메뉴 건너뛰기




Volumn 43, Issue 6, 2013, Pages 1659-1666

PKC-θ exists in an oxidized inactive form in naive human T cells

Author keywords

PKC; Redox regulation; T cell activation; TCR signaling

Indexed keywords

CD28 ANTIGEN; CD3 ANTIGEN; DISULFIDE; GLUTATHIONE; PHOSPHOLIPASE C GAMMA1; PROTEIN KINASE C THETA; T LYMPHOCYTE RECEPTOR; THIOREDOXIN;

EID: 84879483813     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201243140     Document Type: Article
Times cited : (11)

References (54)
  • 1
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase
    • Nishizuka, Y., Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992. 258: 607-614.
    • (1992) C. Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 2
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton, A. C., Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem. Rev.2001. 101: 2353-2364.
    • (2001) Chem. Rev. , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 3
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg, S. F., Structural basis of protein kinase C isoform function.Physiol Rev. 2008. 88: 1341-1378.
    • (2008) Physiol Rev. , vol.88 , pp. 1341-1378
    • Steinberg, S.F.1
  • 4
    • 84874215284 scopus 로고    scopus 로고
    • Involvement of distinct PKC gene products in T cell functions
    • Pfeifhofer-Obermair, C., Thuille, N. and Baier, G., Involvement of distinct PKC gene products in T cell functions. Front Immunol. 2012. 3: 1-12.
    • (2012) Front Immunol. , vol.3 , pp. 1-12
    • Pfeifhofer-Obermair, C.1    Thuille, N.2    Baier, G.3
  • 5
    • 0027418818 scopus 로고
    • Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells
    • Baier, G., Telford, D., Giampa, L., Coggeshall, K. M., Baier-Bitterlich, G., Isakov, N. and Altman, A., Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells. J. Biol. Chem. 1993. 268:4997-5004.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4997-5004
    • Baier, G.1    Telford, D.2    Giampa, L.3    Coggeshall, K.M.4    Baier-Bitterlich, G.5    Isakov, N.6    Altman, A.7
  • 6
    • 18844473151 scopus 로고    scopus 로고
    • PKC-theta is required for TCR-induced NFkappaB activation in mature but not immature T lymphocytes
    • Sun, Z., Arendt, C. W., Ellmeier, W., Schaeffer, E. M., Sunshine, M. J.,Gandhi, L., Annes, J. et al., PKC-theta is required for TCR-induced NFkappaB activation in mature but not immature T lymphocytes. Nature 2000. 404: 402-407.
    • (2000) Nature , vol.404 , pp. 402-407
    • Sun, Z.1    Arendt, C.W.2    Ellmeier, W.3    Schaeffer, E.M.4    Sunshine, M.J.5    Gandhi, L.6    Annes, J.7
  • 7
    • 0038620475 scopus 로고    scopus 로고
    • Protein kinase C theta affects Ca2+ mobilization and NFAT cell activation in primary mouse T cells
    • Pfeifhofer, C., Kofler, K., Gruber, T., Tabrizi, N. G., Lutz, C., Maly, K.,Leitges, M. et al., Protein kinase C theta affects Ca2+ mobilization and NFAT cell activation in primary mouse T cells. J. Exp. Med. 2003. 197:1525-1535.
    • (2003) J. Exp. Med. , vol.197 , pp. 1525-1535
    • Pfeifhofer, C.1    Kofler, K.2    Gruber, T.3    Tabrizi, N.G.4    Lutz, C.5    Maly, K.6    Leitges, M.7
  • 8
    • 0028288591 scopus 로고
    • Structure of the T cell receptor in a TiaVß2,aVß8 positive cell line
    • Hou, X., Dietrich, J., Kuhlmann, J., Wegener, A.-M. K. and Geisler, C.,Structure of the T cell receptor in a TiaVß2,aVß8 positive cell line. Eur. J.Immunol. 1994. 24: 1228-1233.
