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Volumn 22, Issue 12, 2014, Pages 1722-1734

Structural and dynamics aspects of ASC speck assembly

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; INFLAMMASOME; INTERLEUKIN 1BETA CONVERTING ENZYME; PYCARD PROTEIN, HUMAN;

EID: 84914132282     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.09.011     Document Type: Article
Times cited : (45)

References (53)
  • 1
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • I. Bahar, and A.J. Rader Coarse-grained normal mode analysis in structural biology Curr. Opin. Struct. Biol. 15 2005 586 592
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 2
    • 0000496772 scopus 로고    scopus 로고
    • Vibrational dynamics of folded proteins: Significance of slow and fast motions in relation to function and stability
    • I. Bahar, A.R. Atilgan, M.C. Demirel, and B. Erman Vibrational dynamics of folded proteins: significance of slow and fast motions in relation to function and stability Phys. Rev. Lett. 80 1998 2733
    • (1998) Phys. Rev. Lett. , vol.80 , pp. 2733
    • Bahar, I.1    Atilgan, A.R.2    Demirel, M.C.3    Erman, B.4
  • 4
    • 76849101228 scopus 로고    scopus 로고
    • CircStat: A MATLAB toolbox for circular statistics
    • P. Berens CircStat: a MATLAB toolbox for circular statistics J. Stat. Softw. 31 2009 1 21
    • (2009) J. Stat. Softw. , vol.31 , pp. 1-21
    • Berens, P.1
  • 6
    • 77955390094 scopus 로고    scopus 로고
    • Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
    • P. Broz, K. Newton, M. Lamkanfi, S. Mariathasan, V.M. Dixit, and D.M. Monack Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella J. Exp. Med. 207 2010 1745 1755
    • (2010) J. Exp. Med. , vol.207 , pp. 1745-1755
    • Broz, P.1    Newton, K.2    Lamkanfi, M.3    Mariathasan, S.4    Dixit, V.M.5    Monack, D.M.6
  • 7
    • 78650210802 scopus 로고    scopus 로고
    • Differential requirement for Caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing
    • P. Broz, J. von Moltke, J.W. Jones, R.E. Vance, and D.M. Monack Differential requirement for Caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing Cell Host Microbe 8 2010 471 483
    • (2010) Cell Host Microbe , vol.8 , pp. 471-483
    • Broz, P.1    Von Moltke, J.2    Jones, J.W.3    Vance, R.E.4    Monack, D.M.5
  • 8
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • X. Cai, J. Chen, H. Xu, S. Liu, Q.X. Jiang, R. Halfmann, and Z.J. Chen Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation Cell 156 2014 1207 1222
    • (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    Chen, Z.J.7
  • 11
    • 70450250064 scopus 로고    scopus 로고
    • Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC)
    • E. de Alba Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC) J. Biol. Chem. 284 2009 32932 32941
    • (2009) J. Biol. Chem. , vol.284 , pp. 32932-32941
    • De Alba, E.1
  • 12
    • 33749367332 scopus 로고    scopus 로고
    • Association of putative concave protein-binding sites with the fluctuation behavior of residues
    • A. Ertekin, R. Nussinov, and T. Haliloglu Association of putative concave protein-binding sites with the fluctuation behavior of residues Protein Sci. 15 2006 2265 2277
    • (2006) Protein Sci. , vol.15 , pp. 2265-2277
    • Ertekin, A.1    Nussinov, R.2    Haliloglu, T.3
  • 15
    • 61849151934 scopus 로고    scopus 로고
    • Analysis of correlations between energy and residue fluctuations in native proteins and determination of specific sites for binding
    • T. Haliloglu, and B. Erman Analysis of correlations between energy and residue fluctuations in native proteins and determination of specific sites for binding Phys. Rev. Lett. 102 2009 088103
    • (2009) Phys. Rev. Lett. , vol.102 , pp. 088103
    • Haliloglu, T.1    Erman, B.2
  • 17
    • 44949215646 scopus 로고    scopus 로고
    • Prediction of binding sites in receptor-ligand complexes with the Gaussian Network Model
    • 228102-228102
    • T. Haliloglu, E. Seyrek, and B. Erman Prediction of binding sites in receptor-ligand complexes with the Gaussian Network Model Phys. Rev. Lett. 100 2008 228102-228102
    • (2008) Phys. Rev. Lett. , vol.100
    • Haliloglu, T.1    Seyrek, E.2    Erman, B.3
  • 18
    • 35048866000 scopus 로고    scopus 로고
    • Characterization of protein conformational states by normal-mode frequencies
    • B.A. Hall, S.L. Kaye, A. Pang, R. Perera, and P.C. Biggin Characterization of protein conformational states by normal-mode frequencies J. Am. Chem. Soc. 129 2007 11394 11401
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11394-11401
