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Volumn 213, Issue 12, 2016, Pages 2691-2706

CD72 negatively regulates b lymphocyte responses to the lupus-related endogenous toll-like receptor 7 ligand Sm/RNP

Author keywords

[No Author keywords available]

Indexed keywords

CD72 ANTIGEN; RIBONUCLEOPROTEIN; SM ANTIBODY; TOLL LIKE RECEPTOR 7; B LYMPHOCYTE ANTIGEN; CD72 ANTIGEN, MOUSE; LEUKOCYTE ANTIGEN; LIGAND; PROTEIN BINDING; PROTEIN TYROSINE PHOSPHATASE SHP 1; PTPN6 PROTEIN, MOUSE; SMALL NUCLEAR RIBONUCLEOPROTEIN;

EID: 84999752064     PISSN: 00221007     EISSN: 15409538     Source Type: Journal    
DOI: 10.1084/jem.20160560     Document Type: Article
Times cited : (38)

References (69)
  • 1
    • 0032523498 scopus 로고    scopus 로고
    • The B cell surface protein CD72 recruits the tyrosine phosphatase SHP-1 upon tyrosine phosphorylation
    • Adachi, T., H. Flaswinkel, H. Yakura, M. Reth, and T. Tsubata. 1998. The B cell surface protein CD72 recruits the tyrosine phosphatase SHP-1 upon tyrosine phosphorylation.J. Immunol. 160:4662-4665.
    • (1998) J. Immunol , vol.160 , pp. 4662-4665
    • Adachi, T.1    Flaswinkel, H.2    Yakura, H.3    Reth, M.4    Tsubata, T.5
  • 2
    • 0034142376 scopus 로고    scopus 로고
    • CD72 negatively regulates signaling through the antigen receptor of B cells
    • Adachi, T., C. Wakabayashi T. Nakayama H. Yakura and T. Tsubata. 2000. CD72 negatively regulates signaling through the antigen receptor of B cells. J. Immunol. 164:1223-1229. http://dx.doi.org/10.4049/jimmunol.164.3.1223
    • (2000) J. Immunol , vol.164 , pp. 1223-1229
    • Adachi, T.1    Wakabayashi, C.2    Nakayama, T.3    Yakura, H.4    Tsubata, T.5
  • 4
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett, D., E. Kovaleva and PJ. Schatz. 1999. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8:921-929. http://dx.doi.org/10.1110/ps.8.4.921
    • (1999) Protein Sci , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 7
    • 0033053772 scopus 로고    scopus 로고
    • Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors
    • Boyington, J.C., A.N. Riaz A. Patamawenu J.E. Coligan A.G. Brooks and P.D. Sun. 1999. Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors. Immunity. 10:75-82. http://dx.doi.org/10.1016/S1074-7613(00)80008-4
    • (1999) Immunity , vol.10 , pp. 75-82
    • Boyington, J.C.1    Riaz, A.N.2    Patamawenu, A.3    Coligan, J.E.4    Brooks, A.G.5    Sun, P.D.6
  • 9
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcy receptors and their polymorphic variants for human IgG subclasses
    • Bruhns, P., B. Iannascoli P. England D.A. Mancardi N. Fernandez S. Jorieux and M. Daeron. 2009. Specificity and affinity of human Fcy receptors and their polymorphic variants for human IgG subclasses. Blood. 113:3716-3725. http://dx.doi.org/10.1182/blood-2008-09-179754
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1    Iannascoli, B.2    England, P.3    Mancardi, D.A.4    Fernandez, N.5    Jorieux, S.6    Daeron, M.7
  • 10
    • 0029937038 scopus 로고    scopus 로고
    • A quasi-monoclonal mouse
    • Cascalho, M., A. Ma S. Lee L. Masat and M. Wabl. 1996. A quasi-monoclonal mouse. Science.272:1649-1652. http://dx.doi.org/10.1126/science.272.5268.1649
    • (1996) Science , vol.272 , pp. 1649-1652
    • Cascalho, M.1    Ma, A.2    Lee, S.3    Masat, L.4    Wabl, M.5
  • 11
    • 0032492994 scopus 로고    scopus 로고
    • Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes
    • Chan, VW, C.A. Lowell and A.L. DeFranco. 1998. Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes. Curr. Biol. 8:545-553. http://dx.doi.org/10.1016/S0960-9822(98)70223-4
