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Volumn 22, Issue 3, 2000, Pages 152-160

Good or evil: CD26 and HIV infection

Author keywords

CD26 dipeptidyl peptidase IV; Chemokines; HIV infection

Indexed keywords

ADENOSINE DEAMINASE; CHEMOKINE; DIPEPTIDYL PEPTIDASE IV; GLYCOPROTEIN; RANTES;

EID: 0033956421     PISSN: 09231811     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0923-1811(99)00081-X     Document Type: Article
Times cited : (33)

References (62)
  • 1
    • 0025197963 scopus 로고
    • Accessory cell signals involved in T cell activation
    • Geppert T.D., Davis L.S. et al. Accessory cell signals involved in T cell activation. Immunol. Rev. 117:1990;5-66.
    • (1990) Immunol. Rev. , vol.117 , pp. 5-66
    • Geppert, T.D.1    Davis, L.S.2
  • 2
    • 0025325450 scopus 로고
    • Comitogenic effect of solid-phase immobilized anti-1F7 on human CD4 T cell activation via CD3 and CD2 pathways
    • Dang NH, Torimoto Y et al. Comitogenic effect of solid-phase immobilized anti-1F7 on human CD4 T cell activation via CD3 and CD2 pathways. J Immunol 1990:144: 4092-4100.
    • (1990) J Immunol , vol.144 , pp. 4092-4100
    • Dang, N.H.1    Torimoto, Y.2
  • 3
    • 0024331402 scopus 로고
    • 1F7, a novel cell surface molecule involved in helper function of CD4 cells
    • Morimoto C., Torimoto Y. et al. 1F7, a novel cell surface molecule involved in helper function of CD4 cells. J. Immunol. 143:1989;3430-3439.
    • (1989) J. Immunol. , vol.143 , pp. 3430-3439
    • Morimoto, C.1    Torimoto, Y.2
  • 4
    • 0026601838 scopus 로고
    • Biochemical characterization of CD26 (dipeptidyl peptidase IV): Functional comparison of distinct epitopes recognized by various anti-CD26 monoclonal antibodies
    • Torimoto Y., Dang N.H. et al. Biochemical characterization of CD26 (dipeptidyl peptidase IV): functional comparison of distinct epitopes recognized by various anti-CD26 monoclonal antibodies. Mol. Immunol. 29:1992;183-192.
    • (1992) Mol. Immunol. , vol.29 , pp. 183-192
    • Torimoto, Y.1    Dang, N.H.2
  • 5
    • 0025318818 scopus 로고
    • The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity
    • Hegen M., Niedobitek G. et al. The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity. J. Immunol. 144:1990;2908-2914.
    • (1990) J. Immunol. , vol.144 , pp. 2908-2914
    • Hegen, M.1    Niedobitek, G.2
  • 6
    • 0027270023 scopus 로고
    • The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity
    • Tanaka T., Kameoka J. et al. The costimulatory activity of the CD26 antigen requires dipeptidyl peptidase IV enzymatic activity. Proc. Natl. Acad. Sci. USA. 90:1993;4586-4590.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4586-4590
    • Tanaka, T.1    Kameoka, J.2
  • 7
    • 0026633296 scopus 로고
    • Cloning and functional expression of the T cell activation antigen CD26
    • Tanaka T., Camerini D. et al. Cloning and functional expression of the T cell activation antigen CD26. J. Immunol. 149:1992;481-486.
    • (1992) J. Immunol. , vol.149 , pp. 481-486
    • Tanaka, T.1    Camerini, D.2
  • 8
    • 0025992545 scopus 로고
    • Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes
    • Torimoto Y., Dang N.H. et al. Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes. J. Immunol. 147:1991;2514-2517.
    • (1991) J. Immunol. , vol.147 , pp. 2514-2517
    • Torimoto, Y.1    Dang, N.H.2
  • 9
    • 0027201145 scopus 로고
    • Direct association of adenosine deaminase with a T cell activation antigen, CD26
    • Kameoka J., Tanaka T. et al. Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science. 261:1993;466-469.
