메뉴 건너뛰기




Volumn 47, Issue 4, 2014, Pages 220-233

Autoantigens: Novel forms and presentation to the immune system

Author keywords

Antigen presentation; Antigen presenting cells; Diagnostics; Methylation; Post translational modification

Indexed keywords

AUTOANTIGEN; CELL PROTEIN; DEOXYRIBONUCLEOPROTEIN; DNA FRAGMENT; DNA METHYLTRANSFERASE; GLUTAMATE RECEPTOR 3; HISTONE; MYELIN BASIC PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN KINASE ZAP 70; PROTEIN LYSINE METHYLTRANSFERASE; PROTEIN METHYLTRANSFERASE; SERINE ARGININE RICH PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 84901070188     PISSN: 08916934     EISSN: 1607842X     Source Type: Journal    
DOI: 10.3109/08916934.2013.850495     Document Type: Review
Times cited : (35)

References (172)
  • 1
    • 0035171545 scopus 로고    scopus 로고
    • Promiscuous gene expression in medullary thymic epithelial cells mirrors the peripheral self
    • Derbinski, J., A. Schulte, B. Kyewski, and L. Klein. 2001. Promiscuous gene expression in medullary thymic epithelial cells mirrors the peripheral self. Nat. Immunol. 2: 1032-1039.
    • (2001) Nat. Immunol , vol.2 , pp. 1032-1039
    • Derbinski, J.1    Schulte, A.2    Kyewski, B.3    Klein, L.4
  • 2
    • 23744515712 scopus 로고    scopus 로고
    • Posttranslational modifications of self-antigens
    • Doyle, H. A., and M. J. Mamula. 2005. Posttranslational modifications of self-antigens. Ann. N. Y. Acad. Sci. 1050: 1-9.
    • (2005) Ann. N. Y. Acad. Sci , vol.1050 , pp. 1-9
    • Doyle, H.A.1    Mamula, M.J.2
  • 3
    • 84857045897 scopus 로고    scopus 로고
    • Autoantigenesis: The evolution of protein modifications in autoimmune disease
    • Doyle, H. A., and M. J. Mamula. 2012. Autoantigenesis: the evolution of protein modifications in autoimmune disease. Curr. Opin. Immunol. 24: 112-118.
    • (2012) Curr. Opin. Immunol , vol.24 , pp. 112-118
    • Doyle, H.A.1    Mamula, M.J.2
  • 4
    • 84870023807 scopus 로고    scopus 로고
    • The protein arginine deiminases: Structure, function, inhibition, and disease
    • Bicker, K. L., and P. R. Thompson. 2013. The protein arginine deiminases: structure, function, inhibition, and disease. Biopolymers 99: 155-163.
    • (2013) Biopolymers , vol.99 , pp. 155-163
    • Bicker, K.L.1    Thompson, P.R.2
  • 6
    • 73249145617 scopus 로고    scopus 로고
    • Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis
    • Wegner, N., K. Lundberg, A. Kinloch, et al. 2010. Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis. Immunol. Rev. 233: 34-54.
    • (2010) Immunol. Rev , vol.233 , pp. 34-54
    • Wegner, N.1    Lundberg, K.2    Kinloch, A.3
  • 7
    • 78650418591 scopus 로고    scopus 로고
    • All you wanted to know about anti-CCP but were afraid to ask
    • Wiik, A. S., W. J. van Venrooij, and G. J. Pruijn. 2010. All you wanted to know about anti-CCP but were afraid to ask. Autoimmun. Rev. 10: 90-93.
    • (2010) Autoimmun. Rev , vol.10 , pp. 90-93
    • Wiik, A.S.1    Van Venrooij, W.J.2    Pruijn, G.J.3
  • 8
    • 0031838606 scopus 로고    scopus 로고
    • Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus
    • Herrmann, M., R. E. Voll, O. M. Zoller, et al. 1998. Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus. Arthritis Rheum. 41: 1241-1250.
    • (1998) Arthritis Rheum , vol.41 , pp. 1241-1250
    • Herrmann, M.1    Voll, R.E.2    Zoller, O.M.3
  • 9
    • 31144439799 scopus 로고    scopus 로고
    • Macrophages from patients with SLE and rheumatoid arthritis have defective adhesion in vitro, while only SLE macrophages have impaired uptake of apoptotic cells
    • Tas, S. W., P. Quartier, M. Botto, and L. Fossati-Jimack. 2006. Macrophages from patients with SLE and rheumatoid arthritis have defective adhesion in vitro, while only SLE macrophages have impaired uptake of apoptotic cells. Ann. Rheum. Dis. 65: 216-221.
    • (2006) Ann. Rheum. Dis , vol.65 , pp. 216-221
    • Tas, S.W.1    Quartier, P.2    Botto, M.3    Fossati-Jimack, L.4
  • 10
    • 34547180886 scopus 로고    scopus 로고
    • In vivo evidence for apoptosis in the bone marrow in systemic lupus erythematosus
    • Hepburn, A. L., I. A. Lampert, J. J. Boyle, et al. 2007. In vivo evidence for apoptosis in the bone marrow in systemic lupus erythematosus. Ann. Rheum. Dis. 66: 1106-1109.
    • (2007) Ann. Rheum. Dis , vol.66 , pp. 1106-1109
    • Hepburn, A.L.1    Lampert, I.A.2    Boyle, J.J.3
  • 11
    • 33644896511 scopus 로고    scopus 로고
    • Accumulation of apoptotic cells in the epidermis of patients with cutaneous lupus erythematosus after ultraviolet irradiation
    • Kuhn, A., M. Herrmann, S. Kleber, et al. 2006. Accumulation of apoptotic cells in the epidermis of patients with cutaneous lupus erythematosus after ultraviolet irradiation. Arthritis Rheum. 54: 939-950.
    • (2006) Arthritis Rheum , vol.54 , pp. 939-950
    • Kuhn, A.1    Herrmann, M.2    Kleber, S.3
  • 12
    • 0028288510 scopus 로고
    • Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes
    • Casciola-Rosen, L. A., G. Anhalt, and A. Rosen. 1994. Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes. J. Exp. Med. 179: 1317-1330.
    • (1994) J. Exp. Med , vol.179 , pp. 1317-1330
    • Casciola-Rosen, L.A.1    Anhalt, G.2    Rosen, A.3
  • 13
    • 0033938117 scopus 로고    scopus 로고
    • Life and death decisions: Regulation of apoptosis by proteolysis of signaling molecules
    • Utz, P. J., and P. Anderson. 2000. Life and death decisions: regulation of apoptosis by proteolysis of signaling molecules. Cell Death Differ. 7: 589-602.
    • (2000) Cell Death Differ , vol.7 , pp. 589-602
    • Utz, P.J.1    Anderson, P.2
  • 14
    • 0033890806 scopus 로고    scopus 로고
    • SR proteins are autoantigens in patients with systemic lupus erythematosus. Importance of phosphoepitopes
    • Neugebauer, K. M., J. T. Merrill, M. H. Wener, et al. 2000. SR proteins are autoantigens in patients with systemic lupus erythematosus. Importance of phosphoepitopes. Arthritis Rheum. 43: 1768-1778.
    • (2000) Arthritis Rheum , vol.43 , pp. 1768-1778
    • Neugebauer, K.M.1    Merrill, J.T.2    Wener, M.H.3
  • 15
    • 52449094382 scopus 로고    scopus 로고
    • Protein isoaspartate methyltransferase prevents apoptosis induced by oxidative stress in endothelial cells: Role of Bcl-Xl deamidation and methylation
    • Cimmino, A., R. Capasso, F. Muller, et al. 2008. Protein isoaspartate methyltransferase prevents apoptosis induced by oxidative stress in endothelial cells: role of Bcl-Xl deamidation and methylation. PLoS One 3: e3258.
    • (2008) PLoS One , vol.3
    • Cimmino, A.1    Capasso, R.2    Muller, F.3
  • 16
    • 20044376670 scopus 로고    scopus 로고
    • Hydroxytyrosol, a natural antioxidant from olive oil, prevents protein damage induced by long-wave ultraviolet radiation in melanoma cells
    • D'Angelo, S., D. Ingrosso, V. Migliardi, et al. 2005. Hydroxytyrosol, a natural antioxidant from olive oil, prevents protein damage induced by long-wave ultraviolet radiation in melanoma cells. Free Radic. Biol. Med. 38: 908-919.
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 908-919
    • D'Angelo, S.1    Ingrosso, D.2    Migliardi, V.3
  • 17
    • 84872184328 scopus 로고    scopus 로고
    • Autoimmunity to isomerized histone H2B in systemic lupus erythematosus
    • Doyle, H. A., D. W. Aswad, and M. J. Mamula. 2013. Autoimmunity to isomerized histone H2B in systemic lupus erythematosus. Autoimmunity 46: 6-13.
    • (2013) Autoimmunity , vol.46 , pp. 6-13
    • Doyle, H.A.1    Aswad, D.W.2    Mamula, M.J.3
  • 18
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • Brahms, H., J. Raymackers, A. Union, et al. 2000. The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies. J. Biol. Chem. 275: 17122-17129.
    • (2000) J. Biol. Chem , vol.275 , pp. 17122-17129
    • Brahms, H.1    Raymackers, J.2    Union, A.3
  • 19
    • 84862777357 scopus 로고    scopus 로고
    • Specific post-translational histone modifications of neutrophil extracellular traps as immunogens and potential targets of lupus autoantibodies
    • Liu, C. L., S. Tangsombatvisit, J. M. Rosenberg, et al. 2012. Specific post-translational histone modifications of neutrophil extracellular traps as immunogens and potential targets of lupus autoantibodies. Arthritis Res. Ther. 14: R25.
    • (2012) Arthritis Res. Ther , vol.14
    • Liu, C.L.1    Tangsombatvisit, S.2    Rosenberg, J.M.3
  • 20
    • 0033529490 scopus 로고    scopus 로고
    • Isoaspartyl posttranslational modification triggers autoimmune responses to selfproteins
    • Mamula, M. J., R. J. Gee, J. I. Elliott, et al. 1999. Isoaspartyl posttranslational modification triggers autoimmune responses to selfproteins. J. Biol. Chem. 274: 22321-22327.
    • (1999) J. Biol. Chem , vol.274 , pp. 22321-22327
    • Mamula, M.J.1    Gee, R.J.2    Elliott, J.I.3
  • 21
    • 70450222929 scopus 로고    scopus 로고
    • Apoptosisassociated acetylation on histone H2B is an epitope for lupus autoantibodies
    • van Bavel, C. C., J. Dieker, S. Muller, et al. 2009. Apoptosisassociated acetylation on histone H2B is an epitope for lupus autoantibodies. Mol. Immunol. 47: 511-516.
