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Volumn 4, Issue 5, 2003, Pages 399-403

Delivering the kiss of death

Author keywords

[No Author keywords available]

Indexed keywords

PERFORIN; RAB PROTEIN;

EID: 0038731186     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/ni0503-399     Document Type: Review
Times cited : (166)

References (85)
  • 1
    • 0021273768 scopus 로고
    • Purification and properties of cycoplasmic granules from cytotoxic rat LGL tumors
    • Millard, P.J., Henkart, M.P., Reynolds, C.W. & Henkart, P.A. Purification and properties of cycoplasmic granules from cytotoxic rat LGL tumors. J. Immunol. 132, 3197-3204 (1984).
    • (1984) J. Immunol. , vol.132 , pp. 3197-3204
    • Millard, P.J.1    Henkart, M.P.2    Reynolds, C.W.3    Henkart, P.A.4
  • 2
    • 0001041396 scopus 로고
    • Isolation and biochemical and functional characterization of perforin from cytolytic T cell granules
    • Podack, E.R., Young, J.D. & Cohn, Z.A. Isolation and biochemical and functional characterization of perforin from cytolytic T cell granules. Proc. Natl. Acad. Sci. USA 82, 8629-8633 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8629-8633
    • Podack, E.R.1    Young, J.D.2    Cohn, Z.A.3
  • 3
    • 0023693490 scopus 로고    scopus 로고
    • Homology of perforin to the ninth component of complement (C9)
    • Shinkai, Y., Takio, K. & Okumura, K. Homology of perforin to the ninth component of complement (C9). Nature 334, 525-527 (1998).
    • (1998) Nature , vol.334 , pp. 525-527
    • Shinkai, Y.1    Takio, K.2    Okumura, K.3
  • 4
    • 0022466507 scopus 로고
    • Structural-functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis
    • Tschopp, J., Massom, D. & Stanley, K.K. Structural-functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis. Nature 322, 831-834 (1986).
    • (1986) Nature , vol.322 , pp. 831-834
    • Tschopp, J.1    Massom, D.2    Stanley, K.K.3
  • 5
    • 0026060951 scopus 로고
    • Functional size of complement and perforin pores compared by confocal laser scanning microscopy and fluorescent microphotolysis
    • 1063
    • Sauer, H., Pratsch, L., Tschopp, J., Bhakdi, S. & Peters, R. Functional size of complement and perforin pores compared by confocal laser scanning microscopy and fluorescent microphotolysis. Biochim. Biophys. Acta 1063, 137-146 (1991).
    • (1991) Biochim. Biophys. Acta , pp. 137-146
    • Sauer, H.1    Pratsch, L.2    Tschopp, J.3    Bhakdi, S.4    Peters, R.5
  • 6
    • 0020020694 scopus 로고
    • Lymphocyte mediated cytolysis as a secretory phenomenon
    • Henkart, M.P. & Henkart, P.A. Lymphocyte mediated cytolysis as a secretory phenomenon. Adv. Exp. Med. Biol. 146, 227-247 (1982).
    • (1982) Adv. Exp. Med. Biol. , vol.146 , pp. 227-247
    • Henkart, M.P.1    Henkart, P.A.2
  • 7
    • 0028947976 scopus 로고
    • Perforin and granzymes: Crucial effector molecules in cytolytic T lymphocyte and natural killer cell-mediated cytotoxicity
    • Lowin, B., Peitsch, M.C. & Tschopp, J. Perforin and granzymes: crucial effector molecules in cytolytic T lymphocyte and natural killer cell-mediated cytotoxicity. Curr. Top. Microbiol. Immunol. 198, 1-24 (1995).
    • (1995) Curr. Top. Microbiol. Immunol. , vol.198 , pp. 1-24
    • Lowin, B.1    Peitsch, M.C.2    Tschopp, J.3
  • 8
    • 0026532606 scopus 로고
    • A natural killer cell granule protein that induces DNA fragmentation and apoptosis
    • Shi, L., Kraut, R.P., Aebersold, R. & Greenberg, A.H. A natural killer cell granule protein that induces DNA fragmentation and apoptosis. J. Exp. Med. 175, 553-566 (1992).
    • (1992) J. Exp. Med. , vol.175 , pp. 553-566
    • Shi, L.1    Kraut, R.P.2    Aebersold, R.3    Greenberg, A.H.4
  • 9
    • 0028258577 scopus 로고
    • Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells
    • Heusel, J.W., Wesselschmidt, R.L., Shresta, S., Russell, J.H. & Ley T.J. Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells. Cell 76, 977-987 (1994).
