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Volumn 4, Issue SEP, 2013, Pages

Autophagic clearance of bacterial pathogens: Molecular recognition of intracellular microorganisms

Author keywords

Autophagy; Intracellular pathogens; Phagocytosis; Recognition; Xenophagy

Indexed keywords

AUTOPHAGY PROTEIN 12; AUTOPHAGY PROTEIN 5; BECLIN 1; LIPOPOLYSACCHARIDE; LUNG RESISTANCE PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; OPTINEURIN; PEPTIDES AND PROTEINS; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BCL 2; PROTEIN KINASE B; TOLL LIKE RECEPTOR 4; UBIQUITIN CONJUGATING ENZYME; ULK COMPLEX; UNCLASSIFIED DRUG;

EID: 84896728489     PISSN: None     EISSN: 22352988     Source Type: Journal    
DOI: 10.3389/fcimb.2013.00054     Document Type: Review
Times cited : (64)

References (156)
  • 2
    • 80655134731 scopus 로고    scopus 로고
    • Autophagy stimulation by rapamycin suppresses lung inflammation and infection by Burkholderia cenocepacia in a model of cystic fibrosis
    • doi: 10.4161/auto.7.11.17660
    • Abdulrahman, B. A., Abu Khweek, A., Akhter, A., Caution, K., Kotrange, S., Abdelaziz, D. H. A., et al. (2011). Autophagy stimulation by rapamycin suppresses lung inflammation and infection by Burkholderia cenocepacia in a model of cystic fibrosis. Autophagy 7, 1359-1370. doi: 10.4161/auto.7.11.17660
    • (2011) Autophagy , vol.7 , pp. 1359-1370
    • Abdulrahman, B.A.1    Abu Khweek, A.2    Akhter, A.3    Caution, K.4    Kotrange, S.5    Abdelaziz, D.H.A.6
  • 3
    • 84877339040 scopus 로고    scopus 로고
    • The many uses of autophagosomes
    • doi: 10.4161/auto.24146
    • Amer, A. O. (2013). The many uses of autophagosomes. Autophagy 9, 633-634. doi: 10.4161/auto.24146
    • (2013) Autophagy , vol.9 , pp. 633-634
    • Amer, A.O.1
  • 4
    • 19644382161 scopus 로고    scopus 로고
    • Autophagy is an immediate macrophage response to Legionella pneumophila
    • doi: 10.1111/j.1462-5822.2005.00509.x
    • Amer, A. O., and Swanson, M. S. (2005). Autophagy is an immediate macrophage response to Legionella pneumophila. Cell. Microbiol. 7, 765-778. doi: 10.1111/j.1462-5822.2005.00509.x
    • (2005) Cell. Microbiol. , vol.7 , pp. 765-778
    • Amer, A.O.1    Swanson, M.S.2
  • 5
    • 0001211310 scopus 로고
    • Response of cultured macrophages to Mycobacterium tuberculosis, with observations on fusion of lysosomes with phagosomes
    • doi: 10.1084/jem.134.3.713
    • Armstrong, J. A., and Hart, P. D. (1971). Response of cultured macrophages to Mycobacterium tuberculosis, with observations on fusion of lysosomes with phagosomes. J. Exp. Med. 134, 713-740. doi: 10.1084/jem.134.3.713
    • (1971) J. Exp. Med. , vol.134 , pp. 713-740
    • Armstrong, J.A.1    Hart, P.D.2
  • 6
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • doi: 10.1083/jcb.200803137
    • Axe, E. L., Walker, S. A., Manifava, M., Chandra, P., Roderick, H. L., Habermann, A., et al. (2008). Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol. 182, 685-701. doi: 10.1083/jcb.200803137
    • (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
  • 7
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • doi: 10. 1016/S0002-9343(00)00481-2
    • Babior, B. M. (2000). Phagocytes and oxidative stress. Am. J. Med. 109, 33-44. doi: 10.1016/S0002-9343(00)00481-2
    • (2000) Am. J. Med. , vol.109 , pp. 33-44
    • Babior, B.M.1
  • 8
    • 62649088066 scopus 로고    scopus 로고
    • Characterization of a Coxiella burnetii ftsZ mutant generated by Himar1 transposon mutagenesis
    • doi: 10.1128/JB.01580-08
    • Beare, P. A., Howe, D., Cockrell, D. C., Omsland, A., Hansen, B., and Heinzen, R. A. (2009). Characterization of a Coxiella burnetii ftsZ mutant generated by Himar1 transposon mutagenesis. J. Bacteriol. 191, 1369-1381. doi: 10.1128/JB.01580-08
    • (2009) J. Bacteriol. , vol.191 , pp. 1369-1381
    • Beare, P.A.1    Howe, D.2    Cockrell, D.C.3    Omsland, A.4    Hansen, B.5    Heinzen, R.A.6
  • 9
    • 0034157346 scopus 로고    scopus 로고
    • Trafficking and release of mycobacterial lipids from infected macrophages
    • doi: 10.1034/j.1600-0854.2000.010306.x
    • Beatty, W. L., Rhoades, E. R., Ullrich, H. J., Chatterjee, D., Heuser, J. E., and Russell, D. G. (2000). Trafficking and release of mycobacterial lipids from infected macrophages. Traffic 1, 235-247. doi: 10.1034/j.1600-0854.2000.010306.x
    • (2000) Traffic , vol.1 , pp. 235-247
    • Beatty, W.L.1    Rhoades, E.R.2    Ullrich, H.J.3    Chatterjee, D.4    Heuser, J.E.5    Russell, D.G.6
  • 10
    • 0343517154 scopus 로고    scopus 로고
    • Salmonella maintains the integrity of its intracellular vacuole through the action of SifA
    • doi: 10.1093/emboj/19.13.3235
    • Beuzon, C. R., Meresse, S., Unsworth, K. E., Ruiz-Albert, J., Garvis, S., Waterman, S. R., et al. (2000). Salmonella maintains the integrity of its intracellular vacuole through the action of SifA. EMBO J. 19, 3235-3249. doi: 10.1093/emboj/19.13.3235
    • (2000) EMBO J , vol.19 , pp. 3235-3249
    • Beuzon, C.R.1    Meresse, S.2    Unsworth, K.E.3    Ruiz-Albert, J.4    Garvis, S.5    Waterman, S.R.6
  • 11
    • 33745818564 scopus 로고    scopus 로고
    • Autophagy recognizes intracellular Salmonella enterica serovar Typhimurium in damaged vacuoles
    • Birmingham, C. L., and Brumell, J. H. (2006). Autophagy recognizes intracellular Salmonella enterica serovar Typhimurium in damaged vacuoles. Autophagy 2, 156-158.
    • (2006) Autophagy , vol.2 , pp. 156-158
    • Birmingham, C.L.1    Brumell, J.H.2
  • 12
    • 34548067415 scopus 로고    scopus 로고
    • Listeria monocytogenes evades killing by autophagy during colonization of host cells
    • Birmingham, C. L., Canadien, V., Gouin, E., Troy, E. B., Yoshimori, T., Cossart, P., et al. (2007). Listeria monocytogenes evades killing by autophagy during colonization of host cells. Autophagy 3, 442-451.