    • (1998) Curr. Biol , vol.8 , pp. 545-553
    • Chan, V.W.1    Lowell, C.A.2    De Franco, A.L.3
  • 13
    • 33748472865 scopus 로고    scopus 로고
    • Toll-like receptor 7 and TLR9 dictate autoantibody specificity and have opposing inflammatory and regulatory roles in a murine model of lupus
    • Christensen, S.R., J. Shupe K. Nickerson M. Kashgarian R.A. Flavell and M.J. Shlomchik. 2006. Toll-like receptor 7 and TLR9 dictate autoantibody specificity and have opposing inflammatory and regulatory roles in a murine model of lupus. Immunity 25:417-428. http://dx.doi.org/10.1016/j.immuni.2006.07.013
    • (2006) Immunit , vol.25 , pp. 417-428
    • Christensen, S.R.1    Shupe, J.2    Nickerson, K.3    Kashgarian, M.4    Flavell, R.A.5    Shlomchik, M.J.6
  • 14
    • 1542317550 scopus 로고    scopus 로고
    • Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA
    • Diebold, S.S., T. Kaisho H. Hemmi S. Akira and C. Reis e Sousa. 2004. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science.303:1529-1531. http://dx.doi.org/10.1126/science.1093616
    • (2004) Science , vol.303 , pp. 1529-1531
    • Diebold, S.S.1    Kaisho, T.2    Hemmi, H.3    Akira, S.4    Reise Sousa, C.5
  • 16
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg, H., D.A. Mitchell K. Drickamer and W.I. Weis. 2001. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science.294:2163-2166. http://dx.doi.org/10.1126/science.1066371
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 17
    • 0033199096 scopus 로고    scopus 로고
    • Junctional amino acids determine the maturation pathway of an antibody
    • Furukawa, K., A. Akasako-Furukawa H. Shirai H. Nakamura and T. Azuma. 1999. Junctional amino acids determine the maturation pathway of an antibody. Immunity. 11:329-338. http://dx.doi.org/10.1016/S1074-7613(00)80108-9
    • (1999) Immunity , vol.11 , pp. 329-338
    • Furukawa, K.1    Akasako-furukawa, A.2    Shirai, H.3    Nakamura, H.4    Azuma, T.5
  • 18
    • 84905568602 scopus 로고    scopus 로고
    • Contribution of human FcyRs to disease with evidence from human polymorphisms and transgenic animal studies
    • Gillis, C., A. Gouel-Chéron F Jonsson and P Bruhns. 2014. Contribution of human FcyRs to disease with evidence from human polymorphisms and transgenic animal studies. Front. Immunol. 5:254. http://dx.doi.org/10.3389/fimmu.2014.00254
    • (2014) Front. Immunol , vol.5 , pp. 254
    • Gillis, C.1    A., Gouel-chéron2    Jonsson, F.3    Bruhns, P.4
  • 22
    • 9744281876 scopus 로고    scopus 로고
    • CD72 polymorphisms associated with alternative splicing modify susceptibility to human systemic lupus erythematosus through epistatic interaction with FCGR2B
    • Hitomi, Y, N. Tsuchiya A. Kawasaki J. Ohashi T. Suzuki C. Kyogoku T. Fukazawa S. Bejrachandra U. Siriboonrit D. Chandanayingyong et al. 2004. CD72 polymorphisms associated with alternative splicing modify susceptibility to human systemic lupus erythematosus through epistatic interaction with FCGR2B. Hum. Mol. Genet. 13:2907-2917. http://dx.doi.org/10.1093/hmg/ddh318
    • (2004) Hum. Mol. Genet , vol.13 , pp. 2907-2917
    • Hitomi, Y.1    Tsuchiya, N.2    Kawasaki, A.3    Ohashi, J.4    Suzuki, T.5    Kyogoku, C.6    Fukazawa, T.7    Bejrachandra, S.8    Siriboonrit, U.9    Chandanayingyong, D.10
  • 23
    • 0021173447 scopus 로고
    • Induction of various autoantibodies by mutant gene lpr in several strains of mice
    • Izui, S., VE. Kelley K. Masuda H.Yoshida J.B. Roths and E.D. Murphy. 1984. Induction of various autoantibodies by mutant gene lpr in several strains of mice.J. Immunol. 133:227-233.
