메뉴 건너뛰기




Volumn 43, Issue , 2017, Pages 122-130

Towards the structure of the TIR-domain signalosome

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE PROTEIN; MYELOID DIFFERENTIATION FACTOR 88; TOLL INTERLEUKIN 1 RECEPTOR RESISTANCE PROTEIN DOMAIN SIGNALOSOME; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 1; UNCLASSIFIED DRUG; PLANT PROTEIN; PROTEIN;

EID: 85009165959     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2016.12.014     Document Type: Review
Times cited : (57)

References (64)
  • 1
    • 0025774776 scopus 로고
    • Drosophila Toll and Il-1 receptor
    • 1 Gay, N.J., Keith, F.J., Drosophila Toll and Il-1 receptor. Nature 351 (1991), 355–356.
    • (1991) Nature , vol.351 , pp. 355-356
    • Gay, N.J.1    Keith, F.J.2
  • 2
    • 84856540295 scopus 로고    scopus 로고
    • Tracing the origin and evolutionary history of plant nucleotide-binding site-leucine-rich repeat (NBS-LRR) genes
    • 2 Yue, J.X., Meyers, B.C., Chen, J.Q., Tian, D., Yang, S., Tracing the origin and evolutionary history of plant nucleotide-binding site-leucine-rich repeat (NBS-LRR) genes. New Phytol 193 (2012), 1049–1063.
    • (2012) New Phytol , vol.193 , pp. 1049-1063
    • Yue, J.X.1    Meyers, B.C.2    Chen, J.Q.3    Tian, D.4    Yang, S.5
  • 3
    • 84873410279 scopus 로고    scopus 로고
    • Bacterial TIR-containing proteins and host innate immune system evasion
    • 3 Rana, R.R., Zhang, M., Spear, A.M., Atkins, H.S., Byrne, B., Bacterial TIR-containing proteins and host innate immune system evasion. Med Microbiol Immunol 202 (2013), 1–10.
    • (2013) Med Microbiol Immunol , vol.202 , pp. 1-10
    • Rana, R.R.1    Zhang, M.2    Spear, A.M.3    Atkins, H.S.4    Byrne, B.5
  • 4
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • 4 Akira, S., Uematsu, S., Takeuchi, O., Pathogen recognition and innate immunity. Cell 124 (2006), 783–801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 5
    • 84866953674 scopus 로고    scopus 로고
    • Adaptors in Toll-like receptor signaling and their potential as therapeutic targets
    • 5 Ve, T., Gay, N.J., Mansell, A., Kobe, B., Kellie, S., Adaptors in Toll-like receptor signaling and their potential as therapeutic targets. Curr Drug Targets 13 (2012), 1360–1374.
    • (2012) Curr Drug Targets , vol.13 , pp. 1360-1374
    • Ve, T.1    Gay, N.J.2    Mansell, A.3    Kobe, B.4    Kellie, S.5
  • 6
    • 84905050462 scopus 로고    scopus 로고
    • Assembly and localization of Toll-like receptor signalling complexes
    • 6 Gay, N.J., Symmons, M.F., Gangloff, M., Bryant, C.E., Assembly and localization of Toll-like receptor signalling complexes. Nat Rev Immunol 14 (2014), 546–558.
    • (2014) Nat Rev Immunol , vol.14 , pp. 546-558
    • Gay, N.J.1    Symmons, M.F.2    Gangloff, M.3    Bryant, C.E.4
  • 7
    • 33748871187 scopus 로고    scopus 로고
    • The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling
    • 7 Carty, M., Goodbody, R., Schroder, M., Stack, J., Moynagh, P.N., Bowie, A.G., The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling. Nat Immunol 7 (2006), 1074–1081.