    • (2009) Mol. Immunol , vol.47 , pp. 511-516
    • Van Bavel, C.C.1    Dieker, J.2    Muller, S.3
  • 22
    • 0026664422 scopus 로고
    • Spreading of T-cell autoimmunity to cryptic determinants of an autoantigen
    • Lehmann, P. V., T. Forsthuber, A. Miller, and E. E. Sercarz. 1992. Spreading of T-cell autoimmunity to cryptic determinants of an autoantigen. Nature 358: 155-157.
    • (1992) Nature , vol.358 , pp. 155-157
    • Lehmann, P.V.1    Forsthuber, T.2    Miller, A.3    Sercarz, E.E.4
  • 23
    • 54349105949 scopus 로고    scopus 로고
    • Epitope spreading to citrullinated antigens in mouse models of autoimmune arthritis and demyelination
    • Kidd, B. A., P. P. Ho, O. Sharpe, et al. 2008. Epitope spreading to citrullinated antigens in mouse models of autoimmune arthritis and demyelination. Arthritis Res. Ther. 10: R119.
    • (2008) Arthritis Res. Ther , vol.10
    • Kidd, B.A.1    Ho, P.P.2    Sharpe, O.3
  • 24
    • 0142009533 scopus 로고    scopus 로고
    • Development of autoantibodies before the clinical onset of systemic lupus erythematosus
    • Arbuckle, M. R., M. T. McClain, M. V. Rubertone, et al. 2003. Development of autoantibodies before the clinical onset of systemic lupus erythematosus. N. Engl. J. Med. 349: 1526-1533.
    • (2003) N. Engl. J. Med , vol.349 , pp. 1526-1533
    • Arbuckle, M.R.1    McClain, M.T.2    Rubertone, M.V.3
  • 25
    • 0036161789 scopus 로고    scopus 로고
    • Mitochondrial hyperpolarization and ATP depletion in patients with systemic lupus erythematosus
    • Gergely Jr. P., C. Grossman, B. Niland, et al. 2002. Mitochondrial hyperpolarization and ATP depletion in patients with systemic lupus erythematosus. Arthritis Rheum. 46: 175-190.
    • (2002) Arthritis Rheum , vol.46 , pp. 175-190
    • Gergely Jr., P.1    Grossman, C.2    Niland, B.3
  • 26
    • 0037100275 scopus 로고    scopus 로고
    • Persistent mitochondrial hyperpolarization, increased reactive oxygen intermediate production, and cytoplasmic alkalinization characterize altered IL-10 signaling in patients with systemic lupus erythematosus
    • Gergely Jr. P., B. Niland, N. Gonchoroff, et al. 2002. Persistent mitochondrial hyperpolarization, increased reactive oxygen intermediate production, and cytoplasmic alkalinization characterize altered IL-10 signaling in patients with systemic lupus erythematosus. J. Immunol. 169: 1092-1101.
    • (2002) J. Immunol , vol.169 , pp. 1092-1101
    • Gergely Jr., P.1    Niland, B.2    Gonchoroff, N.3
  • 27
    • 0036167693 scopus 로고    scopus 로고
    • Destructive processing by asparagine endopeptidase limits presentation of a dominant T cell epitope in MBP
    • Manoury, B., D. Mazzeo, L. Fugger, et al. 2002. Destructive processing by asparagine endopeptidase limits presentation of a dominant T cell epitope in MBP. Nat. Immunol. 3: 169-174.
    • (2002) Nat. Immunol , vol.3 , pp. 169-174
    • Manoury, B.1    Mazzeo, D.2    Fugger, L.3
  • 28
    • 0035253348 scopus 로고    scopus 로고
    • Granzyme B proteolysis of a neuronal glutamate receptor generates an autoantigen and is modulated by glycosylation
    • Gahring, L., N. G. Carlson, E. L. Meyer, and S. W. Rogers. 2001. Granzyme B proteolysis of a neuronal glutamate receptor generates an autoantigen and is modulated by glycosylation. J. Immunol. 166: 1433-1438.
    • (2001) J. Immunol , vol.166 , pp. 1433-1438
    • Gahring, L.1    Carlson, N.G.2    Meyer, E.L.3    Rogers, S.W.4
  • 29
    • 0025356363 scopus 로고
    • Fragmentation of isoaspartyl peptides and proteins by carboxypeptidase Y: Release of isoaspartyl dipeptides as a result of internal and external cleavage
    • Johnson, B. A., and D. W. Aswad. 1990. Fragmentation of isoaspartyl peptides and proteins by carboxypeptidase Y: release of isoaspartyl dipeptides as a result of internal and external cleavage. Biochemistry 29: 4373-4380.
    • (1990) Biochemistry , vol.29 , pp. 4373-4380
    • Johnson, B.A.1    Aswad, D.W.2
  • 30
    • 24044463891 scopus 로고    scopus 로고
    • Asparagine deamidation perturbs antigen presentation on class II major histocompatibility complex molecules
    • Moss, C. X., S. P. Matthews, D. J. Lamont, and C. Watts. 2005. Asparagine deamidation perturbs antigen presentation on class II major histocompatibility complex molecules. J. Biol. Chem. 280: 18498-18503.
    • (2005) J. Biol. Chem , vol.280 , pp. 18498-18503
    • Moss, C.X.1    Matthews, S.P.2    Lamont, D.J.3    Watts, C.4
  • 31
    • 34250354402 scopus 로고    scopus 로고
    • Altered immunogenicity of isoaspartate containing proteins
    • Doyle, H. A., R. J. Gee, and M. J. Mamula. 2007. Altered immunogenicity of isoaspartate containing proteins. Autoimmunity 40: 131-137.
    • (2007) Autoimmunity , vol.40 , pp. 131-137
    • Doyle, H.A.1    Gee, R.J.2    Mamula, M.J.3
  • 32
    • 0027999537 scopus 로고
    • Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death
    • Casciola-Rosen, L. A., D. K. Miller, G. J. Anhalt, and A. Rosen. 1994. Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J. Biol. Chem. 269: 30757-30760.
    • (1994) J. Biol. Chem , vol.269 , pp. 30757-30760
    • Casciola-Rosen, L.A.1    Miller, D.K.2    Anhalt, G.J.3    Rosen, A.4
  • 33
    • 84855516226 scopus 로고    scopus 로고
    • Autophagy in antigenpresenting cells results in presentation of citrullinated peptides to CD4 T cells
    • Ireland, J. M., and E. R. Unanue. 2011. Autophagy in antigenpresenting cells results in presentation of citrullinated peptides to CD4 T cells. J. Exp. Med. 208: 2625-2632.
    • (2011) J. Exp. Med , vol.208 , pp. 2625-2632
    • Ireland, J.M.1    Unanue, E.R.2
  • 34
    • 10344230928 scopus 로고    scopus 로고
    • Limited plasticity in T cell recognition of modified T cell receptor contact residues in MHC class II bound peptides
    • de Haan, E. C., J. P. Wagenaar-Hilbers, R. M. Liskamp, et al. 2005. Limited plasticity in T cell recognition of modified T cell receptor contact residues in MHC class II bound peptides. Mol. Immunol. 42: 355-364.
    • (2005) Mol. Immunol , vol.42 , pp. 355-364
    • De Haan, E.C.1    Wagenaar-Hilbers, J.P.2    Liskamp, R.M.3
  • 35
    • 0038107566 scopus 로고    scopus 로고
    • Cutting edge: The conversion of arginine to citrulline allows for a high-affinity peptide interaction with the rheumatoid arthritis-associated HLADRB1* 0401 MHC class II molecule
    • Hill, J. A., S. Southwood, A. Sette, et al. 2003. Cutting edge: the conversion of arginine to citrulline allows for a high-affinity peptide interaction with the rheumatoid arthritis-associated HLADRB1* 0401 MHC class II molecule. J. Immunol. 171: 538-541.
    • (2003) J. Immunol , vol.171 , pp. 538-541
    • Hill, J.A.1    Southwood, S.2    Sette, A.3
  • 36
    • 0020616433 scopus 로고
    • Measurements of S-adenosylmethionine and L-homocysteine metabolism in cultured human lymphoid cells
    • German, D. C., C. A. Bloch, and N. M. Kredich. 1983. Measurements of S-adenosylmethionine and L-homocysteine metabolism in cultured human lymphoid cells. J. Biol. Chem. 258: 10997-11003.
    • (1983) J. Biol. Chem , vol.258 , pp. 10997-11003
    • German, D.C.1    Bloch, C.A.2    Kredich, N.M.3
  • 37
    • 0035831040 scopus 로고    scopus 로고
    • Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription
    • Mowen, K. A., J. Tang, W. Zhu, et al. 2001. Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription. Cell 104: 731-741.
    • (2001) Cell , vol.104 , pp. 731-741
    • Mowen, K.A.1    Tang, J.2    Zhu, W.3
  • 38
    • 23744438500 scopus 로고    scopus 로고
    • CD28 costimulatory signal induces protein arginine methylation in T cells
    • Blanchet, F., A. Cardona, F. A. Letimier, et al. 2005. CD28 costimulatory signal induces protein arginine methylation in T cells. J. Exp. Med. 202: 371-377.
    • (2005) J. Exp. Med , vol.202 , pp. 371-377
    • Blanchet, F.1    Cardona, A.2    Letimier, F.A.3
  • 39
    • 42649095663 scopus 로고    scopus 로고
    • Epigenetics in human autoimmunity. Epigenetics in autoimmunity-DNA methylation in systemic lupus erythematosus and beyond
    • Strickland, F. M., and B. C. Richardson. 2008. Epigenetics in human autoimmunity. Epigenetics in autoimmunity-DNA methylation in systemic lupus erythematosus and beyond. Autoimmunity 41: 278-286.
    • (2008) Autoimmunity , vol.41 , pp. 278-286
    • Strickland, F.M.1    Richardson, B.C.2
  • 40
    • 0034625091 scopus 로고    scopus 로고
    • Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D
    • Pritzker, L. B., S. Joshi, J. J. Gowan, et al. 2000. Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D. Biochemistry 39: 5374-5381.
    • (2000) Biochemistry , vol.39 , pp. 5374-5381
    • Pritzker, L.B.1    Joshi, S.2    Gowan, J.J.3
  • 41
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • Lin, W. J., J. D. Gary, M. C. Yang, et al. 1996. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J. Biol. Chem. 271: 15034-15044.
    • (1996) J. Biol. Chem , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3
  • 42
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • Bedford, M. T., and S. G. Clarke. 2009. Protein arginine methylation in mammals: who, what, and why. Mol. Cell. 33: 1-13.
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 43
    • 8844266055 scopus 로고    scopus 로고
    • Arginine methylation of STAT1: A reassessment
    • discussion 589-590
    • Meissner, T., E. Krause, I. Lodige, and U. Vinkemeier. 2004. Arginine methylation of STAT1: a reassessment. Cell 119: 587-589; discussion 589-590.
