메뉴 건너뛰기




Volumn 2, Issue 5, 2001, Pages 389-396

CD45: New jobs for an old acquaintance

Author keywords

[No Author keywords available]

Indexed keywords

CD45 ANTIGEN; CYTOKINE RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0035347144     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/87687     Document Type: Review
Times cited : (259)

References (102)
  • 1
    • 0028346560 scopus 로고
    • CD45: An emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development
    • Trowbridge, I. S. & Thomas, M. L. CD45: an emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development. Annu. Rev. Immunol. 12, 85-116 (1994).
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 85-116
    • Trowbridge, I.S.1    Thomas, M.L.2
  • 2
    • 0024327898 scopus 로고
    • The leukocyte common antigen family
    • Thomas, M. L. The leukocyte common antigen family. Annu. Rev. Immunol. 7, 339-369 (1989).
    • (1989) Annu. Rev. Immunol. , vol.7 , pp. 339-369
    • Thomas, M.L.1
  • 3
    • 0024206455 scopus 로고
    • Demonstration that the leukocyte common antigen CD45 is a protein tyrosine phosphatase
    • Tonks, N. K., Charbonneau, H., Diltz, C. D., Fischer, E. H. & Walsh, K. A. Demonstration that the leukocyte common antigen CD45 is a protein tyrosine phosphatase. Biochemistry 27, 8695-8701. (1988).
    • (1988) Biochemistry , vol.27 , pp. 8695-8701
    • Tonks, N.K.1    Charbonneau, H.2    Diltz, C.D.3    Fischer, E.H.4    Walsh, K.A.5
  • 4
    • 0027296521 scopus 로고
    • Normal B lymphocyte development but impaired T cell maturation in CD45-exon6 protein tyrosine phosphatase-deficient mice
    • Kishihara, K. et al. Normal B lymphocyte development but impaired T cell maturation in CD45-exon6 protein tyrosine phosphatase-deficient mice. Cell 74, 143-156 (1993).
    • (1993) Cell , vol.74 , pp. 143-156
    • Kishihara, K.1
  • 5
    • 0029864147 scopus 로고    scopus 로고
    • + thymocytes, and B cell maturation
    • + thymocytes, and B cell maturation. J. Exp. Med. 183, 1707-1718 (1996).
    • (1996) J. Exp. Med. , vol.183 , pp. 1707-1718
    • Byth, K.F.1
  • 6
    • 0031112267 scopus 로고    scopus 로고
    • T cell development in mice expressing splice variants of the protein tyrosine phosphatase CD45
    • Kozieradzki, I. et al. T cell development in mice expressing splice variants of the protein tyrosine phosphatase CD45. J. Immunol. 158, 3130-3139 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 3130-3139
    • Kozieradzki, I.1
  • 7
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway
    • Koretzky, G. A., Picus, J., Thomas, M. L. & Weiss, A. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway. Nature 346, 66-68 (1990).
    • (1990) Nature , vol.346 , pp. 66-68
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 8
    • 0028358822 scopus 로고
    • Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degranulation of mast cells
    • Berger, S. A., Mak, T. W. & Paige, C. J. Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degranulation of mast cells. J. Exp. Med 180, 471-476 (1994).
    • (1994) J. Exp. Med , vol.180 , pp. 471-476
    • Berger, S.A.1    Mak, T.W.2    Paige, C.J.3
  • 9
    • 0031028993 scopus 로고    scopus 로고
    • Severe combined immunodeficiency with abnormalities in expression of the common leucocyte antigen, CD45
    • Cale, C. M. et al. Severe combined immunodeficiency with abnormalities in expression of the common leucocyte antigen, CD45. Arch. Dis. Child. 76, 163-164 (1997).
    • (1997) Arch. Dis. Child. , vol.76 , pp. 163-164
    • Cale, C.M.1
  • 10
    • 0034064779 scopus 로고    scopus 로고
    • Mutations in the tyrosine phosphatase CD45 gene in a child with severe combined immunodeficiency disease
    • Kung, C. et al. Mutations in the tyrosine phosphatase CD45 gene in a child with severe combined immunodeficiency disease. Nature Med. 6, 343-345 (2000).
    • (2000) Nature Med. , vol.6 , pp. 343-345
    • Kung, C.1
  • 11
    • 0035863892 scopus 로고    scopus 로고
    • A Deletion in the Gene Encoding the CD45 Antigen in a Patient with SCID
    • Tchilian, E. Z. et al. A Deletion in the Gene Encoding the CD45 Antigen in a Patient with SCID. J. Immunol. 166, 1308-1313 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 1308-1313
    • Tchilian, E.Z.1
  • 12
    • 0035905767 scopus 로고    scopus 로고
    • CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling
    • Irie-Sasaki, J. et al. CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling. Nature 409, 349-354 (2001).
