메뉴 건너뛰기




Volumn 2014, Issue , 2014, Pages

Current understanding on the role of standard and immunoproteasomes in inflammatory/immunological pathways of multiple sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; PROTEASOME INHIBITOR;

EID: 84893204344     PISSN: None     EISSN: 20900430     Source Type: Journal    
DOI: 10.1155/2014/739705     Document Type: Review
Times cited : (29)

References (127)
  • 1
    • 33644607018 scopus 로고    scopus 로고
    • Multiple sclerosis. The plaque and its pathogenesis
    • 2-s2.0-33644607018 10.1056/NEJMra052130
    • Frohman E. M., Racke M. K., Raine C. S., Multiple sclerosis. The plaque and its pathogenesis. The New England Journal of Medicine 2006 354 9 942 955 2-s2.0-33644607018 10.1056/NEJMra052130
    • (2006) The New England Journal of Medicine , vol.354 , Issue.9 , pp. 942-955
    • Frohman, E.M.1    Racke, M.K.2    Raine, C.S.3
  • 3
    • 54149084585 scopus 로고    scopus 로고
    • Multiple sclerosis
    • 2-s2.0-54149084585 10.1016/S0140-6736(08)61620-7
    • Compston A., Coles A., Multiple sclerosis. The Lancet 2008 372 9648 1502 1517 2-s2.0-54149084585 10.1016/S0140-6736(08)61620-7
    • (2008) The Lancet , vol.372 , Issue.9648 , pp. 1502-1517
    • Compston, A.1    Coles, A.2
  • 4
    • 34248364052 scopus 로고    scopus 로고
    • Multiple sclerosis: The environment and causation
    • DOI 10.1097/WCO.0b013e32815610c2, PII 0001905220070600000004
    • Giovannoni G., Ebers G., Multiple sclerosis: the environment and causation. Current Opinion in Neurology 2007 20 3 261 268 2-s2.0-34248364052 10.1097/WCO.0b013e32815610c2 (Pubitemid 46743106)
    • (2007) Current Opinion in Neurology , vol.20 , Issue.3 , pp. 261-268
    • Giovannoni, G.1    Ebers, G.2
  • 6
    • 67349179231 scopus 로고    scopus 로고
    • From genes to function: The next challenge to understanding multiple sclerosis
    • 2-s2.0-67349179231 10.1038/nri2554
    • Fugger L., Friese M. A., Bell J. I., From genes to function: the next challenge to understanding multiple sclerosis. Nature Reviews Immunology 2009 9 6 408 417 2-s2.0-67349179231 10.1038/nri2554
    • (2009) Nature Reviews Immunology , vol.9 , Issue.6 , pp. 408-417
    • Fugger, L.1    Friese, M.A.2    Bell, J.I.3
  • 7
    • 48249139449 scopus 로고    scopus 로고
    • Multiple sclerosis: An immune or neurodegenerative disorder?
    • 2-s2.0-48249139449 10.1146/annurev.neuro.30.051606.094313
    • Trapp B. D., Nave K.-A., Multiple sclerosis: an immune or neurodegenerative disorder? Annual Review of Neuroscience 2008 31 247 269 2-s2.0-48249139449 10.1146/annurev.neuro.30.051606.094313
    • (2008) Annual Review of Neuroscience , vol.31 , pp. 247-269
    • Trapp, B.D.1    Nave, K.-A.2
  • 8
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: From protein degradation and immune surveillance to cancer therapy
    • 2-s2.0-33847066706 10.1042/BST0350012
    • Goldberg A. L., Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochemical Society Transactions 2007 35 1 12 17 2-s2.0-33847066706 10.1042/BST0350012
    • (2007) Biochemical Society Transactions , vol.35 , Issue.1 , pp. 12-17
    • Goldberg, A.L.1
  • 9
    • 38449099679 scopus 로고    scopus 로고
    • Role of proteasomes in disease
    • DOI 10.1186/1471-2091-8-S1-S3
    • Dahlmann B., Role of proteasomes in disease. BMC Biochemistry 2007 8 1, article S3 2-s2.0-38449099679 10.1186/1471-2091-8-S1-S3 (Pubitemid 351814004)
    • (2007) BMC Biochemistry , vol.8 , Issue.SUPPL. 1
    • Dahlmann, B.1
  • 11
    • 84864357735 scopus 로고    scopus 로고
    • Emerging roles of immunoproteasomes beyond MHC class i antigen processing
    • 2-s2.0-84857479456 10.1007/s00018-012-0938-0
    • Ebstein F., Kloetzel P.-M., Krüger E., Seifert U., Emerging roles of immunoproteasomes beyond MHC class I antigen processing. Cellular and Molecular Life Sciences 2012 69 15 2543 2558 2-s2.0-84857479456 10.1007/s00018-012-0938-0
    • (2012) Cellular and Molecular Life Sciences , vol.69 , Issue.15 , pp. 2543-2558
    • Ebstein, F.1    Kloetzel, P.-M.2    Krüger, E.3    Seifert, U.4
  • 12
    • 80051978811 scopus 로고    scopus 로고
    • The predator becomes the prey: Regulating the ubiquitin system by ubiquitylation and degradation
    • 2-s2.0-80051978811 10.1038/nrm3173
    • Weissman A. M., Shabek N., Ciechanover A., The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation. Nature Reviews Molecular Cell Biology 2011 12 9 605 620 2-s2.0-80051978811 10.1038/nrm3173
    • (2011) Nature Reviews Molecular Cell Biology , vol.12 , Issue.9 , pp. 605-620
    • Weissman, A.M.1    Shabek, N.2    Ciechanover, A.3
  • 14
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • DOI 10.1146/annurev.biochem.68.1.1015
    • Voges D., Zwickl P., Baumeister W., The 26S proteasome: a molecular machine designed for controlled proteolysis. Annual Review of Biochemistry 1999 68 1015 1068 2-s2.0-0032867676 10.1146/annurev.biochem.68.1.1015 (Pubitemid 29449214)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 15
    • 84860499027 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced neuroinflammation leads to the accumulation of ubiquitinated proteins and increases susceptibility to neurodegeneration induced by proteasome inhibition in rat hippocampus
    • 2-s2.0-84860499027 10.1186/1742-2094-9-87
    • Pintado C., Gavilán M. P., Gavilán E., García-Cuervo L., Gutiérrez A., Vitorica J., Castaño A., Ríos R. M., Ruano D., Lipopolysaccharide-induced neuroinflammation leads to the accumulation of ubiquitinated proteins and increases susceptibility to neurodegeneration induced by proteasome inhibition in rat hippocampus. Journal of Neuroinflammation 2012 9 1, article 87 2-s2.0-84860499027 10.1186/1742-2094-9-87
    • (2012) Journal of Neuroinflammation , vol.9 , Issue.1 ARTICLE 87
    • Pintado, C.1    Gavilán, M.P.2    Gavilán, E.3    García-Cuervo, L.4    Gutiérrez, A.5    Vitorica, J.6    Castaño, A.7    Ríos, R.M.8    Ruano, D.9
  • 17
    • 84866986070 scopus 로고    scopus 로고
    • Proteasome protease mediated regulation of cytokine induction and inflammation
    • Qureshi N., Morrison D. C., Reis J., Proteasome protease mediated regulation of cytokine induction and inflammation. Biochimica et Biophysica Acta 2012 1823 11 2087 2093
    • (2012) Biochimica et Biophysica Acta , vol.1823 , Issue.11 , pp. 2087-2093
    • Qureshi, N.1    Morrison, D.C.2    Reis, J.3
  • 18
    • 79952551776 scopus 로고    scopus 로고
    • Decreased activity of the 20S proteasome in the brain white matter and gray matter of patients with multiple schlerosis
    • 2-s2.0-79952551776 10.1111/j.1471-4159.2011.07182.x
    • Zheng J., Bizzozero O. A., Decreased activity of the 20S proteasome in the brain white matter and gray matter of patients with multiple schlerosis. Journal of Neurochemistry 2011 117 1 143 153 2-s2.0-79952551776 10.1111/j.1471-4159.2011.07182.x