    • (2004) Cell , vol.119 , pp. 587-589
    • Meissner, T.1    Krause, E.2    Lodige, I.3    Vinkemeier, U.4
  • 44
    • 77950189497 scopus 로고    scopus 로고
    • Protein arginine methylation: A new handle on T lymphocytes?
    • Parry, R. V., and S. G. Ward. 2010. Protein arginine methylation: a new handle on T lymphocytes? Trends Immunol. 31: 164-169.
    • (2010) Trends Immunol , vol.31 , pp. 164-169
    • Parry, R.V.1    Ward, S.G.2
  • 45
    • 4344629701 scopus 로고    scopus 로고
    • Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes
    • Mowen, K. A., B. T. Schurter, J. W. Fathman, et al. 2004. Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes. Mol. Cell. 15: 559-571.
    • (2004) Mol. Cell , vol.15 , pp. 559-571
    • Mowen, K.A.1    Schurter, B.T.2    Fathman, J.W.3
  • 46
    • 0035800524 scopus 로고    scopus 로고
    • Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor
    • Wang, H., Z. Q. Huang, L. Xia, et al. 2001. Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. Science 293: 853-857.
    • (2001) Science , vol.293 , pp. 853-857
    • Wang, H.1    Huang, Z.Q.2    Xia, L.3
  • 47
    • 23944435995 scopus 로고    scopus 로고
    • Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications
    • Huang, S., M. Litt, and G. Felsenfeld. 2005. Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications. Genes Dev. 19: 1885-1893.
    • (2005) Genes Dev , vol.19 , pp. 1885-1893
    • Huang, S.1    Litt, M.2    Felsenfeld, G.3
  • 48
    • 77950390899 scopus 로고    scopus 로고
    • H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation
    • Li, X., X. Hu, B. Patel, et al. 2010. H4R3 methylation facilitates beta-globin transcription by regulating histone acetyltransferase binding and H3 acetylation. Blood 115: 2028-2037.
    • (2010) Blood , vol.115 , pp. 2028-2037
    • Li, X.1    Hu, X.2    Patel, B.3
  • 49
    • 44349087706 scopus 로고    scopus 로고
    • Abnormal histone modification patterns in lupus CD4\+ T cells
    • Hu, N., X. Qiu, Y. Luo, et al. 2008. Abnormal histone modification patterns in lupus CD4\+ T cells. J. Rheumatol. 35: 804-810.
    • (2008) J. Rheumatol , vol.35 , pp. 804-810
    • Hu, N.1    Qiu, X.2    Luo, Y.3
  • 50
    • 32244442562 scopus 로고    scopus 로고
    • TGFbeta in the context of an inflammatory cytokine milieu supports de novo differentiation of IL-17-producing T cells
    • Veldhoen, M., R. J. Hocking, C. J. Atkins, et al. 2006. TGFbeta in the context of an inflammatory cytokine milieu supports de novo differentiation of IL-17-producing T cells. Immunity 24: 179-189.
    • (2006) Immunity , vol.24 , pp. 179-189
    • Veldhoen, M.1    Hocking, R.J.2    Atkins, C.J.3
  • 51
    • 34147138648 scopus 로고    scopus 로고
    • Chromatin remodeling of interleukin-17 (IL-17)-IL-17F cytokine gene locus during inflammatory helper T cell differentiation
    • Akimzhanov, A. M., X. O. Yang, and C. Dong. 2007. Chromatin remodeling of interleukin-17 (IL-17)-IL-17F cytokine gene locus during inflammatory helper T cell differentiation. J. Biol. Chem. 282: 5969-5972.
    • (2007) J. Biol. Chem , vol.282 , pp. 5969-5972
    • Akimzhanov, A.M.1    Yang, X.O.2    Dong, C.3
  • 53
    • 80053286823 scopus 로고    scopus 로고
    • Abnormalities of T cell signaling in systemic lupus erythematosus
    • Moulton, V. R., and G. C. Tsokos. 2011. Abnormalities of T cell signaling in systemic lupus erythematosus. Arthritis Res. Ther. 13: 207.
    • (2011) Arthritis Res. Ther , vol.13 , pp. 207
    • Moulton, V.R.1    Tsokos, G.C.2
  • 54
    • 0033509042 scopus 로고    scopus 로고
    • Th1/Th2 balance of peripheral T helper cells in systemic lupus erythematosus
    • Akahoshi, M., H. Nakashima, Y. Tanaka, et al. 1999. Th1/Th2 balance of peripheral T helper cells in systemic lupus erythematosus. Arthritis Rheum. 42: 1644-1648.
    • (1999) Arthritis Rheum , vol.42 , pp. 1644-1648
    • Akahoshi, M.1    Nakashima, H.2    Tanaka, Y.3
  • 55
    • 77955356159 scopus 로고    scopus 로고
    • Cytokine overproduction, T-cell activation, and defective T-regulatory functions promote nephritis in systemic lupus erythematosus
    • Article ID 457146
    • Tucci, M., S. Stucci, S. Strippoli, and F. Silvestris. 2010. Cytokine overproduction, T-cell activation, and defective T-regulatory functions promote nephritis in systemic lupus erythematosus. J. Biomed. Biotechnol. 2010: Article ID 457146.
    • (2010) J. Biomed. Biotechnol , vol.2010
    • Tucci, M.1    Stucci, S.2    Strippoli, S.3    Silvestris, F.4
  • 56
    • 0042834349 scopus 로고    scopus 로고
    • A failure to repair self-proteins leads to T cell hyperproliferation and autoantibody production
    • Doyle, H. A., R. J. Gee, and M. J. Mamula. 2003. A failure to repair self-proteins leads to T cell hyperproliferation and autoantibody production. J. Immunol. 171: 2840-2847.
    • (2003) J. Immunol , vol.171 , pp. 2840-2847
    • Doyle, H.A.1    Gee, R.J.2    Mamula, M.J.3
  • 57
    • 33749143447 scopus 로고    scopus 로고
    • Intracellular protein modification associated with altered T cell functions in autoimmunity
    • Yang, M. L., H. A. Doyle, R. J. Gee, et al. 2006. Intracellular protein modification associated with altered T cell functions in autoimmunity. J. Immunol. 177: 4541-4549.
    • (2006) J. Immunol , vol.177 , pp. 4541-4549
    • Yang, M.L.1    Doyle, H.A.2    Gee, R.J.3
  • 58
    • 33745810970 scopus 로고    scopus 로고
    • Identification of brain cell death associated proteins in human post-mortem cerebrospinal fluid
    • Burgess, J. A., P. Lescuyer, A. Hainard, et al. 2006. Identification of brain cell death associated proteins in human post-mortem cerebrospinal fluid. J. Proteome Res. 5: 1674-1681.
    • (2006) J. Proteome Res , vol.5 , pp. 1674-1681
    • Burgess, J.A.1    Lescuyer, P.2    Hainard, A.3
  • 59
    • 20844433553 scopus 로고    scopus 로고
    • A proteomic analysis of human hemodialysis fluid
    • Molina, H., J. Bunkenborg, G. H. Reddy, et al. 2005. A proteomic analysis of human hemodialysis fluid. Mol. Cell. Proteomics 4: 637-650.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 637-650
    • Molina, H.1    Bunkenborg, J.2    Reddy, G.H.3
  • 60
    • 22544461658 scopus 로고    scopus 로고
    • Protein L-isoaspartyl methyltransferase catalyzes in vivo racemization of Aspartate-25 in mammalian histone H2B
    • Young, G. W., S. A. Hoofring, M. J. Mamula, et al. 2005. Protein L-isoaspartyl methyltransferase catalyzes in vivo racemization of Aspartate-25 in mammalian histone H2B. J. Biol. Chem. 280: 26094-26098.
    • (2005) J. Biol. Chem , vol.280 , pp. 26094-26098
    • Young, G.W.1    Hoofring, S.A.2    Mamula, M.J.3
  • 61
    • 0035827690 scopus 로고    scopus 로고
    • Limited accumulation of damaged proteins in l-isoaspartyl (D-aspartyl) O-methyltransferase-deficient mice
    • Lowenson, J. D., E. Kim, S. G. Young, and S. Clarke. 2001. Limited accumulation of damaged proteins in l-isoaspartyl (D-aspartyl) O-methyltransferase-deficient mice. J. Biol. Chem. 276: 20695-20702.
    • (2001) J. Biol. Chem , vol.276 , pp. 20695-20702
    • Lowenson, J.D.1    Kim, E.2    Young, S.G.3    Clarke, S.4
  • 62
    • 0025853823 scopus 로고
    • Deamidation of soluble CD4 at asparagine-52 results in reduced binding capacity for the HIV-1 envelope glycoprotein gp120
    • Teshima, G., J. Porter, K. Yim, et al. 1991. Deamidation of soluble CD4 at asparagine-52 results in reduced binding capacity for the HIV-1 envelope glycoprotein gp120. Biochemistry 30: 3916-3922.
    • (1991) Biochemistry , vol.30 , pp. 3916-3922
    • Teshima, G.1    Porter, J.2    Yim, K.3
  • 63
    • 84863258188 scopus 로고    scopus 로고
    • Integrin signalling and function in immune cells
    • Zhang, Y., and H. Wang. 2012. Integrin signalling and function in immune cells. Immunology 135:268-275.
    • (2012) Immunology , vol.135 , pp. 268-275
    • Zhang, Y.1    Wang, H.2
  • 64
    • 79953090989 scopus 로고    scopus 로고
    • The integrin LFA-1 signals through ZAP-70 to regulate expression of highaffinity LFA-1 on T lymphocytes
    • Evans, R., A. C. Lellouch, L. Svensson, et al. 2011. The integrin LFA-1 signals through ZAP-70 to regulate expression of highaffinity LFA-1 on T lymphocytes. Blood 117: 3331-3342.
    • (2011) Blood , vol.117 , pp. 3331-3342
    • Evans, R.1    Lellouch, A.C.2    Svensson, L.3
  • 65
    • 79951839235 scopus 로고    scopus 로고
    • Isoaspartate-dependent molecular switches for integrin-ligand recognition
    • Corti, A., and F. Curnis. 2011. Isoaspartate-dependent molecular switches for integrin-ligand recognition. J. Cell Sci. 124: 515-522.
    • (2011) J. Cell Sci , vol.124 , pp. 515-522
    • Corti, A.1    Curnis, F.2
  • 66
    • 84858081105 scopus 로고    scopus 로고
    • Transmethylation in immunity and autoimmunity
    • Lawson, B. R., T. Eleftheriadis, V. Tardif, et al. 2012. Transmethylation in immunity and autoimmunity. Clin. Immunol. 143: 8-21.