    • (2001) Nature , vol.409 , pp. 349-354
    • Irie-Sasaki, J.1
  • 14
    • 0026011310 scopus 로고
    • Tyrosine phosphatase CD45 is required for T-cell antigen receptor and CD2-mediated activation of a protein tyrosine kinase and interleukin 2 production
    • Koretzky, G. A., Picus, J., Schultz, T. & Weiss, A. Tyrosine phosphatase CD45 is required for T-cell antigen receptor and CD2-mediated activation of a protein tyrosine kinase and interleukin 2 production. Proc. Natl Acad. Sci. USA 88, 2037-2041 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2037-2041
    • Koretzky, G.A.1    Picus, J.2    Schultz, T.3    Weiss, A.4
  • 15
    • 0032504217 scopus 로고    scopus 로고
    • Characterization of recombinant CD45 cytoplasmic domain proteins. Evidence for intramolecular and intermolecular interactions
    • Felberg, J. & Johnson, P. Characterization of recombinant CD45 cytoplasmic domain proteins. Evidence for intramolecular and intermolecular interactions. J. Biol. Chem. 273, 17839-17845 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 17839-17845
    • Felberg, J.1    Johnson, P.2
  • 16
    • 0344115338 scopus 로고    scopus 로고
    • CD45: A key regulator of Lck and T cell activation
    • Johnson, P. & Felberg, J. CD45: a key regulator of Lck and T cell activation. Mod. Asp. Immunolbiol. 1, 147-151 (2001).
    • (2001) Mod. Asp. Immunolbiol. , vol.1 , pp. 147-151
    • Johnson, P.1    Felberg, J.2
  • 17
    • 0141544141 scopus 로고
    • Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation
    • Cooper, J. A. & MacAuley, A. Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation. Proc. Natl Acad. Sci USA 85, 4232-4236. (1988).
    • (1988) Proc. Natl Acad. Sci USA , vol.85 , pp. 4232-4236
    • Cooper, J.A.1    MacAuley, A.2
  • 18
    • 0028337397 scopus 로고
    • Structure of the regulatory domains of the Src family tyrosine kinase Lck
    • Eck, M. J., Atwell, S. K., Shoelson, S. E. & Harrison, S. C. Structure of the regulatory domains of the Src family tyrosine kinase Lck. Nature 368, 764-769 (1994).
    • (1994) Nature , vol.368 , pp. 764-769
    • Eck, M.J.1    Atwell, S.K.2    Shoelson, S.E.3    Harrison, S.C.4
  • 19
    • 0025303196 scopus 로고
    • Dephosphorylation and activation of the T cell tyrosine kinase pp56lck by the leukocyte common antigen (CD45)
    • Mustelin, T. & Altman, A. Dephosphorylation and activation of the T cell tyrosine kinase pp56lck by the leukocyte common antigen (CD45). Oncogene 5, 809-513 (1990).
    • (1990) Oncogene , vol.5 , pp. 809-1513
    • Mustelin, T.1    Altman, A.2
  • 20
    • 0033049188 scopus 로고    scopus 로고
    • Expression of the p56(Lck) Y505F mutation in CD45-deficient mice rescues thymocyte development
    • Seavitt, J. R. et al. Expression of the p56(Lck) Y505F mutation in CD45-deficient mice rescues thymocyte development. Mol. Cell Biol. 19, 4200-4208. (1999).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4200-4208
    • Seavitt, J.R.1
  • 21
    • 0031172246 scopus 로고    scopus 로고
    • CD45 regulates Src family member kinase activity associated with macrophage integrin-mediated adhesion
    • Roach, T. et al. CD45 regulates Src family member kinase activity associated with macrophage integrin-mediated adhesion. Curr. Biol. 7, 408-417 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 408-417
    • Roach, T.1
  • 22
    • 0033558102 scopus 로고    scopus 로고
    • The CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes
    • D'Oro, U. & Ashwell, J. D. The CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes. J. Immunol. 162, 1879-1883 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 1879-1883
    • D'Oro, U.1    Ashwell, J.D.2
  • 23
    • 0029846429 scopus 로고    scopus 로고
    • CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells
    • Yanagi, S. et al. CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells. J. Biol. Chem. 271, 30487-30492 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 30487-30492
    • Yanagi, S.1
  • 24
    • 0033200308 scopus 로고    scopus 로고
    • Positive and negative regulation of Src family membrane kinases by CD45
    • Thomas, M. L. & Brown, E. J. Positive and negative regulation of Src family membrane kinases by CD45. Immunol. Today 20, 406-411 (1999).
    • (1999) Immunol. Today , vol.20 , pp. 406-411
    • Thomas, M.L.1    Brown, E.J.2
  • 25
    • 0026681275 scopus 로고
    • The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity
    • Bergman, M. et al. The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 11, 2919-2924 (1992).
    • (1992) EMBO J. , vol.11 , pp. 2919-2924
    • Bergman, M.1
  • 26
    • 0027240587 scopus 로고
    • Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk
    • Chow, L. M., Fournel, M., Davidson, D. & Veillette, A. Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk. Nature 365, 156-160 (1993).
    • (1993) Nature , vol.365 , pp. 156-160
    • Chow, L.M.1    Fournel, M.2    Davidson, D.3    Veillette, A.4
  • 27
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src family tyrosine kinases
    • Kawabuchi, M. et al. Transmembrane phosphoprotein Cbp regulates the activities of Src family tyrosine kinases. Nature 404, 999-1003 (2000).
    • (2000) Nature , vol.404 , pp. 999-1003
    • Kawabuchi, M.1
  • 28
    • 0034703099 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk
    • Takeuchi, S., Takayama, Y., Ogawa, A., Tamura, K. & Okada, M. Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk. J. Biol. Chem. 275, 29183-29186 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29183-29186
    • Takeuchi, S.1    Takayama, Y.2    Ogawa, A.3    Tamura, K.4    Okada, M.5
  • 29
    • 0342313755 scopus 로고    scopus 로고
    • Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation
    • Brdicka, T. et al. Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J. Exp. Med. 191, 1591-1604 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1591-1604
    • Brdicka, T.1
  • 30
    • 0028013487 scopus 로고
    • Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase
    • Autero, M. et al. Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase. Mol. Cell Biol. 14, 1308-1321 (1994).