    • (1994) Cell , vol.76 , pp. 977-987
    • Heusel, J.W.1    Wesselschmidt, R.L.2    Shresta, S.3    Russell, J.H.4    Ley, T.J.5
  • 10
    • 0028967988 scopus 로고
    • Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumours also expressing cytolysin/perforin
    • Nakajima, H., Park, H.L. & Henkart, P.A. Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumours also expressing cytolysin/perforin. J. Exp. Med. 181, 1037-1046 (1995).
    • (1995) J. Exp. Med. , vol.181 , pp. 1037-1046
    • Nakajima, H.1    Park, H.L.2    Henkart, P.A.3
  • 11
    • 0025973806 scopus 로고
    • A noncytotoxic mast cell tumor line exhibits potent IgE-dependent cytotoxicity after transfection with the cytolysin/perforin gene
    • Shiver, J.W. & Henkart, P.A. A noncytotoxic mast cell tumor line exhibits potent IgE-dependent cytotoxicity after transfection with the cytolysin/perforin gene. Cell 64, 1175-1181 (1991).
    • (1991) Cell , vol.64 , pp. 1175-1181
    • Shiver, J.W.1    Henkart, P.A.2
  • 12
    • 0026753388 scopus 로고
    • Cytotoxicity with target DNA breakdown by rat basophilic leukemia cells expressing both cytolysin and granzyme A
    • Shiver, J.W., Su, L. & Henkart, P.A. Cytotoxicity with target DNA breakdown by rat basophilic leukemia cells expressing both cytolysin and granzyme A. Cell 71, 315-322 (1992).
    • (1992) Cell , vol.71 , pp. 315-322
    • Shiver, J.W.1    Su, L.2    Henkart, P.A.3
  • 13
    • 0036595397 scopus 로고    scopus 로고
    • Cytotoxic T lymphocytes: All roads lead to death
    • Barry, M. & Bleackley, R.C. Cytotoxic T lymphocytes: all roads lead to death. Nat. Rev. Immunol. 2, 401-409 (2002).
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 401-409
    • Barry, M.1    Bleackley, R.C.2
  • 14
    • 0035900714 scopus 로고    scopus 로고
    • Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks
    • Beresford, P.J. et al. Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks. J. Biol. Chem. 276, 43285-43293 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43285-43293
    • Beresford, P.J.1
  • 15
    • 0037318731 scopus 로고    scopus 로고
    • Cleaving the oxidative repair protein Ape I enhances cell death mediated by granzyme A
    • Fan, Z. et al. Cleaving the oxidative repair protein Ape I enhances cell death mediated by granzyme A. Nat. Immunol. 4, 145-153 (2003).
    • (2003) Nat. Immunol. , vol.4 , pp. 145-153
    • Fan, Z.1
  • 16
    • 10544252275 scopus 로고    scopus 로고
    • New paradigm for lymphocyte granule mediated cytotoxicity. Targets bind and internalize granzyme B, but an endosomolytic agent is necessary for cytosolic delivery and subsequent apoptosis
    • Froelich, C.J. et al. New paradigm for lymphocyte granule mediated cytotoxicity. Targets bind and internalize granzyme B, but an endosomolytic agent is necessary for cytosolic delivery and subsequent apoptosis. J. Biol. Chem. 271, 29073-29079 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 29073-29079
    • Froelich, C.J.1
  • 17
    • 0034721646 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor II receptor is a death receptor for granzyme B during cytotoxic T cell-induced apoptosis
    • Motyka, B. et al. Mannose 6-phosphate/insulin-like growth factor II receptor is a death receptor for granzyme B during cytotoxic T cell-induced apoptosis. Cell 103, 491-500 (2000).
    • (2000) Cell , vol.103 , pp. 491-500
    • Motyka, B.1
  • 18
    • 0033499729 scopus 로고    scopus 로고
    • Cytosolic delivery of granzyme B by bacterial toxins: Evidence that endosomal disruption, in addition to transmembrane pore formation, is an important function of perforin
    • Browne, K.A. et al. Cytosolic delivery of granzyme B by bacterial toxins: evidence that endosomal disruption, in addition to transmembrane pore formation, is an important function of perforin. Mol. Cell. Biol. 19, 8604-8615 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8604-8615
    • Browne, K.A.1
  • 19
    • 0036195424 scopus 로고    scopus 로고
    • Cytotoxic cell granule-mediated apoptosis: Perforin delivers granzyme B-serglycin complexes into target cells without plasma membrane pore formation
    • Metkar, S.S. et al. Cytotoxic cell granule-mediated apoptosis: perforin delivers granzyme B-serglycin complexes into target cells without plasma membrane pore formation. Immunity 16, 417-428 (2002).