    • (2012) Clin. Immunol , vol.143 , pp. 8-21
    • Lawson, B.R.1    Eleftheriadis, T.2    Tardif, V.3
  • 67
    • 73249146755 scopus 로고    scopus 로고
    • DNA hypomethylation in rheumatoid arthritis synovial fibroblasts
    • Karouzakis, E., R. E. Gay, B. A. Michel, et al. 2009. DNA hypomethylation in rheumatoid arthritis synovial fibroblasts. Arthritis Rheum. 60: 3613-3622.
    • (2009) Arthritis Rheum , vol.60 , pp. 3613-3622
    • Karouzakis, E.1    Gay, R.E.2    Michel, B.A.3
  • 68
    • 20944436684 scopus 로고    scopus 로고
    • Inhibition of S-adenosyl-L-homocysteine hydrolase induces immunosuppression
    • Wu, Q. L., Y. F. Fu, W. L. Zhou, et al. 2005. Inhibition of S-adenosyl-L-homocysteine hydrolase induces immunosuppression. J. Pharmacol. Exp. Ther. 313: 705-711.
    • (2005) J. Pharmacol. Exp. Ther , vol.313 , pp. 705-711
    • Wu, Q.L.1    Fu, Y.F.2    Zhou, W.L.3
  • 69
    • 33644770348 scopus 로고    scopus 로고
    • S-adenosyl-Lhomocysteine hydrolase inactivation curtails ovalbumin-induced immune responses
    • Fu, Y. F., J. X. Wang, Y. Zhao, et al. 2006. S-adenosyl-Lhomocysteine hydrolase inactivation curtails ovalbumin-induced immune responses. J. Pharmacol. Exp. Ther. 316: 1229-1237.
    • (2006) J. Pharmacol. Exp. Ther , vol.316 , pp. 1229-1237
    • Fu, Y.F.1    Wang, J.X.2    Zhao, Y.3
  • 70
    • 0027220379 scopus 로고
    • Immunomodulation by an inhibitor of S-adenosyl-L-homocysteine hydrolase: Inhibition of in vitro and in vivo allogeneic responses
    • Wolos, J. A., K. A. Frondorf, G. F. Babcock, et al. 1993. Immunomodulation by an inhibitor of S-adenosyl-L-homocysteine hydrolase: inhibition of in vitro and in vivo allogeneic responses. Cell. Immunol. 149: 402-408.
    • (1993) Cell. Immunol , vol.149 , pp. 402-408
    • Wolos, J.A.1    Frondorf, K.A.2    Babcock, G.F.3
  • 71
    • 0027314792 scopus 로고
    • Selective inhibition of T cell activation by an inhibitor of S-adenosyl-Lhomocysteine hydrolase
    • Wolos, J. A., K. A. Frondorf, G. F. Davis, et al. 1993. Selective inhibition of T cell activation by an inhibitor of S-adenosyl-Lhomocysteine hydrolase. J. Immunol. 150: 3264-3273.
    • (1993) J. Immunol , vol.150 , pp. 3264-3273
    • Wolos, J.A.1    Frondorf, K.A.2    Davis, G.F.3
  • 72
    • 66549105934 scopus 로고    scopus 로고
    • Multiple sclerosis-a response-to-damage model
    • 't Hart, B. A., R. Q. Hintzen, and J. D. Laman. 2009. Multiple sclerosis-a response-to-damage model. Trends Mol. Med. 15: 235-244.
    • (2009) Trends Mol. Med , vol.15 , pp. 235-244
    • Hart B A, T.1    Hintzen, R.Q.2    Laman, J.D.3
  • 73
    • 0025882122 scopus 로고
    • Enhanced CD3-mediated T lymphocyte proliferation in patients with systemic lupus erythematosus
    • Stekman, I. L., A. M. Blasini, M. Leon-Ponte, et al. 1991. Enhanced CD3-mediated T lymphocyte proliferation in patients with systemic lupus erythematosus. Arthritis Rheum. 34: 459-467.
    • (1991) Arthritis Rheum , vol.34 , pp. 459-467
    • Stekman, I.L.1    Blasini, A.M.2    Leon-Ponte, M.3
  • 74
    • 0035808778 scopus 로고    scopus 로고
    • CD4(\+) T cells from lupus-prone mice are hyperresponsive to T cell receptor engagement with low and high affinity peptide antigens: A model to explain spontaneous T cell activation in lupus
    • Vratsanos, G. S., S. Jung, Y. M. Park, and J. Craft. 2001. CD4(\+) T cells from lupus-prone mice are hyperresponsive to T cell receptor engagement with low and high affinity peptide antigens: a model to explain spontaneous T cell activation in lupus. J. Exp. Med. 193: 329-337.
    • (2001) J. Exp. Med , vol.193 , pp. 329-337
    • Vratsanos, G.S.1    Jung, S.2    Park, Y.M.3    Craft, J.4
  • 75
    • 0035196908 scopus 로고    scopus 로고
    • S-Adenosyl-L-homocysteine hydrolase inhibitor mediates immunosuppressive effects in vivo: Suppression of delayed type hypersensitivity ear swelling and peptidoglycan polysaccharide-induced arthritis
    • Saso, Y., E. M. Conner, B. R. Teegarden, and C. S. Yuan. 2001. S-Adenosyl-L-homocysteine hydrolase inhibitor mediates immunosuppressive effects in vivo: suppression of delayed type hypersensitivity ear swelling and peptidoglycan polysaccharide-induced arthritis. J. Pharmacol. Exp. Ther. 296: 106-112.
    • (2001) J. Pharmacol. Exp. Ther , vol.296 , pp. 106-112
    • Saso, Y.1    Conner, E.M.2    Teegarden, B.R.3    Yuan, C.S.4
  • 76
    • 34247148164 scopus 로고    scopus 로고
    • Inhibition of transmethylation down-regulates CD4 T cell activation and curtails development of autoimmunity in a model system
    • Lawson, B. R., Y. Manenkova, J. Ahamed, et al. 2007. Inhibition of transmethylation down-regulates CD4 T cell activation and curtails development of autoimmunity in a model system. J. Immunol. 178: 5366-5374.
    • (2007) J. Immunol , vol.178 , pp. 5366-5374
    • Lawson, B.R.1    Manenkova, Y.2    Ahamed, J.3
  • 77
    • 84872184582 scopus 로고    scopus 로고
    • Lupus autoimmunity altered by cellular methylation metabolism
    • Yang, M. L., A. J. Gee, R. J. Gee, et al. 2013. Lupus autoimmunity altered by cellular methylation metabolism. Autoimmunity 46: 21-31.
    • (2013) Autoimmunity , vol.46 , pp. 21-31
    • Yang, M.L.1    Gee, A.J.2    Gee, R.J.3
  • 78
    • 2642551574 scopus 로고    scopus 로고
    • Small molecule regulators of protein arginine methyltransferases
    • Cheng, D., N. Yadav, R. W. King, et al. 2004. Small molecule regulators of protein arginine methyltransferases. J. Biol. Chem. 279: 23892-23899.
    • (2004) J. Biol. Chem , vol.279 , pp. 23892-23899
    • Cheng, D.1    Yadav, N.2    King, R.W.3
  • 79
    • 77951237941 scopus 로고    scopus 로고
    • Effects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine production
    • Bonham, K., S. Hemmers, Y. H. Lim, et al. 2010. Effects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine production. FEBS J. 277: 2096-2108.
    • (2010) FEBS J , vol.277 , pp. 2096-2108
    • Bonham, K.1    Hemmers, S.2    Lim, Y.H.3
  • 80
    • 84864125680 scopus 로고    scopus 로고
    • Novel inhibitors for PRMT1 discovered by high-throughput screening using activity-based fluorescence polarization
    • Dillon, M. B., D. A. Bachovchin, S. J. Brown, et al. 2012. Novel inhibitors for PRMT1 discovered by high-throughput screening using activity-based fluorescence polarization. ACS Chem. Biol. 7: 1198-1204.
    • (2012) ACS Chem. Biol , vol.7 , pp. 1198-1204
    • Dillon, M.B.1    Bachovchin, D.A.2    Brown, S.J.3
  • 81
    • 0020436689 scopus 로고
    • The 1982 revised criteria for the classification of systemic lupus erythematosus
    • Tan, E. M., A. S. Cohen, J. F. Fries, et al. 1982. The 1982 revised criteria for the classification of systemic lupus erythematosus. Arthritis Rheum. 25: 1271-1277.
    • (1982) Arthritis Rheum , vol.25 , pp. 1271-1277
    • Tan, E.M.1    Cohen, A.S.2    Fries, J.F.3
  • 82
    • 84875934940 scopus 로고    scopus 로고
    • The critical importance of epigenetics in autoimmunity
    • Lu, Q. 2013. The critical importance of epigenetics in autoimmunity. J. Autoimmun. 41: 1-5.
    • (2013) J. Autoimmun , vol.41 , pp. 1-5
    • Lu, Q.1
  • 84
    • 79251542357 scopus 로고    scopus 로고
    • Epigenetics in lupus
    • Zouali, M. 2011. Epigenetics in lupus. Ann. N. Y. Acad. Sci. 1217: 154-165.
    • (2011) Ann. N. Y. Acad. Sci , vol.1217 , pp. 154-165
    • Zouali, M.1
  • 85
    • 0032774579 scopus 로고    scopus 로고
    • Abnormal DNA methylation and deoxycytosine-deoxyguanine content in nucleosomes from lymphocytes undergoing apoptosis
    • Huck, S., E. Deveaud, A. Namane, and M. Zouali. 1999. Abnormal DNA methylation and deoxycytosine-deoxyguanine content in nucleosomes from lymphocytes undergoing apoptosis. FASEB J. 13: 1415-1422.
    • (1999) FASEB J , vol.13 , pp. 1415-1422
    • Huck, S.1    Deveaud, E.2    Namane, A.3    Zouali, M.4
  • 86
    • 0030199627 scopus 로고    scopus 로고
    • DNA methylation: A potential pathway to abnormal autoreactive lupus B cells
    • Huck, S., and M. Zouali. 1996. DNA methylation: a potential pathway to abnormal autoreactive lupus B cells. Clin. Immunol. Immunopathol. 80: 1-8.
    • (1996) Clin. Immunol. Immunopathol , vol.80 , pp. 1-8
    • Huck, S.1    Zouali, M.2
  • 87
    • 4043079297 scopus 로고    scopus 로고
    • Apoptosis in systemic lupus erythematosus
    • Kaplan, M. J. 2004. Apoptosis in systemic lupus erythematosus. Clin. Immunol. 112: 210-218.
    • (2004) Clin. Immunol , vol.112 , pp. 210-218
    • Kaplan, M.J.1
  • 88
    • 4143140030 scopus 로고    scopus 로고
    • A mouse skin multistage carcinogenesis model reflects the aberrant DNA methylation patterns of human tumors
    • Fraga, M. F., M. Herranz, J. Espada, et al. 2004. A mouse skin multistage carcinogenesis model reflects the aberrant DNA methylation patterns of human tumors. Cancer Res. 64: 5527-5534.