    • (2006) Nat Immunol , vol.7 , pp. 1074-1081
    • Carty, M.1    Goodbody, R.2    Schroder, M.3    Stack, J.4    Moynagh, P.N.5    Bowie, A.G.6
  • 8
    • 84881495428 scopus 로고    scopus 로고
    • Sarm1-mediated axon degeneration requires both SAM and TIR interactions
    • 8 Gerdts, J., Summers, D.W., Sasaki, Y., DiAntonio, A., Milbrandt, J., Sarm1-mediated axon degeneration requires both SAM and TIR interactions. J Neurosci 33 (2013), 13569–13580.
    • (2013) J Neurosci , vol.33 , pp. 13569-13580
    • Gerdts, J.1    Summers, D.W.2    Sasaki, Y.3    DiAntonio, A.4    Milbrandt, J.5
  • 10
    • 84941881013 scopus 로고    scopus 로고
    • Beyond TLR signaling-the role of SARM in antiviral immune defense, apoptosis & development
    • 10 Panneerselvam, P., Ding, J.L., Beyond TLR signaling-the role of SARM in antiviral immune defense, apoptosis & development. Int Rev Immunol 34 (2015), 432–444.
    • (2015) Int Rev Immunol , vol.34 , pp. 432-444
    • Panneerselvam, P.1    Ding, J.L.2
  • 11
    • 84856008042 scopus 로고    scopus 로고
    • Role for B-cell adapter for PI3K (BCAP) as a signaling adapter linking Toll-like receptors (TLRs) to serine/threonine kinases PI3K/Akt
    • 11 Troutman, T.D., Hu, W., Fulenchek, S., Yamazaki, T., Kurosaki, T., Bazan, J.F., Pasare, C., Role for B-cell adapter for PI3K (BCAP) as a signaling adapter linking Toll-like receptors (TLRs) to serine/threonine kinases PI3K/Akt. Proc Natl Acad Sci U S A 109 (2012), 273–278.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 273-278
    • Troutman, T.D.1    Hu, W.2    Fulenchek, S.3    Yamazaki, T.4    Kurosaki, T.5    Bazan, J.F.6    Pasare, C.7
  • 12
    • 85009194978 scopus 로고    scopus 로고
    • Structure of the TIR domain of BCAP which links phosphoinositide metabolism with the negative regulation of the TLR signalosome
    • 12 Halabi, S., Sekine, E., Verstack, B., Gay, N.J., Moncrieffe, M.C., Structure of the TIR domain of BCAP which links phosphoinositide metabolism with the negative regulation of the TLR signalosome. J Biol Chem, 2016.
    • (2016) J Biol Chem
    • Halabi, S.1    Sekine, E.2    Verstack, B.3    Gay, N.J.4    Moncrieffe, M.C.5
  • 13
    • 84892866814 scopus 로고    scopus 로고
    • The interleukin-1 receptor family
    • 13 Boraschi, D., Tagliabue, A., The interleukin-1 receptor family. Semin Immunol 25 (2013), 394–407.
    • (2013) Semin Immunol , vol.25 , pp. 394-407
    • Boraschi, D.1    Tagliabue, A.2
  • 14
    • 85018948407 scopus 로고    scopus 로고
    • Animal NLRs provide structural insights into plant NLR function
    • pii: mcw171, PMID: 27562749
    • 14 Bentham, A., Burdett, H., Anderson, P.A., Williams, S.J., Kobe, B., Animal NLRs provide structural insights into plant NLR function. Ann Bot, 2016, 10.1093/aob/mcw171 pii: mcw171, PMID: 27562749.
    • (2016) Ann Bot
    • Bentham, A.1    Burdett, H.2    Anderson, P.A.3    Williams, S.J.4    Kobe, B.5
  • 15
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: towards an integrated view of plant-pathogen interactions
    • 15 Dodds, P.N., Rathjen, J.P., Plant immunity: towards an integrated view of plant-pathogen interactions. Nat Rev Genet 11 (2010), 539–548.
