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Volumn 22, Issue 1, 2010, Pages 94-108

A whodunit: an appointment with death

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; CD8+ T LYMPHOCYTE; CELL ACTIVITY; CELL DEATH; CELL DIVISION; CROSS PRESENTATION; DENDRITIC CELL; EPITHELIUM CELL; HOST PATHOGEN INTERACTION; IMMUNE RESPONSE; INTERNALIZATION; KILLER CELL; MAJOR HISTOCOMPATIBILITY COMPLEX; MICROBIAL ACTIVITY; NONHUMAN; PHAGOCYTOSIS; REVIEW; SIGNAL TRANSDUCTION; VIRUS IMMUNITY;

EID: 77349085076     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coi.2010.01.023     Document Type: Review
Times cited : (8)

References (130)
  • 1
    • 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 3 (2003) 361-370
    • (2003) Nat Rev Immunol , vol.3 , pp. 361-370
    • Lieberman, J.1
  • 2
    • 34247577498 scopus 로고    scopus 로고
    • Delivering the kiss of death: progress on understanding how perforin works
    • Pipkin M.E., and Lieberman J. Delivering the kiss of death: progress on understanding how perforin works. Curr Opin Immunol 19 (2007) 301-308
    • (2007) Curr Opin Immunol , vol.19 , pp. 301-308
    • Pipkin, M.E.1    Lieberman, J.2
  • 3
    • 0141629512 scopus 로고    scopus 로고
    • Nuclear war: the granzyme A-bomb
    • Lieberman J., and Fan Z. Nuclear war: the granzyme A-bomb. Curr Opin Immunol 15 (2003) 553-559
    • (2003) Curr Opin Immunol , vol.15 , pp. 553-559
    • Lieberman, J.1    Fan, Z.2
  • 4
    • 41849105805 scopus 로고    scopus 로고
    • Two-photon imaging of intratumoral CD8+ T cell cytotoxic activity during adoptive T cell therapy in mice
    • Breart B., Lemaitre F., Celli S., and Bousso P. Two-photon imaging of intratumoral CD8+ T cell cytotoxic activity during adoptive T cell therapy in mice. J Clin Invest 118 (2008) 1390-1397
    • (2008) J Clin Invest , vol.118 , pp. 1390-1397
    • Breart, B.1    Lemaitre, F.2    Celli, S.3    Bousso, P.4
  • 5
    • 0035838984 scopus 로고    scopus 로고
    • Dendritic cells: specialized and regulated antigen processing machines
    • Mellman I., and Steinman R.M. Dendritic cells: specialized and regulated antigen processing machines. Cell 106 (2001) 255-258
    • (2001) Cell , vol.106 , pp. 255-258
    • Mellman, I.1    Steinman, R.M.2
  • 6
    • 0032485487 scopus 로고    scopus 로고
    • Dendritic cells acquire antigen from apoptotic cells and induce class I-restricted CTLs
    • The authors demonstrate that human DCs, but not macrophages, efficiently present antigen derived from apoptotic cells, stimulating class I-restricted CD8+ CTLs.
    • Albert M.L., Sauter B., and Bhardwaj N. Dendritic cells acquire antigen from apoptotic cells and induce class I-restricted CTLs. Nature 392 (1998) 86-89. The authors demonstrate that human DCs, but not macrophages, efficiently present antigen derived from apoptotic cells, stimulating class I-restricted CD8+ CTLs.
    • (1998) Nature , vol.392 , pp. 86-89
    • Albert, M.L.1    Sauter, B.2    Bhardwaj, N.3
  • 7
    • 0035340513 scopus 로고    scopus 로고
    • Human cytomegalovirus pp65- and immediate early 1 antigen-specific HLA class I-restricted cytotoxic T cell responses induced by cross-presentation of viral antigens
    • Tabi Z., Moutaftsi M., and Borysiewicz L.K. Human cytomegalovirus pp65- and immediate early 1 antigen-specific HLA class I-restricted cytotoxic T cell responses induced by cross-presentation of viral antigens. J Immunol 166 (2001) 5695-5703
    • (2001) J Immunol , vol.166 , pp. 5695-5703
    • Tabi, Z.1    Moutaftsi, M.2    Borysiewicz, L.K.3
  • 8
    • 0033522179 scopus 로고    scopus 로고
    • Cytotoxic T-cell immunity to virus-infected non-haematopoietic cells requires presentation of exogenous antigen
    • Sigal L.J., Crotty S., Andino R., and Rock K.L. Cytotoxic T-cell immunity to virus-infected non-haematopoietic cells requires presentation of exogenous antigen. Nature 398 (1999) 77-80
    • (1999) Nature , vol.398 , pp. 77-80
    • Sigal, L.J.1    Crotty, S.2    Andino, R.3    Rock, K.L.4
  • 9
    • 0242539823 scopus 로고    scopus 로고
    • Control of dendritic cell cross-presentation by the major histocompatibility complex class I cytoplasmic domain
    • Lizee G., Basha G., Tiong J., Julien J.P., Tian M., Biron K.E., and Jefferies W.A. Control of dendritic cell cross-presentation by the major histocompatibility complex class I cytoplasmic domain. Nat Immunol 4 (2003) 1065-1073
    • (2003) Nat Immunol , vol.4 , pp. 1065-1073
    • Lizee, G.1    Basha, G.2    Tiong, J.3    Julien, J.P.4    Tian, M.5    Biron, K.E.6    Jefferies, W.A.7
  • 10
    • 22744441633 scopus 로고    scopus 로고
    • Apoptotic cells deliver processed antigen to dendritic cells for cross-presentation
    • Blachere N.E., Darnell R.B., and Albert M.L. Apoptotic cells deliver processed antigen to dendritic cells for cross-presentation. PLoS Biol 3 (2005) e185
    • (2005) PLoS Biol , vol.3
    • Blachere, N.E.1    Darnell, R.B.2    Albert, M.L.3
  • 11
    • 1542511202 scopus 로고    scopus 로고
    • Death-defying immunity: do apoptotic cells influence antigen processing and presentation?
