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Volumn 36, Issue 3, 2012, Pages 337-347

Structure and Functional Characterization of the RNA-Binding Element of the NLRX1 Innate Immune Modulator

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MITOCHONDRIAL PROTEIN; NUCLEOTIDE BINDING DOMAIN AND LEUCINE RICH REPEATCONTAINING PROTEIN 1; UNCLASSIFIED DRUG;

EID: 84858762861     PISSN: 10747613     EISSN: 10974180     Source Type: Journal    
DOI: 10.1016/j.immuni.2011.12.018     Document Type: Article
Times cited : (75)

References (50)
  • 1
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S., Uematsu S., Takeuchi O. Pathogen recognition and innate immunity. Cell 2006, 124:783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 2
    • 28444488986 scopus 로고    scopus 로고
    • Update on the domain architectures of NLRs and R proteins
    • Albrecht M., Takken F.L. Update on the domain architectures of NLRs and R proteins. Biochem. Biophys. Res. Commun. 2006, 339:459-462.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 459-462
    • Albrecht, M.1    Takken, F.L.2
  • 8
    • 79953890803 scopus 로고    scopus 로고
    • The structural biology of Toll-like receptors
    • Botos I., Segal D.M., Davies D.R. The structural biology of Toll-like receptors. Structure 2011, 19:447-459.
    • (2011) Structure , vol.19 , pp. 447-459
    • Botos, I.1    Segal, D.M.2    Davies, D.R.3
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 1994, 50:760-763. Collaborative Computational Project, Number 4.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 14
    • 33846272114 scopus 로고    scopus 로고
    • Plant NBS-LRR proteins in pathogen sensing and host defense
    • DeYoung B.J., Innes R.W. Plant NBS-LRR proteins in pathogen sensing and host defense. Nat. Immunol. 2006, 7:1243-1249.
    • (2006) Nat. Immunol. , vol.7 , pp. 1243-1249
    • DeYoung, B.J.1    Innes, R.W.2
  • 15
    • 79952362007 scopus 로고    scopus 로고
    • NLRP1 influences the systemic sclerosis phenotype: a new clue for the contribution of innate immunity in systemic sclerosis-related fibrosing alveolitis pathogenesis
    • Dieudé P., Guedj M., Wipff J., Ruiz B., Riemekasten G., Airo P., Melchers I., Hachulla E., Cerinic M.M., Diot E., et al. NLRP1 influences the systemic sclerosis phenotype: a new clue for the contribution of innate immunity in systemic sclerosis-related fibrosing alveolitis pathogenesis. Ann. Rheum. Dis. 2011, 70:668-674.
    • (2011) Ann. Rheum. Dis. , vol.70 , pp. 668-674
    • Dieudé, P.1    Guedj, M.2    Wipff, J.3    Ruiz, B.4    Riemekasten, G.5    Airo, P.6    Melchers, I.7    Hachulla, E.8    Cerinic, M.M.9    Diot, E.10
  • 19
    • 58049200723 scopus 로고    scopus 로고
    • Function of Nod-like receptors in microbial recognition and host defense
    • Franchi L., Warner N., Viani K., Nuñez G. Function of Nod-like receptors in microbial recognition and host defense. Immunol. Rev. 2009, 227:106-128.
    • (2009) Immunol. Rev. , vol.227 , pp. 106-128
    • Franchi, L.1    Warner, N.2    Viani, K.3    Nuñez, G.4
  • 21
    • 0037108346 scopus 로고    scopus 로고
    • Cutting edge: CATERPILLER: a large family of mammalian genes containing CARD, pyrin, nucleotide-binding, and leucine-rich repeat domains
    • Harton J.A., Linhoff M.W., Zhang J., Ting J.P. Cutting edge: CATERPILLER: a large family of mammalian genes containing CARD, pyrin, nucleotide-binding, and leucine-rich repeat domains. J. Immunol. 2002, 169:4088-4093.
    • (2002) J. Immunol. , vol.169 , pp. 4088-4093
    • Harton, J.A.1    Linhoff, M.W.2    Zhang, J.3    Ting, J.P.4
  • 22
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 1991, 254:51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 25
    • 0038624558 scopus 로고    scopus 로고
    • NODs: intracellular proteins involved in inflammation and apoptosis
    • Inohara N., Nuñez G. NODs: intracellular proteins involved in inflammation and apoptosis. Nat. Rev. Immunol. 2003, 3:371-382.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 371-382
    • Inohara, N.1    Nuñez, G.2
  • 27
    • 17644366913 scopus 로고    scopus 로고
    • NOD-LRR proteins: role in host-microbial interactions and inflammatory disease
    • Inohara N., Chamaillard M., McDonald C., Nuñez G. NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu. Rev. Biochem. 2005, 74:355-383.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 355-383
    • Inohara, N.1    Chamaillard, M.2    McDonald, C.3    Nuñez, G.4
  • 28
    • 0035234835 scopus 로고    scopus 로고
    • Crystallization and crystal structure determination of ribonuclease A-ribonuclease inhibitor protein complex
    • Kobe B. Crystallization and crystal structure determination of ribonuclease A-ribonuclease inhibitor protein complex. Methods Mol. Biol. 2001, 160:201-211.
    • (2001) Methods Mol. Biol. , vol.160 , pp. 201-211
    • Kobe, B.1
  • 29
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe B., Deisenhofer J. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 1993, 366:751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 30