    • (1993) Science , vol.261 , pp. 466-469
    • Kameoka, J.1    Tanaka, T.2
  • 10
    • 0027401263 scopus 로고
    • A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase
    • Morrison M.E., Vijayasaradhi S. et al. A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase. J. Exp. Med. 177:1993;1135-1143.
    • (1993) J. Exp. Med. , vol.177 , pp. 1135-1143
    • Morrison, M.E.1    Vijayasaradhi, S.2
  • 11
    • 0030045246 scopus 로고    scopus 로고
    • Characterization of adenosine deaminase binding to human CD26 on T cells and its biologic role in immune response
    • Dong R.-P., Kameoka J. et al. Characterization of adenosine deaminase binding to human CD26 on T cells and its biologic role in immune response. J. Immunol. 156:1996;1349-1355.
    • (1996) J. Immunol. , vol.156 , pp. 1349-1355
    • Dong, R.-P.1    Kameoka, J.2
  • 12
    • 0026640693 scopus 로고
    • Selective decrease of CD26 expression in T cells from HIV-1-infected individuals
    • Valle-Blazquez M., Madueño J.A. et al. Selective decrease of CD26 expression in T cells from HIV-1-infected individuals. J. Immunol. 149:1992;3073-3077.
    • (1992) J. Immunol. , vol.149 , pp. 3073-3077
    • Valle-Blazquez, M.1    Madueño, J.A.2
  • 13
    • 0025160079 scopus 로고
    • Preferential infection of CD4+ memory T cells by human immunodeficiency virus type 1: Evidence for a role in the selective T-cell functional defects observed in infected individuals
    • Schenittman S.M., Lane H.C. et al. Preferential infection of CD4+ memory T cells by human immunodeficiency virus type 1: evidence for a role in the selective T-cell functional defects observed in infected individuals. Proc. Natl. Acad. Sci. USA. 87:1990;6058-6062.
    • (1990) Proc. Natl. Acad. Sci. USA. , vol.87 , pp. 6058-6062
    • Schenittman, S.M.1    Lane, H.C.2
  • 14
    • 0027937806 scopus 로고
    • Role of CD26/dipeptidyl peptidase IV in human immunodeficiency virus type 1 infection and apotosis
    • Morimoto C., Lord C.I. et al. Role of CD26/dipeptidyl peptidase IV in human immunodeficiency virus type 1 infection and apotosis. Proc. Natl. Acad. Sci. USA. 91:1994;9960-9964.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9960-9964
    • Morimoto, C.1    Lord, C.I.2
  • 15
    • 0027294596 scopus 로고
    • + T lymphocytes of HIV-infected subjects
    • + T lymphocytes of HIV-infected subjects. J. AIDS. 6:1993;749-757.
    • (1993) J. AIDS , vol.6 , pp. 749-757
    • Vanham, G.1    Kestens, I.2
  • 17
    • 0032526993 scopus 로고    scopus 로고
    • + T cells expressing relatively high levels of CD26
    • + T cells expressing relatively high levels of CD26. Exp. Cell Res. 241:1998;352-362.
    • (1998) Exp. Cell Res. , vol.241 , pp. 352-362
    • Callebaut, C.1    Jacotot, E.2
  • 18
    • 0029029058 scopus 로고
    • Sensitization of T cells to CD95-mediated apoptosis by HIV-1 Tat and gp120
    • Westendorp M.O., Frank R. et al. Sensitization of T cells to CD95-mediated apoptosis by HIV-1 Tat and gp120. Nature. 375:1995;497-500.
    • (1995) Nature , vol.375 , pp. 497-500
    • Westendorp, M.O.1    Frank, R.2
  • 19
    • 0031783562 scopus 로고    scopus 로고
    • Chemokine receptors and their crucial role in human immunodeficiency virus infection: Major breakthroughs in HIV research
    • Kristiansen T.B., Knudsen T.B. et al. Chemokine receptors and their crucial role in human immunodeficiency virus infection: major breakthroughs in HIV research. Scand. J. Immunol. 48:1998;339-346.