    • (2011) Journal of Neurochemistry , vol.117 , Issue.1 , pp. 143-153
    • Zheng, J.1    Bizzozero, O.A.2
  • 23
    • 84859610057 scopus 로고    scopus 로고
    • Changes in 20S subunit composition are largely responsible for altered proteasomal activities in experimental autoimmune encephalomyelitis
    • 2-s2.0-84859610057 10.1111/j.1471-4159.2012.07699.x
    • Zheng J., Dasgupta A., Bizzozero O. A., Changes in 20S subunit composition are largely responsible for altered proteasomal activities in experimental autoimmune encephalomyelitis. Journal of Neurochemistry 2012 121 3 486 494 2-s2.0-84859610057 10.1111/j.1471-4159.2012.07699.x
    • (2012) Journal of Neurochemistry , vol.121 , Issue.3 , pp. 486-494
    • Zheng, J.1    Dasgupta, A.2    Bizzozero, O.A.3
  • 25
    • 78149477289 scopus 로고    scopus 로고
    • Reduced immunoproteasome formation and accumulation of immunoproteasomal precursors in the brains of lymphocytic choriomeningitis virus-infected mice
    • 2-s2.0-78149477289 10.4049/jimmunol.1001517
    • Kremer M., Henn A., Kolb C., Basler M., Moebius J., Guillaume B., Leist M., Van Den Eynde B. J., Groettrup M., Reduced immunoproteasome formation and accumulation of immunoproteasomal precursors in the brains of lymphocytic choriomeningitis virus-infected mice. Journal of Immunology 2010 185 9 5549 5560 2-s2.0-78149477289 10.4049/jimmunol.1001517
    • (2010) Journal of Immunology , vol.185 , Issue.9 , pp. 5549-5560
    • Kremer, M.1    Henn, A.2    Kolb, C.3    Basler, M.4    Moebius, J.5    Guillaume, B.6    Leist, M.7    Van Den Eynde, B.J.8    Groettrup, M.9
  • 28
    • 39449101794 scopus 로고    scopus 로고
    • Immunoproteasome in Macaca fascicularis: No age-dependent modification of abundance and activity in the brain and insight into an in silico structural model
    • DOI 10.1089/rej.2007.0559
    • Bellavista E., Mishto M., Santoro A., Bertoni-Freddari C., Sessions R. B., Franceschi C., Immunoproteasome in Macaca fascicularis: no age-dependent modification of abundance and activity in the brain and insight into an in silico structural model. Rejuvenation Research 2008 11 1 73 82 2-s2.0-39449101794 10.1089/rej.2007.0559 (Pubitemid 351271622)
    • (2008) Rejuvenation Research , vol.11 , Issue.1 , pp. 73-82
    • Bellavista, E.1    Mishto, M.2    Santoro, A.3    Bertoni-Freddari, C.4    Sessions, R.B.5    Franceschi, C.6
  • 29
    • 72949103056 scopus 로고    scopus 로고
    • Proteasomes in immune cells: More than peptide producers?
    • 2-s2.0-72949103056 10.1038/nri2687
    • Groettrup M., Kirk C. J., Basler M., Proteasomes in immune cells: more than peptide producers? Nature Reviews Immunology 2010 10 1 73 78 2-s2.0-72949103056 10.1038/nri2687
    • (2010) Nature Reviews Immunology , vol.10 , Issue.1 , pp. 73-78
    • Groettrup, M.1    Kirk, C.J.2    Basler, M.3
  • 30
    • 77953101405 scopus 로고    scopus 로고
    • Immunoproteasome deficiency alters retinal proteasome's response to stress
    • 2-s2.0-77953101405 10.1111/j.1471-4159.2010.06688.x
    • Hussong S. A., Kapphahn R. J., Phillips S. L., Maldonado M., Ferrington D. A., Immunoproteasome deficiency alters retinal proteasome's response to stress. Journal of Neurochemistry 2010 113 6 1481 1490 2-s2.0-77953101405 10.1111/j.1471-4159.2010.06688.x
    • (2010) Journal of Neurochemistry , vol.113 , Issue.6 , pp. 1481-1490
    • Hussong, S.A.1    Kapphahn, R.J.2    Phillips, S.L.3    Maldonado, M.4    Ferrington, D.A.5
  • 32
    • 84874787780 scopus 로고    scopus 로고
    • Immuno- and constitutive proteasomes do not differ in their abilities to degrade ubiquitinated proteins
    • Nathan J. A., Spinnenhirn V., Schmidtke G., Basler M., Groettrup M., Goldberg A. L., Immuno- and constitutive proteasomes do not differ in their abilities to degrade ubiquitinated proteins. Cell 152 5 1184 1194
    • Cell , vol.152 , Issue.5 , pp. 1184-1194
    • Nathan, J.A.1    Spinnenhirn, V.2    Schmidtke, G.3    Basler, M.4    Groettrup, M.5    Goldberg, A.L.6
  • 33
    • 23444434940 scopus 로고    scopus 로고
    • + T cells in multiple sclerosis: A new target for therapy?
    • DOI 10.1093/brain/awh578
    • Friese M. A., Fugger L., Autoreactive CD8+ T cells in multiple sclerosis: a new target for therapy? Brain 2005 128 8 1747 1763 2-s2.0-23444434940 10.1093/brain/awh578 (Pubitemid 41373647)
    • (2005) Brain , vol.128 , Issue.8 , pp. 1747-1763
    • Friese, M.A.1    Fugger, L.2
  • 34
    • 57149094667 scopus 로고    scopus 로고
    • NKT cell-dependent amelioration of a mouse model of multiple sclerosis by altering gut flora
    • 2-s2.0-57149094667 10.2353/ajpath.2008.080622
    • Yokote H., Miyake S., Croxford J. L., Oki S., Mizusawa H., Yamamura T., NKT cell-dependent amelioration of a mouse model of multiple sclerosis by altering gut flora. The American Journal of Pathology 2008 173 6 1714 1723 2-s2.0-57149094667 10.2353/ajpath.2008.080622
    • (2008) The American Journal of Pathology , vol.173 , Issue.6 , pp. 1714-1723
    • Yokote, H.1    Miyake, S.2    Croxford, J.L.3    Oki, S.4    Mizusawa, H.5    Yamamura, T.6
  • 36
    • 0032521030 scopus 로고    scopus 로고
    • MHC class I-restricted lysis of human oligodendrocytes by myelin basic protein peptide-specific CD8 T lymphocytes
    • Jurewicz A., Biddison W. E., Antel J. P., MHC class I-restricted lysis of human oligodendrocytes by myelin basic protein peptide-specific CD8 T lymphocytes. Journal of Immunology 1998 160 6 3056 3059 2-s2.0-0032521030 (Pubitemid 28136763)
    • (1998) Journal of Immunology , vol.160 , Issue.6 , pp. 3056-3059
    • Jurewicz, A.1    Biddison, W.E.2    Antel, J.P.3
  • 38
    • 80052679971 scopus 로고    scopus 로고
    • Proteasome immunosubunits protect against the development of CD8 T cell-mediated autoimmune diseases
    • 2-s2.0-80052679971 10.4049/jimmunol.1101003
    • Zaiss D. M. W., Bekker C. P. J., Gröne A., Lie B. A., Sijts A. J. A. M., Proteasome immunosubunits protect against the development of CD8 T cell-mediated autoimmune diseases. Journal of Immunology 2011 187 5 2302 2309 2-s2.0-80052679971 10.4049/jimmunol.1101003
    • (2011) Journal of Immunology , vol.187 , Issue.5 , pp. 2302-2309
    • Zaiss, D.M.W.1    Bekker, C.P.J.2    Gröne, A.3    Lie, B.A.4    Sijts, A.J.A.M.5
  • 39
    • 33745104765 scopus 로고    scopus 로고
    • Increased frequency and broadened specificity of latent EBV nuclear antigen-1-specific T cells in multiple sclerosis
    • DOI 10.1093/brain/awl067
    • Lünemann J. D., Edwards N., Muraro P. A., Hayashi S., Cohen J. I., Münz C., Martin R., Increased frequency and broadened specificity of latent EBV nuclear antigen-1-specific T cells in multiple sclerosis. Brain 2006 129 6 1493 1506 2-s2.0-33745104765 10.1093/brain/awl067 (Pubitemid 43999382)