    • (1994) Eur. J.Immunol. , vol.24 , pp. 1228-1233
    • Hou, X.1    Dietrich, J.2    Kuhlmann, J.3    Wegener, A.-M.K.4    Geisler, C.5
  • 9
    • 32244435875 scopus 로고    scopus 로고
    • Deconstructing the form and function of the TCR/CD3 complex
    • Kuhns, M. S., Davis, M. M. and Garcia, K. C., Deconstructing the form and function of the TCR/CD3 complex. Immunity 2006. 24: 133-139.
    • (2006) Immunity , vol.24 , pp. 133-139
    • Kuhns, M.S.1    Davis, M.M.2    Garcia, K.C.3
  • 11
    • 0036201478 scopus 로고    scopus 로고
    • Endo- and exocytic rate constants for spontaneous and protein kinase C-activated T-cell receptor cycling
    • Menné, C., Sorensen, T., Siersma, V., von Essen, M., Odum, N. and Geisler, C., Endo- and exocytic rate constants for spontaneous and protein kinase C-activated T-cell receptor cycling. Eur. J. Immunol. 2002. 32:616-626.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 616-626
    • Menné, C.1    Sorensen, T.2    Siersma, V.3    von Essen, M.4    Odum, N.5    Geisler, C.6
  • 12
    • 2942753079 scopus 로고    scopus 로고
    • TCR trafficking in resting and stimulated T cells
    • Geisler, C., TCR trafficking in resting and stimulated T cells. Crit. Rev.Immunol. 2004. 24: 67-86.
    • (2004) Crit. Rev.Immunol. , vol.24 , pp. 67-86
    • Geisler, C.1
  • 13
    • 0031448209 scopus 로고    scopus 로고
    • Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation
    • D'Oro, U., Vacchio, M. S., Weissman, A. M. and Ashwell, J. D., Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation. Immunity 1997. 7: 619-628.
    • (1997) Immunity , vol.7 , pp. 619-628
    • D'Oro, U.1    Vacchio, M.S.2    Weissman, A.M.3    Ashwell, J.D.4
  • 14
    • 33744923428 scopus 로고    scopus 로고
    • Protein kinase C (PKC)a and PKC? are the major pkc isotypes involved in TCR downregulation
    • von Essen, M., Nielsen, M. W., Bonefeld, C. M., Boding, L., Larsen, J. M., Leitges, M., Baier, G. et al., Protein kinase C (PKC)a and PKC? are the major pkc isotypes involved in TCR downregulation. J. Immunol. 2006. 176: 7502-7510.
    • (2006) J. Immunol. , vol.176 , pp. 7502-7510
    • von Essen, M.1    Nielsen, M.W.2    Bonefeld, C.M.3    Boding, L.4    Larsen, J.M.5    Leitges, M.6    Baier, G.7
  • 15
    • 0028179026 scopus 로고
    • CD3? contains aphosphoserine-dependent di-leucine motif involved in downregulation of the T cell receptor
    • Dietrich, J., Hou, X., Wegener, A.-M. K. and Geisler, C., CD3? contains aphosphoserine-dependent di-leucine motif involved in downregulation of the T cell receptor. EMBO J. 1994. 13: 2156-2166.
    • (1994) EMBO J. , vol.13 , pp. 2156-2166
    • Dietrich, J.1    Hou, X.2    Wegener, A.-M.K.3    Geisler, C.4
  • 16
    • 17544365657 scopus 로고    scopus 로고
    • Molecular characterization of the di-leucine based internalization motif of the T cell receptor
    • Dietrich, J., Hou, X., Wegener, A.-M. K., Pedersen, L. O., Odum, N.and Geisler, C., Molecular characterization of the di-leucine based internalization motif of the T cell receptor. J. Biol. Chem. 1996. 271:11441-11448.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11441-11448
    • Dietrich, J.1    Hou, X.2    Wegener, A.-M.K.3    Pedersen, L.O.4    Odum, N.5    Geisler, C.6
  • 17
    • 0030611594 scopus 로고    scopus 로고
    • Regulation and function of the CD3? DxxxLL motif: a binding site for adaptor protein-1 and adaptor protein-2 in vitro
    • Dietrich, J., Kastrup, J., Nielsen, B. L., Odum, N. and Geisler, C., Regulation and function of the CD3? DxxxLL motif: a binding site for adaptor protein-1 and adaptor protein-2 in vitro. J. Cell Biol. 1997. 138:271-281.