    • (1998) Scand. J. Immunol. , vol.48 , pp. 339-346
    • Kristiansen, T.B.1    Knudsen, T.B.2
  • 20
    • 0031595931 scopus 로고    scopus 로고
    • Naive and memory CD4 T cells differ in their susceptibilities to human immunodeficiency virus type 1 infection following CD28 costimulation: Implications for transmission and pathogenesis
    • Riley J.L., Levine B.L. et al. Naive and memory CD4 T cells differ in their susceptibilities to human immunodeficiency virus type 1 infection following CD28 costimulation: implications for transmission and pathogenesis. J. Virol. 72:1998;8273-8280.
    • (1998) J. Virol. , vol.72 , pp. 8273-8280
    • Riley, J.L.1    Levine, B.L.2
  • 21
    • 0031056631 scopus 로고    scopus 로고
    • Expression pattern of HIV-1 coreceptors on T cells: Implications for viral transmission and lymphocyte homing
    • Unutmaz D., Littman D.R. Expression pattern of HIV-1 coreceptors on T cells: implications for viral transmission and lymphocyte homing. Proc. Natl. Acad. Sci. USA. 94:1997;1615-1618.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1615-1618
    • Unutmaz, D.1    Littman, D.R.2
  • 23
    • 0031852699 scopus 로고    scopus 로고
    • Survival with HIV infection: Good luck or good breeding?
    • Rowland-Jones S.L. Survival with HIV infection: good luck or good breeding? Trends Genet. 14:1998;343-345.
    • (1998) Trends Genet. , vol.14 , pp. 343-345
    • Rowland-Jones, S.L.1
  • 24
    • 0030968495 scopus 로고    scopus 로고
    • Preferential replication of HIV-1 in the CD45RO memory cell subset of primary CD4 lymphocytes in vitro
    • Spina C.A., Prince H.E. et al. Preferential replication of HIV-1 in the CD45RO memory cell subset of primary CD4 lymphocytes in vitro. J. Clin. Invest. 99:1997;1774-1785.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1774-1785
    • Spina, C.A.1    Prince, H.E.2
  • 25
    • 0342601383 scopus 로고    scopus 로고
    • CD95-induced apoptosis contributes to loss of primed/memory but not resting/naive T cells in children infected with human immunodeficiency virus type 1
    • Böhler T., Nedel S. et al. CD95-induced apoptosis contributes to loss of primed/memory but not resting/naive T cells in children infected with human immunodeficiency virus type 1. Pediatr. Res. 41:1997;878-885.
    • (1997) Pediatr. Res. , vol.41 , pp. 878-885
    • Böhler, T.1    Nedel, S.2
  • 26
    • 0028223435 scopus 로고
    • Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): A possible mechanism for Tat's immunosuppressive activity
    • Gutheil W.G., Subramanyam M. et al. Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): a possible mechanism for Tat's immunosuppressive activity. Proc. Natl. Acad. Sci. USA. 91:1994;6594-6598.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6594-6598
    • Gutheil, W.G.1    Subramanyam, M.2
  • 27
    • 0029940265 scopus 로고    scopus 로고
    • Specific binding of adenosine deaminase but not HIV-1 transactivator protein Tat to human CD26
    • Blanco J., Marié I. et al. Specific binding of adenosine deaminase but not HIV-1 transactivator protein Tat to human CD26. Exp. Cell Res. 225:1996;102-111.
    • (1996) Exp. Cell Res. , vol.225 , pp. 102-111
    • Blanco, J.1    Marié, I.2
  • 28
    • 0032503930 scopus 로고    scopus 로고
    • The significance of hypersialylation of dipeptidyl peptidase IV (CD26) in the inhibition of its activity by Tat and other cationic peptides
    • Smith R.E., Talhouk J.W. et al. The significance of hypersialylation of dipeptidyl peptidase IV (CD26) in the inhibition of its activity by Tat and other cationic peptides. AIDS Res. Hum. Retrovir. 14:1998;851-868.