    • Albert M.L. Death-defying immunity: do apoptotic cells influence antigen processing and presentation?. Nat Rev Immunol 4 (2004) 223-231
    • (2004) Nat Rev Immunol , vol.4 , pp. 223-231
    • Albert, M.L.1
  • 12
    • 0037152162 scopus 로고    scopus 로고
    • Constitutive presentation of a natural tissue autoantigen exclusively by dendritic cells in the draining lymph node
    • Scheinecker C., McHugh R., Shevach E.M., and Germain R.N. Constitutive presentation of a natural tissue autoantigen exclusively by dendritic cells in the draining lymph node. J Exp Med 196 (2002) 1079-1090
    • (2002) J Exp Med , vol.196 , pp. 1079-1090
    • Scheinecker, C.1    McHugh, R.2    Shevach, E.M.3    Germain, R.N.4
  • 13
    • 0345448056 scopus 로고    scopus 로고
    • Physiological beta cell death triggers priming of self-reactive T cells by dendritic cells in a type-1 diabetes model
    • Turley S., Poirot L., Hattori M., Benoist C., and Mathis D. Physiological beta cell death triggers priming of self-reactive T cells by dendritic cells in a type-1 diabetes model. J Exp Med 198 (2003) 1527-1537
    • (2003) J Exp Med , vol.198 , pp. 1527-1537
    • Turley, S.1    Poirot, L.2    Hattori, M.3    Benoist, C.4    Mathis, D.5
  • 14
    • 0034614894 scopus 로고    scopus 로고
    • A discrete subpopulation of dendritic cells transports apoptotic intestinal epithelial cells to T cell areas of mesenteric lymph nodes
    • Huang F.P., Platt N., Wykes M., Major J.R., Powell T.J., Jenkins C.D., and MacPherson G.G. A discrete subpopulation of dendritic cells transports apoptotic intestinal epithelial cells to T cell areas of mesenteric lymph nodes. J Exp Med 191 (2000) 435-444
    • (2000) J Exp Med , vol.191 , pp. 435-444
    • Huang, F.P.1    Platt, N.2    Wykes, M.3    Major, J.R.4    Powell, T.J.5    Jenkins, C.D.6    MacPherson, G.G.7
  • 16
    • 0036884424 scopus 로고    scopus 로고
    • A blast from the past: clearance of apoptotic cells regulates immune responses
    • Savill J., Dransfield I., Gregory C., and Haslett C. A blast from the past: clearance of apoptotic cells regulates immune responses. Nat Rev Immunol 2 (2002) 965-975
    • (2002) Nat Rev Immunol , vol.2 , pp. 965-975
    • Savill, J.1    Dransfield, I.2    Gregory, C.3    Haslett, C.4
  • 17
    • 2342584674 scopus 로고    scopus 로고
    • Clearance of apoptotic cells: getting rid of the corpses
    • Lauber K., Blumenthal S.G., Waibel M., and Wesselborg S. Clearance of apoptotic cells: getting rid of the corpses. Mol Cell 14 (2004) 277-287
    • (2004) Mol Cell , vol.14 , pp. 277-287
    • Lauber, K.1    Blumenthal, S.G.2    Waibel, M.3    Wesselborg, S.4
  • 18
    • 33645845142 scopus 로고    scopus 로고
    • Phosphatidylserine recognition by phagocytes: a view to a kill
    • Wu Y., Tibrewal N., and Birge R.B. Phosphatidylserine recognition by phagocytes: a view to a kill. Trends Cell Biol 16 (2006) 189-197
    • (2006) Trends Cell Biol , vol.16 , pp. 189-197
    • Wu, Y.1    Tibrewal, N.2    Birge, R.B.3
  • 20
    • 0030033477 scopus 로고    scopus 로고
    • The ATP binding cassette transporter ABC1, is required for the engulfment of corpses generated by apoptotic cell death
    • Luciani M.F., and Chimini G. The ATP binding cassette transporter ABC1, is required for the engulfment of corpses generated by apoptotic cell death. EMBO J 15 (1996) 226-235
    • (1996) EMBO J , vol.15 , pp. 226-235
    • Luciani, M.F.1    Chimini, G.2
  • 21
    • 0032416392 scopus 로고    scopus 로고
    • Complement-dependent clearance of apoptotic cells by human macrophages
    • Mevorach D., Mascarenhas J.O., Gershov D., and Elkon K.B. Complement-dependent clearance of apoptotic cells by human macrophages. J Exp Med 188 (1998) 2313-2320
    • (1998) J Exp Med , vol.188 , pp. 2313-2320
    • Mevorach, D.1    Mascarenhas, J.O.2    Gershov, D.3    Elkon, K.B.4
  • 23
    • 3543053363 scopus 로고    scopus 로고
    • Immature dendritic cells phagocytose apoptotic cells via alphavbeta5 and CD36, and cross-present antigens to cytotoxic T lymphocytes
    • Albert M.L., Pearce S.F., Francisco L.M., Sauter B., Roy P., Silverstein R.L., and Bhardwaj N. Immature dendritic cells phagocytose apoptotic cells via alphavbeta5 and CD36, and cross-present antigens to cytotoxic T lymphocytes. J Exp Med 188 (1998) 1359-1368
    • (1998) J Exp Med , vol.188 , pp. 1359-1368
    • Albert, M.L.1    Pearce, S.F.2    Francisco, L.M.3    Sauter, B.4    Roy, P.5    Silverstein, R.L.6    Bhardwaj, N.7
  • 26
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses
    • Nimmerjahn F., and Ravetch J.V. Fcgamma receptors as regulators of immune responses. Nat Rev Immunol 8 (2008) 34-47
    • (2008) Nat Rev Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 28
    • 0037083280 scopus 로고    scopus 로고
    • Inhibitory effects of apoptotic cell ingestion upon endotoxin-driven myeloid dendritic cell maturation
    • Stuart L.M., Lucas M., Simpson C., Lamb J., Savill J., and Lacy-Hulbert A. Inhibitory effects of apoptotic cell ingestion upon endotoxin-driven myeloid dendritic cell maturation. J Immunol 168 (2002) 1627-1635
    • (2002) J Immunol , vol.168 , pp. 1627-1635
    • Stuart, L.M.1    Lucas, M.2    Simpson, C.3    Lamb, J.4    Savill, J.5    Lacy-Hulbert, A.6
  • 29
    • 52549125928 scopus 로고    scopus 로고
    • Mincle is an ITAM-coupled activating receptor that senses damaged cells
    • Yamasaki S., Ishikawa E., Sakuma M., Hara H., Ogata K., and Saito T. Mincle is an ITAM-coupled activating receptor that senses damaged cells. Nat Immunol 9 (2008) 1179-1188
    • (2008) Nat Immunol , vol.9 , pp. 1179-1188
    • Yamasaki, S.1    Ishikawa, E.2    Sakuma, M.3    Hara, H.4    Ogata, K.5    Saito, T.6
  • 30
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Martinon F., Petrilli V., Mayor A., Tardivel A., and Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440 (2006) 237-241
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 31
    • 0141998606 scopus 로고    scopus 로고
    • Molecular identification of a danger signal that alerts the immune system to dying cells
    • Shi Y., Evans J.E., and Rock K.L. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425 (2003) 516-521
    • (2003) Nature , vol.425 , pp. 516-521
