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Volumn 194, Issue 11, 2015, Pages 5426-5436

Endoplasmic protein Nogo-B (RTN4-B) interacts with GRAMD4 and regulates TLR9-mediated innate immune responses

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL PROTEIN; CPG OLIGODEOXYNUCLEOTIDE; GLUCOSYLTRANSFERASE; I KAPPA B ALPHA; INTERFERON; INTERLEUKIN 12P40; INTERLEUKIN 6; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE P38; POLYINOSINIC POLYCYTIDYLIC ACID; PROTEIN NOGO A; PROTEIN NOGO B; RAB LIKE GTPASE ACTIVATOR AND MYOTUBULARIN DOMAIN CONTAINING 4; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 9; UNCLASSIFIED DRUG; CARRIER PROTEIN; CYTOKINE; GRAMD4 PROTEIN, MOUSE; MITOCHONDRIAL PROTEIN; MYELIN PROTEIN; OLIGONUCLEOTIDE; PROTEIN BINDING; PROTEIN NOGO; SMALL INTERFERING RNA; TLR9 PROTEIN, MOUSE;

EID: 84929613945     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1402006     Document Type: Article
Times cited : (12)

References (57)
  • 1
    • 84870910920 scopus 로고    scopus 로고
    • Signaling organelles of the innate immune system
    • Kagan, J. C. 2012. Signaling organelles of the innate immune system. Cell 151: 1168-1178.
    • (2012) Cell , vol.151 , pp. 1168-1178
    • Kagan, J.C.1
  • 2
    • 79951676940 scopus 로고    scopus 로고
    • Regulation of innate immunity by signaling pathways emerging from the endoplasmic reticulum
    • Martinon, F., and L. H. Glimcher. 2011. Regulation of innate immunity by signaling pathways emerging from the endoplasmic reticulum. Curr. Opin. Immunol. 23: 35-40.
    • (2011) Curr. Opin. Immunol , vol.23 , pp. 35-40
    • Martinon, F.1    Glimcher, L.H.2
  • 3
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S., S. Uematsu, and O. Takeuchi. 2006. Pathogen recognition and innate immunity. Cell 124: 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 4
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors
    • Kawai, T., and S. Akira. 2010. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol. 11: 373-384.
    • (2010) Nat. Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 5
    • 68849085894 scopus 로고    scopus 로고
    • A cell biological view of Toll-like receptor function: Regulation through compartmentalization
    • Barton, G. M., and J. C. Kagan. 2009. A cell biological view of Toll-like receptor function: regulation through compartmentalization. Nat. Rev. Immunol. 9: 535-542.
    • (2009) Nat. Rev. Immunol , vol.9 , pp. 535-542
    • Barton, G.M.1    Kagan, J.C.2
  • 6
    • 34247484007 scopus 로고    scopus 로고
    • The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling
    • Brinkmann, M. M., E. Spooner, K. Hoebe, B. Beutler, H. L. Ploegh, and Y. M. Kim. 2007. The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9 is crucial for TLR signaling. J. Cell Biol. 177: 265-275.
    • (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
  • 7
    • 40749098665 scopus 로고    scopus 로고
    • UNC93B1 delivers nucleotide-sensing Toll-like receptors to endolysosomes
    • Kim, Y. M., M. M. Brinkmann, M. E. Paquet, and H. L. Ploegh. 2008. UNC93B1 delivers nucleotide-sensing Toll-like receptors to endolysosomes. Nature 452: 234-238.
    • (2008) Nature , vol.452 , pp. 234-238
    • Kim, Y.M.1    Brinkmann, M.M.2    Paquet, M.E.3    Ploegh, H.L.4
  • 8
    • 67449136127 scopus 로고    scopus 로고
    • Unc93B1 biases Toll-like receptor responses to nucleic acid in dendritic cells toward DNA- but against RNA-sensing
    • Fukui, R., S. Saitoh, F. Matsumoto, H. Kozuka-Hata, M. Oyama, K. Tabeta, B. Beutler, and K. Miyake. 2009. Unc93B1 biases Toll-like receptor responses to nucleic acid in dendritic cells toward DNA- but against RNA-sensing. J. Exp. Med. 206: 1339-1350.
