메뉴 건너뛰기




Volumn 4, Issue SEP, 2013, Pages

Proteases: Essential actors in processing antigens and intracellular toll-like receptors

Author keywords

Antigen processing; Endosomal proteases; Intracellular toll like receptors; MHC class II

Indexed keywords

BRUTON TYROSINE KINASE; CATHEPSIN G; CATHEPSIN L; CATHEPSIN S; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MYELIN BASIC PROTEIN; PROTEINASE; PROTEINASE INHIBITOR; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 9;

EID: 84885978134     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2013.00299     Document Type: Short Survey
Times cited : (24)

References (43)
  • 1
    • 0035145332 scopus 로고    scopus 로고
    • Antigen processing in the endocytic compartment
    • doi: 10.1016/S0952-7915(00)00177-1
    • Watts C. Antigen processing in the endocytic compartment. Curr Opin Immunol (2001) 13:26-31. doi: 10.1016/S0952-7915(00)00177-1.
    • (2001) Curr Opin Immunol , vol.13 , pp. 26-31
    • Watts, C.1
  • 2
    • 0029615496 scopus 로고
    • How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway
    • doi:10.1146/annurev.cb.11.110195.001411
    • Wolf PR, Ploegh HL. How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. Annu Rev Cell Dev Biol (1995) 11:267-306. doi:10.1146/annurev.cb.11.110195.001411.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 267-306
    • Wolf, P.R.1    Ploegh, H.L.2
  • 3
    • 0037196549 scopus 로고    scopus 로고
    • Multiple roles of the invariant chain in MHC class II function
    • doi:10.1016/S0167-4889(01)00166-5
    • Stumptner-Cuvelette P, Benaroch P. Multiple roles of the invariant chain in MHC class II function. Biochim Biophys Acta (2002) 1542:1-13. doi:10.1016/S0167-4889(01)00166-5.
    • (2002) Biochim Biophys Acta , vol.1542 , pp. 1-13
    • Stumptner-Cuvelette, P.1    Benaroch, P.2
  • 4
    • 2442549710 scopus 로고    scopus 로고
    • Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice
    • doi:10.1016/S1074-7613(00)80021-7
    • Nakagawa TY, Brissette WH, Lira PD, Griffiths RJ, Petrushova N, Stock J, et al. Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice. Immunity (1999) 10:207-17. doi:10.1016/S1074-7613(00)80021-7.
    • (1999) Immunity , vol.10 , pp. 207-217
    • Nakagawa, T.Y.1    Brissette, W.H.2    Lira, P.D.3    Griffiths, R.J.4    Petrushova, N.5    Stock, J.6
  • 5
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • doi:10.1016/S1074-7613(00)80249-6
    • Riese RJ, Wolf PR, Bromme D, Natkin LR, Villadangos JA, Ploegh HL, et al. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity (1996) 4:357-66. doi:10.1016/S1074-7613(00)80249-6.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6
  • 6
    • 0032540474 scopus 로고    scopus 로고
    • Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus
    • doi:10.1126/science.280.5362.450
    • Nakagawa T, Roth W, Wong P, Nelson A, Farr A, Deussing J, et al. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science (1998) 280:450-3. doi:10.1126/science.280.5362.450.
    • (1998) Science , vol.280 , pp. 450-453
    • Nakagawa, T.1    Roth, W.2    Wong, P.3    Nelson, A.4    Farr, A.5    Deussing, J.6
  • 7
    • 0037087364 scopus 로고    scopus 로고
    • A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation
    • Hsieh CS, deRoos P, Honey K, Beers C, Rudensky AY. A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation. J Immunol (2002) 168:2618-25.
    • (2002) J Immunol , vol.168 , pp. 2618-2625
    • Hsieh, C.S.1    deRoos, P.2    Honey, K.3    Beers, C.4    Rudensky, A.Y.5
  • 8
    • 0036177422 scopus 로고    scopus 로고
    • Specific role for cathepsin S in the generation of antigenic peptides in vivo
    • doi:10.1002/1521-4141(200202)32:2<467::AID-IMMU467>3.0.CO;2-Y
    • Pluger EB, Boes M, Alfonso C, Schroter CJ, Kalbacher H, Ploegh HL, et al. Specific role for cathepsin S in the generation of antigenic peptides in vivo. Eur J Immunol (2002) 32:467-76. doi:10.1002/1521-4141(200202)32:2<467::AID-IMMU467>3.0.CO;2-Y.