    • Shi, Y.1    Evans, J.E.2    Rock, K.L.3
  • 32
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal
    • Lotze M.T., and Tracey K.J. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat Rev Immunol 5 (2005) 331-342
    • (2005) Nat Rev Immunol , vol.5 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 34
    • 0037062934 scopus 로고    scopus 로고
    • Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
    • Scaffidi P., Misteli T., and Bianchi M.E. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 418 (2002) 191-195
    • (2002) Nature , vol.418 , pp. 191-195
    • Scaffidi, P.1    Misteli, T.2    Bianchi, M.E.3
  • 35
    • 77349091352 scopus 로고    scopus 로고
    • Resurrecting the dead: phagocytosis of apoptotic cells by dendritic cells results in the cross-presentation of exogenous antigen
    • Lotze M. (Ed), Academic Press
    • Albert M.L. Resurrecting the dead: phagocytosis of apoptotic cells by dendritic cells results in the cross-presentation of exogenous antigen. In: Lotze M. (Ed). Dendritic Cells: Biology and Clinical Applications (2001), Academic Press
    • (2001) Dendritic Cells: Biology and Clinical Applications
    • Albert, M.L.1
  • 37
    • 0036411680 scopus 로고    scopus 로고
    • Cross-presentation of cell-associated antigens by CD8alpha+ dendritic cells is attributable to their ability to internalize dead cells
    • Schulz O., and Reis e Sousa C. Cross-presentation of cell-associated antigens by CD8alpha+ dendritic cells is attributable to their ability to internalize dead cells. Immunology 107 (2002) 183-189
    • (2002) Immunology , vol.107 , pp. 183-189
    • Schulz, O.1    Reis e Sousa, C.2
  • 38
    • 0034684659 scopus 로고    scopus 로고
    • CD8(+) but not CD8(-) dendritic cells cross-prime cytotoxic T cells in vivo
    • den Haan J.M., Lehar S.M., and Bevan M.J. CD8(+) but not CD8(-) dendritic cells cross-prime cytotoxic T cells in vivo. J Exp Med 192 (2000) 1685-1696
    • (2000) J Exp Med , vol.192 , pp. 1685-1696
    • den Haan, J.M.1    Lehar, S.M.2    Bevan, M.J.3
  • 41
    • 0031798137 scopus 로고    scopus 로고
    • Efficient presentation of phagocytosed cellular fragments on the major histocompatibility complex class II products of dendritic cells [In Process Citation]
    • Inaba K., Turley S., Yamaide F., Iyoda T., Mahnke K., Inaba M., Pack M., Subklewe M., Sauter B., Sheff D., et al. Efficient presentation of phagocytosed cellular fragments on the major histocompatibility complex class II products of dendritic cells [In Process Citation]. J Exp Med 188 (1998) 2163-2173
    • (1998) J Exp Med , vol.188 , pp. 2163-2173
    • Inaba, K.1    Turley, S.2    Yamaide, F.3    Iyoda, T.4    Mahnke, K.5    Inaba, M.6    Pack, M.7    Subklewe, M.8    Sauter, B.9    Sheff, D.10
  • 42
    • 14844340568 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    • The authors link DC and macrophage degradation capacities with their different cross-prime CD8+ T cells.
    • Delamarre L., Pack M., Chang H., Mellman I., and Trombetta E.S. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science 307 (2005) 1630-1634. The authors link DC and macrophage degradation capacities with their different cross-prime CD8+ T cells.
    • (2005) Science , vol.307 , pp. 1630-1634
    • Delamarre, L.1    Pack, M.2    Chang, H.3    Mellman, I.4    Trombetta, E.S.5
  • 44
    • 64449088219 scopus 로고    scopus 로고
    • The small GTPase Rac2 controls phagosomal alkalinization and antigen crosspresentation selectively in CD8(+) dendritic cells
    • Savina A., Peres A., Cebrian I., Carmo N., Moita C., Hacohen N., Moita L.F., and Amigorena S. The small GTPase Rac2 controls phagosomal alkalinization and antigen crosspresentation selectively in CD8(+) dendritic cells. Immunity 30 (2009) 544-555
    • (2009) Immunity , vol.30 , pp. 544-555
    • Savina, A.1    Peres, A.2    Cebrian, I.3    Carmo, N.4    Moita, C.5    Hacohen, N.6    Moita, L.F.7    Amigorena, S.8
  • 45
    • 33748475526 scopus 로고    scopus 로고
    • Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis
    • The authors report that antigen stability to lysosomal proteolysis is an important factor in determining immunogenicity in vivo.
    • Delamarre L., Couture R., Mellman I., and Trombetta E.S. Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis. J Exp Med 203 (2006) 2049-2055. The authors report that antigen stability to lysosomal proteolysis is an important factor in determining immunogenicity in vivo.
    • (2006) J Exp Med , vol.203 , pp. 2049-2055
    • Delamarre, L.1    Couture, R.2    Mellman, I.3    Trombetta, E.S.4
  • 46
    • 33745825951 scopus 로고    scopus 로고
    • NOX2 controls phagosomal pH to regulate antigen processing during crosspresentation by dendritic cells
    • The authors describe the NADPH oxidase NOX2 recruitment to early DC phagosomes to maintain alkalinization of phagosomal lumen for epitope protection from degradation and subsequent more efficient cross-presentation.
    • Savina A., Jancic C., Hugues S., Guermonprez P., Vargas P., Moura I.C., Lennon-Dumenil A.M., Seabra M.C., Raposo G., and Amigorena S. NOX2 controls phagosomal pH to regulate antigen processing during crosspresentation by dendritic cells. Cell 126 (2006) 205-218. The authors describe the NADPH oxidase NOX2 recruitment to early DC phagosomes to maintain alkalinization of phagosomal lumen for epitope protection from degradation and subsequent more efficient cross-presentation.
    • (2006) Cell , vol.126 , pp. 205-218
    • Savina, A.1    Jancic, C.2    Hugues, S.3    Guermonprez, P.4    Vargas, P.5    Moura, I.C.6    Lennon-Dumenil, A.M.7    Seabra, M.C.8    Raposo, G.9    Amigorena, S.10
  • 47
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
    • In these two back-to-back submitted papers, the authors suggest how ER contribution to phagosomes renders the phagosomal compartment competent for cross-presentation.
    • Guermonprez P., Saveanu L., Kleijmeer M., Davoust J., Van Endert P., and Amigorena S. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature 425 (2003) 397-402. In these two back-to-back submitted papers, the authors suggest how ER contribution to phagosomes renders the phagosomal compartment competent for cross-presentation.