    • (2009) J. Exp. Med , vol.206 , pp. 1339-1350
    • Fukui, R.1    Saitoh, S.2    Matsumoto, F.3    Kozuka-Hata, H.4    Oyama, M.5    Tabeta, K.6    Beutler, B.7    Miyake, K.8
  • 9
  • 10
    • 33847260278 scopus 로고    scopus 로고
    • Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages
    • Yang, Y., B. Liu, J. Dai, P. K. Srivastava, D. J. Zammit, L. Lefrançois, and Z. Li. 2007. Heat shock protein gp96 is a master chaperone for Toll-like receptors and is important in the innate function of macrophages. Immunity 26: 215-226.
    • (2007) Immunity , vol.26 , pp. 215-226
    • Yang, Y.1    Liu, B.2    Dai, J.3    Srivastava, P.K.4    Zammit, D.J.5    Lefrançois, L.6    Li, Z.7
  • 12
    • 53349178089 scopus 로고    scopus 로고
    • STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • Ishikawa, H., and G. N. Barber. 2008. STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature 455: 674-678.
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 13
    • 70349943834 scopus 로고    scopus 로고
    • STING regulates intracellular DNA-mediated, type i interferon-dependent innate immunity
    • Ishikawa, H., Z. Ma, and G. N. Barber. 2009. STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity. Nature 461: 788-792.
    • (2009) Nature , vol.461 , pp. 788-792
    • Ishikawa, H.1    Ma, Z.2    Barber, G.N.3
  • 14
    • 84873724533 scopus 로고    scopus 로고
    • Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA
    • Wu, J., L. Sun, X. Chen, F. Du, H. Shi, C. Chen, and Z. J. Chen. 2013. Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA. Science 339: 826-830.
    • (2013) Science , vol.339 , pp. 826-830
    • Wu, J.1    Sun, L.2    Chen, X.3    Du, F.4    Shi, H.5    Chen, C.6    Chen, Z.J.7
  • 15
    • 84873711885 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type i interferon pathway
    • Sun, L., J. Wu, F. Du, X. Chen, and Z. J. Chen. 2013. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 339: 786-791.
    • (2013) Science , vol.339 , pp. 786-791
    • Sun, L.1    Wu, J.2    Du, F.3    Chen, X.4    Chen, Z.J.5
  • 17
    • 0034719371 scopus 로고    scopus 로고
    • Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein
    • GrandPré, T., F. Nakamura, T. Vartanian, and S. M. Strittmatter. 2000. Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein. Nature 403: 439-444.
    • (2000) Nature , vol.403 , pp. 439-444
    • Grandpré, T.1    Nakamura, F.2    Vartanian, T.3    Strittmatter, S.M.4
  • 18
  • 19
    • 0036582979 scopus 로고    scopus 로고
    • Patterns of Nogo mRNA and protein expression in the developing and adult rat and after CNS lesions
    • Huber, A. B., O. Weinmann, C. Brösamle, T. Oertle, and M. E. Schwab. 2002. Patterns of Nogo mRNA and protein expression in the developing and adult rat and after CNS lesions. J. Neurosci. 22: 3553-3567.
    • (2002) J. Neurosci , vol.22 , pp. 3553-3567
    • Huber, A.B.1    Weinmann, O.2    Brösamle, C.3    Oertle, T.4    Schwab, M.E.5
  • 20
    • 0035905799 scopus 로고    scopus 로고
    • Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration
    • Fournier, A. E., T. GrandPre, and S. M. Strittmatter. 2001. Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration. Nature 409: 341-346.
    • (2001) Nature , vol.409 , pp. 341-346
    • Fournier, A.E.1    Grandpre, T.2    Strittmatter, S.M.3
  • 21
    • 33746308062 scopus 로고    scopus 로고
    • Glial inhibition of CNS axon regeneration
    • Yiu, G., and Z. He. 2006. Glial inhibition of CNS axon regeneration. Nat. Rev. Neurosci. 7: 617-627.