    • (2010) Nat Rev Genet , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 16
    • 59749083228 scopus 로고    scopus 로고
    • The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction
    • 16 Swiderski, M.R., Birker, D., Jones, J.D., The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction. Mol Plant Microbe Interact 22 (2009), 157–165.
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 157-165
    • Swiderski, M.R.1    Birker, D.2    Jones, J.D.3
  • 17
    • 79952643473 scopus 로고    scopus 로고
    • Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation
    • 17 Bernoux, M., Ve, T., Williams, S., Warren, C., Hatters, D., Valkov, E., Zhang, X., Ellis, J.G., Kobe, B., Dodds, P.N., Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation. Cell Host Microbe 9 (2011), 200–211.
    • (2011) Cell Host Microbe , vol.9 , pp. 200-211
    • Bernoux, M.1    Ve, T.2    Williams, S.3    Warren, C.4    Hatters, D.5    Valkov, E.6    Zhang, X.7    Ellis, J.G.8    Kobe, B.9    Dodds, P.N.10
  • 19
    • 0036793439 scopus 로고    scopus 로고
    • TIR-X and TIR-NBS proteins: two new families related to disease resistance TIR-NBS-LRR proteins encoded in Arabidopsis and other plant genomes
    • 19 Meyers, B.C., Morgante, M., Michelmore, R.W., TIR-X and TIR-NBS proteins: two new families related to disease resistance TIR-NBS-LRR proteins encoded in Arabidopsis and other plant genomes. Plant J 32 (2002), 77–92.
    • (2002) Plant J , vol.32 , pp. 77-92
    • Meyers, B.C.1    Morgante, M.2    Michelmore, R.W.3
  • 21
    • 85009196010 scopus 로고    scopus 로고
    • A comparative analysis of the mechanism of Toll-like receptor-disruption by TIR-containing protein C from uropathogenic Escherichia coli
    • pii: E25
    • 21 Waldhuber, A., Snyder, G.A., Rommler, F., Cirl, C., Muller, T., Xiao, T.S., Svanborg, C., Miethke, T., A comparative analysis of the mechanism of Toll-like receptor-disruption by TIR-containing protein C from uropathogenic Escherichia coli. Pathogens, 5(1), 2016, 10.3390/pathogens5010025 pii: E25.
    • (2016) Pathogens , vol.5 , Issue.1
    • Waldhuber, A.1    Snyder, G.A.2    Rommler, F.3    Cirl, C.4    Muller, T.5    Xiao, T.S.6    Svanborg, C.7    Miethke, T.8
  • 22
    • 84863324227 scopus 로고    scopus 로고
    • Poxviral protein A46 antagonizes Toll-like receptor 4 signaling by targeting BB loop motifs in Toll-IL-1 receptor adaptor proteins to disrupt receptor:adaptor interactions
    • 22 Stack, J., Bowie, A.G., Poxviral protein A46 antagonizes Toll-like receptor 4 signaling by targeting BB loop motifs in Toll-IL-1 receptor adaptor proteins to disrupt receptor:adaptor interactions. J Biol Chem 287 (2012), 22672–22682.
    • (2012) J Biol Chem , vol.287 , pp. 22672-22682
    • Stack, J.1    Bowie, A.G.2
  • 24
    • 84886301386 scopus 로고    scopus 로고
    • Structure of the Toll/interleukin 1 receptor (TIR) domain of the immunosuppressive Brucella effector BtpA/Btp1/TcpB
    • TIR and uncovered the conserved association mode in the structures of TIR domains from the bacterial proteins PdTLP and TcpB.
    • TIR and uncovered the conserved association mode in the structures of TIR domains from the bacterial proteins PdTLP and TcpB.
    • (2013) FEBS Lett , vol.587 , pp. 3412-3416
    • Kaplan-Turkoz, B.1    Koelblen, T.2    Felix, C.3    Candusso, M.P.4    O'Callaghan, D.5    Vergunst, A.C.6    Terradot, L.7
  • 25
    • 84925465183 scopus 로고    scopus 로고
    • Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains
    • The only available comprehensive review of 3D structures of TIR domains from animals, plants and bacteria.