    • (2007) Autophagy , vol.3 , pp. 442-451
    • Birmingham, C.L.1    Canadien, V.2    Gouin, E.3    Troy, E.B.4    Yoshimori, T.5    Cossart, P.6
  • 13
    • 12844253814 scopus 로고    scopus 로고
    • Salmonella-induced filament formation is a dynamic phenotype induced by rapidly replicating Salmonella enterica serovar typhimurium in epithelial cells
    • doi: 10.1128/IAI.73.2.1204-1208.2005
    • Birmingham, C. L., Jiang, X., Ohlson, M. B., Miller, S. I., and Brumell, J. H. (2005). Salmonella-induced filament formation is a dynamic phenotype induced by rapidly replicating Salmonella enterica serovar typhimurium in epithelial cells. Infect. Immun. 73, 1204-1208. doi: 10.1128/IAI.73.2.1204-1208.2005
    • (2005) Infect. Immun. , vol.73 , pp. 1204-1208
    • Birmingham, C.L.1    Jiang, X.2    Ohlson, M.B.3    Miller, S.I.4    Brumell, J.H.5
  • 14
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • doi: 10.1083/jcb.200507002
    • Bjorkoy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., et al. (2005). p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603-614. doi: 10.1083/jcb.200507002
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6
  • 15
    • 0033230438 scopus 로고    scopus 로고
    • The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes
    • doi: 10.1083/jcb.147.3.683
    • Blocker, A., Gounon, P., Larquet, E., Niebuhr, K., Cabiaux, V., Parsot, C., et al. (1999). The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 147, 683-693. doi: 10.1083/jcb.147.3.683
    • (1999) J. Cell Biol. , vol.147 , pp. 683-693
    • Blocker, A.1    Gounon, P.2    Larquet, E.3    Niebuhr, K.4    Cabiaux, V.5    Parsot, C.6
  • 16
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: insights into their function from structural similarities
    • doi: 10.1073/pnas.0535335100
    • Blocker, A., Komoriya, K., and Aizawa, S. (2003). Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Proc. Natl. Acad. Sci. U.S.A. 100, 3027-3030. doi: 10.1073/pnas.0535335100
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3027-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.3
  • 17
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signalling: a hard Akt to follow
    • doi: 10.1016/S0968-0004(01)01958-2
    • Brazil, D. P., and Hemmings, B. A. (2001). Ten years of protein kinase B signalling: a hard Akt to follow. Trends Biochem. Sci. 26, 657-664. doi: 10.1016/S0968-0004(01)01958-2
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 18
    • 0036300862 scopus 로고    scopus 로고
    • SifA, a type III secreted effector of Salmonella typhimurium, directs Salmonella-induced filament (Sif) formation along microtubules
    • doi: 10.1034/j.1600-0854.2002.30604.x
    • Brumell, J. H., Goosney, D. L., and Finlay, B. B. (2002). SifA, a type III secreted effector of Salmonella typhimurium, directs Salmonella-induced filament (Sif) formation along microtubules. Traffic 3, 407-415. doi: 10.1034/j.1600-0854.2002.30604.x
    • (2002) Traffic , vol.3 , pp. 407-415
    • Brumell, J.H.1    Goosney, D.L.2    Finlay, B.B.3
  • 19
    • 1242284149 scopus 로고    scopus 로고
    • Salmonella redirects phagosomal maturation
    • doi: 10.1016/j.mib.2003.12.005
    • Brumell, J. H., and Grinstein, S. (2004). Salmonella redirects phagosomal maturation. Curr. Opin. Microbiol. 7, 78-84. doi: 10.1016/j.mib.2003.12.005
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 78-84
    • Brumell, J.H.1    Grinstein, S.2
  • 20
    • 0033594472 scopus 로고    scopus 로고
    • Bacterial invasion: force feeding by Salmonella
    • doi: 10.1016/S0960-9822(99)80178-X
    • Brumell, J. H., Steele-Mortimer, O., and Finlay, B. B. (1999). Bacterial invasion: force feeding by Salmonella. Curr. Biol. 9, R277-R280. doi: 10.1016/S0960-9822(99)80178-X
    • (1999) Curr. Biol. , vol.9
    • Brumell, J.H.1    Steele-Mortimer, O.2    Finlay, B.B.3
  • 21
    • 0034839914 scopus 로고    scopus 로고
    • Characterization of Salmonella-induced filaments (Sifs) reveals a delayed interaction between Salmonella-containing vacuoles and late endocytic compartments
    • doi: 10.1034/j.1600-0854.2001.20907.x
    • Brumell, J. H., Tang, P., Mills, S. D., and Finlay, B. B. (2001). Characterization of Salmonella-induced filaments (Sifs) reveals a delayed interaction between Salmonella-containing vacuoles and late endocytic compartments. Traffic 2, 643-653. doi: 10.1034/j.1600-0854.2001.20907.x
    • (2001) Traffic , vol.2 , pp. 643-653
    • Brumell, J.H.1    Tang, P.2    Mills, S.D.3    Finlay, B.B.4
  • 22
    • 51449099913 scopus 로고    scopus 로고
    • Microarray analysis of human monocytes infected with Francisella tularensis identifies new targets of host response subversion
    • doi: 10.1371/journal.pone.0002924
    • Butchar, J. P., Cremer, T. J., Clay, C. D., Gavrilin, M. A., Wewers, M. D., Marsh, C. B., et al. (2008). Microarray analysis of human monocytes infected with Francisella tularensis identifies new targets of host response subversion. PLoS ONE 3:e2924. doi: 10.1371/journal.pone.0002924
    • (2008) PLoS ONE , vol.3
    • Butchar, J.P.1    Cremer, T.J.2    Clay, C.D.3    Gavrilin, M.A.4    Wewers, M.D.5    Marsh, C.B.6
  • 23
    • 78650180144 scopus 로고    scopus 로고
    • Intracellular generation of superoxide by the phagocyte NADPH oxidase: how, where, and what for
    • doi: 10.1016/j.freeradbiomed.2010.09.016
    • Bylund, J., Brown, K. L., Movitz, C., Dahlgren, C., and Karlsson, A. (2010). Intracellular generation of superoxide by the phagocyte NADPH oxidase: how, where, and what for. Free Radic. Biol. Med. 49, 1834-1845. doi: 10.1016/j.freeradbiomed.2010.09.016
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1834-1845
    • Bylund, J.1    Brown, K.L.2    Movitz, C.3    Dahlgren, C.4    Karlsson, A.5
  • 24
    • 84877809004 scopus 로고    scopus 로고
    • Endocytic SNAREs are involved in optimal Coxiella burnetii vacuole development
    • doi: 10.1111/cmi.12087
    • Campoy, E. M., Mansilla, M. E., and Colombo, M. I. (2013). Endocytic SNAREs are involved in optimal Coxiella burnetii vacuole development. Cell. Microbiol. 15, 922-941. doi: 10.1111/cmi.12087
    • (2013) Cell. Microbiol. , vol.15 , pp. 922-941
    • Campoy, E.M.1    Mansilla, M.E.2    Colombo, M.I.3
  • 25
    • 78650919752 scopus 로고    scopus 로고
    • The early secretory pathway contributes to the growth of the Coxiella-replicative niche
    • doi: 10.1128/IAI.00688-10
    • Campoy, E. M., Zoppino, F. C., and Colombo, M. I. (2011). The early secretory pathway contributes to the growth of the Coxiella-replicative niche. Infect. Immun. 79, 402-413. doi: 10.1128/IAI.00688-10
    • (2011) Infect. Immun. , vol.79 , pp. 402-413
    • Campoy, E.M.1    Zoppino, F.C.2    Colombo, M.I.3
  • 26
    • 73549124790 scopus 로고    scopus 로고
    • Rab10 regulates phagosome maturation and its overexpression rescues Mycobacterium-containing phagosomes maturation
    • doi: 10.1111/j.1600-0854.2009.01013.x
    • Cardoso, C. M., Jordao, L., and Vieira, O. V. (2010). Rab10 regulates phagosome maturation and its overexpression rescues Mycobacterium-containing phagosomes maturation. Traffic 11, 221-235. doi: 10.1111/j.1600-0854.2009.01013.x
    • (2010) Traffic , vol.11 , pp. 221-235
    • Cardoso, C.M.1    Jordao, L.2    Vieira, O.V.3
  • 27
    • 7244261884 scopus 로고    scopus 로고
    • TOR signaling in mammals
    • doi: 10.1242/jcs.01311
    • Carrera, A. C. (2004). TOR signaling in mammals. J. Cell Sci. 117, 4615-4616. doi: 10.1242/jcs.01311
    • (2004) J. Cell Sci. , vol.117 , pp. 4615-4616
    • Carrera, A.C.1
  • 28
    • 79952348751 scopus 로고    scopus 로고
    • The ubiquitin-binding adaptor proteins p62/SQSTM1 and NDP52 are recruited independently to bacteria-associated microdomains to target Salmonella to the autophagy pathway
    • doi: 10.4161/auto.7.3.14046
    • Cemma, M., Kim, P. K., and Brumell, J. H. (2011). The ubiquitin-binding adaptor proteins p62/SQSTM1 and NDP52 are recruited independently to bacteria-associated microdomains to target Salmonella to the autophagy pathway. Autophagy 7, 341-345. doi: 10.4161/auto.7.3.14046
    • (2011) Autophagy , vol.7 , pp. 341-345
    • Cemma, M.1    Kim, P.K.2    Brumell, J.H.3
  • 29
    • 34548482499 scopus 로고    scopus 로고
    • siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy
    • doi: 10.1074/jbc.M703663200
    • Chan, E. Y., Kir, S., and Tooze, S. A. (2007). siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy. J. Biol. Chem. 282, 25464-25474. doi: 10.1074/jbc.M703663200
    • (2007) J. Biol. Chem. , vol.282 , pp. 25464-25474
    • Chan, E.Y.1    Kir, S.2    Tooze, S.A.3
  • 30
    • 33749264796 scopus 로고    scopus 로고
    • Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication
    • doi: 10.1073/pnas.0601838103
    • Checroun, C., Wehrly, T. D., Fischer, E. R., Hayes, S. F., and Celli, J. (2006). Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication. Proc. Natl. Acad. Sci. U.S.A. 103, 14578-14583. doi: 10.1073/pnas.0601838103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 14578-14583