    • (2002) Immunity , vol.16 , pp. 417-428
    • Metkar, S.S.1
  • 20
    • 0022098875 scopus 로고
    • Internalization of blocking antibodies against mannose-6-phosphate specific receptors
    • Gartung, C., Braulke, T., Hasilik, A. & von Figura, K. Internalization of blocking antibodies against mannose-6-phosphate specific receptors. EMBO J. 4, 1725-1730 (1985).
    • (1985) EMBO J. , vol.4 , pp. 1725-1730
    • Gartung, C.1    Braulke, T.2    Hasilik, A.3    von Figura, K.4
  • 21
    • 0019307389 scopus 로고
    • Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling
    • Gonzalez-Noriega, A., Grubb, J.H., Talkad, V. & Sly, W.S. Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling. J. Cell Biol. 85, 839-852 (1980).
    • (1980) J. Cell Biol. , vol.85 , pp. 839-852
    • Gonzalez-Noriega, A.1    Grubb, J.H.2    Talkad, V.3    Sly, W.S.4
  • 22
    • 0024341251 scopus 로고
    • Mechanisms of lysis by large granular lymphocyte granule cytolysin: Generation of a stable cytolysin-RBC intermediate
    • Kuta, A.E., Reynolds, C.R. & Henkart, P.A. Mechanisms of lysis by large granular lymphocyte granule cytolysin: generation of a stable cytolysin-RBC intermediate. J. Immunol. 142, 4378-4384 (1989).
    • (1989) J. Immunol. , vol.142 , pp. 4378-4384
    • Kuta, A.E.1    Reynolds, C.R.2    Henkart, P.A.3
  • 23
    • 0031464539 scopus 로고    scopus 로고
    • Perforin is activated by proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain
    • Uellner, R. et al. Perforin is activated by proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain. EMBO J. 16, 7287-7296 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7287-7296
    • Uellner, R.1
  • 24
    • 0031561141 scopus 로고    scopus 로고
    • Perforin-enhancing protein, a low molecular weight protein of cytotoxic lymphocyte granules, enhances perforin lysis
    • Winkler, U., Fraser, S.A. & Hudig, D. Perforin-enhancing protein, a low molecular weight protein of cytotoxic lymphocyte granules, enhances perforin lysis. Biochem. Biophys. Res. Commun. 236, 34-39 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 34-39
    • Winkler, U.1    Fraser, S.A.2    Hudig, D.3
  • 25
    • 0016871811 scopus 로고
    • The mechanism of T cell mediated cytotoxicity. I. The release of different cell components
    • Sanderson, C.J. The mechanism of T cell mediated cytotoxicity. I. The release of different cell components. Proc. R. Soc. Lond. B 192, 221-239 (1976).
    • (1976) Proc. R. Soc. Lond. B , vol.192 , pp. 221-239
    • Sanderson, C.J.1
  • 26
    • 0022592627 scopus 로고
    • On the mechanism of unidirectional killing in mixtures of two cytotoxic T lymphocytes. Unidirectional polarization of cytoplasmic organelles and the membrane-associated cytoskeleton in the effector cell
    • Kupfer, A., Singer, S.J. & Dennert, G. On the mechanism of unidirectional killing in mixtures of two cytotoxic T lymphocytes. Unidirectional polarization of cytoplasmic organelles and the membrane-associated cytoskeleton in the effector cell. J. Exp. Med. 163, 489-498 (1986).