    • (1998) AIDS Res. Hum. Retrovir. , vol.14 , pp. 851-868
    • Smith, R.E.1    Talhouk, J.W.2
  • 29
    • 0031569543 scopus 로고    scopus 로고
    • Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles
    • Valenzuela A., Blanco J. et al. Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles. J. Immunol. 158:1997;3721-3729.
    • (1997) J. Immunol. , vol.158 , pp. 3721-3729
    • Valenzuela, A.1    Blanco, J.2
  • 30
    • 0031908810 scopus 로고    scopus 로고
    • Enzymatic and extraenzymatic role of ecto-denosine deaminase in lymphocytes
    • Franco R., Valenzuela A. et al. Enzymatic and extraenzymatic role of ecto-denosine deaminase in lymphocytes. Immunol. Rev. 161:1998;27-42.
    • (1998) Immunol. Rev. , vol.161 , pp. 27-42
    • Franco, R.1    Valenzuela, A.2
  • 31
    • 0030611937 scopus 로고    scopus 로고
    • Gp120s Derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules
    • Feito M.J., Bragardo M. et al. gp120s Derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules. Int. Immunol. 9:1997;1141-1147.
    • (1997) Int. Immunol. , vol.9 , pp. 1141-1147
    • Feito, M.J.1    Bragardo, M.2
  • 32
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish A.G., Beverly P.C.L. et al. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature. 312:1984;763-767.
    • (1984) Nature , vol.312 , pp. 763-767
    • Dalgleish, A.G.1    Beverly, P.C.L.2
  • 33
    • 0021720872 scopus 로고
    • T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV
    • Klatzmann D., Champagne E. et al. T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV. Nature. 312:1984;767-768.
    • (1984) Nature , vol.312 , pp. 767-768
    • Klatzmann, D.1    Champagne, E.2
  • 35
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G-protein-coupled receptor
    • Feng Y., Broder C.C. et al. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G-protein-coupled receptor. Science. 272:1996;872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2
  • 36
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: A RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib G., Combadiere C. et al. CC CKR5: A RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1. Science. 272:1996;1955-1958.
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2
  • 37
    • 15844419153 scopus 로고    scopus 로고
    • Identification of a major co-receptor for primary isolates of HIV-1
    • Deng H., Liu R. et al. Identification of a major co-receptor for primary isolates of HIV-1. Nature. 381:1996;661-666.
    • (1996) Nature , vol.381 , pp. 661-666
    • Deng, H.1    Liu, R.2
  • 38
    • 15844389650 scopus 로고    scopus 로고
    • HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5
    • Dragic T., Litwin V. et al. HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5. Nature. 381:1996;667-673.
    • (1996) Nature , vol.381 , pp. 667-673
    • Dragic, T.1    Litwin, V.2
  • 39
    • 0005014748 scopus 로고    scopus 로고
    • The α-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates
    • Choe H., Farzan M. et al. The α-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates. Cell. 85:1996;1135-1148.
    • (1996) Cell , vol.85 , pp. 1135-1148
    • Choe, H.1    Farzan, M.2
  • 40
    • 0029775576 scopus 로고    scopus 로고
    • The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry
    • Bleul C.C., Farzan M. et al. The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry. Nature. 382:1996;829-833.
    • (1996) Nature , vol.382 , pp. 829-833
    • Bleul, C.C.1    Farzan, M.2
  • 41
    • 16044370087 scopus 로고    scopus 로고
    • The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1
    • Oberlin E., Amara A. et al. The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1. Nature. 382:1996;833-835.
    • (1996) Nature , vol.382 , pp. 833-835
    • Oberlin, E.1    Amara, A.2
  • 42
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors
    • Doranz B.J., Rucker J. et al. A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors. Cell. 85:1996;1149-1158.
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2
  • 43
    • 0031008794 scopus 로고    scopus 로고
    • STRL33, a novel chemokine receptor-like protein, functions as a fusion cofactor for both macrophage-tropic and T cell line-tropic HIV-1
    • Liao F., Alkhatib G. et al. STRL33, a novel chemokine receptor-like protein, functions as a fusion cofactor for both macrophage-tropic and T cell line-tropic HIV-1. J. Exp. Med. 185:1997;2015-2023.
