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Volumn 6, Issue , 2016, Pages

Lipid peroxidation causes endosomal antigen release for cross-presentation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOCOPHEROL; CYBB PROTEIN, HUMAN; HLA ANTIGEN CLASS 1; MEMBRANE PROTEIN; PHOTOSENSITIZING AGENT; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SCAVENGER;

EID: 84959230147     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep22064     Document Type: Article
Times cited : (119)

References (65)
  • 2
    • 84890407875 scopus 로고    scopus 로고
    • An updated view of the intracellular mechanisms regulating cross-presentation
    • Nair-Gupta, P., & Blander, J. M. An updated view of the intracellular mechanisms regulating cross-presentation. Front. Immunol. 4, 401 (2013
    • (2013) Front. Immunol , vol.4 , pp. 401
    • Nair-Gupta, P.1    Blander, J.M.2
  • 3
    • 48749092592 scopus 로고    scopus 로고
    • The known unknowns of antigen processing and presentation
    • Vyas, J. M., Van der Veen, A. G., & Ploegh, H. L. The known unknowns of antigen processing and presentation. Nat. Rev. Immunol. 8, 607-618 (2008
    • (2008) Nat. Rev. Immunol , vol.8 , pp. 607-618
    • Vyas, J.M.1    Van Der Veen, A.G.2    Ploegh, H.L.3
  • 4
    • 83255188884 scopus 로고    scopus 로고
    • Sec22b regulates phagosomal maturation and antigen crosspresentation by dendritic cells
    • Cebrian, I., et al. Sec22b regulates phagosomal maturation and antigen crosspresentation by dendritic cells. Cell 147, 1355-1368 (2011
    • (2011) Cell , vol.147 , pp. 1355-1368
    • Cebrian, I.1
  • 5
    • 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., et al. Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells. J. Exp. Med. 206, 399-410 (2009
    • (2009) J. Exp. Med , vol.206 , pp. 399-410
    • Goldszmid, R.S.1
  • 6
    • 33749522738 scopus 로고    scopus 로고
    • A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
    • Ackerman, A. L., Giodini, A., & Cresswell, P A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells. Immunity 25, 607-617 (2006
    • (2006) Immunity , vol.25 , pp. 607-617
    • Ackerman, A.L.1    Giodini, A.2    Cresswell, P.3
  • 7
    • 12444339508 scopus 로고    scopus 로고
    • Exogenous antigens are processed through the endoplasmic reticulumassociated degradation (ERAD) in cross-presentation by dendritic cells
    • Imai, J., Hasegawa, H., Maruya, M., Koyasu, S., & Yahara, I. Exogenous antigens are processed through the endoplasmic reticulumassociated degradation (ERAD) in cross-presentation by dendritic cells. Int. Immunol. 17, 45-53 (2005
    • (2005) Int. Immunol , vol.17 , pp. 45-53
    • Imai, J.1    Hasegawa, H.2    Maruya, M.3    Koyasu, S.4    Yahara, I.5
  • 8
    • 84929710209 scopus 로고    scopus 로고
    • The translocon protein Sec61 mediates antigen transport from endosomes in the cytosol for cross-presentation to CD8(+ ) T cells
    • Zehner, M., et al. The translocon protein Sec61 mediates antigen transport from endosomes in the cytosol for cross-presentation to CD8(+ ) T cells. Immunity 42, 850-863 (2015
    • (2015) Immunity , vol.42 , pp. 850-863
    • Zehner, M.1
  • 9
    • 0029149603 scopus 로고
    • Major histocompatibility complex class i presentation of peptides derived from soluble exogenous antigen by a subset of cells engaged in phagocytosis
    • Reis e Sousa, C., & Germain & R. N. Major histocompatibility complex class I presentation of peptides derived from soluble exogenous antigen by a subset of cells engaged in phagocytosis. J. Exp. Med. 182, 841-851 (1995
    • (1995) J. Exp. Med , vol.182 , pp. 841-851
