메뉴 건너뛰기




Volumn 247, Issue 2, 1998, Pages 200-211

The human immunodeficiency virus type 1 NEF protein binds the Src- related tyrosine kinase Lck SH2 domain through a novel phosphotyrosine independent mechanism

Author keywords

[No Author keywords available]

Indexed keywords

NEF PROTEIN; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE;

EID: 0032145709     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9244     Document Type: Article
Times cited : (37)

References (76)
  • 1
    • 0028180868 scopus 로고
    • Nef induces CD4 endocytosis: Requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain
    • Aiken C., Konner J., Landau N. R., Lenburg M. E., Trono D. Nef induces CD4 endocytosis: Requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain. Cell. 76:1994;853-864.
    • (1994) Cell , vol.76 , pp. 853-864
    • Aiken, C.1    Konner, J.2    Landau, N.R.3    Lenburg, M.E.4    Trono, D.5
  • 2
    • 0029015330 scopus 로고
    • Nef stimulates human immunodeficiency virus type 1 proviral dna synthesis
    • Aiken C., Trono D. Nef stimulates human immunodeficiency virus type 1 proviral dna synthesis. J. Virol. 69:1995;5048-5056.
    • (1995) J. Virol. , vol.69 , pp. 5048-5056
    • Aiken, C.1    Trono, D.2
  • 3
    • 0029670763 scopus 로고    scopus 로고
    • Replication and pathogenicity of human immunodeficiency virus type 1 accessory gene mutants in SCID-hu mice
    • Aldrovandi G. M., Zack J. A. Replication and pathogenicity of human immunodeficiency virus type 1 accessory gene mutants in SCID-hu mice. J. Virol. 70:1996;1505-1511.
    • (1996) J. Virol , vol.70 , pp. 1505-1511
    • Aldrovandi, G.M.1    Zack, J.A.2
  • 4
    • 0031572847 scopus 로고    scopus 로고
    • The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling
    • Arold S., Franken P., Strub M. P., Hoh F., Benichou S., Benarous R., Dumas C. The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. Structure. 5:1997;1361-1372.
    • (1997) Structure , vol.5 , pp. 1361-1372
    • Arold, S.1    Franken, P.2    Strub, M.P.3    Hoh, F.4    Benichou, S.5    Benarous, R.6    Dumas, C.7
  • 5
    • 0030887932 scopus 로고    scopus 로고
    • The N-terminus of Nef from HIV-1/SIV associates with a protein complex containing Lck and a serine kinase
    • Baur A. S., Sass G., Laffert B., Willbold D., Cheng M. C., Peterlin B. M. The N-terminus of Nef from HIV-1/SIV associates with a protein complex containing Lck and a serine kinase. Immunity. 6:1997;283-291.
    • (1997) Immunity , vol.6 , pp. 283-291
    • Baur, A.S.1    Sass, G.2    Laffert, B.3    Willbold, D.4    Cheng, M.C.5    Peterlin, B.M.6
  • 6
    • 0028485232 scopus 로고
    • HIV-1 Nef leads to inhibition or activation of T cells depending on its intracellular localization
    • Baur A. S., Sawai E. T., Dazin P., Fantl W. J., Cheng M. C., Peterlin B. M. HIV-1 Nef leads to inhibition or activation of T cells depending on its intracellular localization. Immunity. 1:1994;373-384.