    • (2006) Brain , vol.129 , Issue.6 , pp. 1493-1506
    • Lunemann, J.D.1    Edwards, N.2    Muraro, P.A.3    Hayashi, S.4    Cohen, J.I.5    Munz, C.6    Martin, R.7
  • 41
    • 0347997289 scopus 로고    scopus 로고
    • + T cell responses to selected Epstein-Barr virus immunodominant epitopes in patients with multiple sclerosis
    • DOI 10.1046/j.1365-2249.2003.02114.x
    • Höllsberg P., Hansen H. J., Haahr S., Altered CD8+ T cell responses to selected Epstein-Barr virus immunodominant epitopes in patients with multiple sclerosis. Clinical and Experimental Immunology 2003 132 1 137 143 2-s2.0-0347997289 10.1046/j.1365-2249.2003.02114.x (Pubitemid 36418916)
    • (2003) Clinical and Experimental Immunology , vol.132 , Issue.1 , pp. 137-143
    • Hollsberg, P.1    Hansen, H.J.2    Haahr, S.3
  • 42
    • 18244378502 scopus 로고    scopus 로고
    • Identification of Epstein-Barr virus proteins as putative targets of the immune response in multiple sclerosis
    • DOI 10.1172/JCI200523661
    • Cepok S., Zhou D., Srivastava R., Nessler S., Stei S., Büssow K., Sommer N., Hemmer B., Identification of Epstein-Barr virus proteins as putative targets of the immune response in multiple sclerosis. Journal of Clinical Investigation 2005 115 5 1352 1360 2-s2.0-18244378502 10.1172/JCI200523661 (Pubitemid 40629055)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.5 , pp. 1352-1360
    • Cepok, S.1    Zhou, D.2    Srivastava, R.3    Nessler, S.4    Stei, S.5    Bussow, K.6    Sommer, N.7    Hemmer, B.8
  • 45
    • 77951926376 scopus 로고    scopus 로고
    • Splicing of distant peptide fragments occurs in the proteasome by transpeptidation and produces the spliced antigenic peptide derived from fibroblast growth factor-5
    • 2-s2.0-77951926376 10.4049/jimmunol.0901277
    • Dalet A., Vigneron N., Stroobant V., Hanada K.-I., Van Den Eynde B. J., Splicing of distant peptide fragments occurs in the proteasome by transpeptidation and produces the spliced antigenic peptide derived from fibroblast growth factor-5. Journal of Immunology 2010 184 6 3016 3024 2-s2.0-77951926376 10.4049/jimmunol.0901277
    • (2010) Journal of Immunology , vol.184 , Issue.6 , pp. 3016-3024
    • Dalet, A.1    Vigneron, N.2    Stroobant, V.3    Hanada, K.-I.4    Van Den Eynde, B.J.5
  • 48
    • 1642512398 scopus 로고    scopus 로고
    • Protein surgery
    • DOI 10.1038/427203a
    • Rammensee H.-G., Protein surgery. Nature 2004 427 6971 203 204 2-s2.0-1642512398 10.1038/427203a (Pubitemid 38112021)
    • (2004) Nature , vol.427 , Issue.6971 , pp. 203-204
    • Rammensee, H.-G.1
  • 49
    • 34447570906 scopus 로고    scopus 로고
    • The perivascular space as a path of hematopoietic progenitor cells and mature T cells between the blood circulation and the thymic parenchyma
    • DOI 10.1093/intimm/dxm041
    • Mori K., Itoi M., Tsukamoto N., Kubo H., Amagai T., The perivascular space as a path of hematopoietic progenitor cells and mature T cells between the blood circulation and the thymic parenchyma. International Immunology 2007 19 6 745 753 2-s2.0-34447570906 10.1093/intimm/dxm041 (Pubitemid 47073264)
    • (2007) International Immunology , vol.19 , Issue.6 , pp. 745-753
    • Mori, K.1    Itoi, M.2    Tsukamoto, N.3    Kubo, H.4    Amagai, T.5
  • 50
    • 33646577466 scopus 로고    scopus 로고
    • Reciprocal developmental pathways for the generation of pathogenic effector TH17 and regulatory T cells
    • 2-s2.0-33646577466 10.1038/nature04753
    • Bettelli E., Carrier Y., Gao W., Korn T., Strom T. B., Oukka M., Weiner H. L., Kuchroo V. K., Reciprocal developmental pathways for the generation of pathogenic effector TH17 and regulatory T cells. Nature 2006 441 7090 235 238 2-s2.0-33646577466 10.1038/nature04753
    • (2006) Nature , vol.441 , Issue.7090 , pp. 235-238
    • Bettelli, E.1    Carrier, Y.2    Gao, W.3    Korn, T.4    Strom, T.B.5    Oukka, M.6    Weiner, H.L.7    Kuchroo, V.K.8
  • 51
    • 84862695017 scopus 로고    scopus 로고
    • Th17 cells: Biology, pathogenesis of autoimmune and inflammatory diseases, and therapeutic strategies
    • Maddur M. S., Miossec P., Kaveri S. V., Bayry J., Th17 cells: biology, pathogenesis of autoimmune and inflammatory diseases, and therapeutic strategies. The American Journal of Pathology 2012 181 1 8 18
    • (2012) The American Journal of Pathology , vol.181 , Issue.1 , pp. 8-18
    • Maddur, M.S.1    Miossec, P.2    Kaveri, S.V.3    Bayry, J.4
  • 52
    • 38749143286 scopus 로고    scopus 로고
    • Interleukin-17 production in central nervous system-infiltrating T cells and glial cells is associated with active disease in multiple sclerosis
    • DOI 10.2353/ajpath.2008.070690
    • Tzartos J. S., Friese M. A., Craner M. J., Palace J., Newcombe J., Esiri M. M., Fugger L., Interleukin-17 production in central nervous system-infiltrating T cells and glial cells is associated with active disease in multiple sclerosis. The American Journal of Pathology 2008 172 1 146 155 2-s2.0-38749143286 10.2353/ajpath.2008.070690 (Pubitemid 351186376)
    • (2008) American Journal of Pathology , vol.172 , Issue.1 , pp. 146-155
    • Tzartos, J.S.1    Friese, M.A.2    Craner, M.J.3    Palace, J.4    Newcombe, J.5    Esiri, M.M.6    Fugger, L.7
  • 53
    • 42249114634 scopus 로고    scopus 로고
    • + CXC chemokine pathway is essential for the development of central nervous system autoimmune disease
    • DOI 10.1084/jem.20072404
    • Carlson T., Kroenke M., Rao P., Lane T. E., Segal B., The Th17-ELR+ CXC chemokine pathway is essential for the development of central nervous system autoimmune disease. Journal of Experimental Medicine 2008 205 4 811 823 2-s2.0-42249114634 10.1084/jem.20072404 (Pubitemid 351549880)
    • (2008) Journal of Experimental Medicine , vol.205 , Issue.4 , pp. 811-823
    • Carlson, T.1    Kroenke, M.2    Rao, P.3    Lane, T.E.4    Segal, B.5
  • 55
    • 33745321276 scopus 로고    scopus 로고
    • IL-17 plays an important role in the development of experimental autoimmune encephalomyelitis
    • Komiyama Y., Nakae S., Matsuki T., Nambu A., Ishigame H., Kakuta S., Sudo K., Iwakura Y., IL-17 plays an important role in the development of experimental autoimmune encephalomyelitis. Journal of Immunology 2006 177 1 566 573 2-s2.0-33745321276 (Pubitemid 43939170)
    • (2006) Journal of Immunology , vol.177 , Issue.1 , pp. 566-573
    • Komiyama, Y.1    Nakae, S.2    Matsuki, T.3    Nambu, A.4    Ishigame, H.5    Kakuta, S.6    Sudo, K.7    Iwakura, Y.8
  • 57
    • 84862703353 scopus 로고    scopus 로고
    • Commensal gut flora and brain autoimmunity: A love or hate affair?