    • 25• Ve, T., Williams, S.J., Kobe, B., Structure and function of Toll/interleukin-1 receptor/resistance protein (TIR) domains. Apoptosis 20 (2015), 250–261 The only available comprehensive review of 3D structures of TIR domains from animals, plants and bacteria.
    • (2015) Apoptosis , vol.20 , pp. 250-261
    • Ve, T.1    Williams, S.J.2    Kobe, B.3
  • 26
    • 0034597766 scopus 로고    scopus 로고
    • Structural basis for signal transduction by the Toll/interleukin-1 receptor domains
    • 26 Xu, Y., Tao, X., Shen, B., Horng, T., Medzhitov, R., Manley, J.L., Tong, L., Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature 408 (2000), 111–115.
    • (2000) Nature , vol.408 , pp. 111-115
    • Xu, Y.1    Tao, X.2    Shen, B.3    Horng, T.4    Medzhitov, R.5    Manley, J.L.6    Tong, L.7
  • 27
    • 84876898443 scopus 로고    scopus 로고
    • Identification of binding sites for myeloid differentiation primary response gene 88 (MyD88) and Toll-like receptor 4 in MyD88 adapter-like (Mal)
    • Random mutagenesis and the MAPPIT (mammalian protein-protein interaction trap) approach were used to identify mutations in MAL that disrupt its interaction with TLR4 and MyD88; cooperative binding between these proteins is proposed.
    • 27• Bovijn, C., Desmet, A.S., Uyttendaele, I., Van Acker, T., Tavernier, J., Peelman, F., Identification of binding sites for myeloid differentiation primary response gene 88 (MyD88) and Toll-like receptor 4 in MyD88 adapter-like (Mal). J Biol Chem 288 (2013), 12054–12066 Random mutagenesis and the MAPPIT (mammalian protein-protein interaction trap) approach were used to identify mutations in MAL that disrupt its interaction with TLR4 and MyD88; cooperative binding between these proteins is proposed.
    • (2013) J Biol Chem , vol.288 , pp. 12054-12066
    • Bovijn, C.1    Desmet, A.S.2    Uyttendaele, I.3    Van Acker, T.4    Tavernier, J.5    Peelman, F.6
  • 28
    • 84856710421 scopus 로고    scopus 로고
    • Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4
    • 28 Bovijn, C., Ulrichts, P., De Smet, A.S., Catteeuw, D., Beyaert, R., Tavernier, J., Peelman, F., Identification of interaction sites for dimerization and adapter recruitment in Toll/interleukin-1 receptor (TIR) domain of Toll-like receptor 4. J Biol Chem 287 (2012), 4088–4098.
    • (2012) J Biol Chem , vol.287 , pp. 4088-4098
    • Bovijn, C.1    Ulrichts, P.2    De Smet, A.S.3    Catteeuw, D.4    Beyaert, R.5    Tavernier, J.6    Peelman, F.7
  • 29
    • 84939824619 scopus 로고    scopus 로고
    • The architecture of the TIR domain signalosome in the Toll-like receptor-4 signaling pathway
    • A computational algorithm is used in combination with crystal structures and experimental data to model the TLR4 signalosome.
    • 29• Guven-Maiorov, E., Keskin, O., Gursoy, A., VanWaes, C., Chen, Z., Tsai, C.J., Nussinov, R., The architecture of the TIR domain signalosome in the Toll-like receptor-4 signaling pathway. Sci Rep, 5, 2015, 13128 A computational algorithm is used in combination with crystal structures and experimental data to model the TLR4 signalosome.