    • Checroun, C.1    Wehrly, T.D.2    Fischer, E.R.3    Hayes, S.F.4    Celli, J.5
  • 31
    • 84875308050 scopus 로고    scopus 로고
    • The Francisella intracellular life cycle: toward molecular mechanisms of intracellular survival and proliferation
    • doi: 10.3389/fmicb.2010.00138
    • Chong, A., and J., Celli. (2010). The Francisella intracellular life cycle: toward molecular mechanisms of intracellular survival and proliferation. Front. Microbiol. 1:138. doi: 10.3389/fmicb.2010.00138
    • (2010) Front. Microbiol. , vol.1 , pp. 138
    • Chong, A.1    Celli, J.2
  • 32
    • 57349126161 scopus 로고    scopus 로고
    • The early phagosomal stage of Francisella tularensis determines optimal phagosomal escape and Francisella pathogenicity island protein expression
    • doi: 10.1128/IAI.00682-08
    • Chong, A., Wehrly, T. D., Nair, V., Fischer, E. R., Barker, J. R., Klose, K. E., et al. (2008). The early phagosomal stage of Francisella tularensis determines optimal phagosomal escape and Francisella pathogenicity island protein expression. Infect. Immun. 76, 5488-5499. doi: 10.1128/IAI.00682-08
    • (2008) Infect. Immun. , vol.76 , pp. 5488-5499
    • Chong, A.1    Wehrly, T.D.2    Nair, V.3    Fischer, E.R.4    Barker, J.R.5    Klose, K.E.6
  • 33
    • 84869886358 scopus 로고    scopus 로고
    • The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation
    • doi: 10.1126/science.1227026
    • Choy, A., Dancourt, J., Mugo, B., O'Connor, T. J., Isberg, R. R., Melia, T. J., et al. (2012). The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation. Science 338, 1072-1076. doi: 10.1126/science.1227026
    • (2012) Science , vol.338 , pp. 1072-1076
    • Choy, A.1    Dancourt, J.2    Mugo, B.3    O'Connor, T.J.4    Isberg, R.R.5    Melia, T.J.6
  • 34
    • 0026540462 scopus 로고
    • Membrane sorting during phagocytosis: selective exclusion of major histocompatibility complex molecules but not complement receptor CR3 during conventional and coiling phagocytosis
    • doi: 10.1084/jem.175.5.1317
    • Clemens, D. L., and Horwitz, M. A. (1992). Membrane sorting during phagocytosis: selective exclusion of major histocompatibility complex molecules but not complement receptor CR3 during conventional and coiling phagocytosis. J. Exp. Med. 175, 1317-1326. doi: 10.1084/jem.175.5.1317
    • (1992) J. Exp. Med. , vol.175 , pp. 1317-1326
    • Clemens, D.L.1    Horwitz, M.A.2
  • 35
    • 2542552050 scopus 로고    scopus 로고
    • Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages
    • doi: 10.1128/IAI.72.6.3204-3217.2004
    • Clemens, D. L., Lee, B. Y., and Horwitz, M. A. (2004). Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages. Infect. Immun. 72, 3204-3217. doi: 10.1128/IAI.72.6.3204-3217.2004
    • (2004) Infect. Immun. , vol.72 , pp. 3204-3217
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 36
    • 58149458118 scopus 로고    scopus 로고
    • Francisella tularensis regulates autophagy-related host cell signaling pathways
    • doi: 10.4161/auto.5.1.7305
    • Cremer, T. J., Amer, A., Tridandapani, S., and Butchar, J. P. (2009). Francisella tularensis regulates autophagy-related host cell signaling pathways. Autophagy 5, 125-128. doi: 10.4161/auto.5.1.7305
    • (2009) Autophagy , vol.5 , pp. 125-128
    • Cremer, T.J.1    Amer, A.2    Tridandapani, S.3    Butchar, J.P.4
  • 37
    • 2142758690 scopus 로고    scopus 로고
    • Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system
    • doi: 10.1128/IAI.72.5.3048-3053.2004
    • Derre, I., and Isberg, R. R. (2004). Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system. Infect. Immun. 72, 3048-3053. doi: 10.1128/IAI.72.5.3048-3053.2004
    • (2004) Infect. Immun. , vol.72 , pp. 3048-3053
    • Derre, I.1    Isberg, R.R.2
  • 38
    • 84865693202 scopus 로고    scopus 로고
    • Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses
    • doi: 10.1016/j.cell.2012.06.050
    • Dong, N., Zhu, Y., Lu, Q., Hu, L., Zheng, Y., and Shao, F. (2012). Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses. Cell 150, 1029-1041. doi: 10.1016/j.cell.2012.06.050
    • (2012) Cell , vol.150 , pp. 1029-1041
    • Dong, N.1    Zhu, Y.2    Lu, Q.3    Hu, L.4    Zheng, Y.5    Shao, F.6
  • 39
    • 80052337539 scopus 로고    scopus 로고
    • Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy
    • doi: 10.1371/journal.ppat.1002168
    • Dortet, L., Mostowy, S., Samba-Louaka, A., Gouin, E., Nahori, M. A., Wiemer, E. A., et al. (2011). Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy. PLoS Pathog. 7:e1002168. doi: 10.1371/journal.ppat.1002168
    • (2011) PLoS Pathog , vol.7
    • Dortet, L.1    Mostowy, S.2    Samba-Louaka, A.3    Gouin, E.4    Nahori, M.A.5    Wiemer, E.A.6
  • 40
    • 7944222097 scopus 로고    scopus 로고
    • Molecular determinants of Listeria monocytogenes virulence
    • doi: 10.1146/annurev.micro.57.030502.090934
    • Dussurget, O., Pizarro-Cerda, J., and Cossart, P. (2004). Molecular determinants of Listeria monocytogenes virulence. Annu. Rev. Microbiol. 58, 587-610. doi: 10.1146/annurev.micro.57.030502.090934
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 587-610
    • Dussurget, O.1    Pizarro-Cerda, J.2    Cossart, P.3
  • 42
    • 0034729320 scopus 로고    scopus 로고
    • Salmonella interactions with host cells: in vitro to in vivo
    • doi: 10.1098/rstb.2000.0603
    • Finlay, B. B., and Brumell, J. H. (2000). Salmonella interactions with host cells: in vitro to in vivo. Philos. Trans. R. Soc. Lond. B Biol. Sci. 355, 623-631. doi: 10.1098/rstb.2000.0603
    • (2000) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.355 , pp. 623-631
    • Finlay, B.B.1    Brumell, J.H.2
  • 43
    • 0035817635 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest
    • doi: 10.1083/jcb.200106049
    • Fratti, R. A., Backer, J. M., Gruenberg, J., Corvera, S., and Deretic, V. (2001). Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest. J. Cell Biol. 154, 631-644. doi: 10.1083/jcb.200106049
    • (2001) J. Cell Biol. , vol.154 , pp. 631-644
    • Fratti, R.A.1    Backer, J.M.2    Gruenberg, J.3    Corvera, S.4    Deretic, V.5
  • 44
    • 0037627408 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis glycosylated phosphatidylinositol causes phagosome maturation arrest
    • doi: 10.1073/pnas.0737613100
    • Fratti, R. A., Chua, J., Vergne, I., and Deretic, V. (2003). Mycobacterium tuberculosis glycosylated phosphatidylinositol causes phagosome maturation arrest. Proc. Natl. Acad. Sci. U.S.A. 100, 5437-5442. doi: 10.1073/pnas.0737613100
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5437-5442
    • Fratti, R.A.1    Chua, J.2    Vergne, I.3    Deretic, V.4
  • 45
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • doi: 10.1091/mbc.E07-12-1257
    • Fujita, N., Itoh, T., Omori, H., Fukuda, M., Noda, T., and Yoshimori, T. (2008a). The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell 19, 2092-2100. doi: 10.1091/mbc.E07-12-1257
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 46
    • 79952111090 scopus 로고    scopus 로고
    • [Molecular mechanism of autophagosome formation in mammalian cells]
    • Fujita, N., Matsunaga, K., Noda, T., and Yoshimori, T. (2008b). [Molecular mechanism of autophagosome formation in mammalian cells]. Tanpakushitsu Kakusan Koso 53, 2106-2110.
    • (2008) Tanpakushitsu Kakusan Koso , vol.53 , pp. 2106-2110
    • Fujita, N.1    Matsunaga, K.2    Noda, T.3    Yoshimori, T.4
  • 47
    • 0027818492 scopus 로고
    • Intracellular replication of Salmonella within epithelial cells is associated with filamentous structures containing lysosomal membrane glycoproteins
    • Garcia-del, P. F., Zwick, M. B., Leung, K. Y., and Finlay, B. B. (1993). Intracellular replication of Salmonella within epithelial cells is associated with filamentous structures containing lysosomal membrane glycoproteins. Infect. Agents Dis. 2, 227-231.
    • (1993) Infect. Agents Dis. , vol.2 , pp. 227-231
    • Garcia-del, P.F.1    Zwick, M.B.2    Leung, K.Y.3    Finlay, B.B.4
  • 48
    • 0037108387 scopus 로고    scopus 로고
    • Coxiella burnetii survival in THP-1 monocytes involves the impairment of phagosome maturation: IFN-gamma mediates its restoration and bacterial killing
    • Ghigo, E., Capo, C., Tung, C. H., Raoult, D., Gorvel, J. P., and Mege, J. L. (2002). Coxiella burnetii survival in THP-1 monocytes involves the impairment of phagosome maturation: IFN-gamma mediates its restoration and bacterial killing. J. Immunol. 169, 4488-4495.
    • (2002) J. Immunol. , vol.169 , pp. 4488-4495
    • Ghigo, E.1    Capo, C.2    Tung, C.H.3    Raoult, D.4    Gorvel, J.P.5    Mege, J.L.6
  • 50
    • 0027818845 scopus 로고
    • Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement
    • Goldberg, M. B., Barzu, O., Parsot, C., and Sansonetti, P. J. (1993). Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement. Infect. Agents Dis. 2, 210-211.