    • (1997) J. Exp. Med. , vol.185 , pp. 2015-2023
    • Liao, F.1    Alkhatib, G.2
  • 44
    • 0030825407 scopus 로고    scopus 로고
    • Chemokines
    • Rollins B.J. Chemokines. Blood. 90:1997;909-928.
    • (1997) Blood , vol.90 , pp. 909-928
    • Rollins, B.J.1
  • 45
    • 0032509889 scopus 로고    scopus 로고
    • Chemokines - chemotactic cytokines that mediate inflammation
    • Luster A.D. Chemokines - chemotactic cytokines that mediate inflammation. New Engl. J. Med. 338:1998;436-445.
    • (1998) New Engl. J. Med. , vol.338 , pp. 436-445
    • Luster, A.D.1
  • 46
    • 0032127167 scopus 로고    scopus 로고
    • Chemokines and T lymphocytes: More than an attraction
    • Ward S.G., Bacon K. et al. Chemokines and T lymphocytes: more than an attraction. Immunity. 9:1998;1-11.
    • (1998) Immunity , vol.9 , pp. 1-11
    • Ward, S.G.1    Bacon, K.2
  • 47
    • 0032143524 scopus 로고    scopus 로고
    • Chemokines: Understanding their role in T-lymphocyte biology
    • Ward S.G., Westwick J. Chemokines: understanding their role in T-lymphocyte biology. Biochem. J. 333:1998;457-470.
    • (1998) Biochem. J. , vol.333 , pp. 457-470
    • Ward, S.G.1    Westwick, J.2
  • 49
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz T., Pall M. et al. Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J. Exp. Med. 186:1997;1865-1872.
    • (1997) J. Exp. Med. , vol.186 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2
  • 50
    • 0032571360 scopus 로고    scopus 로고
    • Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV - conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection
    • Proost P., Meester I.D. et al. Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV - conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection. J. Biol. Chem. 273:1998;7222-7227.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7222-7227
    • Proost, P.1    Meester, I.D.2
  • 51
    • 0032992914 scopus 로고    scopus 로고
    • CD26/DPPIV differentially regulates the chemotaxis of T cells and monocytes toward RANTES - Possible mechanism for the switch from innate to acquired immune response
    • Iwata S, Yamaguchi N, et al. 1999. CD26/DPPIV differentially regulates the chemotaxis of T cells and monocytes toward RANTES - possible mechanism for the switch from innate to acquired immune response. Int Immunol 1999;11:417-426.
    • (1999) Int Immunol 1999 , vol.11 , pp. 417-426
    • Iwata, S.1    Yamaguchi, N.2
  • 52
    • 0031981959 scopus 로고    scopus 로고
    • Natural truncation of RANTES abolishes signaling through the CC chemokine receptors CCR1 and CCR3, impairs its chemotactic potency and generates a CC chemokine inhibitor
    • Struyf S., Meester I.D. et al. Natural truncation of RANTES abolishes signaling through the CC chemokine receptors CCR1 and CCR3, impairs its chemotactic potency and generates a CC chemokine inhibitor. Eur. J. Immunol. 28:1998;1262-1271.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 1262-1271
    • Struyf, S.1    Meester, I.D.2
  • 53
    • 0032479921 scopus 로고    scopus 로고
    • HIV-specific T cell cytotoxicity mediated by RANTES via the chemokine receptor CCR3
    • Hadida F., Vieillard V. et al. HIV-specific T cell cytotoxicity mediated by RANTES via the chemokine receptor CCR3. J. Exp. Med. 188:1998;609-614.
    • (1998) J. Exp. Med. , vol.188 , pp. 609-614
    • Hadida, F.1    Vieillard, V.2
  • 54
    • 0029099521 scopus 로고
    • Structure and chromosomal localization of the human stromal cell-derived factor 1 (SDF1) gene
    • Shirozu M., Nakao T. et al. Structure and chromosomal localization of the human stromal cell-derived factor 1 (SDF1) gene. Genomics. 28:1995;495-500.
