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Volumn 8, Issue 14, 2008, Pages 2911-2925

2-D DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells

Author keywords

2 D DIGE; Immunology; NK cells; Secretory lysosome

Indexed keywords

PROTEOME;

EID: 48949087726     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800170     Document Type: Article
Times cited : (27)

References (52)
  • 1
    • 0141741403 scopus 로고    scopus 로고
    • Lytic granules, secretory lysosomes and disease
    • Clark, R., Griffiths, G. M., Lytic granules, secretory lysosomes and disease. Curr. Opin. Immunol. 2003, 15, 516-521.
    • (2003) Curr. Opin. Immunol , vol.15 , pp. 516-521
    • Clark, R.1    Griffiths, G.M.2
  • 3
    • 0032974475 scopus 로고    scopus 로고
    • Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells
    • Bossi, G., Griffiths, G. M., Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells. Nat. Med. 1999, 5, 90-96.
    • (1999) Nat. Med , vol.5 , pp. 90-96
    • Bossi, G.1    Griffiths, G.M.2
  • 4
    • 33645829585 scopus 로고    scopus 로고
    • The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse
    • Lettau, M., Qian, J., Linkermann, A., Latreille, M. et al., The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse. Proc. Natl. Acad. Sci. USA 2006, 103, 5911-5916.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5911-5916
    • Lettau, M.1    Qian, J.2    Linkermann, A.3    Latreille, M.4
  • 5
    • 0036863736 scopus 로고    scopus 로고
    • The secretory synapse: The secrets of a serial killer
    • Bossi, G., Trambas, C., Booth, S., Clark, R. et al., The secretory synapse: the secrets of a serial killer. Immunol. Rev. 2002, 189, 152-160.
    • (2002) Immunol. Rev , vol.189 , pp. 152-160
    • Bossi, G.1    Trambas, C.2    Booth, S.3    Clark, R.4
  • 6
    • 0027515147 scopus 로고
    • The giant organelles in beige and Chediak-Higashi fibroblasts are derived from late endosomes and mature lysosomes
    • Burkhardt, J. K., Wiebel, F. A., Hester, S., Argon, Y., The giant organelles in beige and Chediak-Higashi fibroblasts are derived from late endosomes and mature lysosomes. J. Exp. Med. 1993, 178, 1845-1856.
    • (1993) J. Exp. Med , vol.178 , pp. 1845-1856
    • Burkhardt, J.K.1    Wiebel, F.A.2    Hester, S.3    Argon, Y.4
  • 7
    • 0035989918 scopus 로고    scopus 로고
    • Chediak-Higashi Syndrome: A rare disorder of lysosomes and lysosome related organelles
    • Shiflett, S. L., Kaplan, J., Ward, D. M., Chediak-Higashi Syndrome: a rare disorder of lysosomes and lysosome related organelles. Pigment Cell Res. 2002, 15, 251-257.
    • (2002) Pigment Cell Res , vol.15 , pp. 251-257
    • Shiflett, S.L.1    Kaplan, J.2    Ward, D.M.3
  • 8
    • 0034330540 scopus 로고    scopus 로고
    • Analysis of the lysosomal storage disease Chediak-Higashi syndrome
    • Ward, D. M., Griffiths, G. M., Stinchcombe, J. C., Kaplan, J., Analysis of the lysosomal storage disease Chediak-Higashi syndrome. Traffic 2000, 1, 816-822.
    • (2000) Traffic , vol.1 , pp. 816-822
    • Ward, D.M.1    Griffiths, G.M.2    Stinchcombe, J.C.3    Kaplan, J.4
  • 10
    • 28844438238 scopus 로고    scopus 로고
    • Binding of the intracellular Fas ligand (FasL) domain to the adaptor protein PSTPIP results in a cytoplasmic localization of FasL
    • Baum, W., Kirkin, V., Fernandez, S. B., Pick, R. et al., Binding of the intracellular Fas ligand (FasL) domain to the adaptor protein PSTPIP results in a cytoplasmic localization of FasL. J. Biol. Chem. 2005, 280, 40012-40024.