    • Reis, E.1    Sousa, C.2    Germain, R.N.3
  • 10
    • 33947538274 scopus 로고    scopus 로고
    • Rab27a regulates phagosomal pH and NADPH oxidase recruitment to dendritic cell phagosomes
    • Jancic, C., et al. Rab27a regulates phagosomal pH and NADPH oxidase recruitment to dendritic cell phagosomes. Nat. Cell Biol. 9, 367-378 (2007
    • (2007) Nat. Cell Biol , vol.9 , pp. 367-378
    • Jancic, C.1
  • 11
    • 33745825951 scopus 로고    scopus 로고
    • NOX2 controls phagosomal pH to regulate antigen processing during crosspresentation by dendritic cells
    • Savina, A., et al. NOX2 controls phagosomal pH to regulate antigen processing during crosspresentation by dendritic cells. Cell 126, 205-218 (2006
    • (2006) Cell , vol.126 , pp. 205-218
    • Savina, A.1
  • 12
    • 84872474723 scopus 로고    scopus 로고
    • Reactive oxygen species production in the phagosome: Impact on antigen presentation in dendritic cells
    • Kotsias, F., Hoffmann, E., Amigorena, S., & Savina, A. Reactive oxygen species production in the phagosome: impact on antigen presentation in dendritic cells. Antioxid. Redox Sign. 18, 714-729 (2013
    • (2013) Antioxid. Redox Sign , vol.18 , pp. 714-729
    • Kotsias, F.1    Hoffmann, E.2    Amigorena, S.3    Savina, A.4
  • 13
    • 58149388349 scopus 로고    scopus 로고
    • NADPH oxidase controls phagosomal pH and antigen cross-presentation in human dendritic cells
    • Mantegazza, A. R., et al. NADPH oxidase controls phagosomal pH and antigen cross-presentation in human dendritic cells. Blood 112, 4712-4722 (2008
    • (2008) Blood , vol.112 , pp. 4712-4722
    • Mantegazza, A.R.1
  • 14
    • 84923104227 scopus 로고    scopus 로고
    • Redirecting soluble antigen for MHC class i cross-presentation during phagocytosis
    • Hari, A., et al. Redirecting soluble antigen for MHC class I cross-presentation during phagocytosis. Eur. J. Immunol. 45, 383-395 (2015
    • (2015) Eur. J. Immunol , vol.45 , pp. 383-395
    • Hari, A.1
  • 15
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K., & Krause, K. H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87, 245-313 (2007
    • (2007) Physiol. Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 16
    • 84857053387 scopus 로고    scopus 로고
    • Phagosomal proteolysis in dendritic cells is modulated by NADPH oxidase in a pH-independent manner
    • Rybicka, J. M., Balce, D. R., Chaudhuri, S., Allan, E. R., & Yates, R. M. Phagosomal proteolysis in dendritic cells is modulated by NADPH oxidase in a pH-independent manner. EMBO J. 31, 932-944 (2012
    • (2012) EMBO J. , vol.31 , pp. 932-944
    • Rybicka, J.M.1    Balce, D.R.2    Chaudhuri, S.3    Allan, E.R.4    Yates, R.M.5
  • 17
    • 84901257403 scopus 로고    scopus 로고
    • NADPH oxidase modifies patterns of MHC class II-restricted epitopic repertoires through redox control of antigen processing
    • Allan, E. R., et al. NADPH oxidase modifies patterns of MHC class II-restricted epitopic repertoires through redox control of antigen processing. J. Immunol. 192, 4989-5001 (2014
    • (2014) J. Immunol , vol.192 , pp. 4989-5001
    • Allan, E.R.1
  • 18
    • 0031821531 scopus 로고    scopus 로고
    • Lipid hydroperoxide generation, turnover, and effector action in biological systems
    • Girotti, A. W. Lipid hydroperoxide generation, turnover, and effector action in biological systems. J. Lipid Res. 39, 1529-1542 (1998
    • (1998) J. Lipid Res , vol.39 , pp. 1529-1542
    • Girotti, A.W.1
  • 19
    • 0014832036 scopus 로고
    • Solubility of gases in human red blood cell ghosts