    • (1986) J. Exp. Med. , vol.163 , pp. 489-498
    • Kupfer, A.1    Singer, S.J.2    Dennert, G.3
  • 27
    • 0037136311 scopus 로고    scopus 로고
    • Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation
    • Balaji, K.N., Schaschke, N., Machleidt, W., Catalfamo, M. & Henkart, P.A. Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation. J. Exp. Med. 196, 493-503 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 493-503
    • Balaji, K.N.1    Schaschke, N.2    Machleidt, W.3    Catalfamo, M.4    Henkart, P.A.5
  • 28
    • 0032532013 scopus 로고    scopus 로고
    • FLIP prevents apoptosis induced by death receptors but not by perforin/granzyme B, chemotherapeutic drugs, and γ-irradiation
    • Kataoka, T. et al. FLIP prevents apoptosis induced by death receptors but not by perforin/granzyme B, chemotherapeutic drugs, and γ-irradiation. J. Immunol. 161, 3936-3942 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 3936-3942
    • Kataoka, T.1
  • 29
    • 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. 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. 170, 805-815 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 805-815
    • Hirst, C.E.1
  • 30
    • 0025597939 scopus 로고
    • The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments
    • Burkhardt, J.K., Hester, S., Lapham, C.K. & Argon, Y. The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments. J. Cell Biol. 111, 2327-2340 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 2327-2340
    • Burkhardt, J.K.1    Hester, S.2    Lapham, C.K.3    Argon, Y.4
  • 31
    • 0025905925 scopus 로고
    • Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes
    • Peters, P.J. et al. Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes. J. Exp. Med. 173, 1099-1109 (1991).
    • (1991) J. Exp. Med. , vol.173 , pp. 1099-1109
    • Peters, P.J.1
  • 32
    • 0020365635 scopus 로고
    • Spatial relationships of microtubule organizing centers and the contact area of cytotoxic T lymphocytes and target cells
    • Geiger, B., Rosen, D. & Berke, G. Spatial relationships of microtubule organizing centers and the contact area of cytotoxic T lymphocytes and target cells. J. Cell Biol. 95, 137-143 (1982).
    • (1982) J. Cell Biol. , vol.95 , pp. 137-143
    • Geiger, B.1    Rosen, D.2    Berke, G.3
  • 33
    • 0021714772 scopus 로고
    • Reorientation of the microtubule-organizing center and the Golgi apparatus in cloned cytotoxic lymphocytes triggered by binding to lysable target cells
    • Kupfer, A. & Dennert, G. Reorientation of the microtubule-organizing center and the Golgi apparatus in cloned cytotoxic lymphocytes triggered by binding to lysable target cells. J. Immunol. 133, 2762-2766 (1984).
    • (1984) J. Immunol. , vol.133 , pp. 2762-2766
    • Kupfer, A.1    Dennert, G.2
  • 34
    • 0022362235 scopus 로고
    • The reorientation of the Golgi apparatus and the microtubule-organizing center in the cytotoxic effector cell is a prerequisite in the lysis of bound target cells
    • Kupfer, A., Dennert, G. & Singer, S.J. The reorientation of the Golgi apparatus and the microtubule-organizing center in the cytotoxic effector cell is a prerequisite in the lysis of bound target cells. J. Mol. Cell. Immunol. 2, 37-49 (1985).
    • (1985) J. Mol. Cell. Immunol. , vol.2 , pp. 37-49
    • Kupfer, A.1    Dennert, G.2    Singer, S.J.3
  • 36
    • 0035655587 scopus 로고    scopus 로고
    • The immunological synapse of CTL contains a secretory domain and membrane bridges
    • Stinchcombe, J.C., Bossi, G., Booth, S. & Griffiths, G.M. The immunological synapse of CTL contains a secretory domain and membrane bridges. Immunity 15, 751-761 (2001).
    • (2001) Immunity , vol.15 , pp. 751-761
    • Stinchcombe, J.C.1    Bossi, G.2    Booth, S.3    Griffiths, G.M.4
  • 37
    • 0036604984 scopus 로고    scopus 로고
    • Formation and function of the immunological synapse
    • van der Merwe, P.A. Formation and function of the immunological synapse. Curr. Opin. Immunol. 14, 293-298 (2002).
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 293-298
    • van der Merwe, P.A.1
  • 38
    • 0035654722 scopus 로고    scopus 로고
    • Role of calcium influx in cytotoxic T lymphocyte lytic granule exocytosis during target cell killing
    • Lyubchenko, T.A., Wurth, G.A. & Zweifach, A. Role of calcium influx in cytotoxic T lymphocyte lytic granule exocytosis during target cell killing. Immunity. 15, 847-859 (2001).
    • (2001) Immunity , vol.15 , pp. 847-859
    • Lyubchenko, T.A.1    Wurth, G.A.2    Zweifach, A.3
  • 39
    • 0036166541 scopus 로고    scopus 로고
    • Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing
    • Kuhn, J.R. & Poenie, M. Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing. Immunity 16, 111-121 (2002).