    • (1993) Infect. Agents Dis. , vol.2 , pp. 210-211
    • Goldberg, M.B.1    Barzu, O.2    Parsot, C.3    Sansonetti, P.J.4
  • 51
    • 0036849864 scopus 로고    scopus 로고
    • Macrophage intracellular signaling induced by Listeria monocytogenes
    • doi: 10.1016/S1286-4579(02)00011-4
    • Goldfine, H., and Wadsworth, S. J. (2002). Macrophage intracellular signaling induced by Listeria monocytogenes. Microbes Infect. 4, 1335-1343. doi: 10.1016/S1286-4579(02)00011-4
    • (2002) Microbes Infect , vol.4 , pp. 1335-1343
    • Goldfine, H.1    Wadsworth, S.J.2
  • 52
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • doi: 10.1016/j.cell.2004.11.038
    • Gutierrez, M. G., Master, S. S., Singh, S. B., Taylor, G. A., Colombo, M. I., and Deretic, V. (2004). Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119, 753-766. doi: 10.1016/j.cell.2004.11.038
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 53
    • 21344472825 scopus 로고    scopus 로고
    • Autophagy induction favours the generation and maturation of the Coxiella-replicative vacuoles
    • doi: 10.1111/j.1462-5822.2005.00527.x
    • Gutierrez, M. G., Vazquez, C. L., Munafo, D. B., Zoppino, F. C., Beron, W., Rabinovitch, M., et al. (2005). Autophagy induction favours the generation and maturation of the Coxiella-replicative vacuoles. Cell. Microbiol. 7, 981-993. doi: 10.1111/j.1462-5822.2005.00527.x
    • (2005) Cell. Microbiol. , vol.7 , pp. 981-993
    • Gutierrez, M.G.1    Vazquez, C.L.2    Munafo, D.B.3    Zoppino, F.C.4    Beron, W.5    Rabinovitch, M.6
  • 54
    • 42949139481 scopus 로고    scopus 로고
    • AMPK phosphorylation of raptor mediates a metabolic checkpoint
    • doi: 10.1016/j.molcel.2008.03.003
    • Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., et al. (2008). AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol. Cell 30, 214-226. doi: 10.1016/j.molcel.2008.03.003
    • (2008) Mol. Cell , vol.30 , pp. 214-226
    • Gwinn, D.M.1    Shackelford, D.B.2    Egan, D.F.3    Mihaylova, M.M.4    Mery, A.5    Vasquez, D.S.6
  • 55
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • doi: 10.1074/jbc.C700195200
    • Hanada, T., Noda, N. N., Satomi, Y., Ichimura, Y., Fujioka, Y., Takao, T., et al. (2007). The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J. Biol. Chem. 282, 37298-37302. doi: 10.1074/jbc.C700195200
    • (2007) J. Biol. Chem. , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5    Takao, T.6
  • 56
    • 37349110158 scopus 로고    scopus 로고
    • Salmonellae interplay with host cells
    • doi: 10.1038/nrmicro1788
    • Haraga, A., Ohlson, M. B., and Miller, S. I. (2008). Salmonellae interplay with host cells. Nat. Rev. Microbiol. 6, 53-66. doi: 10.1038/nrmicro1788
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 53-66
    • Haraga, A.1    Ohlson, M.B.2    Miller, S.I.3
  • 57
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
    • doi: 10.1083/jcb.200712064
    • Hara, T., Takamura, A., Kishi, C., Iemura, S., Natsume, T., Guan, J. L., et al. (2008). FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells. J. Cell Biol. 181, 497-510. doi: 10.1083/jcb.200712064
    • (2008) J. Cell Biol. , vol.181 , pp. 497-510
    • Hara, T.1    Takamura, A.2    Kishi, C.3    Iemura, S.4    Natsume, T.5    Guan, J.L.6
  • 58
    • 0030043391 scopus 로고    scopus 로고
    • Differential interaction with endocytic and exocytic pathways distinguish parasitophorous vacuoles of Coxiella burnetii and Chlamydia trachomatis
    • Heinzen, R. A., Scidmore, M. A., Rockey, D. D., and Hackstadt, T. (1996). Differential interaction with endocytic and exocytic pathways distinguish parasitophorous vacuoles of Coxiella burnetii and Chlamydia trachomatis. Infect. Immun. 64, 796-809.
    • (1996) Infect. Immun. , vol.64 , pp. 796-809
    • Heinzen, R.A.1    Scidmore, M.A.2    Rockey, D.D.3    Hackstadt, T.4
  • 59
    • 0021014278 scopus 로고
    • The Legionnaires' disease bacterium (Legionella pneumophila) inhibits phagosome-lysosome fusion in human monocytes
    • doi: 10.1084/jem.158.6.2108
    • Horwitz, M. A. (1983). The Legionnaires' disease bacterium (Legionella pneumophila) inhibits phagosome-lysosome fusion in human monocytes. J. Exp. Med. 158, 2108-2126. doi: 10.1084/jem.158.6.2108
    • (1983) J. Exp. Med. , vol.158 , pp. 2108-2126
    • Horwitz, M.A.1
  • 60
    • 65249119430 scopus 로고    scopus 로고
    • Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy
    • doi: 10.1091/mbc.E08-12-1248
    • Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., et al. (2009a). Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy. Mol. Biol. Cell 20, 1981-1991. doi: 10.1091/mbc.E08-12-1248
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1981-1991
    • Hosokawa, N.1    Hara, T.2    Kaizuka, T.3    Kishi, C.4    Takamura, A.5    Miura, Y.6
  • 61
    • 70349644856 scopus 로고    scopus 로고
    • Atg101, a novel mammalian autophagy protein interacting with Atg13
    • doi: 10.4161/auto.5.7.9296
    • Hosokawa, N., Sasaki, T., Iemura, S., Natsume, T., Hara, T., and Mizushima, N. (2009b). Atg101, a novel mammalian autophagy protein interacting with Atg13. Autophagy 5, 973-979. doi: 10.4161/auto.5.7.9296
    • (2009) Autophagy , vol.5 , pp. 973-979
    • Hosokawa, N.1    Sasaki, T.2    Iemura, S.3    Natsume, T.4    Hara, T.5    Mizushima, N.6
  • 62
    • 0037711627 scopus 로고    scopus 로고
    • Maturation of the Coxiella burnetii parasitophorous vacuole requires bacterial protein synthesis but not replication
    • doi: 10.1046/j.1462-5822.2003.00293.x
    • Howe, D., Melnicakova, J., Barak, I., and Heinzen, R. A. (2003). Maturation of the Coxiella burnetii parasitophorous vacuole requires bacterial protein synthesis but not replication. Cell Microbiol. 5, 469-480. doi: 10.1046/j.1462-5822.2003.00293.x
    • (2003) Cell Microbiol , vol.5 , pp. 469-480
    • Howe, D.1    Melnicakova, J.2    Barak, I.3    Heinzen, R.A.4
  • 63
    • 34250891313 scopus 로고    scopus 로고
    • AMP-activated protein kinase: a universal regulator of autophagy
    • Hoyer-Hansen, M., and Jaattela, M. (2007). AMP-activated protein kinase: a universal regulator of autophagy. Autophagy 3, 381-383.