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1    Saveanu, L.2    Kleijmeer, M.3    Davoust, J.4    Van Endert, P.5    Amigorena, S.6
  • 49
    • 0242331619 scopus 로고    scopus 로고
    • Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens
    • Ackerman A.L., Kyritsis C., Tampe R., and Cresswell P. Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens. Proc Natl Acad Sci USA 100 (2003) 12889-12894
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12889-12894
    • Ackerman, A.L.1    Kyritsis, C.2    Tampe, R.3    Cresswell, P.4
  • 50
    • 62549093613 scopus 로고    scopus 로고
    • Receptor-mediated phagocytosis elicits cross-presentation in nonprofessional antigen-presenting cells
    • Giodini A., Rahner C., and Cresswell P. Receptor-mediated phagocytosis elicits cross-presentation in nonprofessional antigen-presenting cells. Proc Natl Acad Sci USA 106 (2009) 3324-3329
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3324-3329
    • Giodini, A.1    Rahner, C.2    Cresswell, P.3
  • 51
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley B.N., and Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429 (2004) 834-840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 52
    • 26244461724 scopus 로고    scopus 로고
    • Quantitative and dynamic assessment of the contribution of the ER to phagosome formation
    • The authors argue against the contribution of ER membrane and ER membrane to phagosomes previously reported both in DCs and macrophages.
    • Touret N., Paroutis P., Terebiznik M., Harrison R.E., Trombetta S., Pypaert M., Chow A., Jiang A., Shaw J., Yip C., et al. Quantitative and dynamic assessment of the contribution of the ER to phagosome formation. Cell 123 (2005) 157-170. The authors argue against the contribution of ER membrane and ER membrane to phagosomes previously reported both in DCs and macrophages.
    • (2005) Cell , vol.123 , pp. 157-170
    • Touret, N.1    Paroutis, P.2    Terebiznik, M.3    Harrison, R.E.4    Trombetta, S.5    Pypaert, M.6    Chow, A.7    Jiang, A.8    Shaw, J.9    Yip, C.10
  • 53
    • 19344368970 scopus 로고    scopus 로고
    • ER-mediated phagocytosis: myth or reality?
    • Gagnon E., Bergeron J.J., and Desjardins M. ER-mediated phagocytosis: myth or reality?. J Leukoc Biol 77 (2005) 843-845
    • (2005) J Leukoc Biol , vol.77 , pp. 843-845
    • Gagnon, E.1    Bergeron, J.J.2    Desjardins, M.3
  • 55
    • 63049095770 scopus 로고    scopus 로고
    • Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells
    • Goldszmid R.S., Coppens I., Lev A., Caspar P., Mellman I., and Sher A. Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells. J Exp Med 206 (2009) 399-410
    • (2009) J Exp Med , vol.206 , pp. 399-410
    • Goldszmid, R.S.1    Coppens, I.2    Lev, A.3    Caspar, P.4    Mellman, I.5    Sher, A.6
  • 56
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • This paper identifies the role of ERAP1 as an ER-resident protease, which finalizes peptide trimming for MHC class I presentation.
    • York I.A., Chang S.C., Saric T., Keys J.A., Favreau J.M., Goldberg A.L., and Rock K.L. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 3 (2002) 1177-1184. This paper identifies the role of ERAP1 as an ER-resident protease, which finalizes peptide trimming for MHC class I presentation.
    • (2002) Nat Immunol , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5    Goldberg, A.L.6    Rock, K.L.7
  • 57
    • 67650465638 scopus 로고    scopus 로고
    • IRAP identifies an endosomal compartment required for MHC class I cross-presentation
    • This paper identifies IRAP as an essential endosomal protease involved in cross-presentation.
    • Saveanu L., Carroll O., Weimershaus M., Guermonprez P., Firat E., Lindo V., Greer F., Davoust J., Kratzer R., Keller S.R., et al. IRAP identifies an endosomal compartment required for MHC class I cross-presentation. Science (2009). This paper identifies IRAP as an essential endosomal protease involved in cross-presentation.
    • (2009) Science
    • Saveanu, L.1    Carroll, O.2    Weimershaus, M.3    Guermonprez, P.4    Firat, E.5    Lindo, V.6    Greer, F.7    Davoust, J.8    Kratzer, R.9    Keller, S.R.10
  • 58
    • 12344328544 scopus 로고    scopus 로고
    • Access of soluble antigens to the endoplasmic reticulum can explain cross-presentation by dendritic cells
    • Ackerman A.L., Kyritsis C., Tampe R., and Cresswell P. Access of soluble antigens to the endoplasmic reticulum can explain cross-presentation by dendritic cells. Nat Immunol 6 (2005) 107-113
    • (2005) Nat Immunol , vol.6 , pp. 107-113
    • Ackerman, A.L.1    Kyritsis, C.2    Tampe, R.3    Cresswell, P.4
  • 59
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • Bakke O., and Dobberstein B. MHC class II-associated invariant chain contains a sorting signal for endosomal compartments. Cell 63 (1990) 707-716
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 60
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class II antigen presentation
    • Hsing L.C., and Rudensky A.Y. The lysosomal cysteine proteases in MHC class II antigen presentation. Immunol Rev 207 (2005) 229-241
    • (2005) Immunol Rev , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 61
    • 26244455510 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing and cross-presentation
    • Cresswell P., Ackerman A.L., Giodini A., Peaper D.R., and Wearsch P.A. Mechanisms of MHC class I-restricted antigen processing and cross-presentation. Immunol Rev 207 (2005) 145-157
    • (2005) Immunol Rev , vol.207 , pp. 145-157
    • Cresswell, P.1    Ackerman, A.L.2    Giodini, A.3    Peaper, D.R.4    Wearsch, P.A.5
  • 62
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein- chaperoned peptides
    • The first demonstration that heat shock proteins are capable of chaperoning exogenous antigen into APCs for cross-priming.