    • (1994) Immunity , vol.1 , pp. 373-384
    • Baur, A.S.1    Sawai, E.T.2    Dazin, P.3    Fantl, W.J.4    Cheng, M.C.5    Peterlin, B.M.6
  • 7
    • 0029021821 scopus 로고
    • In vitro binding and phosphorylation of human immunodeficiency virus type 1 Nef protein by serine/threonine protein kinase
    • Bodeus M., Maris C. A., Bougeret C., Ramos M. F., Benarous R. In vitro binding and phosphorylation of human immunodeficiency virus type 1 Nef protein by serine/threonine protein kinase. J. Gen. Virol. 76:1995;1337-1344.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1337-1344
    • Bodeus, M.1    Maris, C.A.2    Bougeret, C.3    Ramos, M.F.4    Benarous, R.5
  • 8
    • 0030891168 scopus 로고    scopus 로고
    • Leukocyte protein tyrosine kinases: Potential targets for drug discovery
    • Bolen J. B., Brugge J. S. Leukocyte protein tyrosine kinases: Potential targets for drug discovery. Annu. Rev. Immunol. 15:1997;371-404.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 371-404
    • Bolen, J.B.1    Brugge, J.S.2
  • 10
    • 0027370209 scopus 로고
    • CD4 cell surface downregulation in HIV-1 Nef transgenic mice is a consequence of intracellular sequestration
    • Brady H. J., Pennington D. J., Miles C. G., Dzierzak E. A. CD4 cell surface downregulation in HIV-1 Nef transgenic mice is a consequence of intracellular sequestration. EMBO J. 12:1993;4923-4932.
    • (1993) EMBO J. , vol.12 , pp. 4923-4932
    • Brady, H.J.1    Pennington, D.J.2    Miles, C.G.3    Dzierzak, E.A.4
  • 11
    • 0030792141 scopus 로고    scopus 로고
    • SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1
    • Briggs S. D., Sharkey M., Sevenson M., Smithgall T. E. SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1. J. Biol. Chem. 272:1997;17899-17902.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17899-17902
    • Briggs, S.D.1    Sharkey, M.2    Sevenson, M.3    Smithgall, T.E.4
  • 12
    • 0028302998 scopus 로고
    • Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene
    • Chowers M. Y., Spina C. A., Kwoh T. J., Fitch N. J., Richman D. D., Guatelli J. C. Optimal infectivity in vitro of human immunodeficiency virus type 1 requires an intact nef gene. J. Virol. 68:1994;2906-2914.
    • (1994) J. Virol , vol.68 , pp. 2906-2914
    • Chowers, M.Y.1    Spina, C.A.2    Kwoh, T.J.3    Fitch, N.J.4    Richman, D.D.5    Guatelli, J.C.6
  • 13
    • 0028278201 scopus 로고
    • Raf-1 interacts with Fyn and Src in a non-phosphotyrosine-dependent manner
    • Cleghon V., Morrison D. K. Raf-1 interacts with Fyn and Src in a non-phosphotyrosine-dependent manner. J. Biol. Chem. 269:1994;17749-17755.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17749-17755
    • Cleghon, V.1    Morrison, D.K.2
  • 14
    • 0030924947 scopus 로고    scopus 로고
    • Protein kinase C-mediated phosphorylation of HIV-1 nef in human cell lines
    • Coates K., Cooke S. J., Mann D. A., Harris M. Protein kinase C-mediated phosphorylation of HIV-1 nef in human cell lines. J. Biol. Chem. 272:1997;12289-12294.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12289-12294
    • Coates, K.1    Cooke, S.J.2    Mann, D.A.3    Harris, M.4
  • 15
    • 0028968962 scopus 로고
    • The human immunodeficiency virus type 1 Nef protein functions as a protein kinase C substrate in vitro
    • Coates K., Harris M. The human immunodeficiency virus type 1 Nef protein functions as a protein kinase C substrate in vitro. J. Gen. Virol. 76:1995;837-844.
    • (1995) J. Gen. Virol , vol.76 , pp. 837-844
    • Coates, K.1    Harris, M.2
  • 16
    • 0030027765 scopus 로고    scopus 로고
    • Specific Th1 cytokine down-regulation associated with primary clinically derived human immunodeficiency virus type 1 nef gene-induced expression
    • Collette Y., Chang H. L., Cerdan C., Chambost H., Algarte M., Mawas C., Imbert J., Burny A., Olive D. Specific Th1 cytokine down-regulation associated with primary clinically derived human immunodeficiency virus type 1 nef gene-induced expression. J. Immunol. 156:1996a;360-370.