    • Power, G. G., & Stegall, H. Solubility of gases in human red blood cell ghosts. J. Appl. Physiol. 29, 145-149 (1970
    • (1970) J. Appl. Physiol , vol.29 , pp. 145-149
    • Power, G.G.1    Stegall, H.2
  • 20
    • 75349100762 scopus 로고    scopus 로고
    • Massive oxidation of phospholipid membranes leads to pore creation and bilayer disintegration
    • Cwiklik, L., & Jungwirth, P. Massive oxidation of phospholipid membranes leads to pore creation and bilayer disintegration. Chem. Phys. Lett. 486, 99-103 (2010
    • (2010) Chem. Phys. Lett , vol.486 , pp. 99-103
    • Cwiklik, L.1    Jungwirth, P.2
  • 21
    • 0015155170 scopus 로고
    • Relation of lipid peroxidation to loss of cations trapped in liposomes
    • Leibowitz, M. E., & Johnson, M. C. Relation of lipid peroxidation to loss of cations trapped in liposomes. J. Lipid Res. 12, 662-670 (1971
    • (1971) J. Lipid Res , vol.12 , pp. 662-670
    • Leibowitz, M.E.1    Johnson, M.C.2
  • 22
    • 37349055140 scopus 로고    scopus 로고
    • Effect of lipid peroxidation on the properties of lipid bilayers: A molecular dynamics study
    • Wong-Ekkabut, J., et al. Effect of lipid peroxidation on the properties of lipid bilayers: a molecular dynamics study. Biophys. J. 93, 4225-4236 (2007
    • (2007) Biophys. J. , vol.93 , pp. 4225-4236
    • Wong-Ekkabut, J.1
  • 23
    • 77951168054 scopus 로고    scopus 로고
    • Breaking down the barriers: SiRNA delivery and endosome escape
    • Dominska, M., & Dykxhoorn, D. M. Breaking down the barriers: siRNA delivery and endosome escape. J. Cell Sci. 123, 1183-1189 (2010
    • (2010) J. Cell Sci , vol.123 , pp. 1183-1189
    • Dominska, M.1    Dykxhoorn, D.M.2
  • 24
    • 0033559618 scopus 로고    scopus 로고
    • Photochemical internalization: A novel technology for delivery of macromolecules into cytosol
    • Berg, K., et al. Photochemical internalization: a novel technology for delivery of macromolecules into cytosol. Cancer Res. 59, 1180-1183 (1999
    • (1999) Cancer Res , vol.59 , pp. 1180-1183
    • Berg, K.1
  • 25
    • 67349230238 scopus 로고    scopus 로고
    • Cellular siRNA delivery using cell-penetrating peptides modified for endosomal escape
    • Endoh, T., & Ohtsuki, T. Cellular siRNA delivery using cell-penetrating peptides modified for endosomal escape. Adv. Drug Deliver. Rev. 61, 704-709 (2009
    • (2009) Adv. Drug Deliver. Rev , vol.61 , pp. 704-709
    • Endoh, T.1    Ohtsuki, T.2
  • 26
    • 78649529393 scopus 로고    scopus 로고
    • Photochemical internalization provides time-And space-controlled endolysosomal escape of therapeutic molecules
    • Selbo, P. K., et al. Photochemical internalization provides time-And space-controlled endolysosomal escape of therapeutic molecules. J. Control. Release 148, 2-12 (2010
    • (2010) J. Control. Release , vol.148 , pp. 2-12
    • Selbo, P.K.1
  • 27
    • 0023821578 scopus 로고
    • Introduction of soluble protein into the class i pathway of antigen processing and presentation
    • Moore, M. W., Carbone, F. R., & Bevan, M. J. Introduction of soluble protein into the class I pathway of antigen processing and presentation. Cell 54, 777-785 (1988
    • (1988) Cell , vol.54 , pp. 777-785
    • Moore, M.W.1    Carbone, F.R.2    Bevan, M.J.3
  • 28
    • 0033592871 scopus 로고    scopus 로고
    • Mycobacterial infection of macrophages results in membrane-permeable phagosomes
    • Teitelbaum, R., et al. Mycobacterial infection of macrophages results in membrane-permeable phagosomes. Proc. Natl. Acad. Sci. USA 96, 15190-15195 (1999
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 15190-15195