    • Suto R., and Srivastava P.K. A mechanism for the specific immunogenicity of heat shock protein- chaperoned peptides. Science 269 (1995) 1585-1588. The first demonstration that heat shock proteins are capable of chaperoning exogenous antigen into APCs for cross-priming.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 63
    • 20544433550 scopus 로고    scopus 로고
    • Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells
    • Binder R.J., and Srivastava P.K. Peptides chaperoned by heat-shock proteins are a necessary and sufficient source of antigen in the cross-priming of CD8+ T cells. Nat Immunol 6 (2005) 593-599
    • (2005) Nat Immunol , vol.6 , pp. 593-599
    • Binder, R.J.1    Srivastava, P.K.2
  • 64
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: crosstalk between autophagy and apoptosis
    • Maiuri M.C., Zalckvar E., Kimchi A., and Kroemer G. Self-eating and self-killing: crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol 8 (2007) 741-752
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 65
    • 0034616946 scopus 로고    scopus 로고
    • Apoptotic pathways: paper wraps stone blunts scissors
    • Green D.R. Apoptotic pathways: paper wraps stone blunts scissors. Cell 102 (2000) 1-4
    • (2000) Cell , vol.102 , pp. 1-4
    • Green, D.R.1
  • 66
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: activation, specificity, and regulation
    • Pop C., and Salvesen G.S. Human caspases: activation, specificity, and regulation. J Biol Chem 284 (2009) 21777-21781
    • (2009) J Biol Chem , vol.284 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 67
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk J.E., and Green D.R. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?. Trends Cell Biol 18 (2008) 157-164
    • (2008) Trends Cell Biol , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 68
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., and Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 69
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: coping with stress
    • Rutkowski D.T., and Kaufman R.J. A trip to the ER: coping with stress. Trends Cell Biol 14 (2004) 20-28
    • (2004) Trends Cell Biol , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 70
    • 62849093368 scopus 로고    scopus 로고
    • Death receptor signal transducers: nodes of coordination in immune signaling networks
    • Wilson N.S., Dixit V., and Ashkenazi A. Death receptor signal transducers: nodes of coordination in immune signaling networks. Nat Immunol 10 (2009) 348-355
    • (2009) Nat Immunol , vol.10 , pp. 348-355
    • Wilson, N.S.1    Dixit, V.2    Ashkenazi, A.3
  • 71
    • 61949262034 scopus 로고    scopus 로고
    • Integrins and cell-fate determination
    • Streuli C.H. Integrins and cell-fate determination. J Cell Sci 122 (2009) 171-177
    • (2009) J Cell Sci , vol.122 , pp. 171-177
    • Streuli, C.H.1
  • 72
    • 23944525360 scopus 로고    scopus 로고
    • Caspase inactivation of the proteasome
    • Cohen G.M. Caspase inactivation of the proteasome. Cell Death Differ 12 (2005) 1218
    • (2005) Cell Death Differ , vol.12 , pp. 1218
    • Cohen, G.M.1
  • 73
    • 1842472483 scopus 로고    scopus 로고
    • Caspase activation inhibits proteasome function during apoptosis
    • This is the first paper showing the inactivation of proteasomal activity within cells undergoing apoptosis.
    • Sun X.M., Butterworth M., MacFarlane M., Dubiel W., Ciechanover A., and Cohen G.M. Caspase activation inhibits proteasome function during apoptosis. Mol Cell 14 (2004) 81-93. This is the first paper showing the inactivation of proteasomal activity within cells undergoing apoptosis.
    • (2004) Mol Cell , vol.14 , pp. 81-93
    • Sun, X.M.1    Butterworth, M.2    MacFarlane, M.3    Dubiel, W.4    Ciechanover, A.5    Cohen, G.M.6
  • 74
    • 54949152716 scopus 로고    scopus 로고
    • Caspase-independent cell death: leaving the set without the final cut
    • Tait S.W., and Green D.R. Caspase-independent cell death: leaving the set without the final cut. Oncogene 27 (2008) 6452-6461
    • (2008) Oncogene , vol.27 , pp. 6452-6461
    • Tait, S.W.1    Green, D.R.2
  • 75
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela M., and Tschopp J. Caspase-independent cell death in T lymphocytes. Nat Immunol 4 (2003) 416-423
    • (2003) Nat Immunol , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 77
    • 22344444616 scopus 로고    scopus 로고
    • Does autophagy contribute to cell death?
    • Debnath J., Baehrecke E.H., and Kroemer G. Does autophagy contribute to cell death?. Autophagy 1 (2005) 66-74
    • (2005) Autophagy , vol.1 , pp. 66-74
    • Debnath, J.1    Baehrecke, E.H.2    Kroemer, G.3
  • 78
    • 56749170677 scopus 로고    scopus 로고
    • Autophagic cell death: the story of a misnomer
    • Kroemer G., and Levine B. Autophagic cell death: the story of a misnomer. Nat Rev Mol Cell Biol 9 (2008) 1004-1010
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 1004-1010
    • Kroemer, G.1    Levine, B.2
  • 79
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • The authors formally demonstrate by electron tomography the ER origin of isolation membranes for the formation of autophagosomes.
    • Hayashi-Nishino M., Fujita N., Noda T., Yamaguchi A., Yoshimori T., and Yamamoto A. A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat Cell Biol (2009). The authors formally demonstrate by electron tomography the ER origin of isolation membranes for the formation of autophagosomes.
    • (2009) Nat Cell Biol
    • Hayashi-Nishino, M.1    Fujita, N.2    Noda, T.3    Yamaguchi, A.4    Yoshimori, T.5    Yamamoto, A.6
  • 80
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie Z., and Klionsky D.J. Autophagosome formation: core machinery and adaptations. Nat Cell Biol 9 (2007) 1102-1109
    • (2007) Nat Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 81
    • 70349687405 scopus 로고    scopus 로고
    • Discovery of Atg5/Atg7-independent alternative macroautophagy
    • This is the first report showing an alternative autophagic pathway independent of Atg5 and Atg7, revealing the possibility to form autophagosomes from derived from the trans-Golgi and late endosomes.
    • Nishida Y., Arakawa S., Fujitani K., Yamaguchi H., Mizuta T., Kanaseki T., Komatsu M., Otsu K., Tsujimoto Y., and Shimizu S. Discovery of Atg5/Atg7-independent alternative macroautophagy. Nature 461 (2009) 654-658. This is the first report showing an alternative autophagic pathway independent of Atg5 and Atg7, revealing the possibility to form autophagosomes from derived from the trans-Golgi and late endosomes.