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1308-1321
    • Autero, M.1
  • 31
    • 0030030293 scopus 로고    scopus 로고
    • Demonstration of a direct interaction between p56lck and the cytoplasmic domain of CD45 in vitro
    • Ng, D. H., Watts, J. D., Aebersold, R. & Johnson, P. Demonstration of a direct interaction between p56lck and the cytoplasmic domain of CD45 in vitro. J. Biol. Chem. 271, 1295-1300 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 1295-1300
    • Ng, D.H.1    Watts, J.D.2    Aebersold, R.3    Johnson, P.4
  • 32
    • 0030586542 scopus 로고    scopus 로고
    • Enhanced generation of NK cells with intact cytotoxic function in CD45 exon 6-deficient mice
    • Yamada, H., Kishihara, K., Kong, Y.Y. & Nomoto, K. Enhanced generation of NK cells with intact cytotoxic function in CD45 exon 6-deficient mice. J. Immunol. 157, 1523-1528 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 1523-1528
    • Yamada, H.1    Kishihara, K.2    Kong, Y.Y.3    Nomoto, K.4
  • 33
    • 0031919849 scopus 로고    scopus 로고
    • Jaks and STATs: Biological implications
    • Leonard, W. J. & O'Shea, J. J. Jaks and STATs: biological implications. Annu. Rev. Immunol. 16, 293-322 (1998).
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 293-322
    • Leonard, W.J.1    O'Shea, J.J.2
  • 34
    • 0031018486 scopus 로고    scopus 로고
    • Constitutive activation of JAK1 in Src-transformed cells
    • Campbell, G. S., Yu, C. L., Jove, R. & Carter-Su, C. Constitutive activation of JAK1 in Src-transformed cells. J. Biol. Cnem. 272, 2591-2594 (1997).
    • (1997) J. Biol. Cnem. , vol.272 , pp. 2591-2594
    • Campbell, G.S.1    Yu, C.L.2    Jove, R.3    Carter-Su, C.4
  • 35
    • 0030992813 scopus 로고    scopus 로고
    • Abrogation of interleukin-3 dependence of myeloid cells by the v-src oncogene requires SH2 and SH3 domains which specify activation of STATs
    • Chaturvedi, P., Sharma, S. & Reddy, E. P. Abrogation of interleukin-3 dependence of myeloid cells by the v-src oncogene requires SH2 and SH3 domains which specify activation of STATs. Mol. Cell Biol. 17, 3295-3304 (1997).
    • (1997) Mol. Cell Biol. , vol.17 , pp. 3295-3304
    • Chaturvedi, P.1    Sharma, S.2    Reddy, E.P.3
  • 36
    • 0033520326 scopus 로고    scopus 로고
    • SOCS1 is a critical inhibitor of interferon γ signaling and prevents the potentially fatal neonatal actions of this cytokine
    • Alexander, W. S. et al. SOCS1 is a critical inhibitor of interferon γ signaling and prevents the potentially fatal neonatal actions of this cytokine. Cell 98, 597-608 (1999).
    • (1999) Cell , vol.98 , pp. 597-608
    • Alexander, W.S.1
  • 37
    • 0033520467 scopus 로고    scopus 로고
    • SOCS1 deficiency causes a lymphocyte-dependent perinatal lethality
    • Marine, J. C. et al. SOCS1 deficiency causes a lymphocyte-dependent perinatal lethality. Cell 98, 609-416 (1999).
    • (1999) Cell , vol.98 , pp. 609-1416
    • Marine, J.C.1
  • 38
    • 0030792590 scopus 로고    scopus 로고
    • A family of cytokine-inducible inhibitors of signalling
    • Starr, R. et al. A family of cytokine-inducible inhibitors of signalling. Nature 387, 917-921 (1997).
    • (1997) Nature , vol.387 , pp. 917-921
    • Starr, R.1
  • 39
    • 0030839112 scopus 로고    scopus 로고
    • A new protein containing an SH2 domain that inhibits JAK kinases
    • Endo, T.A. et al. A new protein containing an SH2 domain that inhibits JAK kinases. Nature 387, 921-924 (1997).
    • (1997) Nature , vol.387 , pp. 921-924
    • Endo, T.A.1
  • 40
    • 20244389693 scopus 로고    scopus 로고
    • The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop
    • Yasukawa, H. et al. The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop. EMBO J. 18, 1309-1320 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1309-1320
    • Yasukawa, H.1
  • 41
    • 0028956353 scopus 로고
    • Specific recruitment of SH-PTPI to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals
    • Klingmuller, U., Lorenz, U., Cantley, L. C., Neel, B. G. & Lodish, H. F. Specific recruitment of SH-PTPI to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell 80, 729-738 (1995).