    • (2007) Autophagy , vol.3 , pp. 381-383
    • Hoyer-Hansen, M.1    Jaattela, M.2
  • 64
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck, C. J. (1998). Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62, 379-433.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 65
    • 77956376663 scopus 로고    scopus 로고
    • Inactivation of macrophage Rab7 by Burkholderia cenocepacia
    • doi: 10.1159/000319864
    • Huynh, K. K., Plumb, J. D., Downey, G. P., Valvano, M. A., and Grinstein, S. (2010). Inactivation of macrophage Rab7 by Burkholderia cenocepacia. J. Innate Immun. 2, 522-533. doi: 10.1159/000319864
    • (2010) J. Innate Immun. , vol.2 , pp. 522-533
    • Huynh, K.K.1    Plumb, J.D.2    Downey, G.P.3    Valvano, M.A.4    Grinstein, S.5
  • 66
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • doi: 10.1091/mbc.E08-01-0080
    • Itakura, E., Kishi, C., Inoue, K., and Mizushima, N. (2008). Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol. Biol. Cell 19, 5360-5372. doi: 10.1091/mbc.E08-01-0080
    • (2008) Mol. Biol. Cell 19, 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 67
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • doi: 10.4161/auto.6.6.12709
    • Itakura, E., and Mizushima, N. (2010). Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy 6, 764-776. doi: 10.4161/auto.6.6.12709
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 68
    • 7244255989 scopus 로고    scopus 로고
    • Role for Rab7 in maturation of late autophagic vacuoles
    • doi: 10.1242/jcs.01370
    • Jager, S., Bucci, C., Tanida, I., Ueno, T., Kominami, E., Saftig, P., et al. (2004). Role for Rab7 in maturation of late autophagic vacuoles. J. Cell Sci. 117, 4837-4848. doi: 10.1242/jcs.01370
    • (2004) J. Cell Sci. , vol.117 , pp. 4837-4848
    • Jager, S.1    Bucci, C.2    Tanida, I.3    Ueno, T.4    Kominami, E.5    Saftig, P.6
  • 69
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • doi: 10.1091/mbc.E08-12-1249
    • Jung, C. H., Jun, C. B., Ro, S. H., Kim, Y. M., Otto, N. M., Cao, J., et al. (2009). ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol. Biol. Cell 20, 1992-2003. doi: 10.1091/mbc.E08-12-1249
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3    Kim, Y.M.4    Otto, N.M.5    Cao, J.6
  • 70
    • 0036903907 scopus 로고    scopus 로고
    • Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites
    • doi: 10.1038/ncb883
    • Kagan, J. C., and Roy, C. R. (2002). Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites. Nat. Cell Biol. 4, 945-954. doi: 10.1038/ncb883
    • (2002) Nat. Cell Biol. , vol.4 , pp. 945-954
    • Kagan, J.C.1    Roy, C.R.2
  • 71
    • 84870880537 scopus 로고    scopus 로고
    • Size-dependent mechanism of cargo sorting during lysosome-phagosome fusion is controlled by Rab34
    • doi: 10.1073/pnas.1206811109
    • Kasmapour, B., Gronow, A., Bleck, C. K., Hong, W., and Gutierrez, M. G. (2012). Size-dependent mechanism of cargo sorting during lysosome-phagosome fusion is controlled by Rab34. Proc. Natl. Acad. Sci. U.S.A. 109, 20485-20490. doi: 10.1073/pnas.1206811109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 20485-20490
    • Kasmapour, B.1    Gronow, A.2    Bleck, C.K.3    Hong, W.4    Gutierrez, M.G.5
  • 72
    • 33744948764 scopus 로고    scopus 로고
    • Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions
    • doi: 10.1111/j.1574-6976.2006.00021.x
    • Kayal, S., and Charbit, A. (2006). Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions. FEMS Microbiol. Rev. 30, 514-529. doi: 10.1111/j.1574-6976.2006.00021.x
    • (2006) FEMS Microbiol. Rev. , vol.30 , pp. 514-529
    • Kayal, S.1    Charbit, A.2
  • 73
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • doi: 10.1038/ncb2152
    • Kim, J., Kundu, M., Viollet, B., and Guan, K. L. (2011). AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 13, 132-141. doi: 10.1038/ncb2152
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 74
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • doi: 10.1016/j.molcel.2009.04.026
    • Kirkin, V., McEwan, D. G., Novak, I., and Dikic, I. (2009). A role for ubiquitin in selective autophagy. Mol. Cell 34, 259-269. doi: 10.1016/j.molcel.2009.04.026
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 75
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: unanswered questions
    • doi: 10.1242/jcs.01620
    • Klionsky, D. J. (2005). The molecular machinery of autophagy: unanswered questions. J. Cell Sci. 118, 7-18. doi: 10.1242/jcs.01620
    • (2005) J. Cell Sci. , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 76
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: from phenomenology to molecular understanding in less than a decade
    • doi: 10.1038/nrm2245
    • Klionsky, D. J. (2007). Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 8, 931-937. doi: 10.1038/nrm2245
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 77
    • 0042357064 scopus 로고    scopus 로고
    • Taking possession: biogenesis of the Salmonella-containing vacuole
    • doi: 10.1034/j.1600-0854.2003.00118.x
    • Knodler, L. A., and Steele-Mortimer, O. (2003). Taking possession: biogenesis of the Salmonella-containing vacuole. Traffic 4, 587-599. doi: 10.1034/j.1600-0854.2003.00118.x
    • (2003) Traffic , vol.4 , pp. 587-599
    • Knodler, L.A.1    Steele-Mortimer, O.2
  • 78
    • 0041903802 scopus 로고    scopus 로고
    • Salmonella type III effectors PipB and PipB2 are targeted to detergent-resistant microdomains on internal host cell membranes
    • doi: 10.1046/j.1365-2958.2003.03598.x
    • Knodler, L. A., Vallance, B. A., Hensel, M., Jackel, D., Finlay, B. B., and Steele-Mortimer, O. (2003). Salmonella type III effectors PipB and PipB2 are targeted to detergent-resistant microdomains on internal host cell membranes. Mol. Microbiol. 49, 685-704. doi: 10.1046/j.1365-2958.2003.03598.x
    • (2003) Mol. Microbiol. , vol.49 , pp. 685-704
    • Knodler, L.A.1    Vallance, B.A.2    Hensel, M.3    Jackel, D.4    Finlay, B.B.5    Steele-Mortimer, O.6
  • 79
    • 77950495123 scopus 로고    scopus 로고
    • Physiological significance of selective degradation of p62 by autophagy
    • doi: 10.1016/j.febslet.2010.02.017
    • Komatsu, M., and Ichimura, Y. (2010). Physiological significance of selective degradation of p62 by autophagy. FEBS Lett. 584, 1374-1378. doi: 10.1016/j.febslet.2010.02.017
    • (2010) FEBS Lett , vol.584 , pp. 1374-1378
    • Komatsu, M.1    Ichimura, Y.2
  • 80
    • 84872474723 scopus 로고    scopus 로고
    • Reactive oxygen species production in the phagosome: impact on antigen presentation in dendritic cells
    • doi: 10.1089/ars.2012.4557
    • Kotsias, F., Hoffmann, E., Amigorena, S., and Savina, A. (2013). Reactive oxygen species production in the phagosome: impact on antigen presentation in dendritic cells. Antioxid. Redox Signal. 18, 714-729. doi: 10.1089/ars.2012.4557
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 714-729
    • Kotsias, F.1    Hoffmann, E.2    Amigorena, S.3    Savina, A.4
  • 81
    • 0019326294 scopus 로고
    • [Microbiological aspects of Legionnaires' disease]
    • Krech, U., Pagon, S., and Sonnabend, W. (1980). [Microbiological aspects of Legionnaires' disease]. Schweiz. Med. Wochenschr. 110, 1739-1745.
    • (1980) Schweiz. Med. Wochenschr. , vol.110 , pp. 1739-1745
    • Krech, U.1    Pagon, S.2    Sonnabend, W.3
  • 82
    • 33751115464 scopus 로고    scopus 로고
    • Rab14 is critical for maintenance of Mycobacterium tuberculosis phagosome maturation arrest
    • doi: 10.1038/sj.emboj.7601407
    • Kyei, G. B., Vergne, I., Chua, J., Roberts, E., Harris, J., Junutula, J. R., et al. (2006). Rab14 is critical for maintenance of Mycobacterium tuberculosis phagosome maturation arrest. EMBO J. 25, 5250-5259. doi: 10.1038/sj.emboj.7601407
    • (2006) EMBO J , vol.25 , pp. 5250-5259
    • Kyei, G.B.1    Vergne, I.2    Chua, J.3    Roberts, E.4    Harris, J.5    Junutula, J.R.6
  • 83
    • 84880896860 scopus 로고    scopus 로고
    • Host and bacterial factors that regulate LC3 recruitment to Listeria monocytogenes during the early stages of macrophage infection
    • doi: 10.4161/auto.24406. [Epub ahead of print]
    • Lam, G. Y., Cemma, M., Muise, A. M., Higgins, D. E., and Brumell, J. H. (2013). Host and bacterial factors that regulate LC3 recruitment to Listeria monocytogenes during the early stages of macrophage infection. Autophagy 9. doi: 10.4161/auto.24406. [Epub ahead of print].