    • (1997) J. Cell Biol. , vol.138 , pp. 271-281
    • Dietrich, J.1    Kastrup, J.2    Nielsen, B.L.3    Odum, N.4    Geisler, C.5
  • 18
    • 2442511061 scopus 로고    scopus 로고
    • Activation-induced polarized recycling targets T cell antigen receptors to the immunological synapse; involvement of SNARE complexes
    • Das, V., Nal, B., Dujeancourt, A., Thoulouze, M. I., Galli, T., Roux, P.,Utry-Varsat, A., et al., Activation-induced polarized recycling targets T cell antigen receptors to the immunological synapse; involvement of SNARE complexes. Immunity 2004. 20: 577-588.
    • (2004) Immunity , vol.20 , pp. 577-588
    • Das, V.1    Nal, B.2    Dujeancourt, A.3    Thoulouze, M.I.4    Galli, T.5    Roux, P.6    Utry-Varsat, A.7
  • 20
    • 0036569657 scopus 로고    scopus 로고
    • The CD3? leucine-based receptorsorting motif is required for efficient ligand-mediated TCR downregulation
    • von Essen, M., Menne, C., Nielsen, B. L., Lauritsen, J. P., Dietrich, J.,Andersen, P. S., Karjalainen, K. et al., The CD3? leucine-based receptorsorting motif is required for efficient ligand-mediated TCR downregulation. J. Immunol. 2002. 168: 4519-4523.
    • (2002) J. Immunol. , vol.168 , pp. 4519-4523
    • von Essen, M.1    Menne, C.2    Nielsen, B.L.3    Lauritsen, J.P.4    Dietrich, J.5    Andersen, P.S.6    Karjalainen, K.7
  • 23
    • 79959702357 scopus 로고    scopus 로고
    • TCR downregulation boosts T-cellmediated cytotoxicity and protection against poxvirus infections
    • Hansen, A. K., Regner, M., Bonefeld, C. M., Boding, L., Kongsbak, M.,Odum, N., Mullbacher, A. et al., TCR downregulation boosts T-cellmediated cytotoxicity and protection against poxvirus infections. Eur.J. Immunol. 2011. 41: 1948-1957.
    • (2011) Eur.J. Immunol. , vol.41 , pp. 1948-1957
    • Hansen, A.K.1    Regner, M.2    Bonefeld, C.M.3    Boding, L.4    Kongsbak, M.5    Odum, N.6    Mullbacher, A.7
  • 25
    • 77949873898 scopus 로고    scopus 로고
    • Vitamin D controls T cell antigen receptor signaling and activation of human T cells
    • von Essen, M. R., Kongsbak, M., Schjerling, P., Olgaard, K., Odum,N. and Geisler, C., Vitamin D controls T cell antigen receptor signaling and activation of human T cells. Nat. Immunol. 2010. 11:344-349.
