84881163373     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1245-5     Document Type: Article
Times cited : (40)

References (57)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • 10.1146/annurev.biochem.75.101304.123901 16756495 10.1146/annurev. biochem.75.101304.123901 1:CAS:528:DC%2BD28XosVKhs70%3D
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366. doi: 10.1146/annurev.biochem.75. 101304.123901
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • 10.1073/pnas.96.18.9989 10468546 10.1073/pnas.96.18.9989 1:CAS:528:DyaK1MXlvFehurk%3D
    • Koo EH, Lansbury PT Jr, Kelly JW (1999) Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc Natl Acad Sci USA 96:9989-9990. doi: 10.1073/pnas.96.18.9989
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury, Jr.P.T.2    Kelly, J.W.3
  • 3
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models of amyloid fibril structure
    • 10.1016/j.sbi.2006.03.007 16563741 10.1016/j.sbi.2006.03.007 1:CAS:528:DC%2BD28Xjs1Grsbk%3D
    • Nelson R, Eisenberg D (2006) Recent atomic models of amyloid fibril structure. Curr Opin Struct Biol 16:260-265. doi: 10.1016/j.sbi.2006.03.007
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 4
    • 77957782470 scopus 로고    scopus 로고
    • Biology of amyloid: Structure, function, and regulation
    • 10.1016/j.str.2010.08.009 20947013 10.1016/j.str.2010.08.009 1:CAS:528:DC%2BC3cXhtlSntbbP
    • Greenwald J, Riek R (2010) Biology of amyloid: structure, function, and regulation. Structure 18:1244-1260. doi: 10.1016/j.str.2010.08.009
    • (2010) Structure , vol.18 , pp. 1244-1260
    • Greenwald, J.1    Riek, R.2
  • 5
    • 77956470750 scopus 로고    scopus 로고
    • Alzheimer disease
    • 10.1016/j.disamonth.2010.06.001 20831921 10.1016/j.disamonth.2010.06.001
    • Castellani RJ, Rolston RK, Smith MA (2010) Alzheimer disease. Dis Mon 56:484-546. doi: 10.1016/j.disamonth.2010.06.001
    • (2010) Dis Mon , vol.56 , pp. 484-546
    • Castellani, R.J.1    Rolston, R.K.2    Smith, M.A.3
  • 6
    • 47749126515 scopus 로고    scopus 로고
    • Why neurodegenerative diseases are progressive: Uncontrolled inflammation drives disease progression
    • 10.1016/j.it.2008.05.002 18599350 10.1016/j.it.2008.05.002 1:CAS:528:DC%2BD1cXptVCit7w%3D
    • Gao HM, Hong JS (2008) Why neurodegenerative diseases are progressive: uncontrolled inflammation drives disease progression. Trends Immunol 29:357-365. doi: 10.1016/j.it.2008.05.002
    • (2008) Trends Immunol , vol.29 , pp. 357-365
    • Gao, H.M.1    Hong, J.S.2
  • 7
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • 10.1038/ni.1636 18604209 10.1038/ni.1636 1:CAS:528:DC%2BD1cXoslCmu74%3D
    • Halle A, et al. (2008) The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol 9:857-865. doi: 10.1038/ni.1636
    • (2008) Nat Immunol , vol.9 , pp. 857-865
    • Halle, A.1
  • 8
    • 20144389524 scopus 로고    scopus 로고
    • Aggregated alpha-synuclein activates microglia: A process leading to disease progression in Parkinson's disease
    • 10.1096/fj.04-2751com 15791003 10.1096/fj.04-2751com 1:CAS:528: DC%2BD2MXjtFaqsrc%3D
    • Zhang W, et al. (2005) Aggregated alpha-synuclein activates microglia: a process leading to disease progression in Parkinson's disease. FASEB J 19:533-542. doi: 10.1096/fj.04-2751com
    • (2005) FASEB J , vol.19 , pp. 533-542
    • Zhang, W.1
  • 9
    • 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
    • 10.1038/ni.1935 20835230 10.1038/ni.1935 1:CAS:528:DC%2BC3cXhtFCnsbzF