    • (2006) Nat. Rev. Neurosci , vol.7 , pp. 617-627
    • Yiu, G.1    He, Z.2
  • 22
    • 70849085134 scopus 로고    scopus 로고
    • Central nervous system regeneration inhibitors and their intracellular substrates
    • Nash, M., H. Pribiag, A. E. Fournier, and C. Jacobson. 2009. Central nervous system regeneration inhibitors and their intracellular substrates. Mol. Neurobiol. 40: 224-235.
    • (2009) Mol. Neurobiol , vol.40 , pp. 224-235
    • Nash, M.1    Pribiag, H.2    Fournier, A.E.3    Jacobson, C.4
  • 24
    • 0030912094 scopus 로고    scopus 로고
    • A novel pair of immunoglobulin-like receptors expressed by B cells and myeloid cells
    • Kubagawa, H., P. D. Burrows, and M. D. Cooper. 1997. A novel pair of immunoglobulin-like receptors expressed by B cells and myeloid cells. Proc. Natl. Acad. Sci. USA 94: 5261-5266.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5261-5266
    • Kubagawa, H.1    Burrows, P.D.2    Cooper, M.D.3
  • 26
    • 78649418605 scopus 로고    scopus 로고
    • Epithelial reticulon 4B (Nogo-B) is an endogenous regulator of Th2-driven lung inflammation
    • Wright, P. L., J. Yu, Y. P. Di, R. J. Homer, G. Chupp, J. A. Elias, L. Cohn, and W. C. Sessa. 2010. Epithelial reticulon 4B (Nogo-B) is an endogenous regulator of Th2-driven lung inflammation. J. Exp. Med. 207: 2595-2607.
    • (2010) J. Exp. Med , vol.207 , pp. 2595-2607
    • Wright, P.L.1    Yu, J.2    Di, Y.P.3    Homer, R.J.4    Chupp, G.5    Elias, J.A.6    Cohn, L.7    Sessa, W.C.8
  • 27
    • 79951827653 scopus 로고    scopus 로고
    • Endothelial reticulon-4B (Nogo-B) regulates ICAM-1-mediated leukocyte transmigration and acute inflammation
    • Di Lorenzo, A., T. D. Manes, A. Davalos, P. L. Wright, and W. C. Sessa. 2011. Endothelial reticulon-4B (Nogo-B) regulates ICAM-1-mediated leukocyte transmigration and acute inflammation. Blood 117: 2284-2295.
    • (2011) Blood , vol.117 , pp. 2284-2295
    • Di Lorenzo, A.1    Manes, T.D.2    Davalos, A.3    Wright, P.L.4    Sessa, W.C.5
  • 28
    • 79960386328 scopus 로고    scopus 로고
    • Differential but competitive binding of Nogo protein and class i major histocompatibility complex (MHCI) to the PIR-B ectodomain provides an inhibition of cells
    • Matsushita, H., S. Endo, E. Kobayashi, Y. Sakamoto, K. Kobayashi, K. Kitaguchi, K. Kuroki, A. Söderhäll, K. Maenaka, A. Nakamura, et al. 2011. Differential but competitive binding of Nogo protein and class i major histocompatibility complex (MHCI) to the PIR-B ectodomain provides an inhibition of cells. J. Biol. Chem. 286: 25739-25747.
    • (2011) J. Biol. Chem , vol.286 , pp. 25739-25747
    • Matsushita, H.1    Endo, S.2    Kobayashi, E.3    Sakamoto, Y.4    Kobayashi, K.5    Kitaguchi, K.6    Kuroki, K.7    Söderhäll, A.8    Maenaka, K.9    Nakamura, A.10
  • 29
    • 17144371344 scopus 로고    scopus 로고
    • A novel mitochondrial protein DIP mediates E2F1-induced apoptosis independently of p53
    • Stanelle, J., H. Tu-Rapp, and B. M. Pützer. 2005. A novel mitochondrial protein DIP mediates E2F1-induced apoptosis independently of p53. Cell Death Differ. 12: 347-357.