    • (1996) J. Immunol. , vol.156 , pp. 360-370
    • Collette, Y.1    Chang, H.L.2    Cerdan, C.3    Chambost, H.4    Algarte, M.5    Mawas, C.6    Imbert, J.7    Burny, A.8    Olive, D.9
  • 18
    • 0030812483 scopus 로고    scopus 로고
    • Non-receptor protein tyrosine kinases as immune targets of viruses
    • Collette Y., Olive D. Non-receptor protein tyrosine kinases as immune targets of viruses. Immunol. Today. 18:1997;393-400.
    • (1997) Immunol. Today , vol.18 , pp. 393-400
    • Collette, Y.1    Olive, D.2
  • 19
    • 0030448524 scopus 로고    scopus 로고
    • HIV-1: Is Nef a PAK animal
    • Cullen B. R. HIV-1: Is Nef a PAK animal. Curr. Biol. 6:1996;1557-1559.
    • (1996) Curr. Biol. , vol.6 , pp. 1557-1559
    • Cullen, B.R.1
  • 20
    • 0028021665 scopus 로고
    • Characterization of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains
    • Dechert U., Adam M., Harder K. W., Clark L. I., Jirik F. Characterization of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains. J. Biol. Chem. 269:1994;5602-5611.
    • (1994) J. Biol. Chem , vol.269 , pp. 5602-5611
    • Dechert, U.1    Adam, M.2    Harder, K.W.3    Clark, L.I.4    Jirik, F.5
  • 22
    • 0027502504 scopus 로고
    • Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
    • Eck M. J., Shoelson S. E., Harrison S. C. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature. 362:1993;87-91.
    • (1993) Nature , vol.362 , pp. 87-91
    • Eck, M.J.1    Shoelson, S.E.2    Harrison, S.C.3
  • 23
    • 0022860568 scopus 로고
    • Cytoplasmic localization of the HTLV-III 3′ orf protein in cultured T cells
    • Franchini G., Robert G. M., Ghrayeb J., Chang N. T., Wong S. F. Cytoplasmic localization of the HTLV-III 3′ orf protein in cultured T cells. Virology. 155:1986;593-599.
    • (1986) Virology , vol.155 , pp. 593-599
    • Franchini, G.1    Robert, G.M.2    Ghrayeb, J.3    Chang, N.T.4    Wong, S.F.5
  • 24
    • 0025733252 scopus 로고
    • Serine phosphorylation-independent downregulation of cell-surface CD4 by nef
    • Garcia J. V., Miller A. D. Serine phosphorylation-independent downregulation of cell-surface CD4 by nef. Nature. 350:1991;508-511.
    • (1991) Nature , vol.350 , pp. 508-511
    • Garcia, J.V.1    Miller, A.D.2
  • 25
    • 0029046227 scopus 로고
    • Dissociation of the CD4 downregulation and viral infectivity enhancement functions of human immunodeficiency virus type 1 Nef
    • Goldsmith M. A., Warmerdam M. T., Atchison R. E., Miller M. D., Greene W. C. Dissociation of the CD4 downregulation and viral infectivity enhancement functions of human immunodeficiency virus type 1 Nef. J. Virol. 69:1995;4112-4121.
    • (1995) J. Virol. , vol.69 , pp. 4112-4121
    • Goldsmith, M.A.1    Warmerdam, M.T.2    Atchison, R.E.3    Miller, M.D.4    Greene, W.C.5
  • 26
    • 0028887886 scopus 로고
    • Human immunodeficiency virus type 1 Nef protein inhibits activation pathways in peripheral blood mononuclear cells and T-cell lines
    • Greenway A., Azad A., McPhee D. Human immunodeficiency virus type 1 Nef protein inhibits activation pathways in peripheral blood mononuclear cells and T-cell lines. J. Virol. 69:1995;1842-1850.
    • (1995) J. Virol. , vol.69 , pp. 1842-1850
    • Greenway, A.1    Azad, A.2    McPhee, D.3
  • 27
    • 0029819124 scopus 로고    scopus 로고
    • Human identify virus type 1 Nef binds directly to Lck and mitogen protein kinase, inhibiting kinase activity
    • Greenway A., Azad A., Mills J., McPhee D. Human identify virus type 1 Nef binds directly to Lck and mitogen protein kinase, inhibiting kinase activity. J. Virol. 70:1996;6701-6708.