    • Masters SL, et al. (2010) Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1beta in type 2 diabetes. Nat Immunol 11:897-904. doi: 10.1038/ni.1935
    • (2010) Nat Immunol , vol.11 , pp. 897-904
    • Masters, S.L.1
  • 10
    • 0011742009 scopus 로고    scopus 로고
    • Oppenheim JJ, Feldman M (eds) Academic Press, London doi: 10.1006/rwcy.2000.04004. ftp://195.214.211.1/books /DVD-022/DinarcIIo-C.-IL- 1b-%282000%29%28en%29%2824s%29.pdf
    • Dinarello CA (2001) IL-Iβ, in the cytokine reference. Oppenheim JJ, Feldman M (eds) Academic Press, London, p 351. doi: 10.1006/rwcy.2000.04004. ftp://195.214.211.1/books/DVD-022/DinarcIIo-C.-IL-1b- %282000%29%28en%29%2824s%29.pdf
    • (2001) IL-Iβ, the Cytokine Reference , pp. 351
    • Dinarello, C.A.1
  • 11
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • 10.1016/j.cell.2010.01.022 20303872 10.1016/j.cell.2010.01.022 1:CAS:528:DC%2BC3cXlsVSgu74%3D
    • Takeuchi O, Akira S (2010) Pattern recognition receptors and inflammation. Cell 140:805-820. doi: 10.1016/j.cell.2010.01.022
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 12
    • 79951578449 scopus 로고    scopus 로고
    • Inflammasomes: Current understanding and open questions
    • 10.1007/s00018-010-0567-4 21072676 10.1007/s00018-010-0567-4 1:CAS:528:DC%2BC3MXhvVWhurY%3D
    • Bauernfeind F, et al. (2011) Inflammasomes: current understanding and open questions. Cell Mol Life Sci 68:765-783. doi: 10.1007/s00018-010-0567-4
    • (2011) Cell Mol Life Sci , vol.68 , pp. 765-783
    • Bauernfeind, F.1
  • 13
    • 77955649302 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1-induced IL-1beta accelerates ALS pathogenesis
    • 10.1073/pnas.1002396107 20616033 10.1073/pnas.1002396107 1:CAS:528:DC%2BC3cXpsVCrsb0%3D
    • Meissner F, Molawi K, Zychlinsky A (2010) Mutant superoxide dismutase 1-induced IL-1beta accelerates ALS pathogenesis. Proc Natl Acad Sci USA 107:13046-13050. doi: 10.1073/pnas.1002396107
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13046-13050
    • Meissner, F.1    Molawi, K.2    Zychlinsky, A.3
  • 14
    • 80052650475 scopus 로고    scopus 로고
    • IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction
    • 10.4049/jimmunol.1002854 21813778 10.4049/jimmunol.1002854 1:CAS:528:DC%2BC3MXhtVGmsbzF
    • Westwell-Roper C, et al. (2011) IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction. J Immunol 187:2755-2765. doi: 10.4049/jimmunol.1002854
    • (2011) J Immunol , vol.187 , pp. 2755-2765
    • Westwell-Roper, C.1
  • 15
    • 33644944847 scopus 로고    scopus 로고
    • Lysozyme amyloidosis: Report of 4 cases and a review of the literature
    • 10.1097/01.md.0000200467.51816.6d 10.1097/01.md.0000200467.51816.6d
    • Granel B, et al. (2006) Lysozyme amyloidosis: report of 4 cases and a review of the literature. Medicine (Baltimore) 85:66-73. doi: 10.1097/01.md.0000200467.51816.6d
    • (2006) Medicine (Baltimore) , vol.85 , pp. 66-73
    • Granel, B.1
  • 16
    • 33749831531 scopus 로고    scopus 로고
    • Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants
    • 10.1021/ar050070g 16981676 10.1021/ar050070g 1:CAS:528: DC%2BD28XntVWrsLY%3D
    • Dumoulin M, Kumita JR, Dobson CM (2006) Normal and aberrant biological self-assembly: insights from studies of human lysozyme and its amyloidogenic variants. Acc Chem Res 39:603-610. doi: 10.1021/ar050070g
    • (2006) Acc Chem Res , vol.39 , pp. 603-610
    • Dumoulin, M.1    Kumita, J.R.2    Dobson, C.M.3
  • 17
    • 24344480244 scopus 로고    scopus 로고
    • Rationalising lysozyme amyloidosis: Insights from the structure and solution dynamics of T70N lysozyme