    • (2009) Nature , vol.461 , pp. 654-658
    • Nishida, Y.1    Arakawa, S.2    Fujitani, K.3    Yamaguchi, H.4    Mizuta, T.5    Kanaseki, T.6    Komatsu, M.7    Otsu, K.8    Tsujimoto, Y.9    Shimizu, S.10
  • 82
    • 34548037901 scopus 로고    scopus 로고
    • Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium
    • Hoyer-Hansen M., and Jaattela M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium. Cell Death Differ 14 (2007) 1576-1582
    • (2007) Cell Death Differ , vol.14 , pp. 1576-1582
    • Hoyer-Hansen, M.1    Jaattela, M.2
  • 83
    • 34249668329 scopus 로고    scopus 로고
    • Eating the endoplasmic reticulum: quality control by autophagy
    • Yorimitsu T., and Klionsky D.J. Eating the endoplasmic reticulum: quality control by autophagy. Trends Cell Biol 17 (2007) 279-285
    • (2007) Trends Cell Biol , vol.17 , pp. 279-285
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 84
    • 65749114284 scopus 로고    scopus 로고
    • Macroautophagy in immunity and tolerance
    • Gannage M., and Munz C. Macroautophagy in immunity and tolerance. Traffic 10 (2009) 615-620
    • (2009) Traffic , vol.10 , pp. 615-620
    • Gannage, M.1    Munz, C.2
  • 85
    • 65249108735 scopus 로고    scopus 로고
    • Autophagy genes in immunity
    • Virgin H.W., and Levine B. Autophagy genes in immunity. Nat Immunol 10 (2009) 461-470
    • (2009) Nat Immunol , vol.10 , pp. 461-470
    • Virgin, H.W.1    Levine, B.2
  • 86
    • 18644375874 scopus 로고    scopus 로고
    • In vivo depletion of CD11c(+) dendritic cells abrogates priming of CD8(+) T cells by exogenous cell-associated antigens
    • Jung S., Unutmaz D., Wong P., Sano G., De los Santos K., Sparwasser T., Wu S., Vuthoori S., Ko K., Zavala F., et al. In vivo depletion of CD11c(+) dendritic cells abrogates priming of CD8(+) T cells by exogenous cell-associated antigens. Immunity 17 (2002) 211-220
    • (2002) Immunity , vol.17 , pp. 211-220
    • Jung, S.1    Unutmaz, D.2    Wong, P.3    Sano, G.4    De los Santos, K.5    Sparwasser, T.6    Wu, S.7    Vuthoori, S.8    Ko, K.9    Zavala, F.10
  • 87
    • 51549116148 scopus 로고    scopus 로고
    • Antigen persistence is required for dendritic cell licensing and CD8+ T cell cross-priming
    • The authors point to a key role for antigen persistence to allow multiple DC-T cell engagements for efficient cross-priming in vivo.
    • Jusforgues-Saklani H., Uhl M., Blachere N., Lemaitre F., Lantz O., Bousso P., Braun D., Moon J.J., and Albert M.L. Antigen persistence is required for dendritic cell licensing and CD8+ T cell cross-priming. J Immunol 181 (2008) 3067-3076. The authors point to a key role for antigen persistence to allow multiple DC-T cell engagements for efficient cross-priming in vivo.
    • (2008) J Immunol , vol.181 , pp. 3067-3076
    • Jusforgues-Saklani, H.1    Uhl, M.2    Blachere, N.3    Lemaitre, F.4    Lantz, O.5    Bousso, P.6    Braun, D.7    Moon, J.J.8    Albert, M.L.9
  • 88
    • 0032482274 scopus 로고    scopus 로고
    • Licence to kill [news; comment]
    • Lanzavecchia A:, and Immunology. Licence to kill [news; comment]. Nature 393 (1998) 413-414
    • (1998) Nature , vol.393 , pp. 413-414
    • Lanzavecchia A1    Immunology2
  • 89
    • 0036293726 scopus 로고    scopus 로고
    • An innate sense of danger
    • Matzinger P. An innate sense of danger. Ann N Y Acad Sci 961 (2002) 341-342
    • (2002) Ann N Y Acad Sci , vol.961 , pp. 341-342
    • Matzinger, P.1
  • 90
    • 33748848754 scopus 로고    scopus 로고
    • On regulation of phagosome maturation and antigen presentation
    • Blander J.M., and Medzhitov R. On regulation of phagosome maturation and antigen presentation. Nat Immunol 7 (2006) 1029-1035
    • (2006) Nat Immunol , vol.7 , pp. 1029-1035
    • Blander, J.M.1    Medzhitov, R.2
  • 91
    • 2942627626 scopus 로고    scopus 로고
    • Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses
    • Seong S.Y., and Matzinger P. Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses. Nat Rev Immunol 4 (2004) 469-478
    • (2004) Nat Rev Immunol , vol.4 , pp. 469-478
    • Seong, S.Y.1    Matzinger, P.2
  • 92
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis
    • Matsuyama S., Llopis J., Deveraux Q.L., Tsien R.Y., and Reed J.C. Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat Cell Biol 2 (2000) 318-325
    • (2000) Nat Cell Biol , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 93
    • 0034523187 scopus 로고    scopus 로고
    • Mitochondria-dependent apoptosis and cellular pH regulation
    • Matsuyama S., and Reed J.C. Mitochondria-dependent apoptosis and cellular pH regulation. Cell Death Differ 7 (2000) 1155-1165
    • (2000) Cell Death Differ , vol.7 , pp. 1155-1165
    • Matsuyama, S.1    Reed, J.C.2
  • 94
    • 4544246352 scopus 로고    scopus 로고
    • Alterations of intracellular pH homeostasis in apoptosis: origins and roles
    • Lagadic-Gossmann D., Huc L., and Lecureur V. Alterations of intracellular pH homeostasis in apoptosis: origins and roles. Cell Death Differ 11 (2004) 953-961
    • (2004) Cell Death Differ , vol.11 , pp. 953-961
    • Lagadic-Gossmann, D.1    Huc, L.2    Lecureur, V.3
  • 95
    • 36849094070 scopus 로고    scopus 로고
    • Cross-presentation of caspase-cleaved apoptotic self antigens in HIV infection
    • The authors show that caspase substrates can be cross-presented by DCs.
    • Rawson P.M., Molette C., Videtta M., Altieri L., Franceschini D., Donato T., Finocchi L., Propato A., Paroli M., Meloni F., et al. Cross-presentation of caspase-cleaved apoptotic self antigens in HIV infection. Nat Med 13 (2007) 1431-1439. The authors show that caspase substrates can be cross-presented by DCs.
    • (2007) Nat Med , vol.13 , pp. 1431-1439
    • Rawson, P.M.1    Molette, C.2    Videtta, M.3    Altieri, L.4    Franceschini, D.5    Donato, T.6    Finocchi, L.7    Propato, A.8    Paroli, M.9    Meloni, F.10
  • 96
    • 33846224369 scopus 로고    scopus 로고
    • Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes
    • This is the first paper reporting a role for autophagy in antigen processing for MHC class II peptide presentation.
    • Schmid D., Pypaert M., and Munz C. Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes. Immunity 26 (2007) 79-92. This is the first paper reporting a role for autophagy in antigen processing for MHC class II peptide presentation.
    • (2007) Immunity , vol.26 , pp. 79-92
    • Schmid, D.1    Pypaert, M.2    Munz, C.3
  • 97
    • 33646340673 scopus 로고    scopus 로고
    • Autophagy and antigen presentation
    • Munz C. Autophagy and antigen presentation. Cell Microbiol 8 (2006) 891-898
    • (2006) Cell Microbiol , vol.8 , pp. 891-898
    • Munz, C.1
  • 98
    • 67549117101 scopus 로고    scopus 로고
    • Autophagy within the antigen donor cell facilitates efficient antigen cross-priming of virus-specific CD8(+) T cells
    • This is the first paper pointing to a role for autophagy in the dying cell for viral antigen cross-priming in vivo.