    • (2002) Eur J Immunol , vol.32 , pp. 467-476
    • Pluger, E.B.1    Boes, M.2    Alfonso, C.3    Schroter, C.J.4    Kalbacher, H.5    Ploegh, H.L.6
  • 9
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • doi:10.1084/jem.191.7.1177
    • Shi GP, Bryant RA, Riese R, Verhelst S, Driessen C, Li Z, et al. Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J Exp Med (2000) 191:1177-86. doi:10.1084/jem.191.7.1177.
    • (2000) J Exp Med , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6
  • 10
    • 84861192687 scopus 로고    scopus 로고
    • Cathepsin S dominates autoantigen processing in human thymic dendritic cells
    • doi:10.1016/j.jaut.2012.02.003
    • Stoeckle C, Quecke P, Ruckrich T, Burster T, Reich M, Weber E, et al. Cathepsin S dominates autoantigen processing in human thymic dendritic cells. J Autoimmun (2012) 38:332-43. doi:10.1016/j.jaut.2012.02.003.
    • (2012) J Autoimmun , vol.38 , pp. 332-343
    • Stoeckle, C.1    Quecke, P.2    Ruckrich, T.3    Burster, T.4    Reich, M.5    Weber, E.6
  • 11
    • 79961135430 scopus 로고    scopus 로고
    • Regulation of cathepsin G reduces the activation of proinsu1lin-reactive T cells from type 1 diabetes patients
    • doi:10.1371/journal.pone.0022815
    • Zou F, Schafer N, Palesch D, Brucken R, Beck A, Sienczyk M, et al. Regulation of cathepsin G reduces the activation of proinsu1lin-reactive T cells from type 1 diabetes patients. PLoS ONE (2011) 6:e22815. doi:10.1371/journal.pone.0022815.
    • (2011) PLoS ONE , vol.6
    • Zou, F.1    Schafer, N.2    Palesch, D.3    Brucken, R.4    Beck, A.5    Sienczyk, M.6
  • 12
    • 0033696962 scopus 로고    scopus 로고
    • Control of antigen presentation by a single protease cleavage site
    • doi:10.1016/S1074-7613(00)80191-0
    • Antoniou AN, Blackwood SL, Mazzeo D, Watts C. Control of antigen presentation by a single protease cleavage site. Immunity (2000) 12:391-8. doi:10.1016/S1074-7613(00)80191-0.
    • (2000) Immunity , vol.12 , pp. 391-398
    • Antoniou, A.N.1    Blackwood, S.L.2    Mazzeo, D.3    Watts, C.4
  • 13
    • 0032542285 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation
    • doi:10.1038/25379
    • Manoury B, Hewitt EW, Morrice N, Dando PM, Barrett AJ, Watts C. An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. Nature (1998) 396:695-9. doi:10.1038/25379.
    • (1998) Nature , vol.396 , pp. 695-699
    • Manoury, B.1    Hewitt, E.W.2    Morrice, N.3    Dando, P.M.4    Barrett, A.J.5    Watts, C.6
  • 14
    • 0036167693 scopus 로고    scopus 로고
    • Destructive processing by asparagine endopeptidase limits presentation of a dominant T cell epitope in MBP
    • doi:10.1038/ni754
    • Manoury B, Mazzeo D, Fugger L, Viner N, Ponsford M, Streeter H, et al. Destructive processing by asparagine endopeptidase limits presentation of a dominant T cell epitope in MBP. Nat Immunol (2002) 3:169-74. doi:10.1038/ni754.
    • (2002) Nat Immunol , vol.3 , pp. 169-174
    • Manoury, B.1    Mazzeo, D.2    Fugger, L.3    Viner, N.4    Ponsford, M.5    Streeter, H.6
  • 15
    • 0037396716 scopus 로고    scopus 로고
    • Asparagine endopeptidase can initiate the removal of the MHC class II invariant chain chaperone
    • doi:10.1016/S1074-7613(03)00085-2
    • Manoury B, Mazzeo D, Li DN, Billson J, Loak K, Benaroch P, et al. Asparagine endopeptidase can initiate the removal of the MHC class II invariant chain chaperone. Immunity (2003) 18:489-98. doi:10.1016/S1074-7613(03)00085-2.
    • (2003) Immunity , vol.18 , pp. 489-498
    • Manoury, B.1    Mazzeo, D.2    Li, D.N.3    Billson, J.4    Loak, K.5    Benaroch, P.6
  • 16
    • 21044432199 scopus 로고    scopus 로고
    • Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice
    • Maehr R, Hang HC, Mintern JD, Kim YM, Cuvillier A, Nishimura M, et al. Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice. J Immunol (2005) 174:7066-74.