    • (2015) Sci Rep , vol.5 , pp. 13128
    • Guven-Maiorov, E.1    Keskin, O.2    Gursoy, A.3    VanWaes, C.4    Chen, Z.5    Tsai, C.J.6    Nussinov, R.7
  • 30
    • 3843055773 scopus 로고    scopus 로고
    • Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL
    • 30 Khan, J.A., Brint, E.K., O'Neill, L.A., Tong, L., Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL. J Biol Chem 279 (2004), 31664–31670.
    • (2004) J Biol Chem , vol.279 , pp. 31664-31670
    • Khan, J.A.1    Brint, E.K.2    O'Neill, L.A.3    Tong, L.4
  • 31
    • 40749097627 scopus 로고    scopus 로고
    • A dimer of the Toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteins
    • 31 Nunez Miguel, R., Wong, J., Westoll, J.F., Brooks, H.J., O'Neill, L.A., Gay, N.J., Bryant, C.E., Monie, T.P., A dimer of the Toll-like receptor 4 cytoplasmic domain provides a specific scaffold for the recruitment of signalling adaptor proteins. PLoS One, 2, 2007, e788.
    • (2007) PLoS One , vol.2 , pp. e788
    • Nunez Miguel, R.1    Wong, J.2    Westoll, J.F.3    Brooks, H.J.4    O'Neill, L.A.5    Gay, N.J.6    Bryant, C.E.7    Monie, T.P.8
  • 33
    • 0036435613 scopus 로고    scopus 로고
    • An extensively associated dimer in the structure of the C713S mutant of the TIR domain of human TLR2
    • 33 Tao, X., Xu, Y., Zheng, Y., Beg, A.A., Tong, L., An extensively associated dimer in the structure of the C713S mutant of the TIR domain of human TLR2. Biochem Biophys Res Commun 299 (2002), 216–221.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 216-221
    • Tao, X.1    Xu, Y.2    Zheng, Y.3    Beg, A.A.4    Tong, L.5
  • 34
    • 79955030120 scopus 로고    scopus 로고
    • Targeting TLR4 signaling by TLR4 Toll/IL-1 receptor domain-derived decoy peptides: identification of the TLR4 Toll/IL-1 receptor domain dimerization interface
    • 34 Toshchakov, V.Y., Szmacinski, H., Couture, L.A., Lakowicz, J.R., Vogel, S.N., Targeting TLR4 signaling by TLR4 Toll/IL-1 receptor domain-derived decoy peptides: identification of the TLR4 Toll/IL-1 receptor domain dimerization interface. J Immunol 186 (2011), 4819–4827.
    • (2011) J Immunol , vol.186 , pp. 4819-4827
    • Toshchakov, V.Y.1    Szmacinski, H.2    Couture, L.A.3    Lakowicz, J.R.4    Vogel, S.N.5
  • 35
    • 84959331956 scopus 로고    scopus 로고
    • Reconstructing the TIR side of the Myddosome: a paradigm for TIR-TIR interactions
    • The mammalian two-hybrid system MAPPIT and extensive mutagenesis were combined with the available crystallographic and NMR data and computational modelling to suggest the structure of the MyD88 TIR-domain signalosome.
    • 35• Vyncke, L., Bovijn, C., Pauwels, E., Van Acker, T., Ruyssinck, E., Burg, E., Tavernier, J., Peelman, F., Reconstructing the TIR side of the Myddosome: a paradigm for TIR-TIR interactions. Structure 24 (2016), 437–447 The mammalian two-hybrid system MAPPIT and extensive mutagenesis were combined with the available crystallographic and NMR data and computational modelling to suggest the structure of the MyD88 TIR-domain signalosome.