    • (2005) J. Biol. Chem , vol.280 , pp. 40012-40024
    • Baum, W.1    Kirkin, V.2    Fernandez, S.B.3    Pick, R.4
  • 11
    • 33745882375 scopus 로고    scopus 로고
    • CD28-stimulated ERK2 phosphorylation is required for polarization of the microtubule organizing center and granules in YTS NK cells
    • Chen, X., Allan, D. S., Krzewski, K., Ge, B. et al., CD28-stimulated ERK2 phosphorylation is required for polarization of the microtubule organizing center and granules in YTS NK cells. Proc. Natl. Acad. Sci. USA 2006, 103, 10346-10351.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10346-10351
    • Chen, X.1    Allan, D.S.2    Krzewski, K.3    Ge, B.4
  • 12
    • 34547541753 scopus 로고    scopus 로고
    • Many NK cell receptors activate ERK2 and JNK1 to trigger microtubule organizing center and granule polarization and cytotoxicity
    • Chen, X., Trivedi, P. P., Ge, B., Krzewski, K. et al., Many NK cell receptors activate ERK2 and JNK1 to trigger microtubule organizing center and granule polarization and cytotoxicity. Proc. Natl. Acad. Sci. USA 2007, 104, 6329-6334.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6329-6334
    • Chen, X.1    Trivedi, P.P.2    Ge, B.3    Krzewski, K.4
  • 13
    • 34249668425 scopus 로고    scopus 로고
    • Organelle proteomics: Identification of the exocytic machinery associated with the natural killer cell secretory lysosome
    • Casey, T. M., Meade, J. L., Hewitt, E. W., Organelle proteomics: identification of the exocytic machinery associated with the natural killer cell secretory lysosome. Mol. Cell Proteomics 2007, 6, 767-780.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 767-780
    • Casey, T.M.1    Meade, J.L.2    Hewitt, E.W.3
  • 14
    • 10644255766 scopus 로고    scopus 로고
    • Proteomic analysis of human natural killer cells: Insights on new potential NK immune functions
    • Hanna, J., Fitchett, J., Rowe, T., Daniels, M. et al., Proteomic analysis of human natural killer cells: insights on new potential NK immune functions. Mol. Immunol. 2005, 42, 425-431.
    • (2005) Mol. Immunol , vol.42 , pp. 425-431
    • Hanna, J.1    Fitchett, J.2    Rowe, T.3    Daniels, M.4
  • 15
    • 0025858813 scopus 로고
    • Increased proliferation, lytic activity, and purity of human natural killer cells cocultured with mitogen-activated feeder cells
    • Rabinowich, H., Sedlmayr, P., Herberman, R. B., Whiteside, T. L., Increased proliferation, lytic activity, and purity of human natural killer cells cocultured with mitogen-activated feeder cells. Cell Immunol. 1991, 135, 454-470.
    • (1991) Cell Immunol , vol.135 , pp. 454-470
    • Rabinowich, H.1    Sedlmayr, P.2    Herberman, R.B.3    Whiteside, T.L.4
  • 16
    • 0029986943 scopus 로고    scopus 로고
    • Characterization of a cell line, NKL, derived from an aggressive human natural killer cell leukemia
    • Robertson, M. J., Cochran, K. J., Cameron, C., Le, J. M. et al., Characterization of a cell line, NKL, derived from an aggressive human natural killer cell leukemia. Exp. Hematol. 1996, 24, 406-415.
    • (1996) Exp. Hematol , vol.24 , pp. 406-415
    • Robertson, M.J.1    Cochran, K.J.2    Cameron, C.3    Le, J.M.4
  • 17
    • 0021949046 scopus 로고
    • TCGF (IL 2)-receptor inducing factor(s). I. Regulation of IL 2 receptor on a natural killer-like cell line (YT cells)
    • Yodoi, J., Teshigawara, K., Nikaido, T., Fukui, K. et al., TCGF (IL 2)-receptor inducing factor(s). I. Regulation of IL 2 receptor on a natural killer-like cell line (YT cells). J. Immunol. 1985, 134, 1623-1630.