    • (1995) Cell , vol.80 , pp. 729-738
    • Klingmuller, U.1    Lorenz, U.2    Cantley, L.C.3    Neel, B.G.4    Lodish, H.F.5
  • 42
    • 0032545279 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-1 is a negative regulator of IL-4-and IL-13-dependent signal transduction
    • Haque, S. J., Harbor, P., Tabrizi, M., Yi, T. & Williams, B. R. Protein-tyrosine phosphatase Shp-1 is a negative regulator of IL-4-and IL-13-dependent signal transduction. J. Biol. Chem. 273, 33893-33896 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33893-33896
    • Haque, S.J.1    Harbor, P.2    Tabrizi, M.3    Yi, T.4    Williams, B.R.5
  • 43
    • 0031685495 scopus 로고    scopus 로고
    • Immunophenotype and clinical characteristics of CD45-negative and CD45-positive childhood acute lymphoblastic leukemia
    • Ratei, R. et al. Immunophenotype and clinical characteristics of CD45-negative and CD45-positive childhood acute lymphoblastic leukemia. Ann. Hematol. 77, 107-114 (1998).
    • (1998) Ann. Hematol. , vol.77 , pp. 107-114
    • Ratei, R.1
  • 44
    • 0030030640 scopus 로고    scopus 로고
    • Hodgkin's disease presenting as a solitary bone tumor. A report of four cases and review of the literature
    • Ozdemirli, M., Mankin, H. J., Aisenberg, A. C. & Harris, N. L. Hodgkin's disease presenting as a solitary bone tumor. A report of four cases and review of the literature. Cancer 77, 79-88 (1996).
    • (1996) Cancer , vol.77 , pp. 79-88
    • Ozdemirli, M.1    Mankin, H.J.2    Aisenberg, A.C.3    Harris, N.L.4
  • 45
    • 0033842074 scopus 로고    scopus 로고
    • Proliferation of immature myeloma cells by interleukin-6 is associated with CD45 expression in human multiple myeloma
    • Ishikawa, H., Mahmoud, M. S., Fujii, R., Abroun, S. & Kawano, M. M. Proliferation of immature myeloma cells by interleukin-6 is associated with CD45 expression in human multiple myeloma. Leuk. Lymphoma 39, 51-55 (2000).
    • (2000) Leuk. Lymphoma , vol.39 , pp. 51-55
    • Ishikawa, H.1    Mahmoud, M.S.2    Fujii, R.3    Abroun, S.4    Kawano, M.M.5
  • 46
    • 0034282725 scopus 로고    scopus 로고
    • Development of T-leukaemias in CD45 tyrosine phosphatase-deficient mutant lck mice
    • Baker, M. et al. Development of T-leukaemias in CD45 tyrosine phosphatase-deficient mutant lck mice. EMBO J. 19, 4644-4654 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4644-4654
    • Baker, M.1
  • 47
    • 0025992709 scopus 로고
    • CD45: A leukocyte-specific member of the protein tyrosine phosphatase family
    • Trowbridge, I. S., Ostergaard, H. L. & Johnson, P. CD45: a leukocyte-specific member of the protein tyrosine phosphatase family. Biochim. Biophys. Acta 1095, 46-56 (1991).
    • (1991) Biochim. Biophys. Acta , vol.1095 , pp. 46-56
    • Trowbridge, I.S.1    Ostergaard, H.L.2    Johnson, P.3
  • 48
    • 0026536632 scopus 로고
    • CD45 modulates T cell receptor/CD3-induced activation of human thymocytes via regulation of tyrosine phosphorylation
    • Turka, L. A., Kanner, S. B., Schieven, G. L., Thompson, C. B. & Ledbetter, J. A. CD45 modulates T cell receptor/CD3-induced activation of human thymocytes via regulation of tyrosine phosphorylation. Eur J. Immunol. 22, 551-557 (1992).
    • (1992) Eur J. Immunol. , vol.22 , pp. 551-557
    • Turka, L.A.1    Kanner, S.B.2    Schieven, G.L.3    Thompson, C.B.4    Ledbetter, J.A.5
  • 49
    • 15844415783 scopus 로고    scopus 로고
    • Prevention and reversal of renal allograft rejection by antibody against CD45RB
    • Lazarovits, A. I. et al. Prevention and reversal of renal allograft rejection by antibody against CD45RB. Nature 380, 717-720 (1996).
    • (1996) Nature , vol.380 , pp. 717-720
    • Lazarovits, A.I.1
  • 50
    • 0034719765 scopus 로고    scopus 로고
    • Prolongation of xenograft survival using monoclonal antibody CD45RB and cyclophosphamide in rat-to-mouse kidney and heart transplant models
    • Zhang, Z. et al. Prolongation of xenograft survival using monoclonal antibody CD45RB and cyclophosphamide in rat-to-mouse kidney and heart transplant models. Transplantation 69, 1137-1146 (2000).
    • (2000) Transplantation , vol.69 , pp. 1137-1146
    • Zhang, Z.1
  • 51
    • 0031007024 scopus 로고    scopus 로고
    • Indefinite islet allograft survival in mice after a short course of treatment with anti-CD45 monoclonal antibodies
    • Auersvald, L. A. et al. Indefinite islet allograft survival in mice after a short course of treatment with anti-CD45 monoclonal antibodies. Transplantation 63, 1355-1358 (1997).