    • (1984) J. Immunol , vol.133 , pp. 227-233
    • Izui, S.1    Kelley, V.E.2    Masuda, K.3    Yoshida, H.4    Roths, J.B.5    Murphy, E.D.6
  • 24
    • 0028912625 scopus 로고
    • Immunoglobulin epitope spreading and autoimmune disease after peptide immunization: Sm B/B'-derived PPPGMRPP and PPPGIRGP induce spliceosome autoimmunity
    • James, J.A., T. Gross R.H. Scofield and J.B. Harley. 1995. Immunoglobulin epitope spreading and autoimmune disease after peptide immunization: Sm B/B'-derived PPPGMRPP and PPPGIRGP induce spliceosome autoimmunity. J. Exp. Med. 181:453-461. http://dx.doi.org/10.1084/jem.181.2.453
    • (1995) J. Exp. Med , vol.181 , pp. 453-461
    • James, J.A.1    Gross, T.2    Scofield, R.H.3    Harley, J.B.4
  • 25
    • 77951627428 scopus 로고    scopus 로고
    • CD22 x Siglec-G double-deficient mice have massively increased B1 cell numbers and develop systemic autoimmunity
    • Jellusova, J., U. Wellmann K. Amann T.H. Winkler and L. Nitschke. 2010. CD22 x Siglec-G double-deficient mice have massively increased B1 cell numbers and develop systemic autoimmunity.J. Immunol. 184:36183627. http://dx.doi.org/10.4049/jimmunol.0902711
    • (2010) J. Immunol , vol.184 , pp. 3614-3627
    • Jellusova, J.1    Wellmann, U.2    Amann, K.3    Winkler, T.H.4    Nitschke, L.5
  • 26
    • 69549129469 scopus 로고    scopus 로고
    • Augmented TLR9-induced Btk activation in PIR-B-deficient B-1 cells provokes excessive autoantibody production and autoimmunity
    • Kubo, T., Y. Uchida Y. Watanabe M. Abe A. Nakamura M. Ono S. Akira and T. Takai. 2009. Augmented TLR9-induced Btk activation in PIR-B-deficient B-1 cells provokes excessive autoantibody production and autoimmunity. J. Exp. Med. 206:1971-1982. http://dx.doi.org/10.1084/jem.20082392
    • (2009) J. Exp. Med , vol.206 , pp. 1971-1982
    • Kubo, T.1    Uchida, Y.2    Watanabe, Y.3    Abe, M.4    Nakamura, A.5    Ono, M.6    Akira, S.7    Takai, T.8
  • 31
    • 69949135619 scopus 로고    scopus 로고
    • B cell antigen receptor endocytosis and antigen presentation to T cells require Vav and dynamin
    • Malhotra, S., S. Kovats W. Zhang and K.M. Coggeshall. 2009. B cell antigen receptor endocytosis and antigen presentation to T cells require Vav and dynamin. J. Biol. Chem. 284:24088-24097. http://dx.doi.org/10.1074/jbc.M109.014209
    • (2009) J. Biol. Chem , vol.284 , pp. 24088-24097
    • Malhotra, S.1    Kovats, S.2    Zhang, W.3    Coggeshall, K.M.4
  • 33
    • 0036594594 scopus 로고    scopus 로고
    • Epitope spreading in systemic lupus erythematosus: identification of triggering peptide sequences
    • Monneaux, F, and S. Muller. 2002. Epitope spreading in systemic lupus erythematosus: identification of triggering peptide sequences. Arthritis Rheum. 46:1430-1438. http://dx.doi.org/10.1002/art.10263
    • (2002) Arthritis Rheum , vol.46 , pp. 1430-1438
    • Monneaux, F.1    Muller, S.2
  • 35
    • 0028347321 scopus 로고
    • A 13-amino-acid motif in the cytoplasmic domain of FcyRIIB modulates B-cell receptor signalling
    • Muta, T., T. Kurosaki Z. Misulovin M. Sanchez M.C. Nussenzweig and J.V. Ravetch. 1994. A 13-amino-acid motif in the cytoplasmic domain of FcyRIIB modulates B-cell receptor signalling. Nature. 368:70-73. http://dx.doi.org/10.1038/368070a0
    • (1994) Nature , vol.368 , pp. 70-73
    • Muta, T.1    Kurosaki, T.2    Misulovin, Z.3    Sanchez, M.4    Nussenzweig, M.C.5    Ravetch, J.V.6