    • (1985) J. Immunol , vol.134 , pp. 1623-1630
    • Yodoi, J.1    Teshigawara, K.2    Nikaido, T.3    Fukui, K.4
  • 18
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H., High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975, 250, 4007-4021.
    • (1975) J. Biol. Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 19
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge, R., Shaw, J., Middleton, B., Rowlinson, R. et al., Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001, 1, 377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3    Rowlinson, R.4
  • 20
    • 27744559511 scopus 로고    scopus 로고
    • towards a proteomic analysis of Plasmodium falciparum
    • Fractionation and identification of proteins by 2-DE and MS
    • Gelhaus, C., Fritsch, J., Krause, E., Leippe, M., Fractionation and identification of proteins by 2-DE and MS: towards a proteomic analysis of Plasmodium falciparum. Proteomics 2005, 5, 4213-4222.
    • (2005) Proteomics , vol.5 , pp. 4213-4222
    • Gelhaus, C.1    Fritsch, J.2    Krause, E.3    Leippe, M.4
  • 21
    • 33750632498 scopus 로고    scopus 로고
    • Comparative Bioinformatics Analyses and Profiling of Lysosome-Related Organelle Proteomes
    • Hu, Z. Z., Valencia, J. C., Huang, H., Chi, A. et al., Comparative Bioinformatics Analyses and Profiling of Lysosome-Related Organelle Proteomes. Int. J. Mass Spectrom. 2007, 259, 147-160.
    • (2007) Int. J. Mass Spectrom , vol.259 , pp. 147-160
    • Hu, Z.Z.1    Valencia, J.C.2    Huang, H.3    Chi, A.4
  • 22
    • 3042786293 scopus 로고    scopus 로고
    • A gene network for navigating the literature
    • Hoffmann, R., Valencia, A., A gene network for navigating the literature. Nat. Genet. 2004, 36, 664.
    • (2004) Nat. Genet , vol.36 , pp. 664
    • Hoffmann, R.1    Valencia, A.2
  • 23
    • 0038651151 scopus 로고    scopus 로고
    • Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs
    • Bania, J., Gatti, E., Lelouard, H., David, A. et al., Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs. Proc. Natl. Acad. Sci. USA 2003, 100, 6664-6669.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6664-6669
    • Bania, J.1    Gatti, E.2    Lelouard, H.3    David, A.4
  • 24
    • 12244267707 scopus 로고    scopus 로고
    • Proteomic analysis of early melanosomes: Identification of novel melanosomal proteins
    • Basrur, V., Yang, F., Kushimoto, T., Higashimoto, Y. et al., Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J. Proteome. Res. 2003, 2, 69-79.
    • (2003) J. Proteome. Res , vol.2 , pp. 69-79
    • Basrur, V.1    Yang, F.2    Kushimoto, T.3    Higashimoto, Y.4
  • 25
    • 33750979817 scopus 로고    scopus 로고
    • Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes
    • Chi, A., Valencia, J. C., Hu, Z. Z., Watabe, H. et al., Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J. Proteome. Res. 2006, 5, 3135-3144.
    • (2006) J. Proteome. Res , vol.5 , pp. 3135-3144
    • Chi, A.1    Valencia, J.C.2    Hu, Z.Z.3    Watabe, H.4
  • 26
    • 0025672874 scopus 로고
    • Interaction of chondroitin sulfate with perforin and granzymes of cytolytic T-cells is dependent on pH
    • Masson, D., Peters, P. J., Geuze, H. J., Borst, J. et al., Interaction of chondroitin sulfate with perforin and granzymes of cytolytic T-cells is dependent on pH. Biochemistry 1990, 29, 11229-11235.
    • (1990) Biochemistry , vol.29 , pp. 11229-11235
    • Masson, D.1    Peters, P.J.2    Geuze, H.J.3    Borst, J.4
  • 27
    • 0037147261 scopus 로고    scopus 로고
    • Cytotoxic cell granule-mediated apoptosis. Characterization of the macromolecular complex of granzyme B with serglycin
    • Raja, S. M., Wang, B., Dantuluri, M., Desai, U. R. et al., Cytotoxic cell granule-mediated apoptosis. Characterization of the macromolecular complex of granzyme B with serglycin. J. Biol. Chem. 2002, 277, 49523-49530.