    • 2-s2.0-84856604833 10.1007/s00401-012-0949-9
    • Berer K., Krishnamoorthy G., Commensal gut flora and brain autoimmunity: a love or hate affair? Acta Neuropathologica 2012 123 5 639 651 2-s2.0-84856604833 10.1007/s00401-012-0949-9
    • (2012) Acta Neuropathologica , vol.123 , Issue.5 , pp. 639-651
    • Berer, K.1    Krishnamoorthy, G.2
  • 58
    • 77949362543 scopus 로고    scopus 로고
    • 99th Dahlem Conference on Infection, Inflammation and Chronic Inflammatory Disorders: Psycho-neuroimmunology and the intestinal microbiota: Clinical observations and basic mechanisms
    • 2-s2.0-77949362543 10.1111/j.1365-2249.2010.04124.x
    • Bienenstock J., Collins S., 99th Dahlem Conference on Infection, Inflammation and Chronic Inflammatory Disorders: psycho-neuroimmunology and the intestinal microbiota: clinical observations and basic mechanisms. Clinical and Experimental Immunology 2010 160 1 85 91 2-s2.0-77949362543 10.1111/j.1365-2249. 2010.04124.x
    • (2010) Clinical and Experimental Immunology , vol.160 , Issue.1 , pp. 85-91
    • Bienenstock, J.1    Collins, S.2
  • 59
    • 84867845255 scopus 로고    scopus 로고
    • The interplay between the intestinal microbiota and the brain
    • Collins S. M., Surette M., Bercik P., The interplay between the intestinal microbiota and the brain. Nature Reviews Microbiology 2012 10 11 735 742
    • (2012) Nature Reviews Microbiology , vol.10 , Issue.11 , pp. 735-742
    • Collins, S.M.1    Surette, M.2    Bercik, P.3
  • 63
    • 84884133250 scopus 로고    scopus 로고
    • Biased Treg/Th17 balance away from regulatory toward inflammatory phenotype in relapsed multiple sclerosis and its correlation with severity of symptoms
    • Jamshidian A., Shaygannejad V., Pourazar A., Zarkesh-Esfahani S. H., Gharagozloo M., Biased Treg/Th17 balance away from regulatory toward inflammatory phenotype in relapsed multiple sclerosis and its correlation with severity of symptoms. Journal of Neuroimmunology 2013 262 1-2 106 112
    • (2013) Journal of Neuroimmunology , vol.262 , Issue.1-2 , pp. 106-112
    • Jamshidian, A.1    Shaygannejad, V.2    Pourazar, A.3    Zarkesh-Esfahani, S.H.4    Gharagozloo, M.5
  • 64
    • 77749322389 scopus 로고    scopus 로고
    • A novel probiotic mixture exerts a therapeutic effect on experimental autoimmune encephalomyelitis mediated by IL-10 producing regulatory T cells
    • 2-s2.0-77749322389 10.1371/journal.pone.0009009 e9009
    • Lavasani S., Dzhambazov B., Nouri M., Fåk F., Buske S., Molin G., Thorlacius H., Alenfall J., Jeppsson B., Weström B., A novel probiotic mixture exerts a therapeutic effect on experimental autoimmune encephalomyelitis mediated by IL-10 producing regulatory T cells. PLoS ONE 2010 5 2 2-s2.0-77749322389 10.1371/journal.pone.0009009 e9009
    • (2010) PLoS ONE , vol.5 , Issue.2
    • Lavasani, S.1    Dzhambazov, B.2    Nouri, M.3    Fåk, F.4    Buske, S.5    Molin, G.6    Thorlacius, H.7    Alenfall, J.8    Jeppsson, B.9    Weström, B.10
  • 65
    • 77249096486 scopus 로고    scopus 로고
    • Role of gut commensal microflora in the development of experimental autoimmune encephalomyelitis
    • 2-s2.0-77249096486 10.4049/jimmunol.0900747
    • Ochoa-Repáraz J., Mielcarz D. W., Ditrio L. E., Burroughs A. R., Foureau D. M., Haque-Begum S., Kasper L. H., Role of gut commensal microflora in the development of experimental autoimmune encephalomyelitis. Journal of Immunology 2009 183 10 6041 6050 2-s2.0-77249096486 10.4049/jimmunol.0900747
    • (2009) Journal of Immunology , vol.183 , Issue.10 , pp. 6041-6050
    • Ochoa-Repáraz, J.1    Mielcarz, D.W.2    Ditrio, L.E.3    Burroughs, A.R.4    Foureau, D.M.5    Haque-Begum, S.6    Kasper, L.H.7
  • 66
    • 77955913743 scopus 로고    scopus 로고
    • A polysaccharide from the human commensal Bacteroides fragilis protects against CNS demyelinating disease
    • 2-s2.0-77955913743 10.1038/mi.2010.29
    • Ochoa-Repáraz J., Mielcarz D. W., Wang Y., Begum-Haque S., Dasgupta S., Kasper D. L., Kasper L. H., A polysaccharide from the human commensal Bacteroides fragilis protects against CNS demyelinating disease. Mucosal Immunology 2010 3 5 487 495 2-s2.0-77955913743 10.1038/mi.2010.29
    • (2010) Mucosal Immunology , vol.3 , Issue.5 , pp. 487-495
    • Ochoa-Repáraz, J.1    Mielcarz, D.W.2    Wang, Y.3    Begum-Haque, S.4    Dasgupta, S.5    Kasper, D.L.6    Kasper, L.H.7
  • 67
    • 79952748674 scopus 로고    scopus 로고
    • Proinflammatory T-cell responses to gut microbiota promote experimental autoimmune encephalomyelitis
    • 2-s2.0-79952748674 10.1073/pnas.1000082107
    • Lee Y. K., Menezes J. S., Umesaki Y., Mazmanian S. K., Proinflammatory T-cell responses to gut microbiota promote experimental autoimmune encephalomyelitis. Proceedings of the National Academy of Sciences of the United States of America 2011 108 supplement 1 4615 4622 2-s2.0-79952748674 10.1073/pnas.1000082107
    • (2011) Proceedings of the National Academy of Sciences of the United States of America , vol.108 , Issue.SUPPLEMENT 1 , pp. 4615-4622
    • Lee, Y.K.1    Menezes, J.S.2    Umesaki, Y.3    Mazmanian, S.K.4
  • 68
    • 81855167104 scopus 로고    scopus 로고
    • Commensal microbiota and myelin autoantigen cooperate to trigger autoimmune demyelination
    • 2-s2.0-81855167104 10.1038/nature10554
    • Berer K., Mues M., Koutrolos M., AlRasbi Z., Boziki M., Johner C., Wekerle H., Krishnamoorthy G., Commensal microbiota and myelin autoantigen cooperate to trigger autoimmune demyelination. Nature 2011 479 7374 538 541 2-s2.0-81855167104 10.1038/nature10554
    • (2011) Nature , vol.479 , Issue.7374 , pp. 538-541
    • Berer, K.1    Mues, M.2    Koutrolos, M.3    Alrasbi, Z.4    Boziki, M.5    Johner, C.6    Wekerle, H.7    Krishnamoorthy, G.8
  • 70
    • 84867324545 scopus 로고    scopus 로고
    • Immunoproteasome subunit LMP7 deficiency and inhibition suppresses Th1 and Th17 but enhances regulatory T cell differentiation
    • Kalim K. W., Basler M., Kirk C. J., Groettrup M., Immunoproteasome subunit LMP7 deficiency and inhibition suppresses Th1 and Th17 but enhances regulatory T cell differentiation. Journal of Immunology 2012 189 8 4182 4193