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • Kobe B., Deisenhofer J. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature 1995, 374:183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 31
    • 0030596012 scopus 로고    scopus 로고
    • Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A
    • Kobe B., Deisenhofer J. Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A. J. Mol. Biol. 1996, 264:1028-1043.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1028-1043
    • Kobe, B.1    Deisenhofer, J.2
  • 32
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B., Kajava A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 2001, 11:725-732.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 35
    • 77957588986 scopus 로고    scopus 로고
    • Association of NOD1 (CARD4) insertion/deletion polymorphism with susceptibility to IBD: a meta-analysis
    • Lu W.G., Zou Y.F., Feng X.L., Yuan F.L., Gu Y.L., Li X., Li C.W., Jin C., Li J.P. Association of NOD1 (CARD4) insertion/deletion polymorphism with susceptibility to IBD: a meta-analysis. World J. Gastroenterol. 2010, 16:4348-4356.
    • (2010) World J. Gastroenterol. , vol.16 , pp. 4348-4356
    • Lu, W.G.1    Zou, Y.F.2    Feng, X.L.3    Yuan, F.L.4    Gu, Y.L.5    Li, X.6    Li, C.W.7    Jin, C.8    Li, J.P.9
  • 36
    • 0029887308 scopus 로고    scopus 로고
    • Fluorescence polarization analysis of protein-DNA and protein-protein interactions
    • Lundblad J.R., Laurance M., Goodman R.H. Fluorescence polarization analysis of protein-DNA and protein-protein interactions. Mol. Endocrinol. 1996, 10:607-612.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 607-612
    • Lundblad, J.R.1    Laurance, M.2    Goodman, R.H.3
  • 37
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov R. Recognition of microorganisms and activation of the immune response. Nature 2007, 449:819-826.
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 38
    • 36248971702 scopus 로고    scopus 로고
    • NOD1 gene E266K polymorphism is associated with disease susceptibility but not with disease phenotype or NOD2/CARD15 in Hungarian patients with Crohn's disease
    • Hungarian IBD Study Group
    • Molnar T., Hofner P., Nagy F., Lakatos P.L., Fischer S., Lakatos L., Kovacs A., Altorjay I., Papp M., Palatka K., et al. NOD1 gene E266K polymorphism is associated with disease susceptibility but not with disease phenotype or NOD2/CARD15 in Hungarian patients with Crohn's disease. Dig. Liver Dis. 2007, 39:1064-1070. Hungarian IBD Study Group.
    • (2007) Dig. Liver Dis. , vol.39 , pp. 1064-1070
    • Molnar, T.1    Hofner, P.2    Nagy, F.3    Lakatos, P.L.4    Fischer, S.5    Lakatos, L.6    Kovacs, A.7    Altorjay, I.8    Papp, M.9    Palatka, K.10
  • 40
    • 79952361297 scopus 로고    scopus 로고
    • The missense variation Q705K in CIAS1/NALP3/NLRP3 gene and an NLRP1 haplotype are associated with celiac disease
    • Pontillo A., Vendramin A., Catamo E., Fabris A., Crovella S. The missense variation Q705K in CIAS1/NALP3/NLRP3 gene and an NLRP1 haplotype are associated with celiac disease. Am. J. Gastroenterol. 2011, 106:539-544.
    • (2011) Am. J. Gastroenterol. , vol.106 , pp. 539-544
    • Pontillo, A.1    Vendramin, A.2    Catamo, E.3    Fabris, A.4    Crovella, S.5
  • 42
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl S.J., Li W., Chao Y., Schwarzenbacher R., Shi Y. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 2005, 434:926-933.
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 45
    • 40249111682 scopus 로고    scopus 로고
    • NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-kappaB and JNK pathways by inducing reactive oxygen species production
    • Tattoli I., Carneiro L.A., Jéhanno M., Magalhaes J.G., Shu Y., Philpott D.J., Arnoult D., Girardin S.E. NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-kappaB and JNK pathways by inducing reactive oxygen species production. EMBO Rep. 2008, 9:293-300.
    • (2008) EMBO Rep. , vol.9 , pp. 293-300
    • Tattoli, I.1    Carneiro, L.A.2    Jéhanno, M.3    Magalhaes, J.G.4    Shu, Y.5    Philpott, D.J.6    Arnoult, D.7    Girardin, S.E.8
  • 47
    • 17644396670 scopus 로고    scopus 로고
    • CATERPILLER: a novel gene family important in immunity, cell death, and diseases
    • Ting J.P., Davis B.K. CATERPILLER: a novel gene family important in immunity, cell death, and diseases. Annu. Rev. Immunol. 2005, 23:387-414.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 387-414
    • Ting, J.P.1    Davis, B.K.2
  • 50
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein links oxidative stress to inflammasome activation
    • Zhou R., Tardivel A., Thorens B., Choi I., Tschopp J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat. Immunol. 2010, 11:136-140.
    • (2010) Nat. Immunol. , vol.11 , pp. 136-140
    • Zhou, R.1    Tardivel, A.2    Thorens, B.3    Choi, I.4    Tschopp, J.5


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