    • (2010) Nat. Immunol. , vol.11 , pp. 344-349
    • von Essen, M.R.1    Kongsbak, M.2    Schjerling, P.3    Olgaard, K.4    Odum, N.5    Geisler, C.6
  • 26
    • 0000351142 scopus 로고
    • Activators of protein kinase C down-regulate and phosphorylate the T3/T-cell antigen receptor complex of human T lymphocytes
    • Cantrell, D. A., Davies, A. A. and Crumpton, M. J., Activators of protein kinase C down-regulate and phosphorylate the T3/T-cell antigen receptor complex of human T lymphocytes. Proc. Natl. Acad. Sci. USA 1985. 82:8158-8162.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8158-8162
    • Cantrell, D.A.1    Davies, A.A.2    Crumpton, M.J.3
  • 27
    • 0025312043 scopus 로고
    • Glutathione regulates activation-dependent DNA synthesis in highly purified normal human T lymphocytes stimulated via the CD2 and CD3 antigens
    • Suthanthiran, M., Anderson, M. E., Sharma, V. K. and Meister, A., Glutathione regulates activation-dependent DNA synthesis in highly purified normal human T lymphocytes stimulated via the CD2 and CD3 antigens.Proc. Natl. Acad. Sci. USA 1990. 87: 3343-3347.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3343-3347
    • Suthanthiran, M.1    Anderson, M.E.2    Sharma, V.K.3    Meister, A.4
  • 28
    • 70349314830 scopus 로고    scopus 로고
    • Extracellular redox modulation by regulatory T cells
    • Yan, Z., Garg, S. K., Kipnis, J. and Banerjee, R., Extracellular redox modulation by regulatory T cells. Nat. Chem. Biol. 2009. 5: 721-723.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 721-723
    • Yan, Z.1    Garg, S.K.2    Kipnis, J.3    Banerjee, R.4
  • 29
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna, R. and Jaken, S., Protein kinase C signaling and oxidative stress. Free Radic. Biol. Med. 2000. 28: 1349-1361.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 30
    • 0030006468 scopus 로고    scopus 로고
    • Tamoxifen modulates protein kinase C via oxidative stress in estrogen receptor-negative breast cancer cells
    • Gundimeda, U., Chen, Z. H. and Gopalakrishna, R., Tamoxifen modulates protein kinase C via oxidative stress in estrogen receptor-negative breast cancer cells. J. Biol. Chem. 1996. 271: 13504-13514.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13504-13514
    • Gundimeda, U.1    Chen, Z.H.2    Gopalakrishna, R.3
  • 32
    • 39949085437 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology
    • Kemp, M., Go, Y. M. and Jones, D. P., Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology. Free Radic. Biol. Med. 2008. 44: 921-937.
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 921-937
    • Kemp, M.1    Go, Y.M.2    Jones, D.P.3
  • 33
    • 76749096867 scopus 로고    scopus 로고
    • Redox remodeling as an immunoregulatory strategy
    • Yan, Z. and Banerjee, R., Redox remodeling as an immunoregulatory strategy. Biochemistry 2010. 49: 1059-1066.
    • (2010) Biochemistry , vol.49 , pp. 1059-1066
    • Yan, Z.1    Banerjee, R.2
  • 34
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D. and Powis, G., Thioredoxin reductase. Biochem. J. 2000. 346:1-8.
    • (2000) Biochem. J. , vol.346 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 35
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine)
    • Griffith, O. W. and Meister, A., Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J. Biol. Chem. 1979. 254: 7558-7560.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7558-7560
    • Griffith, O.W.1    Meister, A.2
  • 36
    • 0025906594 scopus 로고
    • Glutathione modulates activation-dependent proliferation of human peripheral blood lymphocyte populations without regulating their activated function
    • Smyth, M. J., Glutathione modulates activation-dependent proliferation of human peripheral blood lymphocyte populations without regulating their activated function. J. Immunol. 1991. 146:1921-1927.
    • (1991) J. Immunol. , vol.146 , pp. 1921-1927
    • Smyth, M.J.1
  • 37
    • 0037081849 scopus 로고    scopus 로고
    • Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction
    • Liu, Y., Graham, C., Li, A., Fisher, R. J. and Shaw, S., Phosphorylation of the protein kinase C-theta activation loop and hydrophobic motif regulates its kinase activity, but only activation loop phosphorylation is critical to in vivo nuclear-factor-kappaB induction. Biochem. J. 2002. 361:255-265.
    • (2002) Biochem. J. , vol.361 , pp. 255-265
    • Liu, Y.1    Graham, C.2    Li, A.3    Fisher, R.J.4    Shaw, S.5
  • 38
    • 80054953932 scopus 로고    scopus 로고
    • The kinase GLK controls autoimmunity and NF-kappaB signaling by activating the kinase PKC-theta in T cells
    • Chuang, H. C., Lan, J. L., Chen, D. Y., Yang, C. Y., Chen, Y. M., Li,J. P., Huang, C. Y. et al., The kinase GLK controls autoimmunity and NF-kappaB signaling by activating the kinase PKC-theta in T cells. Nat.Immunol. 2011. 12: 1113-1118.