    • Teitelbaum, R.1
  • 29
    • 59849086158 scopus 로고    scopus 로고
    • Macrophages generate reactive oxygen species in response to minimally oxidized low-density lipoprotein: Toll-like receptor 4-And spleen tyrosine kinase-dependent activation of NADPH oxidase 2
    • Bae, Y. S., et al. Macrophages generate reactive oxygen species in response to minimally oxidized low-density lipoprotein: toll-like receptor 4-And spleen tyrosine kinase-dependent activation of NADPH oxidase 2. Circ. Res. 104, 210-218 (2009
    • (2009) Circ. Res , vol.104 , pp. 210-218
    • Bae, Y.S.1
  • 30
    • 84863959315 scopus 로고    scopus 로고
    • Lipopolysaccharide-sensitive H+ current in dendritic cells
    • Szteyn, K., Yang, W., Schmid, E., Lang, F., & Shumilina, E. Lipopolysaccharide-sensitive H+ current in dendritic cells. Am. J. Physiol. 303, C204-212 (2012
    • (2012) Am. J. Physiol , vol.303 , pp. C204-212
    • Szteyn, K.1    Yang, W.2    Schmid, E.3    Lang, F.4    Shumilina, E.5
  • 31
    • 84884980535 scopus 로고    scopus 로고
    • Optimization of the C11-BODIPY581/591 dye for the determination of lipid oxidation in chlamydomonas reinhardtii by flow cytometry
    • Cheloni, G., & Slaveykova, V. I. Optimization of the C11-BODIPY581/591 dye for the determination of lipid oxidation in chlamydomonas reinhardtii by flow cytometry. Cytometry A 83, 952-961 (2013
    • (2013) Cytometry A , vol.83 , pp. 952-961
    • Cheloni, G.1    Slaveykova, V.I.2
  • 32
    • 3042527868 scopus 로고    scopus 로고
    • The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems
    • Cross, A. R., & Segal, A. W. The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems. Biochim. Biophys. Acta 1657, 1-22 (2004
    • (2004) Biochim. Biophys. Acta , vol.1657 , pp. 1-22
    • Cross, A.R.1    Segal, A.W.2
  • 33
    • 84884168586 scopus 로고    scopus 로고
    • Probing lipid-protein adduction with alkynyl surrogates: Application to Smith-Lemli-Opitz syndrome
    • Windsor, K., et al. Probing lipid-protein adduction with alkynyl surrogates: application to Smith-Lemli-Opitz syndrome. J. Lipid Res. 54, 2842-2850 (2013
    • (2013) J. Lipid Res , vol.54 , pp. 2842-2850
    • Windsor, K.1
  • 34
    • 84455194883 scopus 로고    scopus 로고
    • Promotion of plasma membrane repair by Vitamin E
    • Howard, A. C., McNeil, A. K., & McNeil, P. L. Promotion of plasma membrane repair by vitamin E. Nat. Commun. 2, 597 (2011
    • (2011) Nat. Commun , vol.2 , pp. 597
    • Howard, A.C.1    McNeil, A.K.2    McNeil, P.L.3
  • 35
    • 42949156865 scopus 로고    scopus 로고
    • Selective suicide of cross-presenting CD8+ dendritic cells by cytochrome c injection shows functional heterogeneity within this subset
    • Lin, M. L., et al. Selective suicide of cross-presenting CD8+ dendritic cells by cytochrome c injection shows functional heterogeneity within this subset. Proc. Natl. Acad. Sci. USA 105, 3029-3034 (2008
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3029-3034
    • Lin, M.L.1
  • 36
    • 77954289641 scopus 로고    scopus 로고
    • Tracking the dynamic interplay between bacterial and host factors during pathogen-induced vacuole rupture in real time
    • Ray, K., et al. Tracking the dynamic interplay between bacterial and host factors during pathogen-induced vacuole rupture in real time. Cell. Microbiol. 12, 545-556 (2010
    • (2010) Cell. Microbiol , vol.12 , pp. 545-556
    • Ray, K.1
  • 37
    • 77954271859 scopus 로고    scopus 로고
    • Galectin-3, a marker for vacuole lysis by invasive pathogens
    • Paz, I., et al. Galectin-3, a marker for vacuole lysis by invasive pathogens. Cell. Microbiol. 12, 530-544 (2010