  • 36
    • 0033573827 scopus 로고    scopus 로고
    • Structural features of protein-nucleic acid recognition sites
    • Nadassy, K., S.J. Wodak and J. Janin. 1999. Structural features of protein-nucleic acid recognition sites. Biochemistry. 38:1999-2017. http://dx.doi.org/10.1021/bi9823 62d
    • (1999) Biochemistry , vol.38 , pp. 1999-2017
    • Nadassy, K.1    Wodak, S.J.2    Janin, J.3
  • 37
    • 0034610309 scopus 로고    scopus 로고
    • Crystal structure of human CD69: a C-type lectin-like activation marker of hematopoietic cells
    • Natarajan, K., M.W Sawicki D.H. Margulies and R.A. Mariuzza. 2000. Crystal structure of human CD69: a C-type lectin-like activation marker of hematopoietic cells. Biochemistry. 39:14779-14786. http://dx.doi.org/10.1021/bi0018180
    • (2000) Biochemistry , vol.39 , pp. 14779-14786
    • Natarajan, K.1    Sawicki, M.W.2    Margulies, D.H.3    Mariuzza, R.A.4
  • 38
    • 77949903821 scopus 로고    scopus 로고
    • TLR9 regulates TLR7-and MyD88-dependent autoantibody production and disease in a murine model of lupus
    • Nickerson, K.M., S.R. Christensen J. Shupe M. Kashgarian D. Kim K. Elkon and M.J. Shlomchik. 2010. TLR9 regulates TLR7-and MyD88-dependent autoantibody production and disease in a murine model of lupus.J Immunol. 184:1840-1848. http://dx.doi.org/10.4049/jimmunol.0902592
    • (2010) Immunol , vol.184 , pp. 1840-1848
    • Nickerson, K.M.1    Christensen, S.R.2    Shupe, J.3    Kashgarian, M.4    Kim, D.5    Elkon, K.6    Shlomchik, M.J.7
  • 39
    • 37549036732 scopus 로고    scopus 로고
    • Fcy receptors as regulators of immune responses
    • Nimmerjahn, F., and J.V Ravetch. 2008. Fcy receptors as regulators of immune responses. Nat. Rev. Immunol. 8:34-47. http://dx.doi.org/10.1038/nri2206
    • (2008) Nat. Rev. Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    J.V, Ravetch2
  • 40
    • 0032550365 scopus 로고    scopus 로고
    • A double-edged kinase Lyn: a positive and negative regulator for antigen receptor-mediated signals
    • Nishizumi, H., K. Horikawa I. Mlinaric-Rascan and T. Yamamoto. 1998. A double-edged kinase Lyn: a positive and negative regulator for antigen receptor-mediated signals. J. Exp. Med. 187:1343-1348. http://dx.doi.org/10.1084/jem.187.8.1343
    • (1998) J. Exp. Med , vol.187 , pp. 1343-1348
    • Nishizumi, H.1    Horikawa, K.2    Mlinaric-rascan, I.3    Yamamoto, T.4
  • 41
    • 19344375741 scopus 로고    scopus 로고
    • Molecular interactions regulate BCR signal inhibition by CD22 and CD72
    • Nitschke, L., and T. Tsubata. 2004. Molecular interactions regulate BCR signal inhibition by CD22 and CD72. Trends Immunol. 25:543-550. http://dx.doi.org/10.1016/j.it.2004.08.002
    • (2004) Trends Immunol , vol.25 , pp. 543-550
    • Nitschke, L.1    Tsubata, T.2
  • 42
    • 0031080328 scopus 로고    scopus 로고
    • CD22 is a negative regulator of B-cell receptor signalling
    • Nitschke, L., R. Carsetti B. Ocker G. Kohler and M.C. Lamers. 1997. CD22 is a negative regulator of B-cell receptor signalling. Curr. Biol. 7:133-143. http://dx.doi.org/10.1016/S0960-9822(06)00057-1
    • (1997) Curr. Biol , vol.7 , pp. 133-143
    • Nitschke, L.1    Carsetti, R.2    Ocker, B.3    Kohler, G.4    Lamers, M.C.5
  • 43
    • 0030005513 scopus 로고    scopus 로고