    • (2013) Autophagy , vol.9
    • Lam, G.Y.1    Cemma, M.2    Muise, A.M.3    Higgins, D.E.4    Brumell, J.H.5
  • 84
    • 34548512821 scopus 로고    scopus 로고
    • Human listeriosis and animal models
    • doi: 10.1016/j.micinf.2007.05.009
    • Lecuit, M. (2007). Human listeriosis and animal models. Microbes Infect. 9, 1216-1225. doi: 10.1016/j.micinf.2007.05.009
    • (2007) Microbes Infect , vol.9 , pp. 1216-1225
    • Lecuit, M.1
  • 85
    • 0030344411 scopus 로고    scopus 로고
    • Tuberculous fibrosing mediastinitis: radiologic findings
    • doi: 10.2214/ajr.167.6.8956619
    • Lee, J. Y., Kim, Y., Lee, K. S., and Chung, M. P. (1996). Tuberculous fibrosing mediastinitis: radiologic findings. AJR Am. J. Roentgenol. 167, 1598-1599. doi: 10.2214/ajr.167.6.8956619
    • (1996) AJR Am. J. Roentgenol. , vol.167 , pp. 1598-1599
    • Lee, J.Y.1    Kim, Y.2    Lee, K.S.3    Chung, M.P.4
  • 86
    • 79955961624 scopus 로고    scopus 로고
    • Mycobacterium marinum induces a marked LC3 recruitment to its containing phagosome that depends on a functional ESX-1 secretion system
    • doi: 10.1111/j.1462-5822.2011.01581.x
    • Lerena, M. C., and Colombo, M. I. (2011). Mycobacterium marinum induces a marked LC3 recruitment to its containing phagosome that depends on a functional ESX-1 secretion system. Cell Microbiol. 13, 814-835. doi: 10.1111/j.1462-5822.2011.01581.x
    • (2011) Cell Microbiol , vol.13 , pp. 814-835
    • Lerena, M.C.1    Colombo, M.I.2
  • 87
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • doi:10.1016/S1534-5807(04)00099-1
    • Levine, B., and Klionsky, D. J. (2004). Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 6, 463-477. doi: 10.1016/S1534-5807(04)00099-1
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 88
    • 46449120732 scopus 로고    scopus 로고
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
    • doi: 10.1038/ncb1740
    • Liang, C., Lee, J. S., Inn, K. S., Gack, M. U., Li, Q., Roberts, E. A., et al. (2008). Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat. Cell Biol. 10, 776-787. doi: 10.1038/ncb1740
    • (2008) Nat. Cell Biol. , vol.10 , pp. 776-787
    • Liang, C.1    Lee, J.S.2    Inn, K.S.3    Gack, M.U.4    Li, Q.5    Roberts, E.A.6
  • 89
    • 84871854233 scopus 로고    scopus 로고
    • Beclin 1 is required for starvation-enhanced, but not rapamycin-enhanced, LC3-associated phagocytosis of Burkholderia pseudomallei in RAW 264.7 cells
    • doi: 10.1128/IAI.00834-12
    • Li, X., Prescott, M., Adler, B., Boyce, J. D., and Devenish, R. J. (2013). Beclin 1 is required for starvation-enhanced, but not rapamycin-enhanced, LC3-associated phagocytosis of Burkholderia pseudomallei in RAW 264.7 cells. Infect. Immun. 81, 271-277. doi: 10.1128/IAI.00834-12
    • (2013) Infect. Immun. , vol.81 , pp. 271-277
    • Li, X.1    Prescott, M.2    Adler, B.3    Boyce, J.D.4    Devenish, R.J.5
  • 90
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control
    • doi:10.1016/S1097-2765(02)00636-6
    • Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J. L., Bonenfant, D., et al. (2002). Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol. Cell 10, 457-468. doi: 10.1016/S1097-2765(02)00636-6
    • (2002) Mol. Cell , vol.10 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3    Lorberg, A.4    Crespo, J.L.5    Bonenfant, D.6
  • 91
    • 77956396747 scopus 로고    scopus 로고
    • Defective CFTR induces aggresome formation and lung inflammation in cystic fibrosis through ROS-mediated autophagy inhibition
    • doi: 10.1038/ncb2090
    • Luciani, A., Villella, V. R., Esposito, S., Brunetti-Pierri, N., Medina, D., Settembre, C., et al. (2010). Defective CFTR induces aggresome formation and lung inflammation in cystic fibrosis through ROS-mediated autophagy inhibition. Nat. Cell Biol. 12, 863-875. doi: 10.1038/ncb2090
    • (2010) Nat. Cell Biol. , vol.12 , pp. 863-875
    • Luciani, A.1    Villella, V.R.2    Esposito, S.3    Brunetti-Pierri, N.4    Medina, D.5    Settembre, C.6
  • 92
    • 0027082580 scopus 로고
    • Genetics of Legionella pneumophila virulence
    • doi: 10.1146/annurev.ge.26.120192.000411
    • Marra, A., and Shuman, H. A. (1992). Genetics of Legionella pneumophila virulence. Annu. Rev. Genet. 26, 51-69. doi: 10.1146/annurev.ge.26.120192.000411
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 51-69
    • Marra, A.1    Shuman, H.A.2
  • 93
    • 77955895424 scopus 로고    scopus 로고
    • Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L
    • doi: 10.1083/jcb.200911141
    • Matsunaga, K., Morita, E., Saitoh, T., Akira, S., Ktistakis, N. T., Izumi, T., et al. (2010). Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L. J. Cell Biol. 190, 511-521. doi: 10.1083/jcb.200911141
    • (2010) J. Cell Biol. , vol.190 , pp. 511-521
    • Matsunaga, K.1    Morita, E.2    Saitoh, T.3    Akira, S.4    Ktistakis, N.T.5    Izumi, T.6
  • 94
    • 67549110195 scopus 로고    scopus 로고
    • A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy
    • doi: 10.4161/auto.5.5.8249
    • Mercer, C. A., Kaliappan, A., and Dennis, P. B. (2009). A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy. Autophagy 5, 649-662. doi: 10.4161/auto.5.5.8249
    • (2009) Autophagy , vol.5 , pp. 649-662
    • Mercer, C.A.1    Kaliappan, A.2    Dennis, P.B.3
  • 95
    • 84863699007 scopus 로고    scopus 로고
    • cAMP and EPAC are key players in the regulation of the signal transduction pathway involved in the alpha-hemolysin autophagic response
    • doi: 10.1371/journal.ppat.1002664
    • Mestre, M. B., and Colombo, M. I. (2012). cAMP and EPAC are key players in the regulation of the signal transduction pathway involved in the alpha-hemolysin autophagic response. PLoS Pathog. 8:e1002664. doi: 10.1371/journal.ppat.1002664
    • (2012) PLoS Pathog , vol.8
    • Mestre, M.B.1    Colombo, M.I.2
  • 96
    • 79551507643 scopus 로고    scopus 로고
    • A conference report from "Down Under": talking autophagy at OzBio2010
    • doi: 10.4161/auto.7.2.14225
    • Mijaljica, D., and Devenish, R. J. (2011). A conference report from "Down Under": talking autophagy at OzBio2010. Autophagy 7, 252-254. doi: 10.4161/auto.7.2.14225
    • (2011) Autophagy , vol.7 , pp. 252-254
    • Mijaljica, D.1    Devenish, R.J.2
  • 97
    • 79953660798 scopus 로고    scopus 로고
    • A membrane is born: origin of the autophagosomal compartment
    • doi: 10.2174/156652411795243441
    • Militello, R. D., and Colombo, M. I. (2011). A membrane is born: origin of the autophagosomal compartment. Curr. Mol. Med. 11, 197-203. doi: 10.2174/156652411795243441
    • (2011) Curr. Mol. Med. , vol.11 , pp. 197-203
    • Militello, R.D.1    Colombo, M.I.2
  • 98
    • 0036636124 scopus 로고    scopus 로고
    • [Molecular mechanism of autophagy: the role of the Apg12 conjugation system]
    • Mizushima, N. (2002). [Molecular mechanism of autophagy: the role of the Apg12 conjugation system]. Seikagaku 74, 523-537.
    • (2002) Seikagaku , vol.74 , pp. 523-537
    • Mizushima, N.1
  • 99
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • doi: 10.1038/nature06639
    • Mizushima, N., Levine, B., Cuervo, A. M., and Klionsky, D. J. (2008). Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075. doi: 10.1038/nature06639
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 100
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • doi: 10.1038/26506
    • Mizushima, N., Noda, T., Yoshimori, T., Tanaka, Y., Ishii, T., George, M. D., et al. (1998). A protein conjugation system essential for autophagy. Nature 395, 395-398. doi: 10.1038/26506
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1    Noda, T.2    Yoshimori, T.3    Tanaka, Y.4    Ishii, T.5    George, M.D.6
  • 101
    • 78349239252 scopus 로고    scopus 로고
    • Entrapment of intracytosolic bacteria by septin cage-like structures
    • doi: 10.1016/j.chom.2010.10.009
    • Mostowy, S., Bonazzi, M., Hamon, M. A., Tham, T. N., Mallet, A., Lelek, M., et al. (2010). Entrapment of intracytosolic bacteria by septin cage-like structures. Cell Host Microbe 8, 433-444. doi: 10.1016/j.chom.2010.10.009
    • (2010) Cell Host Microbe , vol.8 , pp. 433-444
    • Mostowy, S.1    Bonazzi, M.2    Hamon, M.A.3    Tham, T.N.4    Mallet, A.5    Lelek, M.6
  • 102
    • 79960670161 scopus 로고    scopus 로고
    • p62 and NDP52 proteins target intracytosolic Shigella and Listeria to different autophagy pathways
    • doi: 10.1074/jbc.M111.223610
    • Mostowy, S., Sancho-Shimizu, V., Hamon, M. A., Simeone, R., Brosch, R., Johansen, T., et al. (2011). p62 and NDP52 proteins target intracytosolic Shigella and Listeria to different autophagy pathways. J. Biol. Chem. 286, 26987-26995. doi: 10.1074/jbc.M111.223610