    • (2010) Cell. Microbiol , vol.12 , pp. 530-544
    • Paz, I.1
  • 38
    • 84928393912 scopus 로고    scopus 로고
    • Efficient intracellular delivery of native proteins
    • D?Astolfo, D. S., et al. Efficient intracellular delivery of native proteins. Cell 161, 674-690 (2015
    • (2015) Cell , vol.161 , pp. 674-690
    • D'Astolfo, D.S.1
  • 39
    • 84885723472 scopus 로고    scopus 로고
    • Dendritic cells process synthetic long peptides better than whole protein, improving antigen presentation and T-cell activation
    • Rosalia, R. A., et al. Dendritic cells process synthetic long peptides better than whole protein, improving antigen presentation and T-cell activation. Eur. J. Immunol. 43, 2554-2565 (2013
    • (2013) Eur. J. Immunol , vol.43 , pp. 2554-2565
    • Rosalia, R.A.1
  • 40
    • 84872469382 scopus 로고    scopus 로고
    • Human plasmacytoid dendritic cells efficiently cross-present exogenous Ags to CD8+ T cells despite lower Ag uptake than myeloid dendritic cell subsets
    • Tel, J., et al. Human plasmacytoid dendritic cells efficiently cross-present exogenous Ags to CD8+ T cells despite lower Ag uptake than myeloid dendritic cell subsets. Blood 121, 459-467 (2013
    • (2013) Blood , vol.121 , pp. 459-467
    • Tel, J.1
  • 41
    • 84880439539 scopus 로고    scopus 로고
    • Leishmania evades host immunity by inhibiting antigen cross-presentation through direct cleavage of the SNARE VAMP8
    • Matheoud, D., et al Leishmania evades host immunity by inhibiting antigen cross-presentation through direct cleavage of the SNARE VAMP8. Cell Host Microbe 14, 15-25 (2013
    • (2013) Cell Host Microbe , vol.14 , pp. 15-25
    • Matheoud, D.1
  • 42
    • 33846511593 scopus 로고    scopus 로고
    • Proteasome-independent major histocompatibility complex class i cross-presentation mediated by papaya mosaic virus-like particles leads to expansion of specific human T cells
    • Leclerc, D., et al. Proteasome-independent major histocompatibility complex class I cross-presentation mediated by papaya mosaic virus-like particles leads to expansion of specific human T cells. J. Virol. 81, 1319-1326 (2007
    • (2007) J. Virol , vol.81 , pp. 1319-1326
    • Leclerc, D.1
  • 43
    • 30544443562 scopus 로고    scopus 로고
    • A genetically encoded photosensitizer
    • Bulina, M. E., et al A genetically encoded photosensitizer. Nat. Biotechnol. 24, 95-99 (2006
    • (2006) Nat. Biotechnol , vol.24 , pp. 95-99
    • Bulina, M.E.1
  • 44
    • 84878878644 scopus 로고    scopus 로고
    • Mass spectrometry reveals changes in MHC i antigen presentation after lentivector expression of a gene regulation system
    • Vogel, R., et al. Mass spectrometry reveals changes in MHC I antigen presentation after lentivector expression of a gene regulation system. Mol. Ther. Nucleic Acids 2, e75 (2013
    • (2013) Mol. Ther. Nucleic Acids , vol.2 , pp. e75
    • Vogel, R.1
  • 45
    • 30744465074 scopus 로고    scopus 로고
    • Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation
    • Chapiro, J., et al. Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation. J. Immunol. 176, 1053-1061 (2006
    • (2006) J. Immunol , vol.176 , pp. 1053-1061
    • Chapiro, J.1
  • 46
    • 60549094959 scopus 로고    scopus 로고
    • Cross-presenting human gammadelta T cells induce robust CD8+ alphabeta T cell responses
    • Brandes, M., et al. Cross-presenting human gammadelta T cells induce robust CD8+ alphabeta T cell responses. Proc. Natl. Acad. Sci. USA 106, 2307-2312 (2009
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2307-2312