    • (2002) Immunity , vol.16 , pp. 111-121
    • Kuhn, J.R.1    Poenie, M.2
  • 40
    • 8944248275 scopus 로고    scopus 로고
    • Identification of the murine beige gene by YAC complementation and positional cloning
    • Perou, C.M. et al. Identification of the murine beige gene by YAC complementation and positional cloning. Nat. Genet. 13, 303-308 (1996).
    • (1996) Nat. Genet. , vol.13 , pp. 303-308
    • Perou, C.M.1
  • 41
    • 0344002689 scopus 로고    scopus 로고
    • Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
    • Menasche, G. et al. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nat. Genet. 25, 173-176 (2000).
    • (2000) Nat. Genet. , vol.25 , pp. 173-176
    • Menasche, G.1
  • 42
    • 12944255844 scopus 로고    scopus 로고
    • A mutation in Rab27a causes the vesicle transport defects observed in ashen mice
    • Wilson, S.M. et al. A mutation in Rab27a causes the vesicle transport defects observed in ashen mice. Proc. Natl. Acad. Sci. USA 97, 7933-7938 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7933-7938
    • Wilson, S.M.1
  • 43
    • 12944252970 scopus 로고    scopus 로고
    • Rab geranylgeranyl transferase α mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis
    • Detter, J.C. et al. Rab geranylgeranyl transferase α mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis Proc. Natl. Acad. Sci. USA 97, 4144-4149 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4144-4149
    • Detter, J.C.1
  • 44
    • 0033520970 scopus 로고    scopus 로고
    • Perform gene defects in familial haemophagocytic lymphohistiocytosis
    • Stepp, S.E. et al. Perform gene defects in familial haemophagocytic lymphohistiocytosis. Science 286, 1957-1959 (1999).
    • (1999) Science , vol.286 , pp. 1957-1959
    • Stepp, S.E.1
  • 45
    • 0035990982 scopus 로고    scopus 로고
    • Albinism and immunity: What's the link?
    • Griffiths, G.M. Albinism and immunity: what's the link? Curr. Mol. Med. 2, 479-483 (2002).
    • (2002) Curr. Mol. Med. , vol.2 , pp. 479-483
    • Griffiths, G.M.1
  • 46
    • 0033523774 scopus 로고    scopus 로고
    • Regulated secretion from hemopoietic cells
    • Stinchcombe, J.C. & Griffiths, G.M. Regulated secretion from hemopoietic cells. J. Cell Biol. 147, 1-6 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1-6
    • Stinchcombe, J.C.1    Griffiths, G.M.2
  • 47
    • 0035911150 scopus 로고    scopus 로고
    • Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice
    • Haddad, E.K., Wu, X., Hammer, J.A. & Henkart, P.A. Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice. J. Cell Biol. 152, 835-842 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 835-842
    • Haddad, E.K.1    Wu, X.2    Hammer, J.A.3    Henkart, P.A.4
  • 48
    • 0035911160 scopus 로고    scopus 로고
    • Rab27a is required for regulated secretion in cytotoxic T lymphocytes
    • Stinchcombe, J.C. et al. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J. Cell Biol. 152, 825-834 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 825-834
    • Stinchcombe, J.C.1
  • 49
    • 0035911157 scopus 로고    scopus 로고
    • Rab27a regulates the peripheral distribution of melanosomes in melanocytes
    • Hume, A.N. et al. Rab27a regulates the peripheral distribution of melanosomes in melanocytes. J. Cell Biol. 152, 795-808 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 795-808
    • Hume, A.N.1
  • 50
    • 0036000020 scopus 로고    scopus 로고
    • Rab27a is an essential component of melanosome receptor for myosin Va
    • Wu, X., Wang, F., Rao, K., Sellers, J.R. & Hammer, J.A. Rab27a is an essential component of melanosome receptor for myosin Va. Mol. Biol. Cell. 13, 1735-1749 (2002).
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 1735-1749
    • Wu, X.1    Wang, F.2    Rao, K.3    Sellers, J.R.4    Hammer, J.A.5
  • 51
    • 0034144433 scopus 로고    scopus 로고
    • Two genes are responsible for Griscelli syndrome at the same 15q21 locus
    • Pastural, E. et al. Two genes are responsible for Griscelli syndrome at the same 15q21 locus. Genomics 63, 299-306 (2000).