    • 10.1016/j.jmb.2005.07.040 16126226 10.1016/j.jmb.2005.07.040 1:CAS:528:DC%2BD2MXhtVWit7jE
    • Johnson RJ, et al. (2005) Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme. J Mol Biol 352:823-836. doi: 10.1016/j.jmb.2005.07.040
    • (2005) J Mol Biol , vol.352 , pp. 823-836
    • Johnson, R.J.1
  • 18
    • 33750353368 scopus 로고    scopus 로고
    • Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes
    • 10.1021/bi0610653 17042499 10.1021/bi0610653 1:CAS:528: DC%2BD28Xps1Git78%3D
    • Calamai M, et al. (2006) Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes. Biochemistry 45:12806-12815. doi: 10.1021/bi0610653
    • (2006) Biochemistry , vol.45 , pp. 12806-12815
    • Calamai, M.1
  • 19
    • 48749127416 scopus 로고    scopus 로고
    • Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa
    • 18606678 1:CAS:528:DC%2BD1cXotF2rsbY%3D
    • Walsh C, et al. (2008) Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa. J Immunol 181:1245-1254
    • (2008) J Immunol , vol.181 , pp. 1245-1254
    • Walsh, C.1
  • 20
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • 10.1016/S0304-4157(99)00004-0 10393271 10.1016/S0304-4157(99)00004-0 1:CAS:528:DyaK1MXks1Cks7s%3D
    • Goormaghtigh E, Raussens V, Ruysschaert JM (1999) Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim Biophys Acta 1422:105-185. doi: 10.1016/S0304-4157(99)00004-0
    • (1999) Biochim Biophys Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.M.3
  • 21
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films
    • 10.1111/j.1432-1033.1990.tb19354.x 2226461 10.1111/j.1432-1033.1990. tb19354.x 1:CAS:528:DyaK3cXmt1Ons7k%3D
    • Goormaghtigh E, Cabiaux V, Ruysschaert JM (1990) Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur J Biochem 193:409-420. doi: 10.1111/j.1432-1033.1990.tb19354.x
    • (1990) Eur J Biochem , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 22
    • 0042467574 scopus 로고    scopus 로고
    • A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme
    • 10.1038/nature01870 12917687 10.1038/nature01870 1:CAS:528: DC%2BD3sXmt1antrc%3D
    • Dumoulin M, et al. (2003) A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme. Nature 424:783-788. doi: 10.1038/nature01870
    • (2003) Nature , vol.424 , pp. 783-788
    • Dumoulin, M.1
  • 23
    • 77957243833 scopus 로고    scopus 로고
    • The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity
    • 10.1016/j.jmb.2010.07.005 20624399 10.1016/j.jmb.2010.07.005 1:CAS:528:DC%2BC3cXht1Cgu7vE
    • Mossuto MF, et al. (2010) The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity. J Mol Biol 402:783-796. doi: 10.1016/j.jmb.2010.07.005
    • (2010) J Mol Biol , vol.402 , pp. 783-796
    • Mossuto, M.F.1
  • 24
    • 43449118401 scopus 로고    scopus 로고
    • Time-resolved infrared spectroscopy of pH-induced aggregation of the Alzheimer Abeta(1-28) peptide
    • 10.1016/j.jmb.2008.04.014 18462754 10.1016/j.jmb.2008.04.014 1:CAS:528:DC%2BD1cXmtVSis7g%3D
    • Peralvarez-Marin A, Barth A, Graslund A (2008) Time-resolved infrared spectroscopy of pH-induced aggregation of the Alzheimer Abeta(1-28) peptide. J Mol Biol 379:589-596. doi: 10.1016/j.jmb.2008.04.014
    • (2008) J Mol Biol , vol.379 , pp. 589-596
    • Peralvarez-Marin, A.1    Barth, A.2    Graslund, A.3
  • 25
    • 0017250407 scopus 로고
    • Infrared spectra and resonance interaction of amide-I vibration of the parallel-chain pleated sheets
    • 10.1002/bip.1976.360150403 1252598 10.1002/bip.1976.360150403 1:CAS:528:DyaE28Xhs1Giur0%3D