    • (2004) Cancer Res , vol.64 , pp. 5527-5534
    • Fraga, M.F.1    Herranz, M.2    Espada, J.3
  • 89
    • 67650360177 scopus 로고    scopus 로고
    • Epigenetic control in rheumatoid arthritis synovial fibroblasts
    • Karouzakis, E., R. E. Gay, S. Gay, and M. Neidhart. 2009. Epigenetic control in rheumatoid arthritis synovial fibroblasts. Nat. Rev. Rheumatol. 5: 266-272.
    • (2009) Nat. Rev. Rheumatol , vol.5 , pp. 266-272
    • Karouzakis, E.1    Gay, R.E.2    Gay, S.3    Neidhart, M.4
  • 90
    • 84876894882 scopus 로고    scopus 로고
    • The applied basic research of systemic lupus erythematosus based on the biological omics
    • Sui, W., X. Hou, W. Che, et al. 2013. The applied basic research of systemic lupus erythematosus based on the biological omics. Genes Immun. 14: 133-146.
    • (2013) Genes Immun , vol.14 , pp. 133-146
    • Sui, W.1    Hou, X.2    Che, W.3
  • 91
    • 77954088653 scopus 로고    scopus 로고
    • Epigenetic histone code and autoimmunity
    • Dieker, J., and S. Muller. 2010. Epigenetic histone code and autoimmunity. Clin. Rev. Allergy Immunol. 39: 78-84.
    • (2010) Clin. Rev. Allergy Immunol , vol.39 , pp. 78-84
    • Dieker, J.1    Muller, S.2
  • 92
    • 77957942335 scopus 로고    scopus 로고
    • Apoptosisinduced histone H3 methylation is targeted by autoantibodies in systemic lupus erythematosus
    • van Bavel, C. C., J. W. Dieker, Y. Kroeze, et al. 2011. Apoptosisinduced histone H3 methylation is targeted by autoantibodies in systemic lupus erythematosus. Ann. Rheum. Dis. 70: 201-207.
    • (2011) Ann. Rheum. Dis , vol.70 , pp. 201-207
    • Van Bavel, C.C.1    Dieker, J.W.2    Kroeze, Y.3
  • 93
    • 3543004695 scopus 로고    scopus 로고
    • Structural basis for Ca(2\+)-induced activation of human PAD4
    • Arita, K., H. Hashimoto, T. Shimizu, et al. 2004. Structural basis for Ca(2\+)-induced activation of human PAD4. Nat. Struct. Mol. Biol. 11: 777-783.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 777-783
    • Arita, K.1    Hashimoto, H.2    Shimizu, T.3
  • 94
    • 33846691023 scopus 로고    scopus 로고
    • Very recent onset rheumatoid arthritis: Clinical and serological patient characteristics associated with radiographic progression over the first years of disease
    • Machold, K. P., T. A. Stamm, V. P. Nell, et al. 2007. Very recent onset rheumatoid arthritis: clinical and serological patient characteristics associated with radiographic progression over the first years of disease. Rheumatology (Oxford) 46: 342-349.
    • (2007) Rheumatology (Oxford) , vol.46 , pp. 342-349
    • MacHold, K.P.1    Stamm, T.A.2    Nell, V.P.3
  • 95
    • 41149122132 scopus 로고    scopus 로고
    • Proteomics in rheumatology: The beginning of a fairy tale? Proteomics Clin
    • Lambrecht, S., K. Tilleman, D. Elewaut, and D. Deforce. 2008. Proteomics in rheumatology: the beginning of a fairy tale? Proteomics Clin. Appl. 2: 411-419.
    • (2008) Appl , vol.2 , pp. 411-419
    • Lambrecht, S.1    Tilleman, K.2    Elewaut, D.3    Deforce, D.4
  • 96
    • 0031974911 scopus 로고    scopus 로고
    • Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies
    • Schellekens, G. A., B. A. de Jong, F. H. van den Hoogen, et al. 1998. Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies. J. Clin. Invest. 101: 273-281.
    • (1998) J. Clin. Invest , vol.101 , pp. 273-281
    • Schellekens, G.A.1    De Jong, B.A.2    Hoogen Den Van, F.H.3
  • 97
    • 81855194496 scopus 로고    scopus 로고
    • Multicentric evaluation of a second generation assay to detect antiviral citrullinated peptide antibodies: A collaborative study by the Forum Interdisciplinare per la Ricerca nelle Malattie Autoimmuni
    • Bizzaro, N., F. Allegri, C. Alpini, et al. 2011. Multicentric evaluation of a second generation assay to detect antiviral citrullinated peptide antibodies: a collaborative study by the Forum Interdisciplinare per la Ricerca nelle Malattie Autoimmuni. J. Clin. Pathol. 64: 1139-1141.
    • (2011) J. Clin. Pathol , vol.64 , pp. 1139-1141
    • Bizzaro, N.1    Allegri, F.2    Alpini, C.3
  • 98
    • 33751001725 scopus 로고    scopus 로고
    • Histone citrullination by protein arginine deiminase: Is arginine methylation a green light or a roadblock?
    • Thompson, P. R., and W. Fast. 2006. Histone citrullination by protein arginine deiminase: is arginine methylation a green light or a roadblock? ACS Chem. Biol. 1:433-441.
    • (2006) ACS Chem Biol , vol.1 , pp. 433-441
    • Thompson, P.R.1    Fast, W.2
  • 99
    • 85027954125 scopus 로고    scopus 로고
    • DNA methylation profiling in the clinic: Applications and challenges
    • Heyn, H., and M. Esteller. 2012. DNA methylation profiling in the clinic: applications and challenges. Nat. Rev. Genet. 13: 679-692.
    • (2012) Nat. Rev. Genet , vol.13 , pp. 679-692
    • Heyn, H.1    Esteller, M.2
  • 100
    • 0027983579 scopus 로고
    • The role of B cells in lpr/lpr-induced autoimmunity
    • Shlomchik, M. J., M. P. Madaio, D. Ni, et al. 1994. The role of B cells in lpr/lpr-induced autoimmunity. J. Exp. Med. 180: 1295-1306.
    • (1994) J. Exp. Med , vol.180 , pp. 1295-1306
    • Shlomchik, M.J.1    Madaio, M.P.2    Ni, D.3
  • 101
    • 0033214474 scopus 로고    scopus 로고
    • B cells are required for lupus nephritis in the polygenic, Fas-intact MRL model of systemic autoimmunity
    • Chan, O. T., M. P. Madaio, and M. J. Shlomchik. 1999. B cells are required for lupus nephritis in the polygenic, Fas-intact MRL model of systemic autoimmunity. J. Immunol. 163: 3592-3596.
    • (1999) J. Immunol , vol.163 , pp. 3592-3596
    • Chan, O.T.1    Madaio, M.P.2    Shlomchik, M.J.3
  • 102
    • 0023483313 scopus 로고
    • Stochastic control of anti-Sm autoantibodies in MRL/Mplpr/lpr mice
    • Eisenberg, R. A., S. Y. Craven, R. W. Warren, and P. L. Cohen. 1987. Stochastic control of anti-Sm autoantibodies in MRL/Mplpr/lpr mice. J. Clin. Invest. 80: 691-697.
    • (1987) J. Clin. Invest , vol.80 , pp. 691-697
    • Eisenberg, R.A.1    Craven, S.Y.2    Warren, R.W.3    Cohen, P.L.4
  • 103
    • 84855363570 scopus 로고    scopus 로고
    • Discrimination of membrane antigen affinity by B cells requires dominance of kinetic proofreading over serial engagement
    • Tsourkas, P. K., W. Liu, S. C. Das, et al. 2012. Discrimination of membrane antigen affinity by B cells requires dominance of kinetic proofreading over serial engagement. Cell. Mol. Immunol. 9: 62-74.
    • (2012) Cell. Mol. Immunol , vol.9 , pp. 62-74
    • Tsourkas, P.K.1    Liu, W.2    Das, S.C.3
  • 104
    • 79959371732 scopus 로고    scopus 로고
    • B cell receptormediated antigen gathering requires ubiquitin ligase Cbl and adaptors Grb2 and Dok-3 to recruit dynein to the signaling microcluster
    • Schnyder, T., A. Castello, C. Feest, et al. 2011. B cell receptormediated antigen gathering requires ubiquitin ligase Cbl and adaptors Grb2 and Dok-3 to recruit dynein to the signaling microcluster. Immunity 34: 905-918.
    • (2011) Immunity , vol.34 , pp. 905-918
    • Schnyder, T.1    Castello, A.2    Feest, C.3
  • 105
    • 80053607514 scopus 로고    scopus 로고
    • Cellular and molecular pathogenesis of systemic lupus erythematosus: Lessons from animal models
    • Pathak, S., and C. Mohan. 2011. Cellular and molecular pathogenesis of systemic lupus erythematosus: lessons from animal models. Arthritis Res. Ther. 13: 241.
    • (2011) Arthritis Res. Ther , vol.13 , pp. 241
    • Pathak, S.1    Mohan, C.2
  • 106
    • 81955161811 scopus 로고    scopus 로고
    • Monophosphorylation of CD79a and CD79b ITAM motifs initiates a SHIP-1 phosphatase-mediated inhibitory signaling cascade required for B cell anergy
    • O'Neill, S. K., A. Getahun, S. B. Gauld, et al. 2011. Monophosphorylation of CD79a and CD79b ITAM motifs initiates a SHIP-1 phosphatase-mediated inhibitory signaling cascade required for B cell anergy. Immunity 35: 746-756.
    • (2011) Immunity , vol.35 , pp. 746-756
    • O'Neill, S.K.1    Getahun, A.2    Gauld, S.B.3
  • 108
    • 84872943896 scopus 로고    scopus 로고
    • Invariant natural killer T cells: An innate activation scheme linked to diverse effector functions
    • Brennan, P. J., M. Brigl, and M. B. Brenner. 2013. Invariant natural killer T cells: an innate activation scheme linked to diverse effector functions. Nat. Rev. Immunol. 13: 101-117.
    • (2013) Nat. Rev. Immunol , vol.13 , pp. 101-117
    • Brennan, P.J.1    Brigl, M.2    Brenner, M.B.3
  • 109
    • 0029558337 scopus 로고
    • In vivo expression of a single viral DNA-binding protein generates systemic lupus erythematosus-related autoimmunity to doublestranded DNA and histones
    • Moens, U., O. M. Seternes, A. W. Hey, et al. 1995. In vivo expression of a single viral DNA-binding protein generates systemic lupus erythematosus- related autoimmunity to doublestranded DNA and histones. Proc. Natl. Acad. Sci. USA. 92: 12393-12397.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12393-12397
    • Moens, U.1    Seternes, O.M.2    Hey, A.W.3
  • 110
    • 0033739280 scopus 로고    scopus 로고
    • Induction of anti-DNA antibody with DNA-peptide complexes
    • Desai, D. D., and T. N. Marion. 2000. Induction of anti-DNA antibody with DNA-peptide complexes. Int. Immunol. 12: 1569-1578.