    • (2000) Genomics , vol.63 , pp. 299-306
    • Pastural, E.1
  • 52
    • 0036099629 scopus 로고    scopus 로고
    • The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes
    • Hume, A.N. et al. The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes. Traffic 3, 193-202 (2002).
    • (2002) Traffic , vol.3 , pp. 193-202
    • Hume, A.N.1
  • 53
    • 0037023745 scopus 로고    scopus 로고
    • Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: Implications of a tripartite protein complex for melanosome transport
    • Fukuda, M., Kuroda, T.S. & Mikoshiba, K. Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. J. Biol. Chem. 277, 12432-12436 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12432-12436
    • Fukuda, M.1    Kuroda, T.S.2    Mikoshiba, K.3
  • 54
    • 0036298197 scopus 로고    scopus 로고
    • Synaptotagmin-like protein 5: A novel Rab27A effector with C-terminal tandem C2 domains
    • Kuroda, T.S., Fukuda, M., Ariga, H. & Mikoshiba, K. Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains. Biochem. Biophys. Res. Commun. 293, 899-906 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 899-906
    • Kuroda, T.S.1    Fukuda, M.2    Ariga, H.3    Mikoshiba, K.4
  • 55
    • 0037067673 scopus 로고    scopus 로고
    • A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport
    • Strom, M., Hume, A.N., Tarafder, A.K., Barkagianni, E. & Seabra, M.C. A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. J. Biol. Chem. 277, 25423-25430 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25423-25430
    • Strom, M.1    Hume, A.N.2    Tarafder, A.K.3    Barkagianni, E.4    Seabra, M.C.5
  • 56
    • 0032559265 scopus 로고    scopus 로고
    • Interaction of a Golgi-associated kinesin-like protein with Rab6
    • Echard, A. et al. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science. 279, 580-585 (1998).
    • (1998) Science , vol.279 , pp. 580-585
    • Echard, A.1
  • 57
    • 0035975946 scopus 로고    scopus 로고
    • The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
    • Jorders, I. et al. The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. Curr. Biol. 11, 1680-1685 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1680-1685
    • Jorders, I.1
  • 58
    • 0037086443 scopus 로고    scopus 로고
    • Late endosome motility depends on lipids via the small GTPase Rab7
    • Lebrand, C. et al. Late endosome motility depends on lipids via the small GTPase Rab7. EMBO J. 21, 1289-300 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1289-1300
    • Lebrand, C.1
  • 59
    • 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 1, 816-822 (2000).
    • (2000) Traffic , vol.1 , pp. 816-822
    • Ward, D.M.1    Griffiths, G.M.2    Stinchcombe, J.C.3    Kaplan, J.4
  • 60
    • 0029039291 scopus 로고
    • Loss of cytotoxic T lymphocyte function in Chediak-Higashi syndrome arises from a secretory defect that prevents lytic granule exocytosis
    • Baetz, K., Isaaz, S. & Griffiths, G.M. Loss of cytotoxic T lymphocyte function in Chediak-Higashi syndrome arises from a secretory defect that prevents lytic granule exocytosis. J. Immunol. 154, 6122-6131 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 6122-6131
    • Baetz, K.1    Isaaz, S.2    Griffiths, G.M.3
  • 61
    • 15844397403 scopus 로고    scopus 로고
    • Identification of the homologous beige and Chediak-Higashi syndrome genes
    • Barbosa, M.D. et al. Identification of the homologous beige and Chediak-Higashi syndrome genes. Nature 382, 262-265 (1996).
    • (1996) Nature , vol.382 , pp. 262-265
    • Barbosa, M.D.1
  • 62
    • 0034189092 scopus 로고    scopus 로고
    • Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak-Higashi syndrome patients
    • Stinchcombe, J.C., Page, L.J. & Griffiths, G.M. Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak-Higashi syndrome patients. Traffic 1, 435-444 (2000).
    • (2000) Traffic , vol.1 , pp. 435-444
    • Stinchcombe, J.C.1    Page, L.J.2    Griffiths, G.M.3
  • 63
    • 0036253771 scopus 로고    scopus 로고
    • The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins
    • Tchernev, V.T. et al. The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins. Mol. Med. 8, 56-64 (2002).