    • Chirgadze YN, Nevskaya NA (1976) Infrared spectra and resonance interaction of amide-I vibration of the parallel-chain pleated sheets. Biopolymers 15:627-636. doi: 10.1002/bip.1976.360150403
    • (1976) Biopolymers , vol.15 , pp. 627-636
    • Chirgadze, Y.N.1    Nevskaya, N.A.2
  • 26
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds
    • 10.1007/978-1-4615-1863-1 7855877 10.1007/978-1-4615-1863-1-8 1:CAS:528:DyaK2MXmvVWlu70%3D
    • Goormaghtigh E, Cabiaux V, Ruysschaert JM (1994) Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds. Subcell Biochem 23:329-362. doi: 10.1007/978-1-4615-1863-1
    • (1994) Subcell Biochem , vol.23 , pp. 329-362
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 27
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils
    • 10.1073/pnas.230315097 11069287 10.1073/pnas.230315097 1:CAS:528:DC%2BD3cXosVKqtL8%3D
    • Antzutkin ON, et al. (2000) Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci USA 97:13045-13050. doi: 10.1073/pnas.230315097
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13045-13050
    • Antzutkin, O.N.1
  • 28
    • 57649128935 scopus 로고    scopus 로고
    • Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: Molecular insights from electron paramagnetic resonance spectroscopy
    • 10.1017/S0033583508004733 19079806 10.1017/S0033583508004733 1:CAS:528:DC%2BD1cXhsVyru7%2FL
    • Margittai M, Langen R (2008) Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy. Q Rev Biophys 41:265-297. doi: 10.1017/S0033583508004733
    • (2008) Q Rev Biophys , vol.41 , pp. 265-297
    • Margittai, M.1    Langen, R.2
  • 29
    • 84860110592 scopus 로고    scopus 로고
    • Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure
    • 10.1042/BJ20111924 22316405 10.1042/BJ20111924 1:CAS:528: DC%2BC38Xls1Shtr4%3D
    • Celej MS, et al. (2012) Toxic prefibrillar alpha-synuclein amyloid oligomers adopt a distinctive antiparallel beta-sheet structure. Biochem J 443:719-726. doi: 10.1042/BJ20111924
    • (2012) Biochem J , vol.443 , pp. 719-726
    • Celej, M.S.1
  • 30
    • 69249239132 scopus 로고    scopus 로고
    • Antiparallel beta-sheet: A signature structure of the oligomeric amyloid beta-peptide
    • 10.1042/BJ20090379 19435461 10.1042/BJ20090379 1:CAS:528: DC%2BD1MXosV2hu74%3D
    • Cerf E, et al. (2009) Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide. Biochem J 421:415-423. doi: 10.1042/BJ20090379
    • (2009) Biochem J , vol.421 , pp. 415-423
    • Cerf, E.1
  • 31
    • 0017288712 scopus 로고
    • Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet
    • 10.1002/bip.1976.360150402 1252597 10.1002/bip.1976.360150402 1:CAS:528:DyaE28XhsFSqtbc%3D
    • Chirgadze YN, Nevskaya NA (1976) Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet. Biopolymers 15:607-625. doi: 10.1002/bip.1976.360150402
    • (1976) Biopolymers , vol.15 , pp. 607-625
    • Chirgadze, Y.N.1    Nevskaya, N.A.2
  • 32
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    • 10.1016/j.bbapap.2010.04.001 20399286 10.1016/j.bbapap.2010.04.001 1:CAS:528:DC%2BC3cXmsVGlsbs%3D
    • Biancalana M, Koide S (2010) Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochim Biophys Acta 1804:1405-1412. doi: 10.1016/j.bbapap.2010.04.001
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 33
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • 10.1186/1750-1326-2-18 17897471 10.1186/1750-1326-2-18
    • Kayed R, et al. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2:18. doi: 10.1186/1750-1326-2-18
    • (2007) Mol Neurodegener , vol.2 , pp. 18