    • Antigen receptor-mediated B cell death is blocked by signaling via CD72 or treatment with dextran sulfate and is defective in autoimmunity-prone mice
    • Nomura, T., H. Han M.C. Howard H. Yagita H. Yakura T. Honjo and T. Tsubata. 1996. Antigen receptor-mediated B cell death is blocked by signaling via CD72 or treatment with dextran sulfate and is defective in autoimmunity-prone mice. Int. Immunol. 8:867-875. http://dx.doi.org/10.1093/intimm/8.6.867
    • (1996) Int. Immunol , vol.8 , pp. 867-875
    • Nomura, T.1    Han, H.2    Howard, M.C.3    Yagita, H.4    Yakura, H.5    Honjo, T.6    Tsubata, T.7
  • 44
    • 0034947066 scopus 로고    scopus 로고
    • Reevaluation of stoichiometry and affinity/avidity in interactions between anti-hapten antibodies and mono-or multi-valent antigens
    • Oda, M., and T. Azuma. 2000. Reevaluation of stoichiometry and affinity/avidity in interactions between anti-hapten antibodies and mono-or multi-valent antigens. Mol. Immunol. 37:1111-1122. http://dx.doi.org/10.1016/S0161-5890(01)00028-1
    • (2000) Mol. Immunol , vol.37 , pp. 1111-1122
    • Oda, M.1    Azuma, T.2
  • 45
    • 84874260210 scopus 로고    scopus 로고
    • A bacterial artificial chromosome transgene with polymorphic Cd72 inhibits the development of glomerulonephritis and vasculitis in MRL-Faslpr lupus mice
    • Oishi, H., T. Tsubaki T. Miyazaki M. Ono M. Nose and S. Takahashi. 2013. A bacterial artificial chromosome transgene with polymorphic Cd72 inhibits the development of glomerulonephritis and vasculitis in MRL-Faslpr lupus mice. J. Immunol. 190:2129-2137. http://dx.doi.org/10.4049/jimmunol.1202196
    • (2013) J. Immunol , vol.190 , pp. 2129-2137
    • Oishi, H.1    Tsubaki, T.2    Miyazaki, T.3    Ono, M.4    Nose, M.5    Takahashi, S.6
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326. http://dx.doi.org/10.1016/S0076-6879(97)76066-X
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 0035193064 scopus 로고    scopus 로고
    • Visualization of negative signaling in B cells by quantitative confocal microscopy
    • Phee, H., W. Rodgers and K.M. Coggeshall. 2001. Visualization of negative signaling in B cells by quantitative confocal microscopy. Mol. Cell. Biol. 21:8615-8625. http://dx.doi.org/10.1128/MCB.21.24.8615-8625
    • (2001) Mol. Cell. Biol , vol.21 , pp. 8615-8625
    • Phee, H.1    Rodgers, W.2    Coggeshall, K.M.3
  • 50
    • 0033939944 scopus 로고    scopus 로고
    • Genetic dissection of vasculitis in MRL/lpr lupus mice: a novel susceptibility locus involving the CD72c allele
    • Qu, WM., T. Miyazaki M. Terada L.M. Lu M. Nishihara A.Yamada S. Mori Y. Nakamura H. Ogasawara C. Yazawa et al. 2000. Genetic dissection of vasculitis in MRL/lpr lupus mice: a novel susceptibility locus involving the CD72c allele. Eur. J. Immunol. 30:2027-2037. http://dx.doi.org/10.1002/1521-4141(200007)30:7 2027::AID-IMMU20273.0.CO;2-S
    • (2000) Eur. J. Immunol , vol.30 , pp. 2027-2037
    • Qu, WM.1    Miyazaki, T.2    Terada, M.3    Lu, L.M.4    Nishihara, M.5    Yamada, A.6    Mori, S.7    Nakamura, Y.8    Ogasawara, H.9    Yazawa, C.10
  • 51
    • 0026721690 scopus 로고
    • Extensive polymorphism in the extracellular domain of the mouse B cell differentiation antigen Lyb-2/CD72
    • Robinson, W.H., H. Ying M.C. Miceli and J.R. Parnes. 1992. Extensive polymorphism in the extracellular domain of the mouse B cell differentiation antigen Lyb-2/CD72.J. Immunol. 149:880-886.