    • (1997) Transplantation , vol.63 , pp. 1355-1358
    • Auersvald, L.A.1
  • 52
    • 0034711317 scopus 로고    scopus 로고
    • CD45 inhibits CD40L-induced microglial activation via negative regulation of the Src/p44/42 MAPK pathway
    • Tan, J., Town, T. & Mullan, M. CD45 inhibits CD40L-induced microglial activation via negative regulation of the Src/p44/42 MAPK pathway. J. Biol. Chem. 275, 37224-37231 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 37224-37231
    • Tan, J.1    Town, T.2    Mullan, M.3
  • 53
    • 0034667558 scopus 로고    scopus 로고
    • CD45 opposes β-amyloid peptide-induced microglial activation via inhibition of p44/42 mitogen-activated protein kinase
    • Tan, J. et al. CD45 opposes β-amyloid peptide-induced microglial activation via inhibition of p44/42 mitogen-activated protein kinase. J. Neurosci. 20, 7587-7594 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 7587-7594
    • Tan, J.1
  • 54
    • 13144250128 scopus 로고    scopus 로고
    • Antibody-mediated targeting of CD45 isoforms: A novel immunotherapeutic strategy
    • Basadonna, G. P. et al. Antibody-mediated targeting of CD45 isoforms: a novel immunotherapeutic strategy. Proc. Natl Acad. Sci. USA 95, 3821-3826 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3821-3826
    • Basadonna, G.P.1
  • 55
    • 0035236195 scopus 로고    scopus 로고
    • CTLA-4 up-regulation plays a role in tolerance mediated by CD45
    • Fecteau, S. et al. CTLA-4 up-regulation plays a role in tolerance mediated by CD45. Nature Immunol. 2, 58-43 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 58-143
    • Fecteau, S.1
  • 56
    • 0023337322 scopus 로고
    • Structural variants of human T200 glycoprotein (leukocyte-common antigen)
    • Ralph, S. J., Thomas, M. L., Morton, C. C. & Trowbridge, I. S. Structural variants of human T200 glycoprotein (leukocyte-common antigen). EMBO J. 6, 1251-1257 (1987).
    • (1987) EMBO J. , vol.6 , pp. 1251-1257
    • Ralph, S.J.1    Thomas, M.L.2    Morton, C.C.3    Trowbridge, I.S.4
  • 57
    • 0035106072 scopus 로고    scopus 로고
    • SC3S plays a role in T cell development and alternative splicing of CD45
    • Wang, H. Y., Xu, X., Ding, J. H., Bermingham, J. R. Jr & Fu, X. D. SC3S plays a role in T cell development and alternative splicing of CD45. Mol. Cell 7, 331-342 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 331-342
    • Wang, H.Y.1    Xu, X.2    Ding, J.H.3    Bermingham Jr., J.R.4    Fu, X.D.5
  • 58
    • 0026441382 scopus 로고
    • high expression induced by thymic selection events
    • high expression induced by thymic selection events. J. Exp. Med. 176, 1657-1663 (1992).
    • (1992) J. Exp. Med. , vol.176 , pp. 1657-1663
    • Wallace, V.A.1
  • 59
    • 0025648221 scopus 로고
    • Interleukin-4 induces expression of the CD45RA antigen on human thymocyte subpopulations
    • Uittenbogaart, C. H. et al. Interleukin-4 induces expression of the CD45RA antigen on human thymocyte subpopulations. Int. Immunol. 2, 1179-1187 (1990).
    • (1990) Int. Immunol. , vol.2 , pp. 1179-1187
    • Uittenbogaart, C.H.1
  • 60
    • 0025086509 scopus 로고
    • Interconversion of CD45R subsets of CD4 T cells in vivo
    • Bell, E. B. & Sparshott, S. M. Interconversion of CD45R subsets of CD4 T cells in vivo. Nature 348, 163-166 (1990).
    • (1990) Nature , vol.348 , pp. 163-166
    • Bell, E.B.1    Sparshott, S.M.2
  • 61
    • 0027266773 scopus 로고
    • Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase
    • Desai, D. M., Sap, J., Schlessinger, J. & Weiss, A. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 73, 541-554 (1993).
    • (1993) Cell , vol.73 , pp. 541-554
    • Desai, D.M.1    Sap, J.2    Schlessinger, J.3    Weiss, A.4
  • 62
    • 0027289547 scopus 로고
    • Regulation of TCR signaling by CD45 lacking transmembrane and extracellular domains
    • Volarevic, S. et al. Regulation of TCR signaling by CD45 lacking transmembrane and extracellular domains. Science 260, 541-544 (1993).
    • (1993) Science , vol.260 , pp. 541-544
    • Volarevic, S.1
  • 63
    • 0027254049 scopus 로고
    • Rescue of signaling by a chimeric protein containing the cytoplasmic domain of CD45
    • Hovis, R. R. et al. Rescue of signaling by a chimeric protein containing the cytoplasmic domain of CD45. Science 260, 544-546 (1993).
    • (1993) Science , vol.260 , pp. 544-546
    • Hovis, R.R.1
  • 64
    • 0033662317 scopus 로고    scopus 로고
    • A point mutation in PTPRC is associated with the development of multiple sclerosis
    • Jacobsen, M. et al. A point mutation in PTPRC is associated with the development of multiple sclerosis. Nature Genet. 26, 495-499 (2000).
    • (2000) Nature Genet. , vol.26 , pp. 495-499
    • Jacobsen, M.1
  • 65
    • 0025875259 scopus 로고
    • 1pr and gld: Single gene models of systemic autoimmunity and lymphoproliferative disease
    • Cohen, P. L. & Eisenberg, R. A. 1pr and gld: single gene models of systemic autoimmunity and lymphoproliferative disease. Annu. Rev. Immunol. 9, 243-269 (1991).