    • (2011) Nat.Immunol. , vol.12 , pp. 1113-1118
    • Chuang, H.C.1    Lan, J.L.2    Chen, D.Y.3    Yang, C.Y.4    Chen, Y.M.5    Li, J.P.6    Huang, C.Y.7
  • 39
    • 0027732536 scopus 로고
    • Nitric oxide and nitric oxide-generating agents induce a reversible inactivation of protein kinase C activity and phorbol ester binding
    • Gopalakrishna, R., Chen, Z. H. and Gundimeda, U., Nitric oxide and nitric oxide-generating agents induce a reversible inactivation of protein kinase C activity and phorbol ester binding. J. Biol. Chem. 1993. 268:27180-27185.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27180-27185
    • Gopalakrishna, R.1    Chen, Z.H.2    Gundimeda, U.3
  • 40
    • 0344034360 scopus 로고    scopus 로고
    • Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells
    • Kahlos, K., Zhang, J., Block, E. R. and Patel, J. M., Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells. Mol. Cell Biochem. 2003. 254: 47-54.
    • (2003) Mol. Cell Biochem. , vol.254 , pp. 47-54
    • Kahlos, K.1    Zhang, J.2    Block, E.R.3    Patel, J.M.4
  • 41
    • 78951470679 scopus 로고    scopus 로고
    • S-nitrosylation inhibits protein kinase C-mediated contraction in mouse aorta
    • Choi, H., Tostes, R. C. and Webb, R. C., S-nitrosylation inhibits protein kinase C-mediated contraction in mouse aorta. J. Cardiovasc. Pharmacol.2011. 57: 65-71.
    • (2011) J. Cardiovasc. Pharmacol. , vol.57 , pp. 65-71
    • Choi, H.1    Tostes, R.C.2    Webb, R.C.3
  • 42
    • 0027439773 scopus 로고
    • CD3 antigen-mediated calcium signals and protein kinase C activation are higher in CD45R0+ than in CD45RA+ human T lymphocyte subsets
    • Robinson, A. T., Miller, N. and Alexander, D. R., CD3 antigen-mediated calcium signals and protein kinase C activation are higher in CD45R0+ than in CD45RA+ human T lymphocyte subsets. Eur. J. Immunol. 1993. 23:61-68.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 61-68
    • Robinson, A.T.1    Miller, N.2    Alexander, D.R.3
  • 43
    • 0028316562 scopus 로고
    • Naive versus memory CD4 T cell response to antigen. Memory cells are less dependent on accessory cell costimulation and can respond to many antigenpresenting cell types including resting B cells
    • Croft, M., Bradley, L. M. and Swain, S. L., Naive versus memory CD4 T cell response to antigen. Memory cells are less dependent on accessory cell costimulation and can respond to many antigenpresenting cell types including resting B cells. J. Immunol. 1994. 152:2675-2685.
    • (1994) J. Immunol. , vol.152 , pp. 2675-2685
    • Croft, M.1    Bradley, L.M.2    Swain, S.L.3
  • 44
    • 7444222893 scopus 로고    scopus 로고
    • Signaling control of memory T cell generation and function
    • Chandok, M. R. and Farber, D. L., Signaling control of memory T cell generation and function. Semin. Immunol. 2004. 16: 285-293.
    • (2004) Semin. Immunol. , vol.16 , pp. 285-293
    • Chandok, M.R.1    Farber, D.L.2
  • 45
    • 79960429950 scopus 로고    scopus 로고
    • Transcriptional control of rapid recall by memory CD4 T cells
    • Lai, W., Yu, M., Huang, M. N., Okoye, F., Keegan, A. D. and Farber, D. L.,Transcriptional control of rapid recall by memory CD4 T cells. J. Immunol.2011. 187: 133-140.
    • (2011) J. Immunol. , vol.187 , pp. 133-140
    • Lai, W.1    Yu, M.2    Huang, M.N.3    Okoye, F.4    Keegan, A.D.5    Farber, D.L.6
  • 46
    • 84861048532 scopus 로고    scopus 로고
    • Mechanisms behind functional avidity maturation in T Cells
    • von Essen, M. R., Kongsbak,M. and Geisler, C.,Mechanisms behind functional avidity maturation in T Cells. Clin. Dev. Immunol. 2012. 2012: 1-8.