    • Kayed, R.1
  • 34
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • 10.1126/science.1079469 12702875 10.1126/science.1079469 1:CAS:528:DC%2BD3sXivFyms7k%3D
    • Kayed R, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486-489. doi: 10.1126/science.1079469
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1
  • 35
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression
    • 10.4049/jimmunol.0901363 19570822 10.4049/jimmunol.0901363 1:CAS:528:DC%2BD1MXotFWgt78%3D
    • Bauernfeind FG, et al. (2009) Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J Immunol 183:787-791. doi: 10.4049/jimmunol. 0901363
    • (2009) J Immunol , vol.183 , pp. 787-791
    • Bauernfeind, F.G.1
  • 36
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • 10.1038/nature04515 16407890 10.1038/nature04515 1:CAS:528: DC%2BD28XitFGitLs%3D
    • Mariathasan S, et al. (2006) Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440:228-232. doi: 10.1038/nature04515
    • (2006) Nature , vol.440 , pp. 228-232
    • Mariathasan, S.1
  • 37
    • 69549119940 scopus 로고    scopus 로고
    • Molecular mechanisms involved in inflammasome activation
    • 10.1016/j.tcb.2009.06.002 19716304 10.1016/j.tcb.2009.06.002 1:CAS:528:DC%2BD1MXhtV2lu7zP
    • Bryant C, Fitzgerald KA (2009) Molecular mechanisms involved in inflammasome activation. Trends Cell Biol 19:455-464. doi: 10.1016/j.tcb.2009. 06.002
    • (2009) Trends Cell Biol , vol.19 , pp. 455-464
    • Bryant, C.1    Fitzgerald, K.A.2
  • 38
    • 34548027736 scopus 로고    scopus 로고
    • Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
    • 10.1038/sj.cdd.4402195 17599094 10.1038/sj.cdd.4402195 1:CAS:528:DC%2BD2sXptFymurg%3D
    • Petrilli V, et al. (2007) Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ 14:1583-1589. doi: 10.1038/sj.cdd.4402195
    • (2007) Cell Death Differ , vol.14 , pp. 1583-1589
    • Petrilli, V.1
  • 39
    • 77749304033 scopus 로고    scopus 로고
    • Sterile inflammatory responses mediated by the NLRP3 inflammasome
    • 10.1002/eji.200940207 20201012 10.1002/eji.200940207 1:CAS:528: DC%2BC3cXjtVWku7o%3D
    • Cassel SL, Sutterwala FS (2010) Sterile inflammatory responses mediated by the NLRP3 inflammasome. Eur J Immunol 40:607-611. doi: 10.1002/eji.200940207
    • (2010) Eur J Immunol , vol.40 , pp. 607-611
    • Cassel, S.L.1    Sutterwala, F.S.2
  • 40
    • 77951240589 scopus 로고    scopus 로고
    • Anti-inflammatory compounds parthenolide and Bay 11-7082 are direct inhibitors of the inflammasome
    • 10.1074/jbc.M109.082305 20093358 10.1074/jbc.M109.082305 1:CAS:528:DC%2BC3cXjsFehtLk%3D
    • Juliana C, et al. (2010) Anti-inflammatory compounds parthenolide and Bay 11-7082 are direct inhibitors of the inflammasome. J Biol Chem 285:9792-9802. doi: 10.1074/jbc.M109.082305
    • (2010) J Biol Chem , vol.285 , pp. 9792-9802
    • Juliana, C.1
  • 41
    • 33749065328 scopus 로고    scopus 로고
    • Roles for accessory molecules in microbial recognition by Toll-like receptors
    • 10.1179/096805106X118807 16953972 10.1179/096805106X118807 1:CAS:528:DC%2BD28XovVWmtr4%3D
    • Miyake K (2006) Roles for accessory molecules in microbial recognition by Toll-like receptors. J Endotoxin Res 12:195-204. doi: 10.1179/096805106X118807
    • (2006) J Endotoxin Res , vol.12 , pp. 195-204
    • Miyake, K.1
  • 42
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • 10.1016/j.cell.2010.01.040 20303873 10.1016/j.cell.2010.01.040 1:CAS:528:DC%2BC3cXlsVSgu78%3D
    • Schroder K, Tschopp J (2010) The inflammasomes. Cell 140:821-832. doi: 10.1016/j.cell.2010.01.040