    • Hall, B.A.1    Kaye, S.L.2    Pang, A.3    Perera, R.4    Biggin, P.C.5
  • 19
    • 77749304034 scopus 로고    scopus 로고
    • Critical functions of priming and lysosomal damage for NLRP3 activation
    • V. Hornung, and E. Latz Critical functions of priming and lysosomal damage for NLRP3 activation Eur. J. Immunol. 40 2010 620 623
    • (2010) Eur. J. Immunol. , vol.40 , pp. 620-623
    • Hornung, V.1    Latz, E.2
  • 21
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • J.A. Johnston, C.L. Ward, and R.R. Kopito Aggresomes: a cellular response to misfolded proteins J. Cell Biol. 143 1998 1883 1898
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 24
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • M. Landau, I. Mayrose, Y. Rosenberg, F. Glaser, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures Nucleic Acids Res. 33 2005 W299 W302
    • (2005) Nucleic Acids Res. , vol.33 , pp. 299-W302
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7
  • 25
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • E. Latz, T.S. Xiao, and A. Stutz Activation and regulation of the inflammasomes Nat. Rev. Immunol. 13 2013 397 411
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 27
    • 0042386425 scopus 로고    scopus 로고
    • The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition
    • E. Liepinsh, R. Barbals, E. Dahl, A. Sharipo, E. Staub, and G. Otting The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition J. Mol. Biol. 332 2003 1155 1163
    • (2003) J. Mol. Biol. , vol.332 , pp. 1155-1163
    • Liepinsh, E.1    Barbals, R.2    Dahl, E.3    Sharipo, A.4    Staub, E.5    Otting, G.6
  • 28
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • S.C. Lin, Y.C. Lo, and H. Wu Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling Nature 465 2010 885 890
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 30
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: Consequences for binding affinity and allosteric effects
    • I. Luque, and E. Freire Structural stability of binding sites: consequences for binding affinity and allosteric effects Proteins Suppl 4 2000 63 71
    • (2000) Proteins , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 32
    • 0034804347 scopus 로고    scopus 로고
    • Pyrin N-terminal homology domain- and caspase recruitment domain-dependent oligomerization of ASC
    • J. Masumoto, S. Taniguchi, and J. Sagara Pyrin N-terminal homology domain- and caspase recruitment domain-dependent oligomerization of ASC Biochem. Biophys. Res. Commun. 280 2001 652 655
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 652-655
    • Masumoto, J.1    Taniguchi, S.2    Sagara, J.3
  • 34
    • 80052179138 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptotic cell death
    • E.A. Miao, J.V. Rajan, and A. Aderem Caspase-1-induced pyroptotic cell death Immunol. Rev. 243 2011 206 214
    • (2011) Immunol. Rev. , vol.243 , pp. 206-214
    • Miao, E.A.1    Rajan, J.V.2    Aderem, A.3
  • 35
    • 12144284412 scopus 로고    scopus 로고
    • Role of charged and hydrophobic residues in the oligomerization of the PYRIN domain of ASC
    • M. Moriya, S. Taniguchi, P. Wu, E. Liepinsh, G. Otting, and J. Sagara Role of charged and hydrophobic residues in the oligomerization of the PYRIN domain of ASC Biochemistry 44 2005 575 583
    • (2005) Biochemistry , vol.44 , pp. 575-583
    • Moriya, M.1    Taniguchi, S.2    Wu, P.3    Liepinsh, E.4    Otting, G.5    Sagara, J.6
  • 36
    • 84879596906 scopus 로고    scopus 로고
    • K efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • R. Muñoz-Planillo, P. Kuffa, G. Martínez-Colón, B.L. Smith, T.M. Rajendiran, and G. Núñez K efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter Immunity 38 2013 1142 1153
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Muñoz-Planillo, R.1    Kuffa, P.2    Martínez-Colón, G.3    Smith, B.L.4    Rajendiran, T.M.5    Núñez, G.6
  • 37
    • 33845966052 scopus 로고    scopus 로고
    • Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling
    • A. Natarajan, R. Ghose, and J.M. Hill Structure and dynamics of ASC2, a pyrin domain-only protein that regulates inflammatory signaling J. Biol. Chem. 281 2006 31863 31875
    • (2006) J. Biol. Chem. , vol.281 , pp. 31863-31875
    • Natarajan, A.1    Ghose, R.2    Hill, J.M.3
  • 38
    • 77954297726 scopus 로고    scopus 로고
    • DNABINDPROT: Fluctuation-based predictor of DNA-binding residues within a network of interacting residues
    • P. Ozbek, S. Soner, B. Erman, and T. Haliloglu DNABINDPROT: fluctuation-based predictor of DNA-binding residues within a network of interacting residues Nucleic Acids Res. 38 2010 W417 W423