    • (1996) J. Virol. , vol.70 , pp. 6701-6708
    • Greenway, A.1    Azad, A.2    Mills, J.3    McPhee, D.4
  • 28
    • 0030896502 scopus 로고    scopus 로고
    • Deletion of nef slows but does not prevent CD4-positive T-cell depletion in human immunodeficiency virus type 1-infected human-PBL-SCID mice
    • Gulizia R. J., Collman R. G., Levy J. A., Trono D., Mosier D. E. Deletion of nef slows but does not prevent CD4-positive T-cell depletion in human immunodeficiency virus type 1-infected human-PBL-SCID mice. J. Virol. 71:1997;4161-4164.
    • (1997) J. Virol. , vol.71 , pp. 4161-4164
    • Gulizia, R.J.1    Collman, R.G.2    Levy, J.A.3    Trono, D.4    Mosier, D.E.5
  • 29
    • 0023659754 scopus 로고
    • HIV F/3′ orf encodes a phosphorylated GTP-binding protein resembling an oncogene product
    • Guy B., Kieny M. P., Riviere Y., Le P. C., Dott K., Girard M., Montagnier L., Lecocq J. P. HIV F/3′ orf encodes a phosphorylated GTP-binding protein resembling an oncogene product. Nature. 330:1987;266-269.
    • (1987) Nature , vol.330 , pp. 266-269
    • Guy, B.1    Kieny, M.P.2    Riviere, Y.3    Le, P.C.4    Dott, K.5    Girard, M.6    Montagnier, L.7    Lecocq, J.P.8
  • 30
    • 0028887998 scopus 로고
    • Multiple kinases mediate T-cell-receptor signaling
    • Howe L. R., Weiss A. Multiple kinases mediate T-cell-receptor signaling. Trends Biochem. Sci. 20:1995;59-64.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 59-64
    • Howe, L.R.1    Weiss, A.2
  • 31
    • 0031039979 scopus 로고    scopus 로고
    • Separable functions of Nef disrupt two aspects of T cell receptor machinery: CD4 expression and CD3 signaling
    • Iafrate A. J., Bronson S., Skowronski J. Separable functions of Nef disrupt two aspects of T cell receptor machinery: CD4 expression and CD3 signaling. EMBO J. 16:1997;673-684.
    • (1997) EMBO J. , vol.16 , pp. 673-684
    • Iafrate, A.J.1    Bronson, S.2    Skowronski, J.3
  • 33
    • 0028800298 scopus 로고
    • Downregulation of Lck-mediated signal transduction by tip of herpesvirus saimiri
    • Jung J. U., Lang S. M., Jun T., Roberts T. M., Veillette A., Desrosiers R. C. Downregulation of Lck-mediated signal transduction by tip of herpesvirus saimiri. J. Virol. 69:1995a;7814-7822.
    • (1995) J. Virol. , vol.69 , pp. 7814-7822
    • Jung, J.U.1    Lang, S.M.2    Jun, T.3    Roberts, T.M.4    Veillette, A.5    Desrosiers, R.C.6
  • 36
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interaction of cytoplasmic signaling proteins
    • Koch C. A., Anderson D., Moran M. F., Ellis C., Pawson T. SH2 and SH3 domains: Elements that control interaction of cytoplasmic signaling proteins. Science. 252:1991;668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 37
    • 0028805516 scopus 로고
    • A single amino acid in the sh3 domain of hck determines its high affinity and specificity in biding to hiv-1 nef protein
    • Lee C. H., Leung B., Lemon M. A., Zheng J., Cowburn D., Kuriyan J., Saksela K. A single amino acid in the sh3 domain of hck determines its high affinity and specificity in biding to hiv-1 nef protein. EMBO J. 14:1995;5006-5015.
    • (1995) EMBO J. , vol.14 , pp. 5006-5015
    • Lee, C.H.1    Leung, B.2    Lemon, M.A.3    Zheng, J.4    Cowburn, D.5    Kuriyan, J.6    Saksela, K.7
  • 38
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee C. H., Saksela K., Mirza U. A., Chait B. T., Kuriyan J. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell. 85:1996;931-942.