    • (2002) Mol. Med. , vol.8 , pp. 56-64
    • Tchernev, V.T.1
  • 64
    • 0035479955 scopus 로고    scopus 로고
    • The role of cytotoxicity in lymphocyte homeostasis
    • de Saint Basile, G. & Fischer, A. The role of cytotoxicity in lymphocyte homeostasis. Curr. Opin. Immunol. 13, 549-554 (2001).
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 549-554
    • de Saint Basile, G.1    Fischer, A.2
  • 65
    • 0036398422 scopus 로고    scopus 로고
    • Haemophagocytic lymphohistiocytosis: Proposal of a diagnostic algorithm based on perforin expression
    • Arico, M. et al. Haemophagocytic lymphohistiocytosis: proposal of a diagnostic algorithm based on perforin expression. Br. J. Haematol. 119, 180-188 (2002).
    • (2002) Br. J. Haematol. , vol.119 , pp. 180-188
    • Arico, M.1
  • 66
    • 0036277746 scopus 로고    scopus 로고
    • Functional consequences of perforin gene mutations in 22 patients with familial haemophagocytic lymphohistiocytosis
    • Feldmann, J. et al. Functional consequences of perforin gene mutations in 22 patients with familial haemophagocytic lymphohistiocytosis. Br. J. Haematol. 111, 965-972 (2002).
    • (2002) Br. J. Haematol. , vol.111 , pp. 965-972
    • Feldmann, J.1
  • 67
    • 0035092422 scopus 로고    scopus 로고
    • Spectrum of perforin gene mutations in familial hemophagocytic lymphohistiocytosis
    • Goransdotter Ericson, K. et al. Spectrum of perforin gene mutations in familial hemophagocytic lymphohistiocytosis. Am J. Hum. Genet. 68, 590-597 (2001).
    • (2001) Am J. Hum. Genet. , vol.68 , pp. 590-597
    • Goransdotter Ericson, K.1
  • 68
    • 0036181273 scopus 로고    scopus 로고
    • Perforin defects of primary haemophagocytic lymphohistiocytosis in Japan
    • Suga, N. et al. Perforin defects of primary haemophagocytic lymphohistiocytosis in Japan. Br. J. Haematol. 116, 346-349 (2002).
    • (2002) Br. J. Haematol. , vol.116 , pp. 346-349
    • Suga, N.1
  • 69
    • 18644379642 scopus 로고    scopus 로고
    • The ETS protein MEF plays a critical role in perforin gene expression and the development of natural killer and NK-T cells
    • Lacorazza, H.D. et al. The ETS protein MEF plays a critical role in perforin gene expression and the development of natural killer and NK-T cells. Immunity 17, 437-449 (2002).
    • (2002) Immunity , vol.17 , pp. 437-449
    • Lacorazza, H.D.1
  • 71
    • 0033666758 scopus 로고    scopus 로고
    • On the pathogenesis of perforin defects and related immunodeficiencies
    • Moretta, L., Moretta, A., Hengartner, H. & Zinkernagel, R.M. On the pathogenesis of perforin defects and related immunodeficiencies. Immunol. Today 21, 593-594 (2000).
    • (2000) Immunol. Today , vol.21 , pp. 593-594
    • Moretta, L.1    Moretta, A.2    Hengartner, H.3    Zinkernagel, R.M.4
  • 72
    • 0029914331 scopus 로고    scopus 로고
    • Molecular mechanisms of lymphocyte-mediated cytotoxicity and their role in immunological protection and pathogenesis in vivo
    • Kagi, D., Ledermann, B., Burki, K., Zinkernagel, R.M. & Hengartner, H. Molecular mechanisms of lymphocyte-mediated cytotoxicity and their role in immunological protection and pathogenesis in vivo. Annu. Rev. Immunol. 14, 207-232 (1996).
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 207-232
    • Kagi, D.1    Ledermann, B.2    Burki, K.3    Zinkernagel, R.M.4    Hengartner, H.5
  • 73
    • 0027937745 scopus 로고
    • Cytolytic T cell cytotoxicity is mediated through perforin and Fas lytic pathways
    • Lowin, B., Hahne, M., Mattman, C. & Tschopp, J. Cytolytic T cell cytotoxicity is mediated through perforin and Fas lytic pathways. Nature 370, 650-652 (1994).