    • (2012) Journal of Immunology , vol.189 , Issue.8 , pp. 4182-4193
    • Kalim, K.W.1    Basler, M.2    Kirk, C.J.3    Groettrup, M.4
  • 71
    • 33847381116 scopus 로고    scopus 로고
    • The fundamental basis of inflammatory bowel disease
    • DOI 10.1172/JCI30587
    • Strober W., Fuss I., Mannon P., The fundamental basis of inflammatory bowel disease. Journal of Clinical Investigation 2007 117 3 514 521 2-s2.0-33847381116 10.1172/JCI30587 (Pubitemid 46348505)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.3 , pp. 514-521
    • Strober, W.1    Fuss, I.2    Mannon, P.3
  • 72
    • 77954008149 scopus 로고    scopus 로고
    • Targeting the proteasome: Partial inhibition of the proteasome by bortezomib or deletion of the immunosubunit LMP7 attenuates experimental colitis
    • 2-s2.0-77954008149 10.1136/gut.2009.203554
    • Schmidt N., Gonzalez E., Visekruna A., Kühl A. A., Loddenkemper C., Mollenkopf H., Kaufmann S. H. E., Steinhoff U., Joeris T., Targeting the proteasome: partial inhibition of the proteasome by bortezomib or deletion of the immunosubunit LMP7 attenuates experimental colitis. Gut 2010 59 7 896 906 2-s2.0-77954008149 10.1136/gut.2009.203554
    • (2010) Gut , vol.59 , Issue.7 , pp. 896-906
    • Schmidt, N.1    Gonzalez, E.2    Visekruna, A.3    Kühl, A.A.4    Loddenkemper, C.5    Mollenkopf, H.6    Kaufmann, S.H.E.7    Steinhoff, U.8    Joeris, T.9
  • 73
    • 77956198116 scopus 로고    scopus 로고
    • Prevention of experimental colitis by a selective inhibitor of the immunoproteasome
    • 2-s2.0-77956198116 10.4049/jimmunol.0903182
    • Basler M., Dajee M., Moll C., Groettrup M., Kirk C. J., Prevention of experimental colitis by a selective inhibitor of the immunoproteasome. Journal of Immunology 2010 185 1 634 641 2-s2.0-77956198116 10.4049/jimmunol.0903182
    • (2010) Journal of Immunology , vol.185 , Issue.1 , pp. 634-641
    • Basler, M.1    Dajee, M.2    Moll, C.3    Groettrup, M.4    Kirk, C.J.5
  • 74
    • 46149083938 scopus 로고    scopus 로고
    • B-cells and humoral immunity in multiple sclerosis. Implications for therapy
    • DOI 10.1007/s12026-007-8009-6
    • Oh S., Cudrici C., Ito T., Rus H., B-cells and humoral immunity in multiple sclerosis. Implications for therapy. Immunologic Research 2008 40 3 224 234 2-s2.0-46149083938 10.1007/s12026-007-8009-6 (Pubitemid 351903819)
    • (2008) Immunologic Research , vol.40 , Issue.3 , pp. 224-234
    • Oh, S.1    Cudrici, C.2    Ito, T.3    Rus, H.4
  • 75
    • 79952024055 scopus 로고    scopus 로고
    • Therapeutic targeting of B cells for rheumatic autoimmune diseases
    • 2-s2.0-79952024055 10.1124/pr.109.002006
    • Engel P., Gómez-Puerta J. A., Ramos-Casals M., Lozano F., Bosch X., Therapeutic targeting of B cells for rheumatic autoimmune diseases. Pharmacological Reviews 2011 63 1 127 156 2-s2.0-79952024055 10.1124/pr.109.002006
    • (2011) Pharmacological Reviews , vol.63 , Issue.1 , pp. 127-156
    • Engel, P.1    Gómez-Puerta, J.A.2    Ramos-Casals, M.3    Lozano, F.4    Bosch, X.5
  • 76
    • 79956330472 scopus 로고    scopus 로고
    • B cell immunotherapy in autoimmunity: 2010 update
    • 2-s2.0-79956330472 10.1016/j.molimm.2010.11.021
    • Chan A. C., B cell immunotherapy in autoimmunity: 2010 update. Molecular Immunology 2011 48 11 1344 1347 2-s2.0-79956330472 10.1016/j.molimm.2010.11.021
    • (2011) Molecular Immunology , vol.48 , Issue.11 , pp. 1344-1347
    • Chan, A.C.1
  • 77
    • 2442708947 scopus 로고    scopus 로고
    • Detection of ectopic B-cell follicles with germinal centers in the meninges of patients with secondary progressive multiple sclerosis
    • Serafini B., Rosicarelli B., Magliozzi R., Stigliano E., Aloisi F., Detection of ectopic B-cell follicles with germinal centers in the meninges of patients with secondary progressive multiple sclerosis. Brain Pathology 2004 14 2 164 174 2-s2.0-2442708947 (Pubitemid 38656388)
    • (2004) Brain Pathology , vol.14 , Issue.2 , pp. 164-174
    • Serafini, B.1    Rosicarelli, B.2    Magliozzi, R.3    Stigliano, E.4    Aloisi, F.5
  • 78
    • 34248230257 scopus 로고    scopus 로고
    • Distinct effector cytokine profiles of memory and naive human B cell subsets and implication in multiple sclerosis
    • Duddy M., Niino M., Adatia F., Hebert S., Freedman M., Atkins H., Ho J. K., Bar-Or A., Distinct effector cytokine profiles of memory and naive human B cell subsets and implication in multiple sclerosis. Journal of Immunology 2007 178 10 6092 6099 2-s2.0-34248230257 (Pubitemid 46717389)
    • (2007) Journal of Immunology , vol.178 , Issue.10 , pp. 6092-6099
    • Duddy, M.1    Niino, M.2    Adatia, F.3    Hebert, S.4    Freedman, M.5    Atkins, H.6    Ho, J.K.7    Bar-Or, A.8
  • 82
    • 13444274684 scopus 로고    scopus 로고
    • Effect of rituximab on the peripheral blood and cerebrospinal fluid B cells in patients with primary progressive multiple sclerosis
    • DOI 10.1001/archneur.62.2.258
    • Monson N. L., Cravens P. D., Frohman E. M., Hawker K., Racke M. K., Effect of rituximab on the peripheral blood and cerebrospinal fluid B cells in patients with primary progressive multiple sclerosis. Archives of Neurology 2005 62 2 258 264 2-s2.0-13444274684 10.1001/archneur.62.2.258 (Pubitemid 40204747)
    • (2005) Archives of Neurology , vol.62 , Issue.2 , pp. 258-264
    • Monson, N.L.1    Cravens, P.D.2    Frohman, E.M.3    Hawker, K.4    Racke, M.K.5
  • 83
    • 81555202418 scopus 로고    scopus 로고
    • Ocrelizumab in relapsing-remitting multiple sclerosis: A phase 2, randomised, placebo-controlled, multicentre trial
    • 2-s2.0-81555202418 10.1016/S0140-6736(11)61649-8
    • Kappos L., Li D., Calabresi P. A., O'Connor P., Bar-Or A., Barkhof F., Yin M., Leppert D., Glanzman R., Tinbergen J., Hauser S. L., Ocrelizumab in relapsing-remitting multiple sclerosis: a phase 2, randomised, placebo-controlled, multicentre trial. The Lancet 2011 378 9805 1779 1787 2-s2.0-81555202418 10.1016/S0140-6736(11)61649-8
    • (2011) The Lancet , vol.378 , Issue.9805 , pp. 1779-1787
    • Kappos, L.1    Li, D.2    Calabresi, P.A.3    O'Connor, P.4    Bar-Or, A.5    Barkhof, F.6    Yin, M.7    Leppert, D.8    Glanzman, R.9    Tinbergen, J.10    Hauser, S.L.11