    • (1995) Genomics , vol.28 , pp. 495-500
    • Shirozu, M.1    Nakao, T.2
  • 55
    • 13144283654 scopus 로고    scopus 로고
    • Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1α (SDF-1α) and SDF-1β are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage
    • Shioda T., Kato H. et al. Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1α (SDF-1α) and SDF-1β are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage. Proc. Natl. Acad. Sci. USA. 95:1998;6331-6336.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6331-6336
    • Shioda, T.1    Kato, H.2
  • 56
    • 0032541040 scopus 로고    scopus 로고
    • Negative regulation of the anti-human immunodeficiency virus and chemotactic activity of human stromal cell-derived factor 1α by CD26/dipeptidyl peptidase IV
    • Ohtsuki T., Hosono O. et al. Negative regulation of the anti-human immunodeficiency virus and chemotactic activity of human stromal cell-derived factor 1α by CD26/dipeptidyl peptidase IV. FEBS Lett. 431:1998;236-240.
    • (1998) FEBS Lett. , vol.431 , pp. 236-240
    • Ohtsuki, T.1    Hosono, O.2
  • 57
    • 0032584761 scopus 로고    scopus 로고
    • Processing by CD26/dipeptidyl-peptidase IV reduces the chemotactic and anti-HIV-1 activity of stromal-cell-derived factor-1α
    • Proost P., Struyf S. et al. Processing by CD26/dipeptidyl-peptidase IV reduces the chemotactic and anti-HIV-1 activity of stromal-cell-derived factor-1α FEBS Lett. 432:1998;73-76.
    • (1998) FEBS Lett. , vol.432 , pp. 73-76
    • Proost, P.1    Struyf, S.2
  • 58
    • 0030683638 scopus 로고    scopus 로고
    • Solution structure and basis for functional activity of stromal cell-derived factor-1; Dissociation of CXCR4 activation from binding and inhibition of HIV-1
    • Crump M.P., Gong J.-H. et al. Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1. EMBO J. 16:1997;6996-7007.
    • (1997) EMBO J. , vol.16 , pp. 6996-7007
    • Crump, M.P.1    Gong, J.-H.2
  • 59
    • 0032530062 scopus 로고    scopus 로고
    • Enhanced anti-HIV activity and altered chemotactic potency of NH2-terminally processed macrophage-derived chemokine (MDC) imply an additional MDC receptor
    • Struyf S., Proost P. et al. Enhanced anti-HIV activity and altered chemotactic potency of NH2-terminally processed macrophage-derived chemokine (MDC) imply an additional MDC receptor. J. Immunol. 161:1998;2672-2675.
    • (1998) J. Immunol. , vol.161 , pp. 2672-2675
    • Struyf, S.1    Proost, P.2
  • 60
    • 0030722896 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infection by the β-chemokine MDC
    • Pal R., Garzino-Demo A. et al. Inhibition of HIV-1 infection by the β-chemokine MDC. Science. 278:1997;695-698.
    • (1997) Science , vol.278 , pp. 695-698
    • Pal, R.1    Garzino-Demo, A.2
  • 61
    • 0000322967 scopus 로고    scopus 로고
    • Chemokine MDC and HIV-1 infection
    • Lee B., Rucker J. et al. chemokine MDC and HIV-1 infection. Science. 281:1998;487a.
    • (1998) Science , vol.281
    • Lee, B.1    Rucker, J.2
  • 62
    • 0032530316 scopus 로고    scopus 로고
    • CD8 positive T cells influence antigen-specific immune responses through the expression of chemokines
    • Kim J.J., Nottingham L.K. et al. CD8 positive T cells influence antigen-specific immune responses through the expression of chemokines. J. Clin. Invest. 102:1998;1112-1124.
    • (1998) J. Clin. Invest. , vol.102 , pp. 1112-1124
    • Kim, J.J.1    Nottingham, L.K.2


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