    • (1992) J. Immunol , vol.149 , pp. 880-886
    • Robinson, W.H.1    Ying, H.2    Miceli, M.C.3    Parnes, J.R.4
  • 53
    • 0030499431 scopus 로고    scopus 로고
    • CD22 is both a positive and negative regulator of B lymphocyte antigen receptor signal transduction: altered signaling in CD22-deficient mice
    • Sato, S., A.S. Miller M. Inaoki C.B. Bock PJ. Jansen M.L. Tang and T.F. Tedder. 1996. CD22 is both a positive and negative regulator of B lymphocyte antigen receptor signal transduction: altered signaling in CD22-deficient mice. Immunity 5:551-562. http://dx.doi.org/10.1016/S1074-7613(00)80270-8
    • (1996) Immunit , vol.5 , pp. 551-562
    • Sato, S.1    Miller, A.S.2    Inaoki, M.3    Bock, C.B.4    Jansen, P.J.5    Tang, M.L.6    Tedder, T.F.7
  • 54
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz, RJ. 1993. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (N. Y). 11:1138-1143. http://dx.doi.org/10.1038/nbt1093-1138
    • (1993) Biotechnology (N. Y) , vol.11 , pp. 1138-1143
    • Schatz, R.J.1
  • 55
    • 0027411632 scopus 로고
    • CD22 a B cell-specific immunoglobulin superfamily member is a sialic acid-binding lectin
    • Sgroi, D., A.Varki S. Braesch-Andersen and I. Stamenkovic. 1993. CD22 a B cell-specific immunoglobulin superfamily member is a sialic acid-binding lectin.J. Biol. Chem. 268:7011-7018.
    • (1993) J. Biol. Chem , vol.268 , pp. 7011-7018
    • Sgroi, D.1    Varki, A.2    Braesch-andersen, S.3    Stamenkovic, I.4
  • 57
    • 0019418702 scopus 로고
    • Ly-m19: The Lyb-2 region of mouse chromosome 4 controls a new surface alloantigen
    • Tada, N., S. Kimura Y. Liu B.A. Taylor and U. Hammerling. 1981. Ly-m19: The Lyb-2 region of mouse chromosome 4 controls a new surface alloantigen. Immunogenetics. 13:539-546. http://dx.doi.org/10.1007/BF00343721
    • (1981) Immunogenetics , vol.13 , pp. 539-546
    • Tada, N.1    Kimura, S.2    Liu, Y.3    Taylor, B.A.4    Hammerling, U.5
  • 58
    • 26444493671 scopus 로고    scopus 로고
    • A novel recognition system for MHC class I molecules constituted by PIR
    • Takai, T. 2005. A novel recognition system for MHC class I molecules constituted by PIR. Adv. Immunol. 88:161-192. http://dx.doi.org/10.1016/S0065-2776(05) 88005-8
    • (2005) Adv. Immunol , vol.88 , pp. 161-192
    • Takai, T.1
  • 59
    • 78349242154 scopus 로고    scopus 로고
    • Role of PIR-B in autoimmune glomerulonephritis
    • Takai, T., A. Nakamura and S. Endo. 2011. Role of PIR-B in autoimmune glomerulonephritis. J. Biomed. Biotechnol. 2011:275302. http://dx.doi.org/10.1155/2011/275302
    • (2011) J. Biomed. Biotechnol , vol.2011 , pp. 275-302
    • Takai, T.1    Nakamura, A.2    Endo, S.3
  • 60
    • 0024518559 scopus 로고
    • Antinuclear antibodies: diagnostic markers for autoimmune diseases and probes for cell biology
    • Tan, E.M. 1989. Antinuclear antibodies: diagnostic markers for autoimmune diseases and probes for cell biology. Adv. Immunol. 44:93-151. http://dx.doi.org/10.1016/S0065-2776(08)60641-0
    • (1989) Adv. Immunol , vol.44 , pp. 93-151
    • Tan, E.M1
  • 61
    • 84861161715 scopus 로고    scopus 로고