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 39
    • 0031550805 scopus 로고    scopus 로고
    • Human immunodeficiency virus type I Nef independently affects virion incorporation of major histocompatibility complex class I molecules and virus infectivity
    • Legall S., Prevost M. C., Heard J. M., Schwartz O. Human immunodeficiency virus type I Nef independently affects virion incorporation of major histocompatibility complex class I molecules and virus infectivity. Virology. 229:1997;295-301.
    • (1997) Virology , vol.229 , pp. 295-301
    • Legall, S.1    Prevost, M.C.2    Heard, J.M.3    Schwartz, O.4
  • 40
    • 0027955426 scopus 로고
    • Severe immunodeficiency associated with a human immunodeficiency virus 1 NEF/3′-long terminal repeat transgene
    • Lindemann D., Wilhelm R., Renard P., Althage A., Zinkernagel R., Mous J. Severe immunodeficiency associated with a human immunodeficiency virus 1 NEF/3′-long terminal repeat transgene. J. Exp. Med. 179:1994;797-807.
    • (1994) J. Exp. Med. , vol.179 , pp. 797-807
    • Lindemann, D.1    Wilhelm, R.2    Renard, P.3    Althage, A.4    Zinkernagel, R.5    Mous, J.6
  • 41
    • 0031047976 scopus 로고    scopus 로고
    • Induction of phosphorylation of human immunodeficiency virus type 1 Nef and enhancement of CD4 downregulation of phrobol myristate acetate
    • Luo T., Downing J. R., Garcia J. V. Induction of phosphorylation of human immunodeficiency virus type 1 Nef and enhancement of CD4 downregulation of phrobol myristate acetate. J. Virol. 71:1997;2535-2539.
    • (1997) J. Virol. , vol.71 , pp. 2535-2539
    • Luo, T.1    Downing, J.R.2    Garcia, J.V.3
  • 42
    • 0030775332 scopus 로고    scopus 로고
    • Activation of the T-cell receptor signaling pathway by Nef from an aggressive strain of simian immunodeficiency virus
    • Luo W., Peterlin B. M. Activation of the T-cell receptor signaling pathway by Nef from an aggressive strain of simian immunodeficiency virus. J. Virol. 71:1997;9531-9537.
    • (1997) J. Virol. , vol.71 , pp. 9531-9537
    • Luo, W.1    Peterlin, B.M.2
  • 43
    • 0026077650 scopus 로고
    • Expression of the type 1 human immunodeficiency virus Nef protein in T cells prevents antigen receptor-mediated induction of interleukin 2 mRNA
    • Luria S., Chambers I., Berg P. Expression of the type 1 human immunodeficiency virus Nef protein in T cells prevents antigen receptor-mediated induction of interleukin 2 mRNA. Proc. Natl. Acad. Sci. USA. 88:1991;5326-5330.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5326-5330
    • Luria, S.1    Chambers, I.2    Berg, P.3
  • 44
    • 0028587827 scopus 로고
    • A cyclin-dependent kinase homologue, p130PITSLRE is a phosphotyrosine-independent SH2 ligand
    • Malek S. N., Desiderio S. A cyclin-dependent kinase homologue, p130PITSLRE is a phosphotyrosine-independent SH2 ligand. J. Biol. Chem. 269:1994;33009-33020.
    • (1994) J. Biol. Chem , vol.269 , pp. 33009-33020
    • Malek, S.N.1    Desiderio, S.2
  • 45
    • 0031579241 scopus 로고    scopus 로고
    • DNA tumor viruses and Src family tyrosine kinases, an intimate relationship
    • Messerschmitt A. S., Dunant N., Ballmer H. K. DNA tumor viruses and Src family tyrosine kinases, an intimate relationship. Virology. 227:1997;271-280.
    • (1997) Virology , vol.227 , pp. 271-280
    • Messerschmitt, A.S.1    Dunant, N.2    Ballmer, H.K.3
  • 46
    • 0028006247 scopus 로고
    • The human immunodeficiency virus-1 nef gene product: A positive factor for viral infection and replication in primary lymphocytes and macrophages
    • Miller M. D., Warmerdam M. T., Gaston I., Greene W. C., Feinberg M. B. The human immunodeficiency virus-1 nef gene product: A positive factor for viral infection and replication in primary lymphocytes and macrophages. J. Exp. Med. 179:1994;101-113.