    • (2000) Int. Immunol , vol.12 , pp. 1569-1578
    • Desai, D.D.1    Marion, T.N.2
  • 111
    • 0035525528 scopus 로고    scopus 로고
    • From T to B and back again: Positive feedback in systemic autoimmune disease
    • Shlomchik, M. J., J. E. Craft, and M. J. Mamula. 2001. From T to B and back again: positive feedback in systemic autoimmune disease. Nat. Rev. Immunol. 1: 147-153.
    • (2001) Nat. Rev. Immunol , vol.1 , pp. 147-153
    • Shlomchik, M.J.1    Craft, J.E.2    Mamula, M.J.3
  • 112
    • 0032100706 scopus 로고    scopus 로고
    • Affinity dependence of the B cell response to antigen: A threshold, a ceiling, and the importance of off-rate
    • Batista, F. D., and M. S. Neuberger. 1998. Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate. Immunity 8: 751-759.
    • (1998) Immunity , vol.8 , pp. 751-759
    • Batista, F.D.1    Neuberger, M.S.2
  • 113
    • 0032547805 scopus 로고    scopus 로고
    • Antigens varying in affinity for the B cell receptor induce differential B lymphocyte responses
    • Kouskoff, V., S. Famiglietti, G. Lacaud, et al. 1998. Antigens varying in affinity for the B cell receptor induce differential B lymphocyte responses. J. Exp. Med. 188: 1453-1464.
    • (1998) J. Exp. Med , vol.188 , pp. 1453-1464
    • Kouskoff, V.1    Famiglietti, S.2    Lacaud, G.3
  • 114
    • 84861914965 scopus 로고    scopus 로고
    • MHC class II distribution in dendritic cells and B cells is determined by ubiquitin chain length
    • Ma, J. K., M. Y. Platt, J. Eastham-Anderson, et al. 2012. MHC class II distribution in dendritic cells and B cells is determined by ubiquitin chain length. Proc. Natl. Acad. Sci. USA. 109: 8820-8827.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8820-8827
    • Ma, J.K.1    Platt, M.Y.2    Eastham-Anderson, J.3
  • 115
    • 0035942781 scopus 로고    scopus 로고
    • B cells acquire antigen from target cells after synapse formation
    • Batista, F. D., D. Iber, and M. S. Neuberger. 2001. B cells acquire antigen from target cells after synapse formation. Nature 411: 489-494.
    • (2001) Nature , vol.411 , pp. 489-494
    • Batista, F.D.1    Iber, D.2    Neuberger, M.S.3
  • 116
    • 58149097584 scopus 로고    scopus 로고
    • The who, how and where of antigen presentation to B cells
    • Batista, F. D., and N. E. Harwood. 2009. The who, how and where of antigen presentation to B cells. Nat. Rev. Immunol. 9: 15-27.
    • (2009) Nat. Rev. Immunol , vol.9 , pp. 15-27
    • Batista, F.D.1    Harwood, N.E.2
  • 117
    • 80053130049 scopus 로고    scopus 로고
    • Polarized secretion of lysosomes at the B cell synapse couples antigen extraction to processing and presentation
    • Yuseff, M. I., A. Reversat, D. Lankar, et al. 2011. Polarized secretion of lysosomes at the B cell synapse couples antigen extraction to processing and presentation. Immunity 35: 361-374.
    • (2011) Immunity , vol.35 , pp. 361-374
    • Yuseff, M.I.1    Reversat, A.2    Lankar, D.3
  • 118
    • 73949150306 scopus 로고    scopus 로고
    • Macrophages create an acidic extracellular hydrolytic compartment to digest aggregated lipoproteins
    • Haka, A. S., I. Grosheva, E. Chiang, et al. 2009. Macrophages create an acidic extracellular hydrolytic compartment to digest aggregated lipoproteins. Mol. Biol. Cell. 20: 4932-4940.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4932-4940
    • Haka, A.S.1    Grosheva, I.2    Chiang, E.3
  • 119
    • 42149097910 scopus 로고    scopus 로고
    • CD40 Ligand-activated, antigen-specific B cells are comparable to mature dendritic cells in presenting protein antigens and major histocompatibility complex class I-and class II-binding peptides
    • Ahmadi, T., A. Flies, Y. Efebera, and D. H. Sherr. 2008. CD40 Ligand-activated, antigen-specific B cells are comparable to mature dendritic cells in presenting protein antigens and major histocompatibility complex class I-and class II-binding peptides. Immunology 124: 129-140.
    • (2008) Immunology , vol.124 , pp. 129-140
    • Ahmadi, T.1    Flies, A.2    Efebera, Y.3    Sherr, D.H.4
  • 120
    • 0034671618 scopus 로고    scopus 로고
    • Activation of MHC class I, II, and CD40 gene expression by histone deacetylase inhibitors
    • Magner, W. J., A. L. Kazim, C. Stewart, et al. 2000. Activation of MHC class I, II, and CD40 gene expression by histone deacetylase inhibitors. J. Immunol. 165: 7017-7024.
    • (2000) J. Immunol , vol.165 , pp. 7017-7024
    • Magner, W.J.1    Kazim, A.L.2    Stewart, C.3
  • 121
    • 0347717886 scopus 로고    scopus 로고
    • CD40 stimulation induces Pax5/BSAP and EBF activation through a APE/Ref-1-dependent redox mechanism
    • Merluzzi, S., M. Moretti, S. Altamura, et al. 2004. CD40 stimulation induces Pax5/BSAP and EBF activation through a APE/Ref-1-dependent redox mechanism. J. Biol. Chem. 279: 1777-1786.
    • (2004) J. Biol. Chem , vol.279 , pp. 1777-1786
    • Merluzzi, S.1    Moretti, M.2    Altamura, S.3
  • 122
    • 69249245325 scopus 로고    scopus 로고
    • Cell contactdependent acquisition of cellular and viral nonautonomously encoded small RNAs
    • Rechavi, O., Y. Erlich, H. Amram, et al. 2009. Cell contactdependent acquisition of cellular and viral nonautonomously encoded small RNAs. Genes Dev. 23: 1971-1979.
    • (2009) Genes Dev , vol.23 , pp. 1971-1979
    • Rechavi, O.1    Erlich, Y.2    Amram, H.3
  • 123
    • 55249118463 scopus 로고    scopus 로고
    • Intercellular trogocytosis plays an important role in modulation of immune responses
    • Ahmed, K. A., M. A. Munegowda, Y. Xie, and J. Xiang. 2008. Intercellular trogocytosis plays an important role in modulation of immune responses. Cell. Mol. Immunol. 5: 261-269.
    • (2008) Cell. Mol. Immunol , vol.5 , pp. 261-269
    • Ahmed, K.A.1    Munegowda, M.A.2    Xie, Y.3    Xiang, J.4
  • 124
    • 47049090133 scopus 로고    scopus 로고
    • Capture of plasma membrane fragments from target cells by trogocytosis requires signaling in T cells but not in B cells
    • Aucher, A., E. Magdeleine, E. Joly, and D. Hudrisier. 2008. Capture of plasma membrane fragments from target cells by trogocytosis requires signaling in T cells but not in B cells. Blood 111: 5621-5628.
    • (2008) Blood , vol.111 , pp. 5621-5628
    • Aucher, A.1    Magdeleine, E.2    Joly, E.3    Hudrisier, D.4
  • 125
    • 64549145421 scopus 로고    scopus 로고
    • Intercellular exchanges of membrane fragments (trogocytosis) between human muscle cells and immune cells: A potential mechanism for the modulation of muscular immune responses
    • Waschbisch, A., S. G. Meuth, A. M. Herrmann, et al. 2009. Intercellular exchanges of membrane fragments (trogocytosis) between human muscle cells and immune cells: a potential mechanism for the modulation of muscular immune responses. J. Neuroimmunol. 209: 131-138.
    • (2009) J. Neuroimmunol , vol.209 , pp. 131-138
    • Waschbisch, A.1    Meuth, S.G.2    Herrmann, A.M.3
  • 126
    • 84868543217 scopus 로고    scopus 로고
    • Trogocytosis results in sustained intracellular signaling in CD4(\+) T cells
    • Osborne, D. G., and S. A. Wetzel. 2012. Trogocytosis results in sustained intracellular signaling in CD4(\+) T cells. J. Immunol. 189: 4728-4739.
    • (2012) J. Immunol , Issue.189 , pp. 4728-4739
    • Osborne, D.G.1    Wetzel, S.A.2
  • 127
    • 34447573637 scopus 로고    scopus 로고
    • Antigen presentation and transfer between B cells and macrophages
    • Harvey, B. P., R. J. Gee, A. M. Haberman, et al. 2007. Antigen presentation and transfer between B cells and macrophages. Eur. J. Immunol. 37: 1739-1751.
    • (2007) Eur. J. Immunol , vol.37 , pp. 1739-1751
    • Harvey, B.P.1    Gee, R.J.2    Haberman, A.M.3
  • 128
    • 56149106553 scopus 로고    scopus 로고
    • Editing antigen presentation: Antigen transfer between human B lymphocytes and macrophages mediated by class A scavenger receptors
    • Harvey, B. P., T. E. Quan, B. J. Rudenga, et al. 2008. Editing antigen presentation: antigen transfer between human B lymphocytes and macrophages mediated by class A scavenger receptors. J. Immunol. 181: 4043-4051.
    • (2008) J. Immunol , vol.181 , pp. 4043-4051
    • Harvey, B.P.1    Quan, T.E.2    Rudenga, B.J.3
  • 129
    • 84857325942 scopus 로고    scopus 로고
    • Inhibition of antigen trafficking through scavenger receptor A
    • Raycroft, M. T., B. P. Harvey, M. J. Bruck, and M. J. Mamula. 2012. Inhibition of antigen trafficking through scavenger receptor A. J. Biol. Chem. 287: 5310-5316.
    • (2012) J. Biol. Chem , vol.287 , pp. 5310-5316
    • Raycroft, M.T.1    Harvey, B.P.2    Bruck, M.J.3    Mamula, M.J.4
  • 130
    • 33749155438 scopus 로고    scopus 로고
    • B cells drive early T cell autoimmunity in vivo prior to dendritic cell-mediated autoantigen presentation
    • Yan, J., B. P. Harvey, R. J. Gee, et al. 2006. B cells drive early T cell autoimmunity in vivo prior to dendritic cell-mediated autoantigen presentation. J. Immunol. 177: 4481-4487.