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 43
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • 10.1038/ni.1631 18604214 10.1038/ni.1631 1:CAS:528:DC%2BD1cXoslCmurs%3D
    • Hornung V, et al. (2008) Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol 9:847-856. doi: 10.1038/ni.1631
    • (2008) Nat Immunol , vol.9 , pp. 847-856
    • Hornung, V.1
  • 44
    • 77749304032 scopus 로고    scopus 로고
    • Signaling by ROS drives inflammasome activation
    • 10.1002/eji.200940168 20201014 10.1002/eji.200940168 1:CAS:528: DC%2BC3cXjtVWktbc%3D
    • Martinon F (2010) Signaling by ROS drives inflammasome activation. Eur J Immunol 40:616-619. doi: 10.1002/eji.200940168
    • (2010) Eur J Immunol , vol.40 , pp. 616-619
    • Martinon, F.1
  • 45
    • 77954382754 scopus 로고    scopus 로고
    • The effect of surface modification of amorphous silica particles on NLRP3 inflammasome mediated IL-1beta production, ROS production and endosomal rupture
    • 10.1016/j.biomaterials.2010.05.036 20561679 10.1016/j.biomaterials.2010. 05.036 1:CAS:528:DC%2BC3cXosF2iu7o%3D
    • Morishige T, et al. (2010) The effect of surface modification of amorphous silica particles on NLRP3 inflammasome mediated IL-1beta production, ROS production and endosomal rupture. Biomaterials 31:6833-6842. doi: 10.1016/j.biomaterials.2010.05.036
    • (2010) Biomaterials , vol.31 , pp. 6833-6842
    • Morishige, T.1
  • 46
    • 43249125839 scopus 로고    scopus 로고
    • Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
    • 10.1126/science.1156995 18403674 10.1126/science.1156995 1:CAS:528:DC%2BD1cXltFyis7c%3D
    • Dostert C, et al. (2008) Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 320:674-677. doi: 10.1126/science.1156995
    • (2008) Science , vol.320 , pp. 674-677
    • Dostert, C.1
  • 47
    • 44649150510 scopus 로고    scopus 로고
    • Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus
    • 10.1155/2008/421287 18483616 10.1155/2008/421287
    • Khemtemourian L, Killian JA, Hoppener JW, Engel MF (2008) Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus. Exp Diabetes Res 2008:421287. doi: 10.1155/2008/421287
    • (2008) Exp Diabetes Res , vol.2008 , pp. 421287
    • Khemtemourian, L.1    Killian, J.A.2    Hoppener, J.W.3    Engel, M.F.4
  • 48
    • 79953720607 scopus 로고    scopus 로고
    • Heterogeneous amylin fibril growth mechanisms imaged by total internal reflection fluorescence microscopy
    • 10.1021/bi101908m 21391619 10.1021/bi101908m 1:CAS:528: DC%2BC3MXjsVygt7o%3D
    • Patil SM, Mehta A, Jha S, Alexandrescu AT (2011) Heterogeneous amylin fibril growth mechanisms imaged by total internal reflection fluorescence microscopy. Biochemistry 50:2808-2819. doi: 10.1021/bi101908m
    • (2011) Biochemistry , vol.50 , pp. 2808-2819
    • Patil, S.M.1    Mehta, A.2    Jha, S.3    Alexandrescu, A.T.4
  • 49
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • 10.1146/annurev.biophys.050708.133622 19416063 10.1146/annurev.biophys. 050708.133622 1:CAS:528:DC%2BD1MXntlentL8%3D
    • Hebda JA, Miranker AD (2009) The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes. Annu Rev Biophys 38:125-152. doi: 10.1146/annurev.biophys.050708.133622
    • (2009) Annu Rev Biophys , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 50
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • 10.1016/j.jmb.2004.06.086 15321714 10.1016/j.jmb.2004.06.086 1:CAS:528:DC%2BD2cXmsVCrtL4%3D