    • (1994) Nature , vol.370 , pp. 650-652
    • Lowin, B.1    Hahne, M.2    Mattman, C.3    Tschopp, J.4
  • 74
    • 0028110345 scopus 로고
    • Immune function in mice lacking the perforin gene
    • Walsh, C.M. et al. Immune function in mice lacking the perforin gene. Proc. Natl. Acad. Sci. USA 91, 10854-10858 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10854-10858
    • Walsh, C.M.1
  • 75
    • 0032980707 scopus 로고    scopus 로고
    • A role for perforin in downregulating T-cell responses during chronic viral infection
    • Matloubian, M. et al. A role for perforin in downregulating T-cell responses during chronic viral infection. J. Virol. 73, 2527-2536 (1999).
    • (1999) J. Virol. , vol.73 , pp. 2527-2536
    • Matloubian, M.1
  • 78
    • 0033615606 scopus 로고    scopus 로고
    • TCR-mediated internalization of peptide-MHC complexes acquired by T cells
    • Huang, J.F. et al. TCR-mediated internalization of peptide-MHC complexes acquired by T cells. Science 286, 952-954 (1999).
    • (1999) Science , vol.286 , pp. 952-954
    • Huang, J.F.1
  • 79
    • 0034599597 scopus 로고    scopus 로고
    • T cells can use either T cell receptor or CD28 receptors to absorb and internalise cell surface molecules derived from antigen-presenting cells
    • Hwang, I. et al. T cells can use either T cell receptor or CD28 receptors to absorb and internalise cell surface molecules derived from antigen-presenting cells. J. Exp. Med. 191, 1137-1148 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1137-1148
    • Hwang, I.1
  • 80
    • 0035942781 scopus 로고    scopus 로고
    • B cells acquire antigen from target cells after synapse formation
    • Batista, F.D., Iber, D. & Neuberger, M.S. B cells acquire antigen from target cells after synapse formation. Nature 411, 489-494 (2001).
    • (2001) Nature , vol.411 , pp. 489-494
    • Batista, F.D.1    Iber, D.2    Neuberger, M.S.3
  • 81
    • 0035914946 scopus 로고    scopus 로고
    • Intercellular transfer and supramolecular organization of human leucocyte antigen C at inhibitory natural killer cell immune synapses
    • Carlin, L.M., Eleme, K., McCann, F.E. & Davis, D.M. Intercellular transfer and supramolecular organization of human leucocyte antigen C at inhibitory natural killer cell immune synapses. J. Exp. Med. 194, 1507-17 (2001).
    • (2001) J. Exp. Med. , vol.194 , pp. 1507-1517
    • Carlin, L.M.1    Eleme, K.2    McCann, F.E.3    Davis, D.M.4
  • 82
    • 0035914742 scopus 로고    scopus 로고
    • Acquisition of external major histocompatibility complex class I molecules by natural killer cells expressing inhibitory Ly49 receptors
    • Sjostrom, A. et al. Acquisition of external major histocompatibility complex class I molecules by natural killer cells expressing inhibitory Ly49 receptors. J. Exp Med. 194, 1519-1530 (2001).
    • (2001) J. Exp Med. , vol.194 , pp. 1519-1530
    • Sjostrom, A.1
  • 83
    • 0036113274 scopus 로고    scopus 로고
    • Active trans-synaptic capture of membrane fragments by natural killer cells
    • Tabiasco, J. et al. Active trans-synaptic capture of membrane fragments by natural killer cells. Eur. J. Immunol. 32, 1502-1508 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1502-1508
    • Tabiasco, J.1
  • 84
    • 0037097642 scopus 로고    scopus 로고
    • Synaptic transfer by human gamma delta T cells stimulated with soluble or cellular antigens
    • Espinosa, E., Tabiasco, J., Hudrisier, D. & Fournie, J.J. Synaptic transfer by human gamma delta T cells stimulated with soluble or cellular antigens. J. Immunol. 168, 6336-6343 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 6336-6343
    • Espinosa, E.1    Tabiasco, J.2    Hudrisier, D.3    Fournie, J.J.4
  • 85
    • 0035869425 scopus 로고    scopus 로고
    • Cutting edge: CTLs rapidly capture membrane fragments from target cells in a TCR-signaling dependent manner
    • Hudrisier, D., Riond, J., Mazarguil, H., Gairin, J.E. & Jolly, E. Cutting edge: CTLs rapidly capture membrane fragments from target cells in a TCR-signaling dependent manner. J. Immunol. 166, 3645-3649 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 3645-3649
    • Hudrisier, D.1    Riond, J.2    Mazarguil, H.3    Gairin, J.E.4    Jolly, E.5


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