    • (2006) J. Immunol , vol.177 , pp. 4481-4487
    • Yan, J.1    Harvey, B.P.2    Gee, R.J.3
  • 131
    • 1942469387 scopus 로고    scopus 로고
    • Dendritic cells cross-present HIV antigens from live as well as apoptotic infected CD4\+ T lymphocytes
    • Maranon, C., J. F. Desoutter, G. Hoeffel, et al. 2004. Dendritic cells cross-present HIV antigens from live as well as apoptotic infected CD4\+ T lymphocytes. Proc. Natl. Acad. Sci. USA. 101: 6092-6097.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6092-6097
    • Maranon, C.1    Desoutter, J.F.2    Hoeffel, G.3
  • 132
    • 0037369603 scopus 로고    scopus 로고
    • A role for class A scavenger receptor in dendritic cell nibbling from live cells
    • Harshyne, L. A., M. I. Zimmer, S. C. Watkins, and S. M. Barratt-Boyes. 2003. A role for class A scavenger receptor in dendritic cell nibbling from live cells. J. Immunol. 170: 2302-2309.
    • (2003) J. Immunol , vol.170 , pp. 2302-2309
    • Harshyne, L.A.1    Zimmer, M.I.2    Watkins, S.C.3    Barratt-Boyes, S.M.4
  • 133
    • 0032740398 scopus 로고    scopus 로고
    • Macrophage specific overexpression of the human macrophage scavenger receptor in transgenic mice, using a 180-kb yeast artificial chromosome, leads to enhanced foam cell formation of isolated peritoneal macrophages
    • de Winther, M. P., K. W. van Dijk, B. J. van Vlijmen, et al. 1999. Macrophage specific overexpression of the human macrophage scavenger receptor in transgenic mice, using a 180-kb yeast artificial chromosome, leads to enhanced foam cell formation of isolated peritoneal macrophages. Atherosclerosis 147: 339-347.
    • (1999) Atherosclerosis , vol.147 , pp. 339-347
    • De Winther, M.P.1    Van Dijk, K.W.2    Van Vlijmen, B.J.3
  • 134
    • 0027261307 scopus 로고
    • Presence of foam cells containing oxidised low density lipoprotein in the synovial membrane from patients with rheumatoid arthritis
    • Winyard, P. G., F. Tatzber, H. Esterbauer, et al. 1993. Presence of foam cells containing oxidised low density lipoprotein in the synovial membrane from patients with rheumatoid arthritis. Ann. Rheum. Dis. 52: 677-680.
    • (1993) Ann. Rheum. Dis , vol.52 , pp. 677-680
    • Winyard, P.G.1    Tatzber, F.2    Esterbauer, H.3
  • 135
    • 0029951406 scopus 로고    scopus 로고
    • Characterization of inherited scavenger receptor overexpression and abnormal macrophage phenotype in a normolipidemic subject with planar xanthomas
    • Giry, C., L. M. Giroux, M. Roy, et al. 1996. Characterization of inherited scavenger receptor overexpression and abnormal macrophage phenotype in a normolipidemic subject with planar xanthomas. J. Lipid Res. 37: 1422-1435.
    • (1996) J. Lipid Res , vol.37 , pp. 1422-1435
    • Giry, C.1    Giroux, L.M.2    Roy, M.3
  • 136
    • 0030895048 scopus 로고    scopus 로고
    • A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection
    • Suzuki, H., Y. Kurihara, M. Takeya, et al. 1997. A role for macrophage scavenger receptors in atherosclerosis and susceptibility to infection. Nature 386: 292-296.
    • (1997) Nature , vol.386 , pp. 292-296
    • Suzuki, H.1    Kurihara, Y.2    Takeya, M.3
  • 137
    • 79551678138 scopus 로고    scopus 로고
    • Interferon-alpha priming promotes lipid uptake and macrophage-derived foam cell formation: A novel link between interferon-alpha and atherosclerosis in lupus
    • Li, J., Q. Fu, H. Cui, et al. 2011. Interferon-alpha priming promotes lipid uptake and macrophage-derived foam cell formation: a novel link between interferon-alpha and atherosclerosis in lupus. Arthritis Rheum. 63: 492-502.
    • (2011) Arthritis Rheum , vol.63 , pp. 492-502
    • Li, J.1    Fu, Q.2    Cui, H.3
  • 138
    • 79251592852 scopus 로고    scopus 로고
    • Anti-class a scavenger receptor autoantibodies from systemic lupus erythematosus patients impair phagocytic clearance of apoptotic cells by macrophages in vitro
    • Chen, X. W., Y. Shen, C. Y. Sun, et al. 2011. Anti-class a scavenger receptor autoantibodies from systemic lupus erythematosus patients impair phagocytic clearance of apoptotic cells by macrophages in vitro. Arthritis Res. Ther. 13: R9.
    • (2011) Arthritis Res. Ther , vol.13
    • Chen, X.W.1    Shen, Y.2    Sun, C.Y.3
  • 139
    • 34948820567 scopus 로고    scopus 로고
    • Class A scavenger receptors regulate tolerance against apoptotic cells, and autoantibodies against these receptors are predictive of systemic lupus
    • Wermeling, F., Y. Chen, T. Pikkarainen, et al. 2007. Class A scavenger receptors regulate tolerance against apoptotic cells, and autoantibodies against these receptors are predictive of systemic lupus. J. Exp. Med. 204: 2259-2265.
    • (2007) J. Exp. Med , vol.204 , pp. 2259-2265
    • Wermeling, F.1    Chen, Y.2    Pikkarainen, T.3
  • 140
    • 0034194035 scopus 로고    scopus 로고
    • Apoptotic thymocyte clearance in scavenger receptor class A-deficient mice is apparently normal
    • Platt, N., H. Suzuki, T. Kodama, and S. Gordon. 2000. Apoptotic thymocyte clearance in scavenger receptor class A-deficient mice is apparently normal. J. Immunol. 164: 4861-4867.
    • (2000) J. Immunol , vol.164 , pp. 4861-4867
    • Platt, N.1    Suzuki, H.2    Kodama, T.3    Gordon, S.4
  • 141
    • 84872027397 scopus 로고    scopus 로고
    • Clearing the dead: Apoptotic cell sensing, recognition, engulfment, and digestion
    • IDa008748
    • Hochreiter-Hufford, A., and K. S. Ravichandran. 2013. Clearing the dead: apoptotic cell sensing, recognition, engulfment, and digestion. Cold Spring Harb. Perspect. Biol. 5: ID:a008748.
    • (2013) Cold Spring Harb. Perspect. Biol , vol.5
    • Hochreiter-Hufford, A.1    Ravichandran, K.S.2
  • 142
    • 74949094228 scopus 로고    scopus 로고
    • Genetic and epigenetic silencing of SCARA5 may contribute to human hepatocellular carcinoma by activating FAK signaling
    • Huang, J., D. L. Zheng, F. S. Qin, et al. 2010. Genetic and epigenetic silencing of SCARA5 may contribute to human hepatocellular carcinoma by activating FAK signaling. J. Clin. Invest. 120: 223-241.
    • (2010) J. Clin. Invest , vol.120 , pp. 223-241
    • Huang, J.1    Zheng, D.L.2    Qin, F.S.3
  • 143
    • 0036397482 scopus 로고    scopus 로고
    • CD5, an important regulator of lymphocyte selection and immune tolerance
    • Raman, C. 2002. CD5, an important regulator of lymphocyte selection and immune tolerance. Immunol. Res. 26: 255-263.
    • (2002) Immunol. Res , vol.26 , pp. 255-263
    • Raman, C.1
  • 144
    • 0034789444 scopus 로고    scopus 로고
    • High circulating levels of soluble scavenger receptors (sCD5 and sCD6) in patients with primary Sjogren's syndrome
    • Ramos-Casals, M., J. Font, M. Garcia-Carrasco, et al. 2001. High circulating levels of soluble scavenger receptors (sCD5 and sCD6) in patients with primary Sjogren's syndrome. Rheumatology (Oxford) 40: 1056-1059.
    • (2001) Rheumatology (Oxford) , vol.40 , pp. 1056-1059
    • Ramos-Casals, M.1    Font, J.2    Garcia-Carrasco, M.3
  • 145
    • 79955663608 scopus 로고    scopus 로고
    • CD5 expression in B cells from patients with systemic lupus erythematosus
    • Youinou, P., and Y. Renaudineau. 2011. CD5 expression in B cells from patients with systemic lupus erythematosus. Crit. Rev. Immunol. 31: 31-42.
    • (2011) Crit. Rev. Immunol , vol.31 , pp. 31-42
    • Youinou, P.1    Renaudineau, Y.2
  • 146
    • 0030983812 scopus 로고    scopus 로고
    • CD6-ligand interactions: A paradigm for SRCR domain function?
    • Aruffo, A., M. A. Bowen, D. D. Patel, et al. 1997. CD6-ligand interactions: a paradigm for SRCR domain function? Immunol. Today 18: 498-504.
    • (1997) Immunol Today , vol.18 , pp. 498-504
    • Aruffo, A.1    Bowen, M.A.2    Patel, D.D.3
  • 147
    • 78650642560 scopus 로고    scopus 로고
    • A ligand for CD5 is CD5
    • Brown, M. H., and E. Lacey. 2010. A ligand for CD5 is CD5. J. Immunol. 185: 6068-6074.
    • (2010) J. Immunol , vol.185 , pp. 6068-6074
    • Brown, M.H.1    Lacey, E.2
  • 148
    • 0031964445 scopus 로고    scopus 로고
    • Ligand binding to macrophage scavenger receptor-A induces urokinase-type plasminogen activator expression by a protein kinase-dependent signaling pathway
    • Hsu, H. Y., D. P. Hajjar, K. M. Khan, and D. J. Falcone. 1998. Ligand binding to macrophage scavenger receptor-A induces urokinase-type plasminogen activator expression by a protein kinase-dependent signaling pathway. J. Biol. Chem. 273: 1240-1246.
    • (1998) J. Biol. Chem , vol.273 , pp. 1240-1246
    • Hsu, H.Y.1    Hajjar, D.P.2    Khan, K.M.3    Falcone, D.J.4
  • 149
    • 0030891492 scopus 로고    scopus 로고
    • Proteins phosphorylated during stress-induced apoptosis are common targets for autoantibody production in patients with systemic lupus erythematosus
    • Utz, P. J., M. Hottelet, P. H. Schur, and P. Anderson. 1997. Proteins phosphorylated during stress-induced apoptosis are common targets for autoantibody production in patients with systemic lupus erythematosus. J. Exp. Med. 185: 843-854.
    • (1997) J. Exp. Med , vol.185 , pp. 843-854
    • Utz, P.J.1    Hottelet, M.2    Schur, P.H.3    Anderson, P.4
  • 150
    • 40749128547 scopus 로고    scopus 로고
    • Histone deimination as a response to inflammatory stimuli in neutrophils
    • Neeli, I., S. N. Khan, and M. Radic. 2008. Histone deimination as a response to inflammatory stimuli in neutrophils. J. Immunol. 180: 1895-1902.