    • (2011) J. Biol. Chem. , vol.286 , pp. 26987-26995
    • Mostowy, S.1    Sancho-Shimizu, V.2    Hamon, M.A.3    Simeone, R.4    Brosch, R.5    Johansen, T.6
  • 103
    • 8344247016 scopus 로고    scopus 로고
    • Autophagy defends cells against invading group A Streptococcus
    • doi: 10.1126/science.1103966
    • Nakagawa, I., Amano, A., Mizushima, N., Yamamoto, A., Yamaguchi, H., Kamimoto, T., et al. (2004). Autophagy defends cells against invading group A Streptococcus. Science 306, 1037-1040. doi: 10.1126/science.1103966
    • (2004) Science , vol.306 , pp. 1037-1040
    • Nakagawa, I.1    Amano, A.2    Mizushima, N.3    Yamamoto, A.4    Yamaguchi, H.5    Kamimoto, T.6
  • 104
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • doi: 10.1016/j.febslet.2010.01.018
    • Noda, N. N., Ohsumi, Y., and Inagaki, F. (2010). Atg8-family interacting motif crucial for selective autophagy. FEBS Lett. 584, 1379-1385. doi: 10.1016/j.febslet.2010.01.018
    • (2010) FEBS Lett , vol.584 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 105
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • doi: 10.1074/jbc.273.7.3963
    • Noda, T., and Ohsumi, Y. (1998). Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273, 3963-3966. doi: 10.1074/jbc.273.7.3963
    • (1998) J. Biol. Chem. , vol.273 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 106
    • 79956147302 scopus 로고    scopus 로고
    • A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens
    • doi: 10.1016/j.chom.2011.04.010
    • Ogawa, M., Yoshikawa, Y., Kobayashi, T., Mimuro, H., Fukumatsu, M., Kiga, K., et al. (2011). A Tecpr1-dependent selective autophagy pathway targets bacterial pathogens. Cell Host Microbe 9, 376-389. doi: 10.1016/j.chom.2011.04.010
    • (2011) Cell Host Microbe , vol.9 , pp. 376-389
    • Ogawa, M.1    Yoshikawa, Y.2    Kobayashi, T.3    Mimuro, H.4    Fukumatsu, M.5    Kiga, K.6
  • 107
    • 31944448737 scopus 로고    scopus 로고
    • Intracellular survival of Shigella
    • doi: 10.1111/j.1462-5822.2005.00652.x
    • Ogawa, M., and Sasakawa, C. (2006). Intracellular survival of Shigella. Cell. Microbiol. 8, 177-184. doi: 10.1111/j.1462-5822.2005.00652.x
    • (2006) Cell. Microbiol. , vol.8 , pp. 177-184
    • Ogawa, M.1    Sasakawa, C.2
  • 108
    • 80655130334 scopus 로고    scopus 로고
    • The role of Tecpr1 in selective autophagy as a cargo receptor
    • doi: 10.4161/auto.7.11.17151
    • Ogawa, M., and Sasakawa, C. (2011). The role of Tecpr1 in selective autophagy as a cargo receptor. Autophagy 7, 1389-1391. doi: 10.4161/auto.7.11.17151
    • (2011) Autophagy , vol.7 , pp. 1389-1391
    • Ogawa, M.1    Sasakawa, C.2
  • 109
    • 13244256806 scopus 로고    scopus 로고
    • Escape of intracellular Shigella from autophagy
    • doi: 10.1126/science.1106036
    • Ogawa, M., Yoshimori, T., Suzuki, T., Sagara, H., Mizushima, N., and Sasakawa, C. (2005). Escape of intracellular Shigella from autophagy. Science 307, 727-731. doi: 10.1126/science.1106036
    • (2005) Science , vol.307 , pp. 727-731
    • Ogawa, M.1    Yoshimori, T.2    Suzuki, T.3    Sagara, H.4    Mizushima, N.5    Sasakawa, C.6
  • 110
    • 0035431216 scopus 로고    scopus 로고
    • [Molecular mechanism of bulk protein degradation in lysosome/vacuole]
    • Ohsumi, Y. (2001). [Molecular mechanism of bulk protein degradation in lysosome/vacuole]. Tanpakushitsu Kakusan Koso 46, 1710-1716.
    • (2001) Tanpakushitsu Kakusan Koso , vol.46 , pp. 1710-1716
    • Ohsumi, Y.1
  • 111
    • 5044222206 scopus 로고    scopus 로고
    • Immune responses to Listeria monocytogenes
    • doi: 10.1038/nri1461
    • Pamer, E. G. (2004). Immune responses to Listeria monocytogenes. Nat. Rev. Immunol. 4, 812-823. doi: 10.1038/nri1461
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 812-823
    • Pamer, E.G.1
  • 112
    • 0031026639 scopus 로고    scopus 로고
    • Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex
    • doi: 10.1074/jbc.272.4.2477
    • Panaretou, C., Domin, J., Cockcroft, S., and Waterfield, M. D. (1997). Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase complex. J. Biol. Chem. 272, 2477-2485. doi: 10.1074/jbc.272.4.2477
    • (1997) J. Biol. Chem. , vol.272 , pp. 2477-2485
    • Panaretou, C.1    Domin, J.2    Cockcroft, S.3    Waterfield, M.D.4
  • 113
    • 77954271859 scopus 로고    scopus 로고
    • Galectin-3, a marker for vacuole lysis by invasive pathogens
    • doi: 10.1111/j.1462-5822.2009.01415.x
    • Paz, I., Sachse, M., Dupont, N., Mounier, J., Cederfur, C., Enninga, J., et al. (2010). Galectin-3, a marker for vacuole lysis by invasive pathogens. Cell. Microbiol. 12, 530-544. doi: 10.1111/j.1462-5822.2009.01415.x
    • (2010) Cell. Microbiol. , vol.12 , pp. 530-544
    • Paz, I.1    Sachse, M.2    Dupont, N.3    Mounier, J.4    Cederfur, C.5    Enninga, J.6
  • 114
    • 2342464290 scopus 로고    scopus 로고
    • Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system
    • doi: 10.1016/j.cub.2004.04.033
    • Perrin, A. J., Jiang, X., Birmingham, C. L., So, N. S., and Brumell, J. H. (2004). Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system. Curr. Biol. 14, 806-811. doi: 10.1016/j.cub.2004.04.033
    • (2004) Curr. Biol. , vol.14 , pp. 806-811
    • Perrin, A.J.1    Jiang, X.2    Birmingham, C.L.3    So, N.S.4    Brumell, J.H.5
  • 115
    • 84865357562 scopus 로고    scopus 로고
    • TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation
    • doi: 10.1016/j.immuni.2012.04.015
    • Pilli, M., Arko-Mensah, J., Ponpuak, M., Roberts, E., Master, S., Mandell, M. A., et al. (2012). TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation. Immunity 37, 223-234. doi: 10.1016/j.immuni.2012.04.015
    • (2012) Immunity , vol.37 , pp. 223-234
    • Pilli, M.1    Arko-Mensah, J.2    Ponpuak, M.3    Roberts, E.4    Master, S.5    Mandell, M.A.6
  • 116
    • 0037711625 scopus 로고    scopus 로고
    • Cytoplasmic bacteria can be targets for autophagy
    • doi: 10.1046/j.1462-5822.2003.00292.x
    • Rich, K. A., Burkett, C., and Webster, P. (2003). Cytoplasmic bacteria can be targets for autophagy. Cell. Microbiol. 5, 455-468. doi: 10.1046/j.1462-5822.2003.00292.x
    • (2003) Cell. Microbiol. , vol.5 , pp. 455-468
    • Rich, K.A.1    Burkett, C.2    Webster, P.3
  • 117
    • 33748989856 scopus 로고    scopus 로고
    • Higher order Rab programming in phagolysosome biogenesis
    • doi: 10.1083/jcb.200603026
    • Roberts, E. A., Chua, J., Kyei, G. B., and Deretic, V. (2006). Higher order Rab programming in phagolysosome biogenesis. J. Cell Biol. 174, 923-929. doi: 10.1083/jcb.200603026
    • (2006) J. Cell Biol. , vol.174 , pp. 923-929
    • Roberts, E.A.1    Chua, J.2    Kyei, G.B.3    Deretic, V.4
  • 118
    • 84866554596 scopus 로고    scopus 로고
    • ESX-1 dependent impairment of autophagic flux by Mycobacterium tuberculosis in human dendritic cells
    • doi: 10.4161/auto.20881
    • Romagnoli, A., Etna, M. P., Giacomini, E., Pardini, M., Remoli, M. E., Corazzari, M., et al. (2012). ESX-1 dependent impairment of autophagic flux by Mycobacterium tuberculosis in human dendritic cells. Autophagy 8, 1357-1370. doi: 10.4161/auto.20881
    • (2012) Autophagy , vol.8 , pp. 1357-1370
    • Romagnoli, A.1    Etna, M.P.2    Giacomini, E.3    Pardini, M.4    Remoli, M.E.5    Corazzari, M.6
  • 119
    • 33947167752 scopus 로고    scopus 로고
    • The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell
    • doi: 10.1111/j.1462-5822.2006.00838.x
    • Romano, P. S., Gutierrez, M. G., Beron, W., Rabinovitch, M., and Colombo, M. I. (2007). The autophagic pathway is actively modulated by phase II Coxiella burnetii to efficiently replicate in the host cell. Cell. Microbiol. 9, 891-909. doi: 10.1111/j.1462-5822.2006.00838.x
    • (2007) Cell. Microbiol. , vol.9 , pp. 891-909
    • Romano, P.S.1    Gutierrez, M.G.2    Beron, W.3    Rabinovitch, M.4    Colombo, M.I.5
  • 120
    • 0036322591 scopus 로고    scopus 로고
    • Mycobacterium and the coat of many lipids
    • doi: 10.1083/jcb.200205034
    • Russell, D. G., Mwandumba, H. C., and Rhoades, E. E. (2002). Mycobacterium and the coat of many lipids. J. Cell Biol. 158, 421-426. doi: 10.1083/jcb.200205034
    • (2002) J. Cell Biol. , vol.158 , pp. 421-426
    • Russell, D.G.1    Mwandumba, H.C.2    Rhoades, E.E.3
  • 121
    • 0022630209 scopus 로고
    • Multiplication of Shigella flexneri within HeLa cells: lysis of the phagocytic vacuole and plasmid-mediated contact hemolysis
    • Sansonetti, P. J., Ryter, A., Clerc, P., Maurelli, A. T., and Mounier, J. (1986). Multiplication of Shigella flexneri within HeLa cells: lysis of the phagocytic vacuole and plasmid-mediated contact hemolysis. Infect. Immun. 51, 461-469.