    • (2016) Structure , vol.24 , pp. 437-447
    • Vyncke, L.1    Bovijn, C.2    Pauwels, E.3    Van Acker, T.4    Ruyssinck, E.5    Burg, E.6    Tavernier, J.7    Peelman, F.8
  • 37
    • 80052578340 scopus 로고    scopus 로고
    • Crystal structure of Toll-like receptor adaptor MAL/TIRAP reveals the molecular basis for signal transduction and disease protection
    • 37 Valkov, E., Stamp, A., Dimaio, F., Baker, D., Verstak, B., Roversi, P., Kellie, S., Sweet, M.J., Mansell, A., Gay, N.J., et al. Crystal structure of Toll-like receptor adaptor MAL/TIRAP reveals the molecular basis for signal transduction and disease protection. Proc Natl Acad Sci U S A 108 (2011), 14879–14884.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14879-14884
    • Valkov, E.1    Stamp, A.2    Dimaio, F.3    Baker, D.4    Verstak, B.5    Roversi, P.6    Kellie, S.7    Sweet, M.J.8    Mansell, A.9    Gay, N.J.10
  • 38
    • 84941805448 scopus 로고    scopus 로고
    • A structural view of negative regulation of the Toll-like receptor-mediated inflammatory pathway
    • 38 Guven-Maiorov, E., Keskin, O., Gursoy, A., Nussinov, R., A structural view of negative regulation of the Toll-like receptor-mediated inflammatory pathway. Biophys J 109 (2015), 1214–1226.
    • (2015) Biophys J , vol.109 , pp. 1214-1226
    • Guven-Maiorov, E.1    Keskin, O.2    Gursoy, A.3    Nussinov, R.4
  • 40
    • 45549086115 scopus 로고    scopus 로고
    • The crystal structure of the human Toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer
    • 40 Nyman, T., Stenmark, P., Flodin, S., Johansson, I., Hammarstrom, M., Nordlund, P., The crystal structure of the human Toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer. J Biol Chem 283 (2008), 11861–11865.
    • (2008) J Biol Chem , vol.283 , pp. 11861-11865
    • Nyman, T.1    Stenmark, P.2    Flodin, S.3    Johansson, I.4    Hammarstrom, M.5    Nordlund, P.6
  • 41
    • 84859227566 scopus 로고    scopus 로고
    • Structural insights into TIR domain specificity of the bridging adaptor Mal in TLR4 signaling
    • 41 Lin, Z., Lu, J., Zhou, W., Shen, Y., Structural insights into TIR domain specificity of the bridging adaptor Mal in TLR4 signaling. PLoS One, 7, 2012, e34202.
    • (2012) PLoS One , vol.7 , pp. e34202
    • Lin, Z.1    Lu, J.2    Zhou, W.3    Shen, Y.4
  • 43
    • 84920184268 scopus 로고    scopus 로고
    • Crystal structure of TIR domain of TLR6 reveals novel dimeric interface of TIR-TIR interaction for Toll-like receptor signaling pathway
    • 43 Jang, T.H., Park, H.H., Crystal structure of TIR domain of TLR6 reveals novel dimeric interface of TIR-TIR interaction for Toll-like receptor signaling pathway. J Mol Biol 426 (2014), 3305–3313.
    • (2014) J Mol Biol , vol.426 , pp. 3305-3313
    • Jang, T.H.1    Park, H.H.2
  • 44
    • 33749574498 scopus 로고    scopus 로고
    • Structural and functional evidence for the role of the TLR2 DD loop in TLR1/TLR2 heterodimerization and signaling
    • 44 Gautam, J.K., Ashish, Comeau, L.D., Krueger, J.K., Smith, M.F. Jr., Structural and functional evidence for the role of the TLR2 DD loop in TLR1/TLR2 heterodimerization and signaling. J Biol Chem 281 (2006), 30132–30142.