    • (2005) Cell Death Differ , vol.12 , pp. 347-357
    • Stanelle, J.1    Tu-Rapp, H.2    Pützer, B.M.3
  • 30
    • 79954423424 scopus 로고    scopus 로고
    • GRAMD4 mimics p53 and mediates the apoptotic function of p73 at mitochondria
    • John, K., V. Alla, C. Meier, and B. M. Pützer. 2011. GRAMD4 mimics p53 and mediates the apoptotic function of p73 at mitochondria. Cell Death Differ. 18: 874-886.
    • (2011) Cell Death Differ , vol.18 , pp. 874-886
    • John, K.1    Alla, V.2    Meier, C.3    Pützer, B.M.4
  • 31
    • 0028168798 scopus 로고
    • Three NF-k B binding sites in the human E-selectin gene required for maximal tumor necrosis factor a-induced expression
    • Schindler, U., and V. R. Baichwal. 1994. Three NF-k B binding sites in the human E-selectin gene required for maximal tumor necrosis factor a-induced expression. Mol. Cell. Biol. 14: 5820-5831.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 5820-5831
    • Schindler, U.1    Baichwal, V.R.2
  • 33
    • 0037225041 scopus 로고    scopus 로고
    • Genomic structure and functional characterisation of the promoters of human and mouse nogo/rtn4
    • Oertle, T., C. Huber, H. van der Putten, and M. E. Schwab. 2003. Genomic structure and functional characterisation of the promoters of human and mouse nogo/rtn4. J. Mol. Biol. 325: 299-323.
    • (2003) J. Mol. Biol , vol.325 , pp. 299-323
    • Oertle, T.1    Huber, C.2    Putten Der H.Van3    Schwab, M.E.4
  • 35
    • 0742289969 scopus 로고    scopus 로고
    • Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9
    • Takeshita, F., I. Gursel, K. J. Ishii, K. Suzuki, M. Gursel, and D. M. Klinman. 2004. Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9. Semin. Immunol. 16: 17-22.
    • (2004) Semin. Immunol , vol.16 , pp. 17-22
    • Takeshita, F.1    Gursel, I.2    Ishii, K.J.3    Suzuki, K.4    Gursel, M.5    Klinman, D.M.6
  • 36
    • 84870871486 scopus 로고    scopus 로고
    • Designing a type i interferon signaling phagosome
    • Blander, J. M. 2012. Designing a type I interferon signaling phagosome. Immunity 37: 947-949.
    • (2012) Immunity , vol.37 , pp. 947-949
    • Blander, J.M.1
  • 37
    • 76149126141 scopus 로고    scopus 로고
    • Pincher-generated Nogo-A endosomes mediate growth cone collapse and retrograde signaling
    • Joset, A., D. A. Dodd, S. Halegoua, and M. E. Schwab. 2010. Pincher-generated Nogo-A endosomes mediate growth cone collapse and retrograde signaling. J. Cell Biol. 188: 271-285.
    • (2010) J. Cell Biol , vol.188 , pp. 271-285
    • Joset, A.1    Dodd, D.A.2    Halegoua, S.3    Schwab, M.E.4
  • 39
    • 70449377144 scopus 로고    scopus 로고
    • Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis
    • Yang, Y. S., N. Y. Harel, and S. M. Strittmatter. 2009. Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis. J. Neurosci. 29: 13850-13859.
    • (2009) J. Neurosci , vol.29 , pp. 13850-13859
    • Yang, Y.S.1    Harel, N.Y.2    Strittmatter, S.M.3
  • 40
    • 41949122637 scopus 로고    scopus 로고
    • Reticulon RTN2B regulates trafficking and function of neuronal glutamate transporter EAAC1
    • Liu, Y., S. Vidensky, A. M. Ruggiero, S. Maier, H. H. Sitte, and J. D. Rothstein. 2008. Reticulon RTN2B regulates trafficking and function of neuronal glutamate transporter EAAC1. J. Biol. Chem. 283: 6561-6571.