    • (1986) Infect. Immun. , vol.51 , pp. 461-469
    • Sansonetti, P.J.1    Ryter, A.2    Clerc, P.3    Maurelli, A.T.4    Mounier, J.5
  • 122
    • 46249110662 scopus 로고    scopus 로고
    • Acquisition of the vacuolar ATPase proton pump and phagosome acidification are essential for escape of Francisella tularensis into the macrophage cytosol
    • doi: 10.1128/IAI.00185-08
    • Santic, M., Asare, R., Skrobonja, I., Jones, S., and Abu, K. Y. (2008). Acquisition of the vacuolar ATPase proton pump and phagosome acidification are essential for escape of Francisella tularensis into the macrophage cytosol. Infect. Immun. 76, 2671-2677. doi: 10.1128/IAI.00185-08
    • (2008) Infect. Immun. , vol.76 , pp. 2671-2677
    • Santic, M.1    Asare, R.2    Skrobonja, I.3    Jones, S.4    Abu, K.Y.5
  • 123
    • 23344445007 scopus 로고    scopus 로고
    • Specificity of Legionella pneumophila and Coxiella burnetii vacuoles and versatility of Legionella pneumophila revealed by coinfection
    • doi: 10.1128/IAI.73.8.4494-4504.2005
    • Sauer, J. D., Shannon, J. G., Howe, D., Hayes, S. F., Swanson, M. S., and Heinzen, R. A. (2005). Specificity of Legionella pneumophila and Coxiella burnetii vacuoles and versatility of Legionella pneumophila revealed by coinfection. Infect. Immun. 73, 4494-4504. doi: 10.1128/IAI.73.8.4494-4504.2005
    • (2005) Infect. Immun. , vol.73 , pp. 4494-4504
    • Sauer, J.D.1    Shannon, J.G.2    Howe, D.3    Hayes, S.F.4    Swanson, M.S.5    Heinzen, R.A.6
  • 125
    • 79952807443 scopus 로고    scopus 로고
    • Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes
    • doi: 10.1111/j.1600-0854.2011.01165.x
    • Seto, S., Tsujimura, K., and Koide, Y. (2011). Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic 12, 407-420. doi: 10.1111/j.1600-0854.2011.01165.x
    • (2011) Traffic , vol.12 , pp. 407-420
    • Seto, S.1    Tsujimura, K.2    Koide, Y.3
  • 126
    • 77956310643 scopus 로고    scopus 로고
    • A diacylglycerol-dependent signaling pathway contributes to regulation of antibacterial autophagy
    • doi: 10.1016/j.chom.2010.07.002
    • Shahnazari, S., Yen, W. L., Birmingham, C. L., Shiu, J., Namolovan, A., Zheng, Y. T., et al. (2010). A diacylglycerol-dependent signaling pathway contributes to regulation of antibacterial autophagy. Cell Host Microbe 8, 137-146. doi: 10.1016/j.chom.2010.07.002
    • (2010) Cell Host Microbe , vol.8 , pp. 137-146
    • Shahnazari, S.1    Yen, W.L.2    Birmingham, C.L.3    Shiu, J.4    Namolovan, A.5    Zheng, Y.T.6
  • 127
    • 20844459331 scopus 로고    scopus 로고
    • Virulent Coxiella burnetii does not activate human dendritic cells: role of lipopolysaccharide as a shielding molecule
    • doi: 10.1073/pnas.0501863102
    • Shannon, J. G., Howe, D., and Heinzen, R. A. (2005). Virulent Coxiella burnetii does not activate human dendritic cells: role of lipopolysaccharide as a shielding molecule. Proc. Natl. Acad. Sci. U.S.A. 102, 8722-8727. doi: 10.1073/pnas.0501863102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8722-8727
    • Shannon, J.G.1    Howe, D.2    Heinzen, R.A.3
  • 128
    • 78651226124 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis eis regulates autophagy, inflammation, and cell death through redox-dependent signaling SHIN2010
    • doi: 10.1371/journal.ppat.1001230
    • Shin, D. M., Jeon, B. Y., Lee, H. M., Jin, H. S., Yuk, J. M., Song, C. H., et al. (2010). Mycobacterium tuberculosis eis regulates autophagy, inflammation, and cell death through redox-dependent signaling SHIN2010. PLoS Pathog. 6:e1001230. doi: 10.1371/journal.ppat.1001230
    • (2010) PLoS Pathog , vol.6
    • Shin, D.M.1    Jeon, B.Y.2    Lee, H.M.3    Jin, H.S.4    Yuk, J.M.5    Song, C.H.6
  • 129
    • 84859972311 scopus 로고    scopus 로고
    • Phagosomal rupture by Mycobacterium tuberculosis results in toxicity and host cell death
    • doi: 10.1371/journal.ppat.1002507
    • Simeone, R., Bobard, A., Lippmann, J., Bitter, W., Majlessi, L., Brosch, R., et al. (2012). Phagosomal rupture by Mycobacterium tuberculosis results in toxicity and host cell death. PLoS Pathog. 8:e1002507. doi: 10.1371/journal.ppat.1002507
    • (2012) PLoS Pathog , vol.8
    • Simeone, R.1    Bobard, A.2    Lippmann, J.3    Bitter, W.4    Majlessi, L.5    Brosch, R.6
  • 130
    • 57349164051 scopus 로고    scopus 로고
    • Evidence for pore formation in host cell membranes by ESX-1-secreted ESAT-6 and its role in Mycobacterium marinum escape from the vacuole
    • doi: 10.1128/IAI.00614-08
    • Smith, J., Manoranjan, J., Pan, M., Bohsali, A., Xu, J., Liu, J., et al. (2008). Evidence for pore formation in host cell membranes by ESX-1-secreted ESAT-6 and its role in Mycobacterium marinum escape from the vacuole. Infect. Immun. 76, 5478-5487. doi: 10.1128/IAI.00614-08
    • (2008) Infect. Immun. , vol.76 , pp. 5478-5487
    • Smith, J.1    Manoranjan, J.2    Pan, M.3    Bohsali, A.4    Xu, J.5    Liu, J.6
  • 131
    • 0242611003 scopus 로고    scopus 로고
    • Mycobacterium marinum escapes from phagosomes and is propelled by actin-based motility
    • doi: 10.1084/jem.20031072
    • Stamm, L. M., Morisaki, J. H., Gao, L. Y., Jeng, R. L., McDonald, K. L., Roth, R., et al. (2003). Mycobacterium marinum escapes from phagosomes and is propelled by actin-based motility. J. Exp. Med. 198, 1361-1368. doi: 10.1084/jem.20031072
    • (2003) J. Exp. Med. , vol.198 , pp. 1361-1368
    • Stamm, L.M.1    Morisaki, J.H.2    Gao, L.Y.3    Jeng, R.L.4    McDonald, K.L.5    Roth, R.6
  • 132
    • 0036161224 scopus 로고    scopus 로고
    • The invasion-associated type III secretion system of Salmonella enterica serovar Typhimurium is necessary for intracellular proliferation and vacuole biogenesis in epithelial cells
    • doi: 10.1046/j.1462-5822.2002.00170.x
    • Steele-Mortimer, O., Brumell, J. H., Knodler, L. A., Meresse, S., Lopez, A., and Finlay, B. B. (2002). The invasion-associated type III secretion system of Salmonella enterica serovar Typhimurium is necessary for intracellular proliferation and vacuole biogenesis in epithelial cells. Cell. Microbiol. 4, 43-54. doi: 10.1046/j.1462-5822.2002.00170.x
    • (2002) Cell. Microbiol. , vol.4 , pp. 43-54
    • Steele-Mortimer, O.1    Brumell, J.H.2    Knodler, L.A.3    Meresse, S.4    Lopez, A.5    Finlay, B.B.6
  • 133
    • 0034613726 scopus 로고    scopus 로고
    • Legionella pneumophila replication vacuoles mature into acidic, endocytic organelles
    • doi: 10.1084/jem.192.9.1261
    • Sturgill-Koszycki, S., and Swanson, M. S. (2000). Legionella pneumophila replication vacuoles mature into acidic, endocytic organelles. J. Exp. Med. 192, 1261-1272. doi: 10.1084/jem.192.9.1261
    • (2000) J. Exp. Med. , vol.192 , pp. 1261-1272
    • Sturgill-Koszycki, S.1    Swanson, M.S.2
  • 134
    • 37249083417 scopus 로고    scopus 로고
    • Mycobacterium bovis BCG disrupts the interaction of Rab7 with RILP contributing to inhibition of phagosome maturation
    • doi: 10.1189/jlb.0507289
    • Sun, J., Deghmane, A. E., Soualhine, H., Hong, T., Bucci, C., Solodkin, A., et al. (2007). Mycobacterium bovis BCG disrupts the interaction