    • (2002) J. Biol. Chem , vol.277 , pp. 49523-49530
    • Raja, S.M.1    Wang, B.2    Dantuluri, M.3    Desai, U.R.4
  • 28
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon, A. J., Nicholson, D. W., Bleackley, R. C., Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 1995, 377, 446-448.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 29
    • 33845781550 scopus 로고    scopus 로고
    • Secretory lysosomes and their cargo in T and NK cells
    • Lettau, M., Schmidt, H., Kabelitz, D., Janssen, O., Secretory lysosomes and their cargo in T and NK cells. Immunol. Lett. 2007, 108, 10-19.
    • (2007) Immunol. Lett , vol.108 , pp. 10-19
    • Lettau, M.1    Schmidt, H.2    Kabelitz, D.3    Janssen, O.4
  • 30
    • 0038725690 scopus 로고    scopus 로고
    • The ABCs of granule-mediated cytotoxicity: New weapons in the arsenal
    • Lieberman, J., The ABCs of granule-mediated cytotoxicity: new weapons in the arsenal. Nat. Rev. Immunol. 2003, 3, 361-370.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 361-370
    • Lieberman, J.1
  • 31
    • 33847642636 scopus 로고    scopus 로고
    • Granzyme B leakage-induced apoptosis is a crucial mechanism of cell death in nasal-type NK/T-cell lymphoma
    • Ko, Y. H., Park, S., Jin, H., Woo, H. et al., Granzyme B leakage-induced apoptosis is a crucial mechanism of cell death in nasal-type NK/T-cell lymphoma. Lab Invest 2007, 87, 241-250.
    • (2007) Lab Invest , vol.87 , pp. 241-250
    • Ko, Y.H.1    Park, S.2    Jin, H.3    Woo, H.4
  • 32
    • 19544385609 scopus 로고    scopus 로고
    • Selective chemical functional probes of granzymes A and B reveal granzyme B is a major effector of natural killer cell-mediated lysis of target cells
    • Mahrus, S., Craik, C. S., Selective chemical functional probes of granzymes A and B reveal granzyme B is a major effector of natural killer cell-mediated lysis of target cells. Chem. Biol. 2005, 12, 567-577.
    • (2005) Chem. Biol , vol.12 , pp. 567-577
    • Mahrus, S.1    Craik, C.S.2
  • 33
    • 34247577498 scopus 로고    scopus 로고
    • Delivering the kiss of death: Progress on understanding how perforin works
    • Pipkin, M. E., Lieberman, J., Delivering the kiss of death: progress on understanding how perforin works. Curr. Opin. Immunol. 2007, 19, 301-308.
    • (2007) Curr. Opin. Immunol , vol.19 , pp. 301-308
    • Pipkin, M.E.1    Lieberman, J.2
  • 34
    • 85047690749 scopus 로고    scopus 로고
    • Novel APC-like properties of human NK cells directly regulate T cell activation
    • Hanna, J., Gonen-Gross, T., Fitchett, J., Rowe, T. et al., Novel APC-like properties of human NK cells directly regulate T cell activation. J. Clin. Invest 2004, 114, 1612-1623.
    • (2004) J. Clin. Invest , vol.114 , pp. 1612-1623
    • Hanna, J.1    Gonen-Gross, T.2    Fitchett, J.3    Rowe, T.4
  • 35
    • 0030687649 scopus 로고    scopus 로고
    • Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation
    • Raposo, G., Tenza, D., Mecheri, S., Peronet, R. et al., Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation. Mol. Biol. Cell 1997, 8, 2631-2645.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2631-2645
    • Raposo, G.1    Tenza, D.2    Mecheri, S.3    Peronet, R.4
  • 36
    • 0035124102 scopus 로고    scopus 로고
    • Secretory granules of mast cells accumulate mature and immature MHC class II molecules
    • Vincent-Schneider, H., Thery, C., Mazzeo, D., Tenza, D. et al., Secretory granules of mast cells accumulate mature and immature MHC class II molecules. J. Cell Sci. 2001, 114, 323-334.