    • Uhl M., Kepp O., Jusforgues-Saklani H., Vicencio J.M., Kroemer G., and Albert M.L. Autophagy within the antigen donor cell facilitates efficient antigen cross-priming of virus-specific CD8(+) T cells. Cell Death Differ (2009). This is the first paper pointing to a role for autophagy in the dying cell for viral antigen cross-priming in vivo.
    • (2009) Cell Death Differ
    • Uhl, M.1    Kepp, O.2    Jusforgues-Saklani, H.3    Vicencio, J.M.4    Kroemer, G.5    Albert, M.L.6
  • 99
    • 52049102433 scopus 로고    scopus 로고
    • Efficient cross-presentation depends on autophagy in tumor cells
    • This is the first paper pointing to a role for autophagy in the dying cell for tumor antigen cross-presentation.
    • Li Y., Wang L.X., Yang G., Hao F., Urba W.J., and Hu H.M. Efficient cross-presentation depends on autophagy in tumor cells. Cancer Res 68 (2008) 6889-6895. This is the first paper pointing to a role for autophagy in the dying cell for tumor antigen cross-presentation.
    • (2008) Cancer Res , vol.68 , pp. 6889-6895
    • Li, Y.1    Wang, L.X.2    Yang, G.3    Hao, F.4    Urba, W.J.5    Hu, H.M.6
  • 100
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • The authors suggest for the first time the ER origin of autophagosomal membranes.
    • Axe E.L., Walker S.A., Manifava M., Chandra P., Roderick H.L., Habermann A., Griffiths G., and Ktistakis N.T. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 182 (2008) 685-701. The authors suggest for the first time the ER origin of autophagosomal membranes.
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 101
    • 33750341482 scopus 로고    scopus 로고
    • Dendritic cells cross-dressed with peptide MHC class I complexes prime CD8+ T cells
    • Dolan B.P., Gibbs Jr. K.D., and Ostrand-Rosenberg S. Dendritic cells cross-dressed with peptide MHC class I complexes prime CD8+ T cells. J Immunol 177 (2006) 6018-6024
    • (2006) J Immunol , vol.177 , pp. 6018-6024
    • Dolan, B.P.1    Gibbs Jr., K.D.2    Ostrand-Rosenberg, S.3
  • 102
    • 2942666042 scopus 로고    scopus 로고
    • CD8+ T cells maintain tolerance to myelin basic protein by 'epitope theft'
    • Perchellet A., Stromnes I., Pang J.M., and Goverman J. CD8+ T cells maintain tolerance to myelin basic protein by 'epitope theft'. Nat Immunol 5 (2004) 606-614
    • (2004) Nat Immunol , vol.5 , pp. 606-614
    • Perchellet, A.1    Stromnes, I.2    Pang, J.M.3    Goverman, J.4
  • 103
    • 69449090071 scopus 로고    scopus 로고
    • A novel link between autophagy and the ubiquitin-proteasome system
    • Korolchuk V.I., Menzies F.M., and Rubinsztein D.C. A novel link between autophagy and the ubiquitin-proteasome system. Autophagy 5 (2009) 862-863
    • (2009) Autophagy , vol.5 , pp. 862-863
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 104
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • These two papers identify p62 as the key molecule interconnecting the proteasomal and autophagic pathways.
    • Korolchuk V.I., Mansilla A., Menzies F.M., and Rubinsztein D.C. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 33 (2009) 517-527. These two papers identify p62 as the key molecule interconnecting the proteasomal and autophagic pathways.
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 106
    • 0031811949 scopus 로고    scopus 로고
    • Emerging infections: an evolutionary perspective
    • A succinct and provocative articulation of the selective pressures at work during evolution.
    • Lederberg J. Emerging infections: an evolutionary perspective. Emerg Infect Dis 4 (1998) 366-371. A succinct and provocative articulation of the selective pressures at work during evolution.
    • (1998) Emerg Infect Dis , vol.4 , pp. 366-371
    • Lederberg, J.1
  • 108
    • 26244439658 scopus 로고    scopus 로고
    • Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond
    • Lilley B.N., and Ploegh H.L. Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond. Immunol Rev 207 (2005) 126-144
    • (2005) Immunol Rev , vol.207 , pp. 126-144
    • Lilley, B.N.1    Ploegh, H.L.2
  • 109
    • 0141565119 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 induces rapid cell death and functional impairment of murine dendritic cells in vitro
    • Jones C.A., Fernandez M., Herc K., Bosnjak L., Miranda-Saksena M., Boadle R.A., and Cunningham A. Herpes simplex virus type 2 induces rapid cell death and functional impairment of murine dendritic cells in vitro. J Virol 77 (2003) 11139-11149
    • (2003) J Virol , vol.77 , pp. 11139-11149
    • Jones, C.A.1    Fernandez, M.2    Herc, K.3    Bosnjak, L.4    Miranda-Saksena, M.5    Boadle, R.A.6    Cunningham, A.7
  • 110
    • 0141789676 scopus 로고    scopus 로고
    • Human cytomegalovirus inhibits differentiation of monocytes into dendritic cells with the consequence of depressed immunological functions
    • Gredmark S., and Soderberg-Naucler C. Human cytomegalovirus inhibits differentiation of monocytes into dendritic cells with the consequence of depressed immunological functions. J Virol 77 (2003) 10943-10956
    • (2003) J Virol , vol.77 , pp. 10943-10956
    • Gredmark, S.1    Soderberg-Naucler, C.2
  • 111
    • 0030954837 scopus 로고    scopus 로고
    • Measles virus suppresses cell-mediated immunity by interfering with the survival and functions of dendritic and T cells
    • Fugier-Vivier I., Servet-Delprat C., Rivailler P., Rissoan M.C., Liu Y.J., and Rabourdin-Combe C. Measles virus suppresses cell-mediated immunity by interfering with the survival and functions of dendritic and T cells. J Exp Med 186 (1997) 813-823
    • (1997) J Exp Med , vol.186 , pp. 813-823
    • Fugier-Vivier, I.1    Servet-Delprat, C.2    Rivailler, P.3    Rissoan, M.C.4    Liu, Y.J.5    Rabourdin-Combe, C.6
  • 112
    • 33645065882 scopus 로고    scopus 로고
    • Insights into the mechanisms of CMV-mediated interference with cellular apoptosis
    • Andoniou C.E., and Degli-Esposti M.A. Insights into the mechanisms of CMV-mediated interference with cellular apoptosis. Immunol Cell Biol 84 (2006) 99-106
    • (2006) Immunol Cell Biol , vol.84 , pp. 99-106
    • Andoniou, C.E.1    Degli-Esposti, M.A.2
  • 113
    • 33751398479 scopus 로고    scopus 로고
    • Modulation of apoptosis by human papillomavirus (HPV) oncoproteins
    • Garnett T.O., and Duerksen-Hughes P.J. Modulation of apoptosis by human papillomavirus (HPV) oncoproteins. Arch Virol 151 (2006) 2321-2335
    • (2006) Arch Virol , vol.151 , pp. 2321-2335
    • Garnett, T.O.1    Duerksen-Hughes, P.J.2
  • 114
    • 41449101843 scopus 로고    scopus 로고
    • Viral evasion of autophagy
    • Orvedahl A., and Levine B. Viral evasion of autophagy. Autophagy 4 (2008) 280-285
    • (2008) Autophagy , vol.4 , pp. 280-285
    • Orvedahl, A.1    Levine, B.2
  • 115
    • 36048964024 scopus 로고    scopus 로고
    • Analysis of the role of autophagy in replication of herpes simplex virus in cell culture
    • Alexander D.E., Ward S.L., Mizushima N., Levine B., and Leib D.A. Analysis of the role of autophagy in replication of herpes simplex virus in cell culture. J Virol 81 (2007) 12128-12134
    • (2007) J Virol , vol.81 , pp. 12128-12134
    • Alexander, D.E.1    Ward, S.L.2    Mizushima, N.3    Levine, B.4    Leib, D.A.5
  • 117
    • 33947715151 scopus 로고    scopus 로고
    • HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein
    • The authors report ICP34.5-mediated autophagy inhibition by HSV-1, providing the first example of viral interference with autophagy to evade immune responses.