    • (1994) J. Exp. Med. , vol.179 , pp. 101-113
    • Miller, M.D.1    Warmerdam, M.T.2    Gaston, I.3    Greene, W.C.4    Feinberg, M.B.5
  • 48
    • 0026701228 scopus 로고
    • A limited set of SH2 domains binds BCR through a high-affinity phosphotyrosine-independent interaction
    • Muller A. J., Pendergast A. M., Havlik M. H., Puil L., Pawson T., Witte O. N. A limited set of SH2 domains binds BCR through a high-affinity phosphotyrosine-independent interaction. Mol. Cell. Biol. 12:1992;5087-5093.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 5087-5093
    • Muller, A.J.1    Pendergast, A.M.2    Havlik, M.H.3    Puil, L.4    Pawson, T.5    Witte, O.N.6
  • 49
    • 0030030293 scopus 로고    scopus 로고
    • Demonstration of a direct interaction between p561ck and the cytoplasmic domain of CD45 in vitro
    • Ng D. H., Watts J. D., Aebersold R., Johnson P. Demonstration of a direct interaction between p561ck and the cytoplasmic domain of CD45 in vitro. J. Biol. Chem. 271:1996;1295-1300.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1295-1300
    • Ng, D.H.1    Watts, J.D.2    Aebersold, R.3    Johnson, P.4
  • 50
    • 0030207577 scopus 로고    scopus 로고
    • Immunodeficiencies caused by genetic defects in protein kinases
    • Notarangelo L. D. Immunodeficiencies caused by genetic defects in protein kinases. Curr. Opin. Immunol. 8:1996;448-453.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 448-453
    • Notarangelo, L.D.1
  • 51
    • 0029793714 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef associates with a member of the p21-activated kinase family
    • Nunn M. F., Marsh J. W. Human immunodeficiency virus type 1 Nef associates with a member of the p21-activated kinase family. J. Virol. 70:1996;6157-6161.
    • (1996) J. Virol. , vol.70 , pp. 6157-6161
    • Nunn, M.F.1    Marsh, J.W.2
  • 52
    • 0026669472 scopus 로고
    • Three-dimensional solution structure of the src homology 2 domain of c-abl
    • Overduin M., Rios C. B., Mayer B. J., Baltimore D., Cowburn D. Three-dimensional solution structure of the src homology 2 domain of c-abl. Cell. 70:1992;697-704.
    • (1992) Cell , vol.70 , pp. 697-704
    • Overduin, M.1    Rios, C.B.2    Mayer, B.J.3    Baltimore, D.4    Cowburn, D.5
  • 54
    • 0029616212 scopus 로고
    • Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region
    • Park I., Chung J., Walsh C. T., Yun Y., Strominger J. L., Shin J. Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region. Proc. Natl. Acad. Sci. USA. 92:1995;12338-12342.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12338-12342
    • Park, I.1    Chung, J.2    Walsh, C.T.3    Yun, Y.4    Strominger, J.L.5    Shin, J.6
  • 55
    • 0028354446 scopus 로고
    • Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide
    • Pascal S. M., Singer A. U., Gish G., Yamazaki T., Shoelson S. E., Pawson T., Kay L. E., Forman K. J. Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide. Cell. 77:1994;461-472.
    • (1994) Cell , vol.77 , pp. 461-472
    • Pascal, S.M.1    Singer, A.U.2    Gish, G.3    Yamazaki, T.4    Shoelson, S.E.5    Pawson, T.6    Kay, L.E.7    Forman, K.J.8
  • 56
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature. 373:1995;573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 57
    • 0027336898 scopus 로고
    • Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance
    • Payne G., Shoelson S. E., Gish G. D., Pawson T., Walsh C. T. Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance. Proc. Natl. Acad. Sci. USA. 90:1993;4902-4906.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4902-4906
    • Payne, G.1    Shoelson, S.E.2    Gish, G.D.3    Pawson, T.4    Walsh, C.T.5
  • 58
    • 0025766195 scopus 로고
    • BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner
    • Pendergast A. M., Muller A. J., Havlik M. H., Maru Y., Witte O. N. BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner. Cell. 66:1991;161-171.