  • 84
    • 84873117834 scopus 로고    scopus 로고
    • Humoral-targeted immunotherapies in multiple sclerosis
    • Lulu S., Waubant E., Humoral-targeted immunotherapies in multiple sclerosis. Neurotherapeutics 2013 10 1 34 43
    • (2013) Neurotherapeutics , vol.10 , Issue.1 , pp. 34-43
    • Lulu, S.1    Waubant, E.2
  • 87
    • 84863683766 scopus 로고    scopus 로고
    • Differentiating patterns of oligoclonal banding in the cerebrospinal fluid improves diagnostic utility for multiple sclerosis
    • Lin M. W., Suan D., Lenton K., Henniker T., Burke T., Vucic S., Fulcher D. A., Differentiating patterns of oligoclonal banding in the cerebrospinal fluid improves diagnostic utility for multiple sclerosis. Pathology 2012 44 3 248 250
    • (2012) Pathology , vol.44 , Issue.3 , pp. 248-250
    • Lin, M.W.1    Suan, D.2    Lenton, K.3    Henniker, T.4    Burke, T.5    Vucic, S.6    Fulcher, D.A.7
  • 88
    • 33846820308 scopus 로고    scopus 로고
    • Specific antibody index in cerebrospinal fluid from patients with central and peripheral paraneoplastic neurological syndromes
    • DOI 10.1016/j.jneuroim.2006.11.008, PII S0165572806004619
    • Stich O., Jarius S., Kleer B., Rasiah C., Voltz R., Rauer S., Specific antibody index in cerebrospinal fluid from patients with central and peripheral paraneoplastic neurological syndromes. Journal of Neuroimmunology 2007 183 1-2 220 224 2-s2.0-33846820308 10.1016/j.jneuroim.2006.11.008 (Pubitemid 46204909)
    • (2007) Journal of Neuroimmunology , vol.183 , Issue.1-2 , pp. 220-224
    • Stich, O.1    Jarius, S.2    Kleer, B.3    Rasiah, C.4    Voltz, R.5    Rauer, S.6
  • 89
    • 0031748566 scopus 로고    scopus 로고
    • Multiple sclerosis: In situ evidence for antibody- and complement- mediated demyelination
    • DOI 10.1002/ana.410430409
    • Storch M. K., Piddlesden S., Haltia M., Iivanainen M., Morgan P., Lassmann H., Multiple sclerosis: in situ evidence for antibody- and complement-mediated demyelination. Annals of Neurology 1998 43 4 465 471 2-s2.0-0031748566 10.1002/ana.410430409 (Pubitemid 28231721)
    • (1998) Annals of Neurology , vol.43 , Issue.4 , pp. 465-471
    • Storch, M.K.1    Piddlesden, S.2    Haltia, M.3    Iivanainen, M.4    Morgan, P.5    Lassmann, H.6
  • 91
    • 40849083783 scopus 로고    scopus 로고
    • Proteasome antibodies in patients with cancer or multiple sclerosis
    • DOI 10.1111/j.1365-3083.2008.02073.x
    • Thuy-Tien H., Haugen M., Aarseth J., Storstein A., Vedeler C. A., Proteasome antibodies in patients with cancer or multiple sclerosis. Scandinavian Journal of Immunology 2008 67 4 400 403 2-s2.0-40849083783 10.1111/j.1365-3083.2008.02073.x (Pubitemid 351392922)
    • (2008) Scandinavian Journal of Immunology , vol.67 , Issue.4 , pp. 400-403
    • Thuy-Tien, H.1    Haugen, M.2    Aarseth, J.3    Storstein, A.4    Vedeler, C.A.5
  • 92
    • 35649006958 scopus 로고    scopus 로고
    • Autoantibodies to the proteasome in monosymptomatic optic neuritis may predict progression to multiple sclerosis
    • DOI 10.1080/00365510701342062, PII 779683145
    • Beyer N. H., Milthers J., Lauridsen B. A.-M., Houen G., Frederiksen L. J., Autoantibodies to the proteasome in monosymptomatic optic neuritis may predict progression to multiple sclerosis. Scandinavian Journal of Clinical and Laboratory Investigation 2007 67 7 696 706 2-s2.0-35649006958 10.1080/00365510701342062 (Pubitemid 350034644)
    • (2007) Scandinavian Journal of Clinical and Laboratory Investigation , vol.67 , Issue.7 , pp. 696-706
    • Beyer, N.H.1    Milthers, J.2    Lauridsen, B.A.-M.3    Houen, G.4    Frederiksen, L.J.5
  • 93
    • 33745890229 scopus 로고    scopus 로고
    • Anti-20S proteasome autoantibodies inhibit proteasome stimulation by proteasome activator PA28
    • DOI 10.1002/art.21970
    • Brychcy M., Kuckelkorn U., Hausdorf G., Egerer K., Kloetzel P.-M., Burmester G.-R., Feist E., Anti-20S proteasome autoantibodies inhibit proteasome stimulation by proteasome activator PA28. Arthritis and Rheumatism 2006 54 7 2175 2183 2-s2.0-33745890229 10.1002/art.21970 (Pubitemid 44051074)
    • (2006) Arthritis and Rheumatism , vol.54 , Issue.7 , pp. 2175-2183
    • Brychcy, M.1    Kuckelkorn, U.2    Hausdorf, G.3    Egerer, K.4    Kloetzel, P.-M.5    Burmester, G.-R.6    Feist, E.7
  • 94
    • 56449112645 scopus 로고    scopus 로고
    • Extracellular, circulating proteasomes and ubiquitin: Incidence and relevance
    • 2-s2.0-56449112645 10.1016/j.bbadis.2008.06.005
    • Sixt S. U., Dahlmann B., Extracellular, circulating proteasomes and ubiquitin: incidence and relevance. Biochimica et Biophysica Acta 2008 1782 12 817 823 2-s2.0-56449112645 10.1016/j.bbadis.2008.06.005
    • (2008) Biochimica et Biophysica Acta , vol.1782 , Issue.12 , pp. 817-823
    • Sixt, S.U.1    Dahlmann, B.2
  • 97
    • 84866524463 scopus 로고    scopus 로고
    • Proteolytic potential of the MSC exosome proteome: Implications for an exosome-mediated delivery of therapeutic proteasome
    • 971907 10.1155/2012/971907
    • Lai R. C., Tan S. S., Teh B. J., Sze S. K., Arslan F., de Kleijn D. P., Choo A., Lim S. K., Proteolytic potential of the MSC exosome proteome: implications for an exosome-mediated delivery of therapeutic proteasome. International Journal of Proteomics 2012 2012 14 971907 10.1155/2012/971907
    • (2012) International Journal of Proteomics , vol.2012 , pp. 14
    • Lai, R.C.1    Tan, S.S.2    Teh, B.J.3    Sze, S.K.4    Arslan, F.5    De Kleijn, D.P.6    Choo, A.7    Lim, S.K.8
  • 99
    • 84864106711 scopus 로고    scopus 로고
    • Plasma ubiquitin-proteasome system profile in patients with multiple sclerosis: Correlation with clinical features, neuroimaging, and treatment with interferon-beta-1b
    • Minagar A., Ma W., Zhang X., Wang X., Zhang K., Alexander J. S., Gonzalez-Toledo E., Albitar M., Plasma ubiquitin-proteasome system profile in patients with multiple sclerosis: correlation with clinical features, neuroimaging, and treatment with interferon-beta-1b. Journal of Neurology Research 2012 34 6 611 618