    • (2012) Clin. Dev. Immunol. , vol.2012 , pp. 1-8
    • von Essen, M.R.1    Kongsbak, M.2    Geisler, C.3
  • 48
    • 0032480279 scopus 로고    scopus 로고
    • Threedimensional segregation of supramolecular activation clusters in T cells
    • Monks, C. R., Freiberg, B. A., Kupfer, H., Sciaky, N. and Kupfer, A., Threedimensional segregation of supramolecular activation clusters in T cells. Nature 1998. 395: 82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 49
    • 34249013684 scopus 로고    scopus 로고
    • Opposing effects of PKCtheta andWASp on symmetry breaking and relocation of the immunological synapse
    • Sims, T. N., Soos, T. J., Xenias, H. S., Dubin-Thaler, B., Hofman, J. M.,Waite, J. C., Cameron, T. O. et al., Opposing effects of PKCtheta andWASp on symmetry breaking and relocation of the immunological synapse. Cell 2007. 129: 773-785.
    • (2007) Cell , vol.129 , pp. 773-785
    • Sims, T.N.1    Soos, T.J.2    Xenias, H.S.3    Dubin-Thaler, B.4    Hofman, J.M.5    Waite, J.C.6    Cameron, T.O.7
  • 50
    • 0034889233 scopus 로고    scopus 로고
    • Functional avidity maturation of CD8(+)T cells without selection of higher affinity TCR.
    • Slifka, M. K. and Whitton, J. L., Functional avidity maturation of CD8(+)T cells without selection of higher affinity TCR. Nat. Immunol. 2001. 2:711-717.
    • (2001) Nat. Immunol. , vol.2 , pp. 711-717
    • Slifka, M.K.1    Whitton, J.L.2
  • 51
    • 0023726588 scopus 로고
    • Characterization and expression of the human T cell receptor-T3 complex by monoclonal antibody F101.01
    • Geisler, C., Plesner, T., Pallesen, G., Skjodt, K., Odum, N. and Larsen,J. K., Characterization and expression of the human T cell receptor-T3 complex by monoclonal antibody F101.01. Scand. J. Immunol. 1988. 27:685-696.
    • (1988) Scand. J. Immunol. , vol.27 , pp. 685-696
    • Geisler, C.1    Plesner, T.2    Pallesen, G.3    Skjodt, K.4    Odum, N.5    Larsen, J.K.6
  • 52
    • 0032500501 scopus 로고    scopus 로고
    • T cell receptor zeta allows stable expression of receptors containing the CD3? leucine-based receptor-sorting motif
    • Dietrich, J. and Geisler, C., T cell receptor zeta allows stable expression of receptors containing the CD3? leucine-based receptor-sorting motif. J.Biol. Chem. 1998. 273: 26281-26284.
    • (1998) J.Biol. Chem. , vol.273 , pp. 26281-26284
    • Dietrich, J.1    Geisler, C.2
  • 54
    • 0030589286 scopus 로고    scopus 로고
    • IL-2 induces beta2-integrin adhesion via a wortmannin/LY294002-sensitive, rapamycin-resistant pathway
    • Phosphorylation of a 125-kilodalton protein correlates with induction of adhesion, but not mitogenesis
    • Nielsen, M., Svejgaard, A., Skov, S., Dobson, P., Bendtzen, K.,Geisler, C. and Odum, N., IL-2 induces beta2-integrin adhesion via a wortmannin/LY294002-sensitive, rapamycin-resistant pathway. Phosphorylation of a 125-kilodalton protein correlates with induction of adhesion, but not mitogenesis. J. Immunol. 1996. 157:5350-5358.
    • (1996) J. Immunol. , vol.157 , pp. 5350-5358
    • Nielsen, M.1    Svejgaard, A.2    Skov, S.3    Dobson, P.4    Bendtzen, K.5    Geisler, C.6    Odum, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.