    • (1991) Cell , vol.66 , pp. 161-171
    • Pendergast, A.M.1    Muller, A.J.2    Havlik, M.H.3    Maru, Y.4    Witte, O.N.5
  • 59
    • 0029865609 scopus 로고    scopus 로고
    • In vivo association of v-Abl with Shc mediated by a non-phosphotyrosine-dependent SH2 interaction
    • Raffel G. D., Parmar K., Rosenberg N. In vivo association of v-Abl with Shc mediated by a non-phosphotyrosine-dependent SH2 interaction. J. Biol. Chem. 271:1996;4640-4645.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4640-4645
    • Raffel, G.D.1    Parmar, K.2    Rosenberg, N.3
  • 60
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren R., Mayer B. J., Cicchetti P., Baltimore D. Identification of a ten-amino acid proline-rich SH3 binding site. Science. 259:1993;1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 61
    • 0028181498 scopus 로고
    • Two-step TCR zeta/CD3-CD4 and CD28 signaling in T cells: SH2/SH3 domains, protein-tyrosine and lipid kinases
    • Rudd C. E., Janssen O., Cai Y. C., da S. A., Raab M., Prasad K. V. Two-step TCR zeta/CD3-CD4 and CD28 signaling in T cells: SH2/SH3 domains, protein-tyrosine and lipid kinases. Immunol. Today. 15:1994;225-234.
    • (1994) Immunol. Today , vol.15 , pp. 225-234
    • Rudd, C.E.1    Janssen, O.2    Cai, Y.C.3    Da, S.A.4    Raab, M.5    Prasad, K.V.6
  • 62
    • 0028878783 scopus 로고
    • Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4
    • Saksela K., Cheng G., Baltimore D. Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4. EMBO J. 14:1995;484-491.
    • (1995) EMBO J. , vol.14 , pp. 484-491
    • Saksela, K.1    Cheng, G.2    Baltimore, D.3
  • 63
    • 0027958148 scopus 로고
    • Human immunodeficiency virus type 1 Nef associates with a cellular serine kinase in T lymphocytes
    • Sawai E. T., Baur A., Struble H., Peterlin B. M., Levy J. A., Cheng M. C. Human immunodeficiency virus type 1 Nef associates with a cellular serine kinase in T lymphocytes. Proc. Natl. Acad. Sci. USA. 91:1994;1539-1543.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1539-1543
    • Sawai, E.T.1    Baur, A.2    Struble, H.3    Peterlin, B.M.4    Levy, J.A.5    Cheng, M.C.6
  • 65
    • 0029875421 scopus 로고    scopus 로고
    • Endocytosis of major histocompatibility complex class i molecules is induced by the hiv-1 nef protein
    • Schwartz O., Marechal V., Legall S., Lemonnier F., Heard J. M. Endocytosis of major histocompatibility complex class i molecules is induced by the hiv-1 nef protein. Nat. Med. 2:1996;338-342.
    • (1996) Nat. Med. , vol.2 , pp. 338-342
    • Schwartz, O.1    Marechal, V.2    Legall, S.3    Lemonnier, F.4    Heard, J.M.5
  • 66
    • 0027259393 scopus 로고
    • Analysis of human immunodeficiency virus type 1 nef gene sequences present in vivo [published erratum appears inJ. Virol
    • Shugars D. C., Smith M. S., Glueck D. H., Nantermet P. V., Seillier M. F., Swanstrom R. Analysis of human immunodeficiency virus type 1 nef gene sequences present in vivo [published erratum appears inJ. Virol. J. Virol. 67:1993;4639-4650.
    • (1993) J. Virol. , vol.67 , pp. 4639-4650
    • Shugars, D.C.1    Smith, M.S.2    Glueck, D.H.3    Nantermet, P.V.4    Seillier, M.F.5    Swanstrom, R.6
  • 67
    • 0027533215 scopus 로고
    • Altered T cell activation and development in transgenic mice expressing the HIV-1 nef gene
    • Skowronski J., Parks D., Mariani R. Altered T cell activation and development in transgenic mice expressing the HIV-1 nef gene. EMBO J. 12:1993;703-713.