    • Brandes, M.1
  • 47
    • 84860544922 scopus 로고    scopus 로고
    • CD4(+ ) T cell vaccination overcomes defective cross-presentation of fungal antigens in a mouse model of chronic granulomatous disease
    • De Luca, A., et al. CD4(+ ) T cell vaccination overcomes defective cross-presentation of fungal antigens in a mouse model of chronic granulomatous disease. J. Clin. Invest. 122, 1816-1831 (2012
    • (2012) J. Clin. Invest , vol.122 , pp. 1816-1831
    • De Luca, A.1
  • 48
    • 44449148317 scopus 로고    scopus 로고
    • Inflammatory manifestations in chronic granulomatous disease (CGD
    • Rosenzweig, S. D. Inflammatory manifestations in chronic granulomatous disease (CGD). J. Clin. Immunol. 28 Suppl 1, S67-72 (2008
    • (2008) J. Clin. Immunol , vol.28 , pp. S67-72
    • Rosenzweig, S.D.1
  • 49
    • 84861468560 scopus 로고    scopus 로고
    • Cdc42-dependent activation of NADPH oxidase is involved in ethanol-induced neuronal oxidative stress
    • Wang, X., et al. Cdc42-dependent activation of NADPH oxidase is involved in ethanol-induced neuronal oxidative stress. PloS one 7, e38075 (2012
    • (2012) PloS One , vol.7 , pp. e38075
    • Wang, X.1
  • 50
    • 77951666702 scopus 로고    scopus 로고
    • Regulation of apoptosis-Associated lysosomal membrane permeabilization
    • Johansson, A. C., et al. Regulation of apoptosis-Associated lysosomal membrane permeabilization. Apoptosis 15, 527-540 (2010
    • (2010) Apoptosis , vol.15 , pp. 527-540
    • Johansson, A.C.1
  • 52
    • 35549008123 scopus 로고    scopus 로고
    • Neutrophils efficiently cross-prime naive T cells in vivo
    • Beauvillain, C., et al. Neutrophils efficiently cross-prime naive T cells in vivo. Blood 110, 2965-2973 (2007
    • (2007) Blood , vol.110 , pp. 2965-2973
    • Beauvillain, C.1
  • 53
    • 0037022671 scopus 로고    scopus 로고
    • Replication of Cryptococcus neoformans in macrophages is accompanied by phagosomal permeabilization and accumulation of vesicles containing polysaccharide in the cytoplasm
    • Tucker, S. C., & Casadevall, A. Replication of Cryptococcus neoformans in macrophages is accompanied by phagosomal permeabilization and accumulation of vesicles containing polysaccharide in the cytoplasm. Proc. Natl. Acad. Sci. USA 99, 3165-3170 (2002
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3165-3170
    • Tucker, S.C.1    Casadevall, A.2
  • 54
    • 79958765451 scopus 로고    scopus 로고
    • Alternative pathways for MHC class i presentation: A new function for autophagy
    • Chemali, M., Radtke, K., Desjardins, M., & English, L. Alternative pathways for MHC class I presentation: a new function for autophagy. Cell. Mol. Life Sci. 68, 1533-1541 (2011
    • (2011) Cell. Mol. Life Sci , vol.68 , pp. 1533-1541
    • Chemali, M.1    Radtke, K.2    Desjardins, M.3    English, L.4
  • 55
    • 65549094988 scopus 로고    scopus 로고
    • Activation of antibacterial autophagy by NADPH oxidases
    • Huang, J., et al. Activation of antibacterial autophagy by NADPH oxidases. Proc. Natl. Acad. Sci. USA 106, 6226-6231 (2009
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6226-6231
    • Huang, J.1
  • 56
    • 84890828734 scopus 로고    scopus 로고
    • Autophagy proteins stabilize pathogen-containing phagosomes for prolonged MHC II antigen processing
    • Romao, S., et al. Autophagy proteins stabilize pathogen-containing phagosomes for prolonged MHC II antigen processing. J. Cell Biol. 203, 757-766 (2013
    • (2013) J. Cell Biol , vol.203 , pp. 757-766
    • Romao, S.1
  • 57
    • 84882684320 scopus 로고    scopus 로고