    • Role of inhibitory BCR co-receptors in immunity
    • Tsubata, T. 2012. Role of inhibitory BCR co-receptors in immunity. Infect. Disord. Drug Targets. 12:181-190. http://dx.doi.org/10.2174/187152612800564455
    • (2012) Infect. Disord. Drug Targets , vol.12 , pp. 181-190
    • Tsubata, T.1
  • 62
    • 0022623067 scopus 로고
    • Antigenic complexity and protein-structural polymorphism in the Lyb-2 system
    • Tung, J.S., FW Shen V. LaRegina and E.A. Boyse. 1986. Antigenic complexity and protein-structural polymorphism in the Lyb-2 system. Immunogenetics. 23:208-210. http://dx.doi.org/10.1007/BF00373822
    • (1986) Immunogenetics , vol.23 , pp. 208-210
    • Tung, J.S.1    Shen, F.W.2    La Regina, V.3    Boyse, E.A.4
  • 63
    • 0036078081 scopus 로고    scopus 로고
    • Impaired dendritic cell maturation and increased TH2 responses in PIR-B-/-mice
    • Ujike, A., K. Takeda A. Nakamura S. Ebihara K. Akiyama and T. Takai. 2002. Impaired dendritic cell maturation and increased TH2 responses in PIR-B-/-mice. Nat. Immunol. 3:542-548. http://dx.doi.org/10.1038/ni801
    • (2002) Nat. Immunol , vol.3 , pp. 542-548
    • Ujike, A.1    Takeda, K.2    Nakamura, A.3    Ebihara, S.4    Akiyama, K.5    Takai, T.6
  • 64
    • 0025339005 scopus 로고
    • Identification of a human protein homologous to the mouse Lyb-2 B cell differentiation antigen and sequence of the corresponding cDNA
    • Von Hoegen, I., E. Nakayama and J.R. Parnes. 1990. Identification of a human protein homologous to the mouse Lyb-2 B cell differentiation antigen and sequence of the corresponding cDNA. J. Immunol. 144:4870-4877.
    • (1990) J. Immunol , vol.144 , pp. 4870-4877
    • Von Hoegen, I.1    Nakayama, E.2    Parnes, J.R.3
  • 65
    • 84903191755 scopus 로고    scopus 로고
    • NA-protein n-interactions in nature: abundance structure composition and strength of contacts between aromatic amino acids and DNA nucleobases or deoxyribose sugar
    • Wilson, K.A.J.L.Kellie, and S.D.Wetmore. 2014.DNA-protein n-interactions in nature: abundance structure composition and strength of contacts between aromatic amino acids and DNA nucleobases or deoxyribose sugar. Nucleic Acids Res. 42:6726-6741. http://dx.doi.org/10.1093/nar/gku269
    • (2014) Nucleic Acids Res , vol.42 , pp. 6726-6741
    • Wilson, K.A.1    Kellie, J.L.2    Wetmore, S.D.3
  • 68
    • 0029094929 scopus 로고
    • Structure of the mouse CD72 (Lyb-2) gene and its alternatively spliced transcripts
    • Ying, H., E. Nakayama W.H. Robinson and J.R. Parnes. 1995. Structure of the mouse CD72 (Lyb-2) gene and its alternatively spliced transcripts. J. Immunol. 155:1637.
    • (1995) J. Immunol , vol.155 , pp. 1637
    • Ying, H.1    Nakayama, E.2    Robinson, W.H.3    Parnes, J.R.4
  • 69
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky, A.N., and J.E. Gready. 2005. The C-type lectin-like domain superfamily. FEBS J. 272:6179-6217.http://dx.doi.org/10.1111/j.1742-4658.2005.05031.x
    • (2005) FEBS J , vol.272 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2


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