    • (2001) J. Cell Sci , vol.114 , pp. 323-334
    • Vincent-Schneider, H.1    Thery, C.2    Mazzeo, D.3    Tenza, D.4
  • 37
    • 0032103322 scopus 로고    scopus 로고
    • Cathepsin S activity regulates antigen presentation and immunity
    • Riese, R. J., Mitchell, R. N., Villadangos, J. A., Shi, G. P. et al., Cathepsin S activity regulates antigen presentation and immunity. J. Clin. Invest. 1998, 101, 2351-2363.
    • (1998) J. Clin. Invest , vol.101 , pp. 2351-2363
    • Riese, R.J.1    Mitchell, R.N.2    Villadangos, J.A.3    Shi, G.P.4
  • 38
    • 0033083688 scopus 로고    scopus 로고
    • Cathepsin S required for normal MHC class II peptide loading and germinal center development
    • Shi, G. P., Villadangos, J. A., Dranoff, G., Small, C. et al., Cathepsin S required for normal MHC class II peptide loading and germinal center development. Immunity 1999, 10, 197-206.
    • (1999) Immunity , vol.10 , pp. 197-206
    • Shi, G.P.1    Villadangos, J.A.2    Dranoff, G.3    Small, C.4
  • 39
    • 0032940071 scopus 로고    scopus 로고
    • ERM proteins in cell adhesion and membrane dynamics
    • Mangeat, P., Roy, C., Martin, M., ERM proteins in cell adhesion and membrane dynamics. Trends Cell Biol. 1999, 9, 187-192.
    • (1999) Trends Cell Biol , vol.9 , pp. 187-192
    • Mangeat, P.1    Roy, C.2    Martin, M.3
  • 40
    • 0033521010 scopus 로고    scopus 로고
    • lessons from ERM (ezrin/radixin/moesin) proteins
    • Cortical actin organization
    • Tsukita, S., Yonemura, S., Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J. Biol. Chem. 1999, 274, 34507-34510.
    • (1999) J. Biol. Chem , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 41
    • 0034524664 scopus 로고    scopus 로고
    • Bretscher, A., Chambers, D., Nguyen, R., Reczek, D., ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu. Rev. Cell Dev. Biol. 2000, 16, 113-143.
    • Bretscher, A., Chambers, D., Nguyen, R., Reczek, D., ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu. Rev. Cell Dev. Biol. 2000, 16, 113-143.
  • 42
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
    • Delon, J., Kaibuchi, K., Germain, R. N., Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Immunity 2001, 15, 691-701.
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.N.3
  • 43
    • 1542377326 scopus 로고    scopus 로고
    • ERM proteins regulate cytoskeleton relaxation promoting T cell-APC conjugation
    • Faure, S., Salazar-Fontana, L. I., Semichon, M., Tybulewicz, V. L. et al., ERM proteins regulate cytoskeleton relaxation promoting T cell-APC conjugation. Nat. Immunol. 2004, 5, 272-279.
    • (2004) Nat. Immunol , vol.5 , pp. 272-279
    • Faure, S.1    Salazar-Fontana, L.I.2    Semichon, M.3    Tybulewicz, V.L.4
  • 44
    • 0035951076 scopus 로고    scopus 로고
    • The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites
    • Cooley, J., Takayama, T. K., Shapiro, S. D., Schechter, N. M. et al., The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites. Biochemistry 2001, 40, 15762-15770.
    • (2001) Biochemistry , vol.40 , pp. 15762-15770
    • Cooley, J.1    Takayama, T.K.2    Shapiro, S.D.3    Schechter, N.M.4
  • 45
    • 0842326035 scopus 로고    scopus 로고
    • auto-regulation of target cell attack by cathepsin G
    • Monoclonal LYM-1 antibody-dependent cytolysis by human neutrophils exposed to GM-CSF
    • Ottonello, L., Epstein, A. L., Mancini, M., Dapino, P. et al., Monoclonal LYM-1 antibody-dependent cytolysis by human neutrophils exposed to GM-CSF: auto-regulation of target cell attack by cathepsin G. J. Leukoc. Biol. 2004, 75, 99-105.