    • (1993) EMBO J. , vol.12 , pp. 703-713
    • Skowronski, J.1    Parks, D.2    Mariani, R.3
  • 68
    • 0029953176 scopus 로고    scopus 로고
    • The HIV nef protein associates with protein kinase C theta
    • Smith B. L., Krushelnycky B. W., Mochly R. D., Berg P. The HIV nef protein associates with protein kinase C theta. J. Biol. Chem. 271:1996;16753-16757.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16753-16757
    • Smith, B.L.1    Krushelnycky, B.W.2    Mochly, R.D.3    Berg, P.4
  • 70
    • 0027952787 scopus 로고
    • The importance of nef in the induction of human immunodeficiency virus type 1 replication from primary quiescent CD4 lymphocytes
    • Spina C. A., Kwoh T. J., Chowers M. Y., Guatelli J. C., Richman D. D. The importance of nef in the induction of human immunodeficiency virus type 1 replication from primary quiescent CD4 lymphocytes. J. Exp. Med. 179:1994;115-123.
    • (1994) J. Exp. Med. , vol.179 , pp. 115-123
    • Spina, C.A.1    Kwoh, T.J.2    Chowers, M.Y.3    Guatelli, J.C.4    Richman, D.D.5
  • 71
    • 0029939787 scopus 로고    scopus 로고
    • Sh2 domain function is essential for the role of the lck tyrosine kinase in t cell receptor signal transduction
    • Straus D. B., Chan A. C., Patai B., Weiss A. Sh2 domain function is essential for the role of the lck tyrosine kinase in t cell receptor signal transduction. J. Biol. Chem. 271:1996;9976-9981.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9976-9981
    • Straus, D.B.1    Chan, A.C.2    Patai, B.3    Weiss, A.4
  • 72
    • 0030947406 scopus 로고    scopus 로고
    • The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix
    • Swingler S., Gallay P., Camaur D., Song J., Abo A., Trono D. The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix. J. Virol. 71:1997;4372-4377.
    • (1997) J. Virol. , vol.71 , pp. 4372-4377
    • Swingler, S.1    Gallay, P.2    Camaur, D.3    Song, J.4    Abo, A.5    Trono, D.6
  • 73
    • 0029150052 scopus 로고
    • HIV accessory proteins: Leading roles for the supporting case
    • Trono D. HIV accessory proteins: Leading roles for the supporting case. Cell. 82:1995;189-192.
    • (1995) Cell , vol.82 , pp. 189-192
    • Trono, D.1
  • 74
    • 0029809134 scopus 로고    scopus 로고
    • P62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
    • Vadlamudi R. K., Joung I., Strominger J. L., Shin J. p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. J. Biol. Chem. 271:1996;20235-20237.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20235-20237
    • Vadlamudi, R.K.1    Joung, I.2    Strominger, J.L.3    Shin, J.4
  • 75
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides [see comments]
    • Waksman G., Kominos D., Robertson S. C., Pant N., Baltimore D., Birge R. B., Cowburn D., Hanafusa H., Mayer B. J., Overduin M., et a. l. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides [see comments]. Nature. 358:1992;646-653.
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1    Kominos, D.2    Robertson, S.C.3    Pant, N.4    Baltimore, D.5    Birge, R.B.6    Cowburn, D.7    Hanafusa, H.8    Mayer, B.J.9    Overduin, M.10
  • 76
    • 0030273317 scopus 로고    scopus 로고
    • HIV-1 Nef association with cellular serine kinase correlates with enhanced virion infectivity and efficienty proviral DNA synthesis
    • Wiskerchen M., Cheng M. C. HIV-1 Nef association with cellular serine kinase correlates with enhanced virion infectivity and efficienty proviral DNA synthesis. Virology. 224:1996;292-301.
    • (1996) Virology , vol.224 , pp. 292-301
    • Wiskerchen, M.1    Cheng, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.