    • (2008) J. Biol. Chem , vol.283 , pp. 6561-6571
    • Liu, Y.1    Vidensky, S.2    Ruggiero, A.M.3    Maier, S.4    Sitte, H.H.5    Rothstein, J.D.6
  • 42
    • 80055025138 scopus 로고    scopus 로고
    • Arabidopsis RTNLB1 and RTNLB2 Reticulon-like proteins regulate intracellular trafficking and activity of the FLS2 immune receptor
    • Lee, H. Y., C. H. Bowen, G. V. Popescu, H. G. Kang, N. Kato, S. Ma, S. Dinesh-Kumar, M. Snyder, and S. C. Popescu. 2011. Arabidopsis RTNLB1 and RTNLB2 Reticulon-like proteins regulate intracellular trafficking and activity of the FLS2 immune receptor. Plant Cell 23: 3374-3391.
    • (2011) Plant Cell , vol.23 , pp. 3374-3391
    • Lee, H.Y.1    Bowen, C.H.2    Popescu, G.V.3    Kang, H.G.4    Kato, N.5    Ma, S.6    Dinesh-Kumar, S.7    Snyder, M.8    Popescu, S.C.9
  • 43
    • 0033592854 scopus 로고    scopus 로고
    • Constitutive tyrosine phosphorylation of the inhibitory paired Ig-like receptor PIR-B
    • Ho, L. H., T. Uehara, C. C. Chen, H. Kubagawa, and M. D. Cooper. 1999. Constitutive tyrosine phosphorylation of the inhibitory paired Ig-like receptor PIR-B. Proc. Natl. Acad. Sci. USA 96: 15086-15090.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 15086-15090
    • Ho, L.H.1    Uehara, T.2    Chen, C.C.3    Kubagawa, H.4    Cooper, M.D.5
  • 44
    • 0033535614 scopus 로고    scopus 로고
    • Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1
    • Maeda, A., A. M. Scharenberg, S. Tsukada, J. B. Bolen, J. P. Kinet, and T. Kurosaki. 1999. Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1. Oncogene 18: 2291-2297.
    • (1999) Oncogene , vol.18 , pp. 2291-2297
    • Maeda, A.1    Scharenberg, A.M.2    Tsukada, S.3    Bolen, J.B.4    Kinet, J.P.5    Kurosaki, T.6
  • 45
    • 69549129469 scopus 로고    scopus 로고
    • Augmented TLR9-induced Btk activation in PIR-B-deficient B-1 cells provokes excessive autoantibody production and autoimmunity
    • Kubo, T., Y. Uchida, Y. Watanabe, M. Abe, A. Nakamura, M. Ono, S. Akira, and T. Takai. 2009. Augmented TLR9-induced Btk activation in PIR-B-deficient B-1 cells provokes excessive autoantibody production and autoimmunity. J. Exp. Med. 206: 1971-1982.
    • (2009) J. Exp. Med , vol.206 , pp. 1971-1982
    • Kubo, T.1    Uchida, Y.2    Watanabe, Y.3    Abe, M.4    Nakamura, A.5    Ono, M.6    Akira, S.7    Takai, T.8
  • 47
    • 69949092735 scopus 로고    scopus 로고
    • Polar Mapper: A computational tool for integrated visualization of protein interaction networks and mRNA expression data
    • Gonçalves, J. P., M. Grãos, and A. X. Valente. 2009. Polar Mapper: a computational tool for integrated visualization of protein interaction networks and mRNA expression data. J. R. Soc. Interface 6: 881-896.
    • (2009) J. R. Soc. Interface , vol.6 , pp. 881-896
    • Gonçalves, J.P.1    Grãos, M.2    Valente, A.X.3
  • 49
    • 0037119581 scopus 로고    scopus 로고
    • Myelinassociated glycoprotein as a functional ligand for the Nogo-66 receptor
    • Liu, B. P., A. Fournier, T. GrandPré, and S. M. Strittmatter. 2002. Myelinassociated glycoprotein as a functional ligand for the Nogo-66 receptor. Science 297: 1190-1193.