    • (2005) J Immunol , vol.174 , pp. 7066-7074
    • Maehr, R.1    Hang, H.C.2    Mintern, J.D.3    Kim, Y.M.4    Cuvillier, A.5    Nishimura, M.6
  • 17
    • 77951904981 scopus 로고    scopus 로고
    • Distinct protease requirements for antigen presentation in vitro and in vivo
    • doi:10.4049/jimmunol.0901486
    • Matthews SP, Werber I, Deussing J, Peters C, Reinheckel T, Watts C. Distinct protease requirements for antigen presentation in vitro and in vivo. J Immunol (2010) 184:2423-31. doi:10.4049/jimmunol.0901486.
    • (2010) J Immunol , vol.184 , pp. 2423-2431
    • Matthews, S.P.1    Werber, I.2    Deussing, J.3    Peters, C.4    Reinheckel, T.5    Watts, C.6
  • 18
    • 0035834410 scopus 로고    scopus 로고
    • Defective antigen processing in GILT-free mice
    • doi:10.1126/science.1065500
    • Maric M, Arunachalam B, Phan UT, Dong C, Garrett WS, Cannon KS, et al. Defective antigen processing in GILT-free mice. Science (2001) 294:1361-5. doi:10.1126/science.1065500.
    • (2001) Science , vol.294 , pp. 1361-1365
    • Maric, M.1    Arunachalam, B.2    Phan, U.T.3    Dong, C.4    Garrett, W.S.5    Cannon, K.S.6
  • 19
    • 78049356430 scopus 로고    scopus 로고
    • GILT accelerates autoimmunity to the melanoma antigen tyrosinase-related protein 1
    • doi:10.4049/jimmunol.1000945
    • Rausch MP, Irvine KR, Antony PA, Restifo NP, Cresswell P, Hastings KT. GILT accelerates autoimmunity to the melanoma antigen tyrosinase-related protein 1. J Immunol (2010) 185:2828-35. doi:10.4049/jimmunol.1000945.
    • (2010) J Immunol , vol.185 , pp. 2828-2835
    • Rausch, M.P.1    Irvine, K.R.2    Antony, P.A.3    Restifo, N.P.4    Cresswell, P.5    Hastings, K.T.6
  • 20
    • 47049115921 scopus 로고    scopus 로고
    • Target peptide sequence within infectious human immunodeficiency virus type 1 does not ensure envelope-specific T-helper cell reactivation: influences of cysteine protease and gamma interferon-induced thiol reductase activities
    • doi:10.1128/CVI.00412-07
    • Sealy R, Chaka W, Surman S, Brown SA, Cresswell P, Hurwitz JL. Target peptide sequence within infectious human immunodeficiency virus type 1 does not ensure envelope-specific T-helper cell reactivation: influences of cysteine protease and gamma interferon-induced thiol reductase activities. Clin Vaccine Immunol (2008) 15:713-9. doi:10.1128/CVI.00412-07.
    • (2008) Clin Vaccine Immunol , vol.15 , pp. 713-719
    • Sealy, R.1    Chaka, W.2    Surman, S.3    Brown, S.A.4    Cresswell, P.5    Hurwitz, J.L.6
  • 21
    • 84872228952 scopus 로고    scopus 로고
    • MHC class II-restricted presentation of the major house dust mite allergen Der p 1 Is GILT-dependent: implications for allergic asthma
    • doi:10.1371/journal.pone.0051343
    • West LC, Grotzke JE, Cresswell P. MHC class II-restricted presentation of the major house dust mite allergen Der p 1 Is GILT-dependent: implications for allergic asthma. PLoS ONE (2013) 8:e51343. doi:10.1371/journal.pone.0051343.
    • (2013) PLoS ONE , vol.8
    • West, L.C.1    Grotzke, J.E.2    Cresswell, P.3
  • 22
    • 0037141017 scopus 로고    scopus 로고
    • Absence of gamma-interferon-inducible lysosomal thiol reductase in melanomas disrupts T cell recognition of select immunodominat epitopes
    • doi:10.1084/jem.20011853
    • Haque MA, Li P, Jackson SJ, Zarour HM, Hawes JW, Phan UT, et al. Absence of gamma-interferon-inducible lysosomal thiol reductase in melanomas disrupts T cell recognition of select immunodominat epitopes. J Exp Med (2002) 195:1267-77. doi:10.1084/jem.20011853.