    • (2004) J. Leukoc. Biol , vol.75 , pp. 99-105
    • Ottonello, L.1    Epstein, A.L.2    Mancini, M.3    Dapino, P.4
  • 46
    • 0031056611 scopus 로고    scopus 로고
    • Cathepsin G binds to human lymphocytes
    • Yamazaki, T., Aoki, Y., Cathepsin G binds to human lymphocytes. J. Leukoc. Biol. 1997, 61, 73-79.
    • (1997) J. Leukoc. Biol , vol.61 , pp. 73-79
    • Yamazaki, T.1    Aoki, Y.2
  • 47
    • 0031915757 scopus 로고    scopus 로고
    • Cathepsin G enhances human natural killer cytotoxicity
    • Yamazaki, T., Aoki, Y., Cathepsin G enhances human natural killer cytotoxicity. Immunology 1998, 93, 115-121.
    • (1998) Immunology , vol.93 , pp. 115-121
    • Yamazaki, T.1    Aoki, Y.2
  • 48
    • 33645075197 scopus 로고    scopus 로고
    • Serpins prevent granzyme-induced death in a species-specific manner
    • Bots, M., VAN, B. L., Rademaker, M. T., Offringa, R. et al., Serpins prevent granzyme-induced death in a species-specific manner. Immunol. Cell Biol. 2006, 84, 79-86.
    • (2006) Immunol. Cell Biol , vol.84 , pp. 79-86
    • Bots, M.1    VAN, B.L.2    Rademaker, M.T.3    Offringa, R.4
  • 49
    • 0029914132 scopus 로고    scopus 로고
    • A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes
    • Sun, J., Bird, C. H., Sutton, V., McDonald, L. et al., A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes. J. Biol. Chem. 1996, 271, 27802-27809.
    • (1996) J. Biol. Chem , vol.271 , pp. 27802-27809
    • Sun, J.1    Bird, C.H.2    Sutton, V.3    McDonald, L.4
  • 50
    • 0034932940 scopus 로고    scopus 로고
    • Nucleocytoplasmic distribution of the ovalbumin serpin PI-9 requires a nonconventional nuclear import pathway and the export factor Crm1
    • Bird, C. H., Blink, E. J., Hirst, C. E., Buzza, M. S. et al., Nucleocytoplasmic distribution of the ovalbumin serpin PI-9 requires a nonconventional nuclear import pathway and the export factor Crm1. Mol. Cell Biol. 2001, 21, 5396-5407.
    • (2001) Mol. Cell Biol , vol.21 , pp. 5396-5407
    • Bird, C.H.1    Blink, E.J.2    Hirst, C.E.3    Buzza, M.S.4
  • 51
    • 0031792776 scopus 로고    scopus 로고
    • Selective regulation of apoptosis: The cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway
    • Bird, C. H., Sutton, V. R., Sun, J., Hirst, C. E. et al., Selective regulation of apoptosis: the cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway. Mol. Cell Biol. 1998, 18, 6387-6398.
    • (1998) Mol. Cell Biol , vol.18 , pp. 6387-6398
    • Bird, C.H.1    Sutton, V.R.2    Sun, J.3    Hirst, C.E.4
  • 52
    • 0037438474 scopus 로고    scopus 로고
    • The intracellular granzyme B inhibitor, proteinase inhibitor 9, is up-regulated during accessory cell maturation and effector cell degranulation, and its overexpression enhances CTL potency
    • Hirst, C. E., Buzza, M. S., Bird, C. H., Warren, H. S. et al., The intracellular granzyme B inhibitor, proteinase inhibitor 9, is up-regulated during accessory cell maturation and effector cell degranulation, and its overexpression enhances CTL potency. J. Immunol. 2003, 170, 805-815.
    • (2003) J. Immunol , vol.170 , pp. 805-815
    • Hirst, C.E.1    Buzza, M.S.2    Bird, C.H.3    Warren, H.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.