    • (2012) Journal of Neurology Research , vol.34 , Issue.6 , pp. 611-618
    • Minagar, A.1    Ma, W.2    Zhang, X.3    Wang, X.4    Zhang, K.5    Alexander, J.S.6    Gonzalez-Toledo, E.7    Albitar, M.8
  • 100
    • 78650172976 scopus 로고    scopus 로고
    • Inflammation, demyelination, and degeneration: Recent insights from MS pathology
    • 2-s2.0-78650172976 10.1016/j.bbadis.2010.07.007
    • Stadelmann C., Wegner C., Brück W., Inflammation, demyelination, and degeneration: recent insights from MS pathology. Biochimica et Biophysica Acta 2011 1812 2 275 282 2-s2.0-78650172976 10.1016/j.bbadis.2010.07.007
    • (2011) Biochimica et Biophysica Acta , vol.1812 , Issue.2 , pp. 275-282
    • Stadelmann, C.1    Wegner, C.2    Brück, W.3
  • 101
    • 53049093018 scopus 로고    scopus 로고
    • Neurodegeneration in multiple sclerosis: The role of oxidative stress and excitotoxicity
    • 2-s2.0-53049093018 10.1016/j.jns.2008.06.029
    • Gonsette R. E., Neurodegeneration in multiple sclerosis: the role of oxidative stress and excitotoxicity. Journal of the Neurological Sciences 2008 274 1-2 48 53 2-s2.0-53049093018 10.1016/j.jns.2008.06.029
    • (2008) Journal of the Neurological Sciences , vol.274 , Issue.1-2 , pp. 48-53
    • Gonsette, R.E.1
  • 102
    • 81555223903 scopus 로고    scopus 로고
    • The molecular basis of neurodegeneration in multiple sclerosis
    • 2-s2.0-81555223903 10.1016/j.febslet.2011.08.004
    • Lassmann H., van Horssen J., The molecular basis of neurodegeneration in multiple sclerosis. FEBS Letters 2011 585 23 3715 3723 2-s2.0-81555223903 10.1016/j.febslet.2011.08.004
    • (2011) FEBS Letters , vol.585 , Issue.23 , pp. 3715-3723
    • Lassmann, H.1    Van Horssen, J.2
  • 104
    • 42449141602 scopus 로고    scopus 로고
    • Cytoskeletal protein carbonylation and degradation in experimental autoimmune encephalomyelitis
    • DOI 10.1111/j.1471-4159.2007.05178.x
    • Smerjac S. M., Bizzozero O. A., Cytoskeletal protein carbonylation and degradation in experimental autoimmune encephalomyelitis. Journal of Neurochemistry 2008 105 3 763 772 2-s2.0-42449141602 10.1111/j.1471-4159.2007. 05178.x (Pubitemid 351562723)
    • (2008) Journal of Neurochemistry , vol.105 , Issue.3 , pp. 763-772
    • Smerjac, S.M.1    Bizzozero, O.A.2
  • 105
    • 78649392988 scopus 로고    scopus 로고
    • Accumulation of protein carbonyls within cerebellar astrocytes in murine experimental autoimmune encephalomyelitis
    • 2-s2.0-78649392988 10.1002/jnr.22488
    • Zheng J., Bizzozero O. A., Accumulation of protein carbonyls within cerebellar astrocytes in murine experimental autoimmune encephalomyelitis. Journal of Neuroscience Research 2010 88 15 3376 3385 2-s2.0-78649392988 10.1002/jnr.22488
    • (2010) Journal of Neuroscience Research , vol.88 , Issue.15 , pp. 3376-3385
    • Zheng, J.1    Bizzozero, O.A.2
  • 106
    • 41149164588 scopus 로고    scopus 로고
    • Persistent mitochondrial dysfunction and oxidative stress hinder neuronal cell recovery from reversible proteasome inhibition
    • 2-s2.0-41149164588 10.1007/s10495-008-0182-0
    • Papa L., Rockwell P., Persistent mitochondrial dysfunction and oxidative stress hinder neuronal cell recovery from reversible proteasome inhibition. Apoptosis 2008 13 4 588 599 2-s2.0-41149164588 10.1007/s10495-008-0182-0
    • (2008) Apoptosis , vol.13 , Issue.4 , pp. 588-599
    • Papa, L.1    Rockwell, P.2
  • 108
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • R110.006924 2-s2.0-79955757695 10.1074/mcp.R110.006924
    • Aiken C. T., Kaake R. M., Wang X., Huang L., Oxidative stress-mediated regulation of proteasome complexes. Molecular and Cellular Proteomics 2011 10 5 R110.006924 2-s2.0-79955757695 10.1074/mcp.R110.006924
    • (2011) Molecular and Cellular Proteomics , vol.10 , Issue.5
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 109
    • 79959534486 scopus 로고    scopus 로고
    • Oxidative protein damage and the proteasome
    • 2-s2.0-79959534486 10.1007/s00726-010-0646-8
    • Grimm S., Höhn A., Grune T., Oxidative protein damage and the proteasome. Amino acids 2012 42 1 23 38 2-s2.0-79959534486 10.1007/s00726-010- 0646-8
    • (2012) Amino Acids , vol.42 , Issue.1 , pp. 23-38
    • Grimm, S.1    Höhn, A.2    Grune, T.3
  • 110
    • 58149350129 scopus 로고    scopus 로고
    • The proteasome and its role in the degradation of oxidized proteins
    • 2-s2.0-58149350129 10.1002/iub.114
    • Jung T., Grune T., The proteasome and its role in the degradation of oxidized proteins. IUBMB Life 2008 60 11 743 752 2-s2.0-58149350129 10.1002/iub.114
    • (2008) IUBMB Life , vol.60 , Issue.11 , pp. 743-752
    • Jung, T.1    Grune, T.2
  • 111
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • DOI 10.1016/S0006-291X(03)00809-X
    • Grune T., Merker K., Sandig G., Davies K. J. A., Selective degradation of oxidatively modified protein substrates by the proteasome. Biochemical and Biophysical Research Communications 2003 305 3 709 718 2-s2.0-0038239701 10.1016/S0006-291X(03)00809-X (Pubitemid 36579287)
    • (2003) Biochemical and Biophysical Research Communications , vol.305 , Issue.3 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.A.4
  • 112
    • 33644662970 scopus 로고    scopus 로고
    • Proteasome function in aging and oxidative stress: Implications in protein maintenance failure
    • DOI 10.1089/ars.2006.8.205
    • Farout L., Friguet B., Proteasome function in aging and oxidative stress: implications in protein maintenance failure. Antioxidants and Redox Signaling 2006 8 1-2 205 216 2-s2.0-33644662970 10.1089/ars.2006.8.205 (Pubitemid 43324547)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.1-2 , pp. 205-216
    • Farout, L.1    Friguet, B.2
  • 113
    • 0032212875 scopus 로고    scopus 로고
    • Comparative resistance of the 20 S and 26 S proteasome to oxidative stress
    • 2-s2.0-0032212875
    • Reinheckel T., Sitte N., Ullrich O., Kuckelkorn U., Davies K. J. A., Grune T., Comparative resistance of the 20 S and 26 S proteasome to oxidative stress. Biochemical Journal 1998 335 3 637 642 2-s2.0-0032212875
    • (1998) Biochemical Journal , vol.335 , Issue.3 , pp. 637-642