    • (2002) J Exp Med , vol.195 , pp. 1267-1277
    • Haque, M.A.1    Li, P.2    Jackson, S.J.3    Zarour, H.M.4    Hawes, J.W.5    Phan, U.T.6
  • 23
    • 84872498812 scopus 로고    scopus 로고
    • GILT expression in B cells diminishes cathepsin S steady-state protein expression and activity
    • doi:10.1002/eji.201242379
    • Phipps-Yonas H, Semik V, Hastings KT. GILT expression in B cells diminishes cathepsin S steady-state protein expression and activity. Eur J Immunol (2013) 43:65-74. doi:10.1002/eji.201242379.
    • (2013) Eur J Immunol , vol.43 , pp. 65-74
    • Phipps-Yonas, H.1    Semik, V.2    Hastings, K.T.3
  • 24
    • 70449477746 scopus 로고    scopus 로고
    • Critical role for asparagine endopeptidase in endocytic toll-like receptor signaling in dendritic cells
    • doi:10.1016/j.immuni.2009.09.013
    • Sepulveda FE, Maschalidi S, Colisson R, Heslop L, Ghirelli C, Sakka E, et al. Critical role for asparagine endopeptidase in endocytic toll-like receptor signaling in dendritic cells. Immunity (2009) 31:737-48. doi:10.1016/j.immuni.2009.09.013.
    • (2009) Immunity , vol.31 , pp. 737-748
    • Sepulveda, F.E.1    Maschalidi, S.2    Colisson, R.3    Heslop, L.4    Ghirelli, C.5    Sakka, E.6
  • 25
    • 0041876230 scopus 로고    scopus 로고
    • Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice
    • doi:10.1074/jbc. M302742200
    • Shirahama-Noda K, Yamamoto A, Sugihara K, Hashimoto N, Asano M, Nishimura M, et al. Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice. J Biol Chem (2003) 278:33194-9. doi:10.1074/jbc. M302742200.
    • (2003) J Biol Chem , vol.278 , pp. 33194-9
    • Shirahama-Noda, K.1    Yamamoto, A.2    Sugihara, K.3    Hashimoto, N.4    Asano, M.5    Nishimura, M.6
  • 26
    • 0032525023 scopus 로고    scopus 로고
    • CpG motifs in bacterial DNA activate leukocytes through the pH-dependent generation of reactive oxygen species
    • Yi AK, Tuetken R, Redford T, Waldschmidt M, Kirsch J, Krieg AM. CpG motifs in bacterial DNA activate leukocytes through the pH-dependent generation of reactive oxygen species. J Immunol (1998) 160:4755-61.
    • (1998) J Immunol , vol.160 , pp. 4755-4761
    • Yi, A.K.1    Tuetken, R.2    Redford, T.3    Waldschmidt, M.4    Kirsch, J.5    Krieg, A.M.6
  • 27
    • 0036212849 scopus 로고    scopus 로고
    • Innate immune recognition
    • doi:10.1146/annurev.immunol.20.083001.084359
    • Janeway CA Jr, Medzhitov R. Innate immune recognition. Annu Rev Immunol (2002) 20:197-216. doi:10.1146/annurev.immunol.20.083001.084359.
    • (2002) Annu Rev Immunol , vol.20 , pp. 197-216
    • Janeway Jr., C.A.1    Medzhitov, R.2
  • 28
    • 34247236200 scopus 로고    scopus 로고
    • toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and rage
    • doi:10.1038/ni1457
    • Tian T, Avalos AM, Mao SY, Chen B, Senthil H, Wu H, et al. toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and rage. Nat Immunol (2007) 8:487-96. doi:10.1038/ni1457.
    • (2007) Nat Immunol , vol.8 , pp. 487-496
    • Tian, T.1    Avalos, A.M.2    Mao, S.Y.3    Chen, B.4    Senthil, H.5    Wu, H.6
  • 29
    • 57349191215 scopus 로고    scopus 로고
    • The ectodomain of toll-like receptor 9 is cleaved to generate a functional receptor
    • doi:10.1038/nature07405
    • Ewald SE, Lee BL, Lau L, Wickliffe KE, Shi GP, Chapman HA, et al. The ectodomain of toll-like receptor 9 is cleaved to generate a functional receptor. Nature (2008) 456:658-62. doi:10.1038/nature07405.