    • Knight JD, Miranker AD (2004) Phospholipid catalysis of diabetic amyloid assembly. J Mol Biol 341:1175-1187. doi: 10.1016/j.jmb.2004.06.086
    • (2004) J Mol Biol , vol.341 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 51
    • 0036468673 scopus 로고    scopus 로고
    • Role of Escherichia coli curli operons in directing amyloid fiber formation
    • 10.1126/science.1067484 11823641 10.1126/science.1067484 1:CAS:528:DC%2BD38XhtFaktbc%3D
    • Chapman MR, et al. (2002) Role of Escherichia coli curli operons in directing amyloid fiber formation. Science 295:851-855. doi: 10.1126/science.1067484
    • (2002) Science , vol.295 , pp. 851-855
    • Chapman, M.R.1
  • 52
    • 67749116427 scopus 로고    scopus 로고
    • Responses to amyloids of microbial and host origin are mediated through toll-like receptor 2
    • 10.1016/j.chom.2009.05.020 19616765 10.1016/j.chom.2009.05.020 1:CAS:528:DC%2BD1MXhsVChsLzN
    • Tukel C, et al. (2009) Responses to amyloids of microbial and host origin are mediated through toll-like receptor 2. Cell Host Microbe 6:45-53. doi: 10.1016/j.chom.2009.05.020
    • (2009) Cell Host Microbe , vol.6 , pp. 45-53
    • Tukel, C.1
  • 53
    • 37349069999 scopus 로고    scopus 로고
    • Toll-like receptors 2 and 4 mediate Abeta(1-42) activation of the innate immune response in a human monocytic cell line
    • 10.1111/j.1471-4159.2007.05001.x 17986235 1:CAS:528:DC%2BD1cXhtlSqs7c%3D
    • Udan ML, Ajit D, Crouse NR, Nichols MR (2008) Toll-like receptors 2 and 4 mediate Abeta(1-42) activation of the innate immune response in a human monocytic cell line. J Neurochem 104:524-533. doi: 10.1111/j.1471-4159.2007. 05001.x
    • (2008) J Neurochem , vol.104 , pp. 524-533
    • Udan, M.L.1    Ajit, D.2    Crouse, N.R.3    Nichols, M.R.4
  • 54
    • 84863523165 scopus 로고    scopus 로고
    • Lateral clustering of TLR3: DsRNA signaling units revealed by TLR3ecd:3Fabs quaternary structure
    • 10.1016/j.jmb.2012.05.006
    • Luo J, et al. (2012) Lateral clustering of TLR3:dsRNA signaling units revealed by TLR3ecd:3Fabs quaternary structure. J Mol Biol doi. doi: 10.1016/j.jmb.2012.05.006
    • (2012) J Mol Biol Doi
    • Luo, J.1
  • 55
    • 70450222517 scopus 로고    scopus 로고
    • Endosomal damage and TLR2 mediated inflammasome activation by alkane particles in the generation of aseptic osteolysis
    • 10.1016/j.molimm.2009.09.023 19804908 10.1016/j.molimm.2009.09.023 1:CAS:528:DC%2BD1MXhsVyjurvO
    • Maitra R, et al. (2009) Endosomal damage and TLR2 mediated inflammasome activation by alkane particles in the generation of aseptic osteolysis. Mol Immunol 47:175-184. doi: 10.1016/j.molimm.2009.09.023
    • (2009) Mol Immunol , vol.47 , pp. 175-184
    • Maitra, R.1
  • 56
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • 10.1016/S0968-0004(99)01445-0 10470028 10.1016/S0968-0004(99)01445-0 1:CAS:528:DyaK1MXls1ygtLg%3D
    • Dobson CM (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24:329-332. doi: 10.1016/S0968-0004(99)01445-0
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 57
    • 15944405779 scopus 로고    scopus 로고
    • Amyloids - A functional coat for microorganisms
    • 10.1038/nrmicro1127 15806095 10.1038/nrmicro1127 1:CAS:528: DC%2BD2MXivVGmu7w%3D
    • Gebbink MF, Claessen D, Bouma B, Dijkhuizen L, Wosten HA (2005) Amyloids - a functional coat for microorganisms. Nat Rev Microbiol 3:333-341. doi: 10.1038/nrmicro1127
    • (2005) Nat Rev Microbiol , vol.3 , pp. 333-341
    • Gebbink, M.F.1    Claessen, D.2    Bouma, B.3    Dijkhuizen, L.4    Wosten, H.A.5


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