    • Orvedahl A., Alexander D., Talloczy Z., Sun Q., Wei Y., Zhang W., Burns D., Leib D.A., and Levine B. HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein. Cell Host Microbe 1 (2007) 23-35. The authors report ICP34.5-mediated autophagy inhibition by HSV-1, providing the first example of viral interference with autophagy to evade immune responses.
    • (2007) Cell Host Microbe , vol.1 , pp. 23-35
    • Orvedahl, A.1    Alexander, D.2    Talloczy, Z.3    Sun, Q.4    Wei, Y.5    Zhang, W.6    Burns, D.7    Leib, D.A.8    Levine, B.9
  • 118
    • 33947732765 scopus 로고    scopus 로고
    • Viral evasion of autophagy
    • Munz C. Viral evasion of autophagy. Cell Host Microbe 1 (2007) 9-11
    • (2007) Cell Host Microbe , vol.1 , pp. 9-11
    • Munz, C.1
  • 119
    • 59849116269 scopus 로고    scopus 로고
    • Contribution of direct and cross-presentation to CTL immunity against herpes simplex virus 1
    • Jirmo A.C., Nagel C.H., Bohnen C., Sodeik B., and Behrens G.M. Contribution of direct and cross-presentation to CTL immunity against herpes simplex virus 1. J Immunol 182 (2009) 283-292
    • (2009) J Immunol , vol.182 , pp. 283-292
    • Jirmo, A.C.1    Nagel, C.H.2    Bohnen, C.3    Sodeik, B.4    Behrens, G.M.5
  • 121
    • 72649105081 scopus 로고    scopus 로고
    • Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes
    • The authors report M2-mediated interference of autophagosome fusion with lysosomes by influenza A, providing an important example of viral interference for the decision making of the type of death triggered by viral infection.
    • Gannage M., Dormann D., Albrecht R., Dengjel J., Torossi T., Ramer P.C., Lee M., Strowig T., Arrey F., Conenello G., et al. Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes. Cell Host Microbe 6 (2009) 367-380. The authors report M2-mediated interference of autophagosome fusion with lysosomes by influenza A, providing an important example of viral interference for the decision making of the type of death triggered by viral infection.
    • (2009) Cell Host Microbe , vol.6 , pp. 367-380
    • Gannage, M.1    Dormann, D.2    Albrecht, R.3    Dengjel, J.4    Torossi, T.5    Ramer, P.C.6    Lee, M.7    Strowig, T.8    Arrey, F.9    Conenello, G.10
  • 125
    • 0029893702 scopus 로고    scopus 로고
    • The origin of programmed cell death [see comments]
    • Ameisen J.C. The origin of programmed cell death [see comments]. Science 272 (1996) 1278-1279
    • (1996) Science , vol.272 , pp. 1278-1279
    • Ameisen, J.C.1
  • 126
    • 0036311492 scopus 로고    scopus 로고
    • On the origin, evolution, and nature of programmed cell death: a timeline of four billion years
    • Ameisen J.C. On the origin, evolution, and nature of programmed cell death: a timeline of four billion years. Cell Death Differ 9 (2002) 367-393
    • (2002) Cell Death Differ , vol.9 , pp. 367-393
    • Ameisen, J.C.1
  • 127
    • 0033539017 scopus 로고    scopus 로고
    • Identification of caspases and apoptosis in the simple metazoan Hydra
    • Cikala M., Wilm B., Hobmayer E., Bottger A., and David C.N. Identification of caspases and apoptosis in the simple metazoan Hydra. Curr Biol 9 (1999) 959-962
    • (1999) Curr Biol , vol.9 , pp. 959-962
    • Cikala, M.1    Wilm, B.2    Hobmayer, E.3    Bottger, A.4    David, C.N.5
  • 128
    • 0021468999 scopus 로고
    • Growth regulation in Hydra: relationship between epithelial cell cycle length and growth rate
    • Bosch T.C., and David C.N. Growth regulation in Hydra: relationship between epithelial cell cycle length and growth rate. Dev Biol 104 (1984) 161-171
    • (1984) Dev Biol , vol.104 , pp. 161-171
    • Bosch, T.C.1    David, C.N.2
  • 129
    • 5444236546 scopus 로고    scopus 로고
    • Uth1p: a yeast mitochondrial protein at the crossroads of stress, degradation and cell death
    • Camougrand N., Kissova I., Velours G., and Manon S. Uth1p: a yeast mitochondrial protein at the crossroads of stress, degradation and cell death. FEMS Yeast Res 5 (2004) 133-140
    • (2004) FEMS Yeast Res , vol.5 , pp. 133-140
    • Camougrand, N.1    Kissova, I.2    Velours, G.3    Manon, S.4
  • 130
    • 69349088740 scopus 로고    scopus 로고
    • Autophagy in Hydra: a response to starvation and stress in early animal evolution
    • Chera S., Buzgariu W., Ghila L., and Galliot B. Autophagy in Hydra: a response to starvation and stress in early animal evolution. Biochim Biophys Acta 1793 (2009) 1432-1443
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1432-1443
    • Chera, S.1    Buzgariu, W.2    Ghila, L.3    Galliot, B.4


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