    • (2006) J Biol Chem , vol.281 , pp. 30132-30142
    • Gautam, J.K.1    Ashish2    Comeau, L.D.3    Krueger, J.K.4    Smith, M.F.5
  • 45
    • 76749092614 scopus 로고    scopus 로고
    • Inhibition of Toll-like receptors TLR4 and 7 signaling pathways by SIGIRR: a computational approach
    • 45 Gong, J., Wei, T., Stark, R.W., Jamitzky, F., Heckl, W.M., Anders, H.J., Lech, M., Rossle, S.C., Inhibition of Toll-like receptors TLR4 and 7 signaling pathways by SIGIRR: a computational approach. J Struct Biol 169 (2010), 323–330.
    • (2010) J Struct Biol , vol.169 , pp. 323-330
    • Gong, J.1    Wei, T.2    Stark, R.W.3    Jamitzky, F.4    Heckl, W.M.5    Anders, H.J.6    Lech, M.7    Rossle, S.C.8
  • 46
    • 80052294520 scopus 로고    scopus 로고
    • In silico approach to inhibition of signaling pathways of Toll-like receptors 2 and 4 by ST2L
    • 46 Basith, S., Manavalan, B., Govindaraj, R.G., Choi, S., In silico approach to inhibition of signaling pathways of Toll-like receptors 2 and 4 by ST2L. PLoS One, 6, 2011, e23989.
    • (2011) PLoS One , vol.6 , pp. e23989
    • Basith, S.1    Manavalan, B.2    Govindaraj, R.G.3    Choi, S.4
  • 47
    • 84866381972 scopus 로고    scopus 로고
    • X-ray crystallographic structure of TIR-domain from the human TIR-domain containing adaptor protein/MyD88-adaptor-like protein (TIRAP/MAL)
    • 47 Woo, J.R., Kim, S., Shoelson, S.E., Park, S., X-ray crystallographic structure of TIR-domain from the human TIR-domain containing adaptor protein/MyD88-adaptor-like protein (TIRAP/MAL). Bull Korean Chem Soc 33 (2012), 3091–3094.
    • (2012) Bull Korean Chem Soc , vol.33 , pp. 3091-3094
    • Woo, J.R.1    Kim, S.2    Shoelson, S.E.3    Park, S.4
  • 48
    • 84886915828 scopus 로고    scopus 로고
    • Mutational analysis identifies residues crucial for homodimerization of myeloid differentiation factor 88 (MyD88) and for its function in immune cells
    • 48 Loiarro, M., Volpe, E., Ruggiero, V., Gallo, G., Furlan, R., Maiorino, C., Battistini, L., Sette, C., Mutational analysis identifies residues crucial for homodimerization of myeloid differentiation factor 88 (MyD88) and for its function in immune cells. J Biol Chem 288 (2013), 30210–30222.
    • (2013) J Biol Chem , vol.288 , pp. 30210-30222
    • Loiarro, M.1    Volpe, E.2    Ruggiero, V.3    Gallo, G.4    Furlan, R.5    Maiorino, C.6    Battistini, L.7    Sette, C.8
  • 50
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • 50 Lin, S.C., Lo, Y.C., Wu, H., 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
  • 51
    • 84866072549 scopus 로고    scopus 로고
    • Toll/interleukin-1 receptor domain dimers as the platform for activation and enhanced inhibition of Toll-like receptor signaling
    • 51 Fekonja, O., Bencina, M., Jerala, R., Toll/interleukin-1 receptor domain dimers as the platform for activation and enhanced inhibition of Toll-like receptor signaling. J Biol Chem 287 (2012), 30993–31002.
    • (2012) J Biol Chem , vol.287 , pp. 30993-31002
    • Fekonja, O.1    Bencina, M.2    Jerala, R.3
  • 52
    • 38449098414 scopus 로고    scopus 로고
    • Spatiotemporal mobilization of Toll/IL-1 receptor domain-containing adaptor molecule-1 in response to dsRNA
    • 52 Funami, K., Sasai, M., Ohba, Y., Oshiumi, H., Seya, T., Matsumoto, M., Spatiotemporal mobilization of Toll/IL-1 receptor domain-containing adaptor molecule-1 in response to dsRNA. J Immunol 179 (2007), 6867–6872.