    • (2010) Nucleic Acids Res. , vol.38 , pp. 417-W423
    • Ozbek, P.1    Soner, S.2    Erman, B.3    Haliloglu, T.4
  • 39
    • 84892143727 scopus 로고    scopus 로고
    • Hot spots in a network of functional sites
    • P. Ozbek, S. Soner, and T. Haliloglu Hot spots in a network of functional sites PLoS ONE 8 2013 e74320
    • (2013) PLoS ONE , vol.8 , pp. 74320
    • Ozbek, P.1    Soner, S.2    Haliloglu, T.3
  • 40
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • H.H. Park, E. Logette, S. Raunser, S. Cuenin, T. Walz, J. Tschopp, and H. Wu Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex Cell 128 2007 533 546
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1    Logette, E.2    Raunser, S.3    Cuenin, S.4    Walz, T.5    Tschopp, J.6    Wu, H.7
  • 42
    • 84872451259 scopus 로고    scopus 로고
    • The CARD plays a critical role in ASC foci formation and inflammasome signalling
    • M. Proell, M. Gerlic, P.D. Mace, J.C. Reed, and S.J. Riedl The CARD plays a critical role in ASC foci formation and inflammasome signalling Biochem. J. 449 2013 613 621
    • (2013) Biochem. J. , vol.449 , pp. 613-621
    • Proell, M.1    Gerlic, M.2    Mace, P.D.3    Reed, J.C.4    Riedl, S.J.5
  • 43
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • H. Qin, S.M. Srinivasula, G. Wu, T. Fernandes-Alnemri, E.S. Alnemri, and Y. Shi Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1 Nature 399 1999 549 557
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 44
    • 0035914452 scopus 로고    scopus 로고
    • Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis
    • N. Richards, P. Schaner, A. Diaz, J. Stuckey, E. Shelden, A. Wadhwa, and D.L. Gumucio Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis J. Biol. Chem. 276 2001 39320 39329
    • (2001) J. Biol. Chem. , vol.276 , pp. 39320-39329
    • Richards, N.1    Schaner, P.2    Diaz, A.3    Stuckey, J.4    Shelden, E.5    Wadhwa, A.6    Gumucio, D.L.7
  • 45
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • K. Schroder, and J. Tschopp The inflammasomes Cell 140 2010 821 832
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 46
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction
    • C.S. Shi, K. Shenderov, N.N. Huang, J. Kabat, M. Abu-Asab, K.A. Fitzgerald, A. Sher, and J.H. Kehrl Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction Nat. Immunol. 13 2012 255 263
    • (2012) Nat. Immunol. , vol.13 , pp. 255-263
    • Shi, C.S.1    Shenderov, K.2    Huang, N.N.3    Kabat, J.4    Abu-Asab, M.5    Fitzgerald, K.A.6    Sher, A.7    Kehrl, J.H.8
  • 48
    • 84859738249 scopus 로고    scopus 로고
    • Roles of residues in the interface of transient protein-protein complexes before complexation
    • L.S. Swapna, R.M. Bhaskara, J. Sharma, and N. Srinivasan Roles of residues in the interface of transient protein-protein complexes before complexation Sci Rep 2 2012
    • (2012) Sci Rep , vol.2
    • Swapna, L.S.1    Bhaskara, R.M.2    Sharma, J.3    Srinivasan, N.4
  • 49
    • 84871314266 scopus 로고    scopus 로고
    • Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein
    • P.R. Vajjhala, R.E. Mirams, and J.M. Hill Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein J. Biol. Chem. 287 2012 41732 41743
    • (2012) J. Biol. Chem. , vol.287 , pp. 41732-41743
    • Vajjhala, P.R.1    Mirams, R.E.2    Hill, J.M.3
  • 50
    • 84906544294 scopus 로고    scopus 로고
    • Identification of Multifaceted Binding Modes for Pyrin and ASC Pyrin Domains Gives Insights into Pyrin Inflammasome Assembly
    • jbc. M114. 553305
    • P.R. Vajjhala, S. Kaiser, S.J. Smith, Q.R. Ong, S.L. Soh, K.J. Stacey, and J.M. Hill Identification of Multifaceted Binding Modes for Pyrin and ASC Pyrin Domains Gives Insights into Pyrin Inflammasome Assembly J Biol Chem 2014 jbc. M114. 553305
    • (2014) J Biol Chem
    • Vajjhala, P.R.1    Kaiser, S.2    Smith, S.J.3    Ong, Q.R.4    Soh, S.L.5    Stacey, K.J.6    Hill, J.M.7
  • 51
    • 0036802356 scopus 로고    scopus 로고
    • The role of NF-kappaB in the regulation of cell stress responses
    • T. Wang, X. Zhang, and J.J. Li The role of NF-kappaB in the regulation of cell stress responses Int. Immunopharmacol. 2 2002 1509 1520
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 1509-1520
    • Wang, T.1    Zhang, X.2    Li, J.J.3
  • 53
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • R. Zhou, A.S. Yazdi, P. Menu, and J. Tschopp A role for mitochondria in NLRP3 inflammasome activation Nature 469 2011 221 225
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4


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