    • (2008) Nature , vol.456 , pp. 658-662
    • Ewald, S.E.1    Lee, B.L.2    Lau, L.3    Wickliffe, K.E.4    Shi, G.P.5    Chapman, H.A.6
  • 31
    • 56349114913 scopus 로고    scopus 로고
    • Proteolytic cleavage in an endolysosomal compartment is required for activation of toll-like receptor 9
    • doi:10.1038/ni.1669
    • Park B, Brinkmann MM, Spooner E, Lee CC, Kim YM, Ploegh HL. Proteolytic cleavage in an endolysosomal compartment is required for activation of toll-like receptor 9. Nat Immunol (2008) 9:1407-14. doi:10.1038/ni.1669.
    • (2008) Nat Immunol , vol.9 , pp. 1407-1414
    • Park, B.1    Brinkmann, M.M.2    Spooner, E.3    Lee, C.C.4    Kim, Y.M.5    Ploegh, H.L.6
  • 32
    • 38849127573 scopus 로고    scopus 로고
    • Cathepsin K-dependent toll-like receptor 9 signaling revealed in experimental arthritis
    • doi:10.1126/science.1150110
    • Asagiri M, Hirai T, Kunigami T, Kamano S, Gober HJ, Okamoto K, et al. Cathepsin K-dependent toll-like receptor 9 signaling revealed in experimental arthritis. Science (2008) 319:624-7. doi:10.1126/science.1150110.
    • (2008) Science , vol.319 , pp. 624-627
    • Asagiri, M.1    Hirai, T.2    Kunigami, T.3    Kamano, S.4    Gober, H.J.5    Okamoto, K.6
  • 33
    • 79955743119 scopus 로고    scopus 로고
    • Nucleic acid recognition by toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase
    • doi:10.1084/jem.20100682
    • Ewald SE, Engel A, Lee J, Wang M, Bogyo M, Barton GM. Nucleic acid recognition by toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase. J Exp Med (2011) 208:643-51. doi:10.1084/jem.20100682.
    • (2011) J Exp Med , vol.208 , pp. 643-651
    • Ewald, S.E.1    Engel, A.2    Lee, J.3    Wang, M.4    Bogyo, M.5    Barton, G.M.6
  • 34
    • 84866145569 scopus 로고    scopus 로고
    • Asparagine endopeptidase controls anti-influenza virus immune responses through TLR7 activation
    • doi:10.1371/journal.ppat.1002841
    • Maschalidi S, Hassler S, Blanc F, Sepulveda FE, Tohme M, Chignard M, et al. Asparagine endopeptidase controls anti-influenza virus immune responses through TLR7 activation. PLoS Pathog (2012) 8:e1002841. doi:10.1371/journal.ppat.1002841.
    • (2012) PLoS Pathog , vol.8
    • Maschalidi, S.1    Hassler, S.2    Blanc, F.3    Sepulveda, F.E.4    Tohme, M.5    Chignard, M.6
  • 35
    • 84880260267 scopus 로고    scopus 로고
    • Essential role for toll-like receptor 7 (TLR7)-unique cysteines in an intramolecular disulfide bond, proteolytic cleavage and RNA sensing
    • doi:10.1093/intimm/dxt007
    • Kanno A, Yamamoto C, Onji M, Fukui R, Saitoh S, Motoi Y, et al. Essential role for toll-like receptor 7 (TLR7)-unique cysteines in an intramolecular disulfide bond, proteolytic cleavage and RNA sensing. Int Immunol (2013) 25:413-22. doi:10.1093/intimm/dxt007.
    • (2013) Int Immunol , vol.25 , pp. 413-422
    • Kanno, A.1    Yamamoto, C.2    Onji, M.3    Fukui, R.4    Saitoh, S.5    Motoi, Y.6
  • 36
    • 84866558003 scopus 로고    scopus 로고
    • Proteolytic processing regulates toll-like receptor 3 stability and endosomal localization
    • doi:10.1074/jbc. M112.387803
    • Qi R, Singh D, Kao CC. Proteolytic processing regulates toll-like receptor 3 stability and endosomal localization. J Biol Chem (2012) 287:32617-29. doi:10.1074/jbc. M112.387803.
    • (2012) J Biol Chem , vol.287 , pp. 32617-29
    • Qi, R.1    Singh, D.2    Kao, C.C.3
  • 37
    • 84872178810 scopus 로고    scopus 로고
    • Cleaved/associated TLR3 represents the primary form of the signaling receptor
    • doi:10.4049/jimmunol.1202173
    • Toscano F, Estornes Y, Virard F, Garcia-Cattaneo A, Pierrot A, Vanbervliet B, et al. Cleaved/associated TLR3 represents the primary form of the signaling receptor. J Immunol (2013) 190:764-73. doi:10.4049/jimmunol.1202173.