    • (2002) Science , vol.297 , pp. 1190-1193
    • Liu, B.P.1    Fournier, A.2    Grandpré, T.3    Strittmatter, S.M.4
  • 50
    • 0037182860 scopus 로고    scopus 로고
    • Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that inhibits neurite outgrowth
    • Wang, K. C., V. Koprivica, J. A. Kim, R. Sivasankaran, Y. Guo, R. L. Neve, and Z. He. 2002. Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that inhibits neurite outgrowth. Nature 417: 941-944.
    • (2002) Nature , vol.417 , pp. 941-944
    • Wang, K.C.1    Koprivica, V.2    Kim, J.A.3    Sivasankaran, R.4    Guo, Y.5    Neve, R.L.6    He, Z.7
  • 51
    • 78650511371 scopus 로고    scopus 로고
    • Functions of Nogo proteins and their receptors in the nervous system
    • Schwab, M. E. 2010. Functions of Nogo proteins and their receptors in the nervous system. Nat. Rev. Neurosci. 11: 799-811.
    • (2010) Nat. Rev. Neurosci , vol.11 , pp. 799-811
    • Schwab, M.E.1
  • 52
    • 34547953017 scopus 로고    scopus 로고
    • Lysosome-associated small Rab GTPase Rab7b negatively regulates TLR4 signaling in macrophages by promoting lysosomal degradation of TLR4
    • Wang, Y., T. Chen, C. Han, D. He, H. Liu, H. An, Z. Cai, and X. Cao. 2007. Lysosome-associated small Rab GTPase Rab7b negatively regulates TLR4 signaling in macrophages by promoting lysosomal degradation of TLR4. Blood 110: 962-971.
    • (2007) Blood , vol.110 , pp. 962-971
    • Wang, Y.1    Chen, T.2    Han, C.3    He, D.4    Liu, H.5    An, H.6    Cai, Z.7    Cao, X.8
  • 53
    • 77956358594 scopus 로고    scopus 로고
    • Ras-related protein Rab10 facilitates TLR4 signaling by promoting replenishment of TLR4 onto the plasma membrane
    • Wang, D., J. Lou, C. Ouyang, W. Chen, Y. Liu, X. Liu, X. Cao, J. Wang, and L. Lu. 2010. Ras-related protein Rab10 facilitates TLR4 signaling by promoting replenishment of TLR4 onto the plasma membrane. Proc. Natl. Acad. Sci. USA 107: 13806-13811.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 13806-13811
    • Wang, D.1    Lou, J.2    Ouyang, C.3    Chen, W.4    Liu, Y.5    Liu, X.6    Cao, X.7    Wang, J.8    Lu, L.9
  • 54
    • 84881559292 scopus 로고    scopus 로고
    • UNC93B1 mediates differential trafficking of endosomal TLRs
    • Lee, B. L., J. E. Moon, J. H. Shu, L. Yuan, Z. R. Newman, R. Schekman, and G. M. Barton. 2013. UNC93B1 mediates differential trafficking of endosomal TLRs. eLife 2: e00291. Available at: http://elifesciences.org/content/2/e00291.
    • (2013) ELife , vol.2
    • Lee, B.L.1    Moon, J.E.2    Shu, J.H.3    Yuan, L.4    Newman, Z.R.5    Schekman, R.6    Barton, G.M.7
  • 55
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
    • Allan, B. B., B. D. Moyer, and W. E. Balch. 2000. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 289: 444-448.
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 56
    • 20544455617 scopus 로고    scopus 로고
    • Golgins and GTPases, giving identity and structure to the Golgi apparatus
    • Short, B., A. Haas, and F. A. Barr. 2005. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim. Biophys. Acta 1744: 383-395.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 383-395
    • Short, B.1    Haas, A.2    Barr, F.A.3
  • 57
    • 0034306454 scopus 로고    scopus 로고
    • GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins
    • Doerks, T., M. Strauss, M. Brendel, and P. Bork. 2000. GRAM, a novel domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Trends Biochem. Sci. 25: 483-485.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 483-485
    • Doerks, T.1    Strauss, M.2    Brendel, M.3    Bork, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.