    • (1991) Annu. Rev. Immunol. , vol.9 , pp. 243-269
    • Cohen, P.L.1    Eisenberg, R.A.2
  • 66
    • 0027216143 scopus 로고
    • + T cells in the development of autoimmune diabetes in the non-obese diabetic (NOD) mouse
    • + T cells in the development of autoimmune diabetes in the non-obese diabetic (NOD) mouse. Int. Immunol. 5, 479-489 (1993).
    • (1993) Int. Immunol. , vol.5 , pp. 479-489
    • Sempe, P.1
  • 67
    • 77956981608 scopus 로고
    • + T cells in autoimmune infiltrates in experimental allergic encephalomyelitis
    • + T cells in autoimmune infiltrates in experimental allergic encephalomyelitis. Int. Immunol. 6, 347-354 (1994).
    • (1994) Int. Immunol. , vol.6 , pp. 347-354
    • Renno, T.1
  • 68
    • 0035862539 scopus 로고    scopus 로고
    • + T lymphocytes in children with infantile cholestasis
    • + T lymphocytes in children with infantile cholestasis. Immunol. Lett. 75, 179-184 (2001).
    • (2001) Immunol. Lett. , vol.75 , pp. 179-184
    • Socha, P.1
  • 69
    • 0029907786 scopus 로고    scopus 로고
    • + peripheral blood T-lymphocytes is related to auto-immune processes and hematological manifestations in systemic lupus erythematosus
    • + peripheral blood T-lymphocytes is related to auto-immune processes and hematological manifestations in systemic lupus erythematosus. Schweiz Med. Wochenschr. 126, 1922-1925 (1996).
    • (1996) Schweiz Med. Wochenschr. , vol.126 , pp. 1922-1925
    • Neidhart, M.1    Pataki, F.2    Michel, B.A.3    Fehr, K.4
  • 70
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • Grakoui, A. et al. The immunological synapse: a molecular machine controlling T cell activation. Science 285, 221-227 (1999).
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 71
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C. R. F., Freiberg, B. A., Kupfer, H., Sciaky, N. & Kupfer, A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 395, 82-86 (1998).
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.F.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 72
    • 0030927323 scopus 로고    scopus 로고
    • Making the T cell receptor go the distance: A topological view of T cell activation
    • Shaw, A. S. & Dustin, M. L. Making the T cell receptor go the distance: A topological view of T cell activation. Immunity 6, 361-369 (1997).
    • (1997) Immunity , vol.6 , pp. 361-369
    • Shaw, A.S.1    Dustin, M.L.2
  • 73
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains
    • Rodgers, W. & Rose, J. K. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. J. Cell Biol. 135, 1515-1523 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 1515-1523
    • Rodgers, W.1    Rose, J.K.2
  • 74
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes, P. W., Ley, S. C. & Magee, A. I. Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J. Cell Biol. 147, 447-461 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 75
    • 0034730188 scopus 로고    scopus 로고
    • A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation
    • Johnson, K. G., Bromley, S. K., Dustin, M. L. & Thomas, M. L. A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation. Proc. Natl Acad. Sci. USA 97, 10138-10143 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10138-10143
    • Johnson, K.G.1    Bromley, S.K.2    Dustin, M.L.3    Thomas, M.L.4
  • 76
    • 0034624809 scopus 로고    scopus 로고
    • Exclusion of CD45 from the T-cell receptor signaling area in antigen-stimulated T lymphocytes
    • Leupin, O., Zaru, R., Laroche, T., Muller, S. & Valitutti, S. Exclusion of CD45 from the T-cell receptor signaling area in antigen-stimulated T lymphocytes. Curr. Biol. 10, 277-280 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 277-280
    • Leupin, O.1    Zaru, R.2    Laroche, T.3    Muller, S.4    Valitutti, S.5
  • 77
    • 0032534304 scopus 로고    scopus 로고
    • TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site
    • Sperling, A. I. et al. TCR signaling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site. J. Immunol. 161, 6459-6462 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 6459-6462
    • Sperling, A.I.1
  • 78
    • 0030000401 scopus 로고    scopus 로고
    • Signal transduction and glycophosphatidylinositol-linked proteins (lyn, lck, CD4, CD45, G proteins, and CD55) selectively localize in Triton-insoluble plasma membrane domains of human leukemic cell lines and normal granulocytes
    • Parolini, I., Sargiacomo, M., Lisanti, M. P. & Peschle, C. Signal transduction and glycophosphatidylinositol-linked proteins (lyn, lck, CD4, CD45, G proteins, and CD55) selectively localize in Triton-insoluble plasma membrane domains of human leukemic cell lines and normal granulocytes. Blood 87, 3783-3794 (1996).
    • (1996) Blood , vol.87 , pp. 3783-3794
    • Parolini, I.1    Sargiacomo, M.2    Lisanti, M.P.3    Peschle, C.4
  • 79
    • 0025130728 scopus 로고
    • Intimate association of Thy-1 and the T-cell antigen receptor with the CD45 tyrosine phosphatase
    • Volarevic, S., Burns, C. M., Sussman, J. J. & Ashwell, J. D. Intimate association of Thy-1 and the T-cell antigen receptor with the CD45 tyrosine phosphatase. Proc. Natl Acad. Sci. USA 87, 7085-7089 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 7085-7089
    • Volarevic, S.1    Burns, C.M.2    Sussman, J.J.3    Ashwell, J.D.4
  • 80
    • 0026600993 scopus 로고
    • Src-related protein tyrosine kinases and T-cell receptor signalling
    • Veillette, A. & Davidson, D. Src-related protein tyrosine kinases and T-cell receptor signalling. Trends Genet. 8, 61-66 (1992).