    • The tumor microenvironment: Characterization, redox considerations, and novel approaches for reactive oxygen species-targeted gene therapy
    • Policastro, L. L., Ibanez, I. L., Notcovich, C., Duran, H. A., & Podhajcer, O. L. The tumor microenvironment: characterization, redox considerations, and novel approaches for reactive oxygen species-targeted gene therapy. Antioxid. Redox Sign. 19, 854-895 (2013
    • (2013) Antioxid. Redox Sign , vol.19 , pp. 854-895
    • Policastro, L.L.1    Ibanez, I.L.2    Notcovich, C.3    Duran, H.A.4    Podhajcer, O.L.5
  • 58
    • 0036911138 scopus 로고    scopus 로고
    • Hydrogen peroxide as second messenger in lymphocyte activation
    • Reth, M. Hydrogen peroxide as second messenger in lymphocyte activation. Nat. Immunol. 3, 1129-1134 (2002
    • (2002) Nat. Immunol , vol.3 , pp. 1129-1134
    • Reth, M.1
  • 59
    • 0042834309 scopus 로고    scopus 로고
    • Generation and function of reactive oxygen species in dendritic cells during antigen presentation
    • Matsue, H., et al. Generation and function of reactive oxygen species in dendritic cells during antigen presentation. J. Immunol. 171, 3010-3018 (2003
    • (2003) J. Immunol , vol.171 , pp. 3010-3018
    • Matsue, H.1
  • 60
    • 0036734814 scopus 로고    scopus 로고
    • Phenotypical and functional characterization of clinical grade dendritic cells
    • de Vries, I. J., et al. Phenotypical and functional characterization of clinical grade dendritic cells. J. Immunother. 25, 429-438 (2002
    • (2002) J. Immunother , vol.25 , pp. 429-438
    • De Vries, I.J.1
  • 61
    • 84877962878 scopus 로고    scopus 로고
    • Chloroquine modulates the fungal immune response in phagocytic cells from patients with chronic granulomatous disease
    • Henriet, S. S., et al. Chloroquine modulates the fungal immune response in phagocytic cells from patients with chronic granulomatous disease. J. Infect. Dis. 207, 1932-1939 (2013
    • (2013) J. Infect. Dis , vol.207 , pp. 1932-1939
    • Henriet, S.S.1
  • 62
    • 0026639652 scopus 로고
    • Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens
    • Karttunen, J., Sanderson, S., & Shastri, N. Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens. Proc. Natl. Acad. Sci. USA 89, 6020-6024 (1992
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6020-6024
    • Karttunen, J.1    Sanderson, S.2    Shastri, N.3
  • 63
    • 84896900563 scopus 로고    scopus 로고
    • Podosomes of dendritic cells facilitate antigen sampling
    • Baranov, M. V., et al. Podosomes of dendritic cells facilitate antigen sampling. J. Cell Sci. 127, 1052-1064 (2014
    • (2014) J. Cell Sci , vol.127 , pp. 1052-1064
    • Baranov, M.V.1
  • 64
    • 84938898581 scopus 로고    scopus 로고
    • Visualizing lipid-formulated siRNA release from endosomes and target gene knockdown
    • Wittrup, A., et al. Visualizing lipid-formulated siRNA release from endosomes and target gene knockdown. Nat. Biotechnol. 33, 870-876 (2015
    • (2015) Nat. Biotechnol , vol.33 , pp. 870-876
    • Wittrup, A.1
  • 65
    • 0142043428 scopus 로고    scopus 로고
    • Flexible and sensitive method to functionally validate tumorspecific receptors via activation of NFAT
    • Schaft, N., Lankiewicz, B., Gratama, J. W., Bolhuis, R. L., & Debets, R. Flexible and sensitive method to functionally validate tumorspecific receptors via activation of NFAT. J. Immunol. Methods 280, 13-24 (2003
    • (2003) J. Immunol. Methods , vol.280 , pp. 13-24
    • Schaft, N.1    Lankiewicz, B.2    Gratama, J.W.3    Bolhuis, R.L.4    Debets, R.5


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