    • (2008) J. Immunol , vol.180 , pp. 1895-1902
    • Neeli, I.1    Khan, S.N.2    Radic, M.3
  • 151
    • 34447523785 scopus 로고    scopus 로고
    • Apoptosis-induced acetylation of histones is pathogenic in systemic lupus erythematosus
    • Dieker, J. W., J. H. Fransen, C. C. van Bavel, et al. 2007. Apoptosis-induced acetylation of histones is pathogenic in systemic lupus erythematosus. Arthritis Rheum. 56: 1921-1933.
    • (2007) Arthritis Rheum , vol.56 , pp. 1921-1933
    • Dieker, J.W.1    Fransen, J.H.2    Van Bavel, C.C.3
  • 152
    • 84864016492 scopus 로고    scopus 로고
    • Altered posttranslational modification on U1 small nuclear ribonucleoprotein 68k in systemic autoimmune diseases detected by 2D Western blot
    • Nagai, K., M. Arito, Y. Takakuwa, et al. 2012. Altered posttranslational modification on U1 small nuclear ribonucleoprotein 68k in systemic autoimmune diseases detected by 2D Western blot. Electrophoresis 33: 2028-2035.
    • (2012) Electrophoresis , vol.33 , pp. 2028-2035
    • Nagai, K.1    Arito, M.2    Takakuwa, Y.3
  • 153
    • 0036090284 scopus 로고    scopus 로고
    • Apoptotic U1-70 kd is antigenically distinct from the intact form of the U1-70-kd molecule
    • Greidinger, E. L., M. F. Foecking, S. Ranatunga, and R. W. Hoffman. 2002. Apoptotic U1-70 kd is antigenically distinct from the intact form of the U1-70-kd molecule. Arthritis Rheum. 46: 1264-1269.
    • (2002) Arthritis Rheum , vol.46 , pp. 1264-1269
    • Greidinger, E.L.1    Foecking, M.F.2    Ranatunga, S.3    Hoffman, R.W.4
  • 154
    • 33748709099 scopus 로고    scopus 로고
    • Post-translational modifications of the major linear epitope 169-190aa of Ro60 kDa autoantigen alter the autoantibody binding
    • Terzoglou, A. G., J. G. Routsias, H. M. Moutsopoulos, and A. G. Tzioufas. 2006. Post-translational modifications of the major linear epitope 169-190aa of Ro60 kDa autoantigen alter the autoantibody binding. Clin. Exp. Immunol. 146: 60-65.
    • (2006) Clin. Exp. Immunol , vol.146 , pp. 60-65
    • Terzoglou, A.G.1    Routsias, J.G.2    Moutsopoulos, H.M.3    Tzioufas, A.G.4
  • 155
    • 10644293824 scopus 로고    scopus 로고
    • Apoptotic cells with oxidation-specific epitopes are immunogenic and proinflammatory
    • Chang, M. K., C. J. Binder, Y. I. Miller, et al. 2004. Apoptotic cells with oxidation-specific epitopes are immunogenic and proinflammatory. J. Exp. Med. 200: 1359-1370.
    • (2004) J. Exp. Med , vol.200 , pp. 1359-1370
    • Chang, M.K.1    Binder, C.J.2    Miller, Y.I.3
  • 156
    • 84859412916 scopus 로고    scopus 로고
    • Upregulated protein arginine methyltransferase 1 by IL-4 increases eotaxin-1 expression in airway epithelial cells and participates in antigen-induced pulmonary inflammation in rats
    • Sun, Q., X. Yang, B. Zhong, et al. 2012. Upregulated protein arginine methyltransferase 1 by IL-4 increases eotaxin-1 expression in airway epithelial cells and participates in antigen-induced pulmonary inflammation in rats. J. Immunol. 188: 3506-3512.
    • (2012) J. Immunol , vol.188 , pp. 3506-3512
    • Sun, Q.1    Yang, X.2    Zhong, B.3
  • 157
    • 45549102968 scopus 로고    scopus 로고
    • The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation
    • Kleinschmidt, M. A., G. Streubel, B. Samans, et al. 2008. The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation. Nucleic. Acids Res. 36: 3202-3213.
    • (2008) Nucleic. Acids Res , vol.36 , pp. 3202-3213
    • Kleinschmidt, M.A.1    Streubel, G.2    Samans, B.3
  • 158
    • 0343247114 scopus 로고    scopus 로고
    • P68 Sam is a substrate of the insulin receptor and associates with the SH2 domains of p85 PI3K
    • Sanchez-Margalet, V., and S. Najib. 1999. p68 Sam is a substrate of the insulin receptor and associates with the SH2 domains of p85 PI3K. FEBS. Lett. 455: 307-310.
    • (1999) FEBS. Lett , vol.455 , pp. 307-310
    • Sanchez-Margalet, V.1    Najib, S.2
  • 159
    • 47549090307 scopus 로고    scopus 로고
    • Regulation of estrogen rapid signaling through arginine methylation by PRMT1
    • Le Romancer, M., I. Treilleux, N. Leconte, et al. 2008. Regulation of estrogen rapid signaling through arginine methylation by PRMT1. Mol. Cell. 31: 212-221.
    • (2008) Mol. Cell , vol.31 , pp. 212-221
    • Le Romancer, M.1    Treilleux, I.2    Leconte, N.3
  • 160
    • 58149498873 scopus 로고    scopus 로고
    • PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling
    • Weber, S., F. Maass, M. Schuemann, et al. 2009. PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling. Genes Dev. 23: 118-132.
    • (2009) Genes Dev , vol.23 , pp. 118-132
    • Weber, S.1    Maass, F.2    Schuemann, M.3
  • 161
    • 77951045295 scopus 로고    scopus 로고
    • Arginine methylation of the B cell antigen receptor promotes differentiation
    • Infantino, S., B. Benz, T. Waldmann, et al. 2010. Arginine methylation of the B cell antigen receptor promotes differentiation. J. Exp. Med. 207: 711-719.
    • (2010) J. Exp. Med , vol.207 , pp. 711-719
    • Infantino, S.1    Benz, B.2    Waldmann, T.3
  • 162
    • 77958471611 scopus 로고    scopus 로고
    • Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation
    • Iwasaki, H., J. C. Kovacic, M. Olive, et al. 2010. Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation. Circ. Res. 107: 992-1001.
    • (2010) Circ. Res , vol.107 , pp. 992-1001
    • Iwasaki, H.1    Kovacic, J.C.2    Olive, M.3
  • 163
    • 2942537778 scopus 로고    scopus 로고
    • Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development
    • Kim, J., J. Lee, N. Yadav, et al. 2004. Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development. J. Biol. Chem. 279: 25339-25344.
    • (2004) J. Biol. Chem , vol.279 , pp. 25339-25344
    • Kim, J.1    Lee, J.2    Yadav, N.3
  • 164
    • 84872189994 scopus 로고    scopus 로고
    • Coactivator-associated arginine methyltransferase 1 regulates fetal hematopoiesis and thymocyte development
    • Li, J., Z. Zhao, C. Carter, et al. 2013. Coactivator-associated arginine methyltransferase 1 regulates fetal hematopoiesis and thymocyte development. J. Immunol. 190: 597-604.
    • (2013) J. Immunol , vol.190 , pp. 597-604
    • Li, J.1    Zhao, Z.2    Carter, C.3
  • 165
    • 32844468049 scopus 로고    scopus 로고
    • Histone arginine methylation and its dynamic regulation
    • Wysocka, J., C. D. Allis, and S. Coonrod. 2006. Histone arginine methylation and its dynamic regulation. Front. Biosci. 11: 344-355.
    • (2006) Front. Biosci , vol.11 , pp. 344-355
    • Wysocka, J.1    Allis, C.D.2    Coonrod, S.3
  • 166
    • 19544379490 scopus 로고    scopus 로고
    • Arginine methylation regulates IL-2 gene expression: A role for protein arginine methyltransferase 5 (PRMT5)
    • Richard, S., M. Morel, and P. Cleroux. 2005. Arginine methylation regulates IL-2 gene expression: a role for protein arginine methyltransferase 5 (PRMT5). Biochem. J. 388: 379-386.
    • (2005) Biochem. J , vol.388 , pp. 379-386
    • Richard, S.1    Morel, M.2    Cleroux, P.3
  • 167
    • 58149277374 scopus 로고    scopus 로고
    • Expression of BLIMP1/PRMT5 and concurrent histone H2A/H4 arginine 3 dimethylation in fetal germ cells, CIS/IGCNU and germ cell tumors
    • Eckert, D., K. Biermann, D. Nettersheim, et al. 2008. Expression of BLIMP1/PRMT5 and concurrent histone H2A/H4 arginine 3 dimethylation in fetal germ cells, CIS/IGCNU and germ cell tumors. BMC Dev. Biol. 8: 106.
    • (2008) BMC Dev. Biol , vol.8 , pp. 106
    • Eckert, D.1    Biermann, K.2    Nettersheim, D.3
  • 168
    • 34547741040 scopus 로고    scopus 로고
    • Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphoma
    • Pal, S., R. A. Baiocchi, J. C. Byrd, et al. 2007. Low levels of miR-92b/96 induce PRMT5 translation and H3R8/H4R3 methylation in mantle cell lymphoma. EMBO. J. 26: 3558-3569.
    • (2007) EMBO. J , vol.26 , pp. 3558-3569
    • Pal, S.1    Baiocchi, R.A.2    Byrd, J.C.3
  • 169
    • 53549103598 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells
    • Wang, L., S. Pal, and S. Sif. 2008. Protein arginine methyltransferase 5 suppresses the transcription of the RB family of tumor suppressors in leukemia and lymphoma cells. Mol. Cell. Biol. 28: 6262-6277.
    • (2008) Mol. Cell. Biol , vol.28 , pp. 6262-6277
    • Wang, L.1    Pal, S.2    Sif, S.3
  • 170
    • 84856733701 scopus 로고    scopus 로고
    • Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance
    • Migliori, V., J. Muller, S. Phalke, et al. 2012. Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance. Nat. Struct. Mol. Biol. 19: 136-144.
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 136-144
    • Migliori, V.1    Muller, J.2    Phalke, S.3
  • 171
    • 13544277696 scopus 로고    scopus 로고
    • PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine
    • Lee, J. H., J. R. Cook, Z. H. Yang, et al. 2005. PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. J. Biol. Chem. 280: 3656-3664.
    • (2005) J. Biol. Chem , vol.280 , pp. 3656-3664
    • Lee, J.H.1    Cook, J.R.2    Yang, Z.H.3
  • 172
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • Miranda, T. B., M. Miranda, A. Frankel, and S. Clarke. 2004. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J. Biol. Chem. 279: 22902-22907.
    • (2004) J. Biol. Chem , vol.279 , pp. 22902-22907
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.