    • (1992) Trends Genet. , vol.8 , pp. 61-66
    • Veillette, A.1    Davidson, D.2
  • 81
    • 0032472226 scopus 로고    scopus 로고
    • Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge
    • Majeti, R., Bilwes, A. M., Noel, J. P., Hunter, T. & Weiss, A. Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. Science 279, 88-91 (1998).
    • (1998) Science , vol.279 , pp. 88-91
    • Majeti, R.1    Bilwes, A.M.2    Noel, J.P.3    Hunter, T.4    Weiss, A.5
  • 82
    • 0033859771 scopus 로고    scopus 로고
    • Receptor-like protein tyrosine phosphatase α homodimerizes on the cell surface
    • Jiang, G., den Hertog, J. & Hunter, T. Receptor-like protein tyrosine phosphatase α homodimerizes on the cell surface. Mol. Cell Biol. 20. 5917-5929 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5917-5929
    • Jiang, G.1    Den Hertog, J.2    Hunter, T.3
  • 83
    • 0029759927 scopus 로고    scopus 로고
    • Structural basis for inhibition of receptor protein-tyrosine phosphatase-α by dimerization
    • Bilwes, A. M., den Hertog, J., Hunter, T. & Noel, J. P. Structural basis for inhibition of receptor protein-tyrosine phosphatase-α by dimerization. Nature 382, 555-559 (1996).
    • (1996) Nature , vol.382 , pp. 555-559
    • Bilwes, A.M.1    Den Hertog, J.2    Hunter, T.3    Noel, J.P.4
  • 84
    • 0034704180 scopus 로고    scopus 로고
    • An Inactivating Point Mutation in the Inhibitory Wedge of CD45 Causes Lymphoproliferation and Autoimmunity
    • Majeti, R. et al. An Inactivating Point Mutation in the Inhibitory Wedge of CD45 Causes Lymphoproliferation and Autoimmunity. Cell 103, 1059-1070 (2000).
    • (2000) Cell , vol.103 , pp. 1059-1070
    • Majeti, R.1
  • 85
    • 0039846522 scopus 로고    scopus 로고
    • Phosphorylation of CD45 by casein kinase 2. Modulation of activity and mutational analysis
    • Wang, Y., Guo, W., Liang, L. & Esselman, W. J. Phosphorylation of CD45 by casein kinase 2. Modulation of activity and mutational analysis. J. Biol. Chem. 274, 7454-7461 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7454-7461
    • Wang, Y.1    Guo, W.2    Liang, L.3    Esselman, W.J.4
  • 86
    • 0028017607 scopus 로고
    • Protein-tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases
    • Stover, D. R. & Walsh, K. A. Protein-tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases. Mol. Cell Biol. 14, 5523-5532 (1994).
    • (1994) Mol. Cell Biol. , vol.14 , pp. 5523-5532
    • Stover, D.R.1    Walsh, K.A.2
  • 87
    • 0031154586 scopus 로고    scopus 로고
    • Inhibition of CD45 during neutrophil activation
    • Fialkow, L., Chan, C. K. & Downey, G. P. Inhibition of CD45 during neutrophil activation. J. Immunol. 158, 5409-5417 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 5409-5417
    • Fialkow, L.1    Chan, C.K.2    Downey, G.P.3
  • 88
    • 0033838825 scopus 로고    scopus 로고
    • + T cells: Specific inhibition of cytokine production but not proliferation of human naive T cells
    • + T cells: specific inhibition of cytokine production but not proliferation of human naive T cells. Clin. Exp. Immunol. 121, 283-288, (2000).
    • (2000) Clin. Exp. Immunol. , vol.121 , pp. 283-288
    • Eriksson, K.1    Nordstrom, I.2    Czerkinsky, C.3    Holmgren, J.4
  • 89
    • 0025901099 scopus 로고
    • Protein-tyrosine-phosphatase CD45 is phosphorylated transiently on tyrosine upon activation of Jurkat T cells
    • Stover, D. R., Charbonneau, H., Tonks, N. K. & Walsh, K. A. Protein-tyrosine-phosphatase CD45 is phosphorylated transiently on tyrosine upon activation of Jurkat T cells. Proc. Natl. Acad. Sci. USA 88, 7704-7707 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7704-7707
    • Stover, D.R.1    Charbonneau, H.2    Tonks, N.K.3    Walsh, K.A.4
  • 90
    • 0030664027 scopus 로고    scopus 로고
    • The role of CD45 and CD45-associated molecules in T cell activation
    • Altin, J. G. & Sloan, E. K. The role of CD45 and CD45-associated molecules in T cell activation. Immunol. Cell Biol. 75, 430-445 (1997).