    • Reinheckel, T.1    Sitte, N.2    Ullrich, O.3    Kuckelkorn, U.4    Davies, K.J.A.5    Grune, T.6
  • 114
    • 79955063530 scopus 로고    scopus 로고
    • Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated
    • 2-s2.0-79955063530 10.1016/j.biochi.2011.03.004
    • Kästle M., Grune T., Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated. Biochimie 2011 93 6 1076 1079 2-s2.0-79955063530 10.1016/j.biochi.2011.03.004
    • (2011) Biochimie , vol.93 , Issue.6 , pp. 1076-1079
    • Kästle, M.1    Grune, T.2
  • 115
    • 33644852960 scopus 로고    scopus 로고
    • Upregulation of immunoproteasomes by nitric oxide: Potential antioxidative mechanism in endothelial cells
    • DOI 10.1016/j.freeradbiomed.2005.10.052, PII S0891584905006635
    • Kotamraju S., Matalon S., Matsunaga T., Shang T., Hickman-Davis J. M., Kalyanaraman B., Upregulation of immunoproteasomes by nitric oxide: potential antioxidative mechanism in endothelial cells. Free Radical Biology and Medicine 2006 40 6 1034 1044 2-s2.0-33644852960 10.1016/j.freeradbiomed.2005.10.052 (Pubitemid 43376013)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.6 , pp. 1034-1044
    • Kotamraju, S.1    Matalon, S.2    Matsunaga, T.3    Shang, T.4    Hickman-Davis, J.M.5    Kalyanaraman, B.6
  • 116
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome,the 20S proteasome and the PA28 β proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • 2-s2.0-78649848069 10.1042/BJ20100878
    • Pickering A.M.,Koop A.L.,Teoh C.Y.,Ermak G.,Grune T.,Davies K.J.A.,The immunoproteasome,the 20S proteasome and the PA28 β proteasome regulator are oxidative-stress-adaptive proteolytic complexes. Biochemical Journal 2010 432 3 585 594 2-s2.0-78649848069 10.1042/BJ20100878
    • (2010) Biochemical Journal , vol.432 , Issue.3 , pp. 585-594
    • Pickering, A.M.1    Koop, A.L.2    Teoh, C.Y.3    Ermak, G.4    Grune, T.5    Davies, K.J.A.6
  • 117
    • 84861869794 scopus 로고    scopus 로고
    • Differential roles of proteasome and immunoproteasome regulators Pa28alphabeta, Pa28gamma and Pa200 in the degradation of oxidized proteins
    • Pickering A. M., Davies K. J., Differential roles of proteasome and immunoproteasome regulators Pa28alphabeta, Pa28gamma and Pa200 in the degradation of oxidized proteins. Archives of Biochemistry and Biophysics 2012 523 2 181 190
    • (2012) Archives of Biochemistry and Biophysics , vol.523 , Issue.2 , pp. 181-190
    • Pickering, A.M.1    Davies, K.J.2
  • 118
    • 33644656207 scopus 로고    scopus 로고
    • LMP2 knock-out mice have reduced proteasome activities and increased levels of oxidatively damaged proteins
    • DOI 10.1089/ars.2006.8.130
    • Ding Q., Martin S., Dimayuga E., Bruce-Keller A. J., Keller J. N., LMP2 knock-out mice have reduced proteasome activities and increased levels of oxidatively damaged proteins. Antioxidants and Redox Signaling 2006 8 1-2 130 135 2-s2.0-33644656207 10.1089/ars.2006.8.130 (Pubitemid 43324539)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.1-2 , pp. 130-135
    • Ding, Q.1    Martin, S.2    Dimayuga, E.3    Bruce-Keller, A.J.4    Keller, J.N.5
  • 119
    • 78751613188 scopus 로고    scopus 로고
    • Treatment effects of immunomodulatory therapies at different stages of multiple sclerosis in short-term trials
    • 2-s2.0-78751613188 10.1212/WNL.0b013e3182050388
    • Bates D., Treatment effects of immunomodulatory therapies at different stages of multiple sclerosis in short-term trials. Neurology 2011 76 1 supplement 1 S14 S25 2-s2.0-78751613188 10.1212/WNL.0b013e3182050388
    • (2011) Neurology , vol.76 , Issue.1 SUPPLEMENT 1
    • Bates, D.1
  • 120
    • 12344335574 scopus 로고    scopus 로고
    • The pathology of multiple sclerosis
    • DOI 10.1016/j.ncl.2004.09.002, PII S0733861904000866
    • Lucchinetti C. F., Parisi J., Bruck W., The pathology of multiple sclerosis. Neurologic Clinics 2005 23 1 77 105 2-s2.0-12344335574 10.1016/j.ncl.2004.09.002 (Pubitemid 40126916)
    • (2005) Neurologic Clinics , vol.23 , Issue.1 , pp. 77-105
    • Lucchinetti, C.F.1    Parisi, J.2    Bruck, W.3
  • 123
    • 2942666042 scopus 로고    scopus 로고
    • + T cells maintain tolerance to myelin basis protein by 'epitope theft'
    • DOI 10.1038/ni1073
    • Perchellet A., Stromnes I., Pang J. M., Goverman J., CD8+ T cells maintain tolerance to myelin basis protein by 'epitope theft'. Nature Immunology 2004 5 6 606 614 2-s2.0-2942666042 10.1038/ni1073 (Pubitemid 38811885)
    • (2004) Nature Immunology , vol.5 , Issue.6 , pp. 606-614
    • Perchellet, A.1    Stromnes, I.2    Pang, J.M.3    Goverman, J.4
  • 125
    • 84862276328 scopus 로고    scopus 로고
    • Structure, function and diversity of the healthy human microbiome
    • Human Microbiome Project Consortium, Structure, function and diversity of the healthy human microbiome. Nature 2012 486 7402 207 214
    • (2012) Nature , vol.486 , Issue.7402 , pp. 207-214
    • Microbiome Project Consortium, H.1
  • 126
    • 84864311638 scopus 로고    scopus 로고
    • Intestinal microbiota is a plastic factor responding to environmental changes
    • Candela M., Biagi E., Maccaferri S., Turroni S., Brigidi P., Intestinal microbiota is a plastic factor responding to environmental changes. Trends in Microbiology 2012 20 8 385 391
    • (2012) Trends in Microbiology , vol.20 , Issue.8 , pp. 385-391
    • Candela, M.1    Biagi, E.2    Maccaferri, S.3    Turroni, S.4    Brigidi, P.5
  • 127
    • 52949084680 scopus 로고    scopus 로고
    • Crosspresentation by nonhematopoietic and direct presentation by hematopoietic cells induce central tolerance to myelin basic protein
    • 2-s2.0-52949084680 10.1073/pnas.0804970105
    • Perchellet A., Brabb T., Goverman J. M., Crosspresentation by nonhematopoietic and direct presentation by hematopoietic cells induce central tolerance to myelin basic protein. Proceedings of the National Academy of Sciences of the United States of America 2008 105 37 14040 14045 2-s2.0-52949084680 10.1073/pnas.0804970105
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.37 , pp. 14040-14045
    • Perchellet, A.1    Brabb, T.2    Goverman, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.