    • (2007) J Immunol , vol.179 , pp. 6867-6872
    • Funami, K.1    Sasai, M.2    Ohba, Y.3    Oshiumi, H.4    Seya, T.5    Matsumoto, M.6
  • 53
    • 84891942344 scopus 로고    scopus 로고
    • Crystal structures of the Toll/Interleukin-1 receptor (TIR) domains from the Brucella protein TcpB and host adaptor TIRAP reveal mechanisms of molecular mimicry
    • See annotations for Ref.[23••].
    • 53•• Snyder, G.A., Deredge, D., Waldhuber, A., Fresquez, T., Wilkins, D.Z., Smith, P.T., Durr, S., Cirl, C., Jiang, J., Jennings, W., et al. Crystal structures of the Toll/Interleukin-1 receptor (TIR) domains from the Brucella protein TcpB and host adaptor TIRAP reveal mechanisms of molecular mimicry. J Biol Chem 289 (2014), 669–679 See annotations for Ref.[23••].
    • (2014) J Biol Chem , vol.289 , pp. 669-679
    • Snyder, G.A.1    Deredge, D.2    Waldhuber, A.3    Fresquez, T.4    Wilkins, D.Z.5    Smith, P.T.6    Durr, S.7    Cirl, C.8    Jiang, J.9    Jennings, W.10
  • 57
    • 75149175757 scopus 로고    scopus 로고
    • The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants
    • 57 Chan, S.L., Mukasa, T., Santelli, E., Low, L.Y., Pascual, J., The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants. Protein Sci 19 (2010), 155–161.
    • (2010) Protein Sci , vol.19 , pp. 155-161
    • Chan, S.L.1    Mukasa, T.2    Santelli, E.3    Low, L.Y.4    Pascual, J.5
  • 59
  • 62
    • 84891946034 scopus 로고    scopus 로고
    • Mechanism of bacterial interference with TLR4 signaling by Brucella Toll/interleukin-1 receptor domain-containing protein TcpB
    • See annotations for Ref.[23••].
    • 62•• Alaidarous, M., Ve, T., Casey, L.W., Valkov, E., Ericsson, D.J., Ullah, M.O., Schembri, M.A., Mansell, A., Sweet, M.J., Kobe, B., Mechanism of bacterial interference with TLR4 signaling by Brucella Toll/interleukin-1 receptor domain-containing protein TcpB. J Biol Chem 289 (2014), 654–668 See annotations for Ref.[23••].
    • (2014) J Biol Chem , vol.289 , pp. 654-668
    • Alaidarous, M.1    Ve, T.2    Casey, L.W.3    Valkov, E.4    Ericsson, D.J.5    Ullah, M.O.6    Schembri, M.A.7    Mansell, A.8    Sweet, M.J.9    Kobe, B.10
  • 63
    • 84876221513 scopus 로고    scopus 로고
    • Higher-order assemblies in a new paradigm of signal transduction
    • 63 Wu, H., Higher-order assemblies in a new paradigm of signal transduction. Cell 153 (2013), 287–292.
    • (2013) Cell , vol.153 , pp. 287-292
    • Wu, H.1
  • 64
    • 84975159042 scopus 로고    scopus 로고
    • The structure and dynamics of higher-order assemblies: amyloids, signalosomes, and granules
    • An attempt to compare different higher-order assemblies, including various signalosomes, amyloids and cellular granules, at structural, dynamic and regulatory levels.
    • 64•• Wu, H., Fuxreiter, M., The structure and dynamics of higher-order assemblies: amyloids, signalosomes, and granules. Cell 165 (2016), 1055–1066 An attempt to compare different higher-order assemblies, including various signalosomes, amyloids and cellular granules, at structural, dynamic and regulatory levels.
    • (2016) Cell , vol.165 , pp. 1055-1066
    • Wu, H.1    Fuxreiter, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.