    • (1997) Immunol. Cell Biol. , vol.75 , pp. 430-445
    • Altin, J.G.1    Sloan, E.K.2
  • 91
    • 0028036712 scopus 로고
    • LPAP, a novel 32-kD phosphoprotein that interacts with CD45 in human lymphocytes
    • Schraven, B. et al. LPAP, a novel 32-kD phosphoprotein that interacts with CD45 in human lymphocytes. J. Biol. Chem. 269, 29102-29111 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 29102-29111
    • Schraven, B.1
  • 92
    • 0029597411 scopus 로고
    • Identification of the sites of interaction between lymphocyte phosphatase-associated phosphoprotein (LPAP) and CD45
    • Bruyns, E., Hendricks-Taylor, L. R., Meuer, S., Koretzky, G. A. & Schraven, B. Identification of the sites of interaction between lymphocyte phosphatase-associated phosphoprotein (LPAP) and CD45. J. Biol. Chem. 270, 31372-31376 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 31372-31376
    • Bruyns, E.1    Hendricks-Taylor, L.R.2    Meuer, S.3    Koretzky, G.A.4    Schraven, B.5
  • 93
    • 0032101050 scopus 로고    scopus 로고
    • Disruption of lymphocyte function and signaling in CD45-associated protein-null mice
    • Matsuda, A. et al. Disruption of lymphocyte function and signaling in CD45-associated protein-null mice. J. Exp. Med. 187, 1863-1870 (1998).
    • (1998) J. Exp. Med. , vol.187 , pp. 1863-1870
    • Matsuda, A.1
  • 94
    • 0031931137 scopus 로고    scopus 로고
    • Biochemical analysis of the CD45-p56(lck) complex in Jurkat T cells lacking expression of lymphocyte phosphatase-associated phosphoprotein
    • Bruyns, E., Kirchgessner, H., Meuer, S. & Schraven, B. Biochemical analysis of the CD45-p56(lck) complex in Jurkat T cells lacking expression of lymphocyte phosphatase-associated phosphoprotein. Int. Immunol. 10, 185-194 (1998).
    • (1998) Int. Immunol. , vol.10 , pp. 185-194
    • Bruyns, E.1    Kirchgessner, H.2    Meuer, S.3    Schraven, B.4
  • 95
    • 0032709886 scopus 로고    scopus 로고
    • Biochemical and functional analysis of mice deficient in expression of the CD45-associated phosphoprotein LPAP
    • Ding, I. et al. Biochemical and functional analysis of mice deficient in expression of the CD45-associated phosphoprotein LPAP. Eur J. Immunol. 29, 3956-3961 (1999).
    • (1999) Eur J. Immunol. , vol.29 , pp. 3956-3961
    • Ding, I.1
  • 96
    • 0032711859 scopus 로고    scopus 로고
    • CD45-associated protein is not essential for the regulation of antigen receptor-mediated signal transduction
    • Kung, C. et al. CD45-associated protein is not essential for the regulation of antigen receptor-mediated signal transduction. Eur J. Immunol. 29, 3951-3955 (1999).
    • (1999) Eur J. Immunol. , vol.29 , pp. 3951-3955
    • Kung, C.1
  • 97
    • 0025913892 scopus 로고
    • The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2-6 sialyltransferase, CD75, on B cells
    • Stamenkovic, I., Sgroi, D., Aruffo, A., Sy, M. S. & Anderson, T. The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2-6 sialyltransferase, CD75, on B cells. Cell 66, 1133-1144 (1991).
    • (1991) Cell , vol.66 , pp. 1133-1144
    • Stamenkovic, I.1    Sgroi, D.2    Aruffo, A.3    Sy, M.S.4    Anderson, T.5
  • 98
    • 0027411632 scopus 로고
    • CD22, a B cell-specific immunoglobulin superfamily member, is a sialic acid-binding lectin
    • Sgroi, D., Varki, A., Braesch-Andersen, S. & Stamenkovic, I. CD22, a B cell-specific immunoglobulin superfamily member, is a sialic acid-binding lectin. J. Biol. Chem. 268, 7011-7018 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 7011-7018
    • Sgroi, D.1    Varki, A.2    Braesch-Andersen, S.3    Stamenkovic, I.4
  • 99
    • 0034046951 scopus 로고    scopus 로고
    • Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1
    • Symons, A., Cooper, D. N. & Barclay, A. N. Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1. Glycobiology 10, 559-563. (2000).
    • (2000) Glycobiology , vol.10 , pp. 559-563
    • Symons, A.1    Cooper, D.N.2    Barclay, A.N.3
  • 100
    • 0029589620 scopus 로고
    • Apoptosis of T cells mediated by galectin-1
    • Perillo, N. L., Pace, K. E., Seilhamer, J. J. & Baum, L. G. Apoptosis of T cells mediated by galectin-1. Nature 378, 736-739 (1995).
    • (1995) Nature , vol.378 , pp. 736-739
    • Perillo, N.L.1    Pace, K.E.2    Seilhamer, J.J.3    Baum, L.G.4
  • 101
    • 0035825644 scopus 로고    scopus 로고
    • Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
    • Demetriou, M., Granovsky, M., Quaggin, S. & Dennis, J. W. Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Nature 409, 733-739 (2001).
    • (2001) Nature , vol.409 , pp. 733-739
    • Demetriou, M.1    Granovsky, M.2    Quaggin, S.3    Dennis, J.W.4
  • 102
    • 0031441901 scopus 로고    scopus 로고
    • Antiproliferative action of interferon-a requires components of T-cell-receptor signalling
    • Petricoin, E. F. I. et al. Antiproliferative action of interferon-a requires components of T-cell-receptor signalling. Nature 390, 629-632 (1997).
    • (1997) Nature , vol.390 , pp. 629-632
    • Petricoin, E.F.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.