    • (2013) J Immunol , vol.190 , pp. 764-773
    • Toscano, F.1    Estornes, Y.2    Virard, F.3    Garcia-Cattaneo, A.4    Pierrot, A.5    Vanbervliet, B.6
  • 38
    • 84861861142 scopus 로고    scopus 로고
    • Cleavage of toll-like receptor 3 by cathepsins B and H is essential for signaling
    • doi:10.1073/pnas.1115091109
    • Garcia-Cattaneo A, Gobert FX, Muller M, Toscano F, Flores M, Lescure A, et al. Cleavage of toll-like receptor 3 by cathepsins B and H is essential for signaling. Proc Natl Acad Sci U S A (2012) 109:9053-8. doi:10.1073/pnas.1115091109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 9053-9058
    • Garcia-Cattaneo, A.1    Gobert, F.X.2    Muller, M.3    Toscano, F.4    Flores, M.5    Lescure, A.6
  • 39
    • 34247484007 scopus 로고    scopus 로고
    • The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling
    • doi:10.1083/jcb.200612056
    • Brinkmann MM, Spooner E, Hoebe K, Beutler B, Ploegh HL, Kim YM. The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling. J Cell Biol (2007) 177:265-75. doi:10.1083/jcb.200612056.
    • (2007) J Cell Biol , vol.177 , pp. 265-275
    • Brinkmann, M.M.1    Spooner, E.2    Hoebe, K.3    Beutler, B.4    Ploegh, H.L.5    Kim, Y.M.6
  • 40
    • 40749098665 scopus 로고    scopus 로고
    • UNC93B1 delivers nucleotide-sensing toll-like receptors to endolysosomes
    • doi:10.1038/nature06726
    • Kim YM, Brinkmann MM, Paquet ME, Ploegh HL. UNC93B1 delivers nucleotide-sensing toll-like receptors to endolysosomes. Nature (2008) 452:234-8. doi:10.1038/nature06726.
    • (2008) Nature , vol.452 , pp. 234-238
    • Kim, Y.M.1    Brinkmann, M.M.2    Paquet, M.E.3    Ploegh, H.L.4
  • 41
    • 33750016788 scopus 로고    scopus 로고
    • Herpes simplex virus encephalitis in human UNC-93B deficiency
    • doi:10.1126/science.1128346
    • Casrouge A, Zhang SY, Eidenschenk C, Jouanguy E, Puel A, Yang K, et al. Herpes simplex virus encephalitis in human UNC-93B deficiency. Science (2006) 314:308-12. doi:10.1126/science.1128346.
    • (2006) Science , vol.314 , pp. 308-312
    • Casrouge, A.1    Zhang, S.Y.2    Eidenschenk, C.3    Jouanguy, E.4    Puel, A.5    Yang, K.6
  • 42
    • 31344466165 scopus 로고    scopus 로고
    • The Unc93b1 mutation 3d disrupts exogenous antigen presentation and signaling via toll-like receptors 3, 7 and 9
    • doi:10.1038/ni1297
    • Tabeta K, Hoebe K, Janssen EM, Du X, Georgel P, Crozat K, et al. The Unc93b1 mutation 3d disrupts exogenous antigen presentation and signaling via toll-like receptors 3, 7 and 9. Nat Immunol (2006) 7:156-64. doi:10.1038/ni1297.
    • (2006) Nat Immunol , vol.7 , pp. 156-164
    • Tabeta, K.1    Hoebe, K.2    Janssen, E.M.3    Du, X.4    Georgel, P.5    Crozat, K.6
  • 43
    • 79954997147 scopus 로고    scopus 로고
    • Intracellular MHC class II molecules promote TLR-triggered innate immune responses by maintaining activation of the kinase Btk
    • doi:10.1038/ni.2015
    • Liu X, Zhan Z, Li D, Xu L, Ma F, Zhang P, et al. Intracellular MHC class II molecules promote TLR-triggered innate immune responses by maintaining activation of the kinase Btk. Nat Immunol (2011) 12:416-24. doi:10.1038/ni.2015.
    • (2011) Nat Immunol , vol.12 , pp. 416-424
    • Liu, X.1    Zhan, Z.2    Li, D.3    Xu, L.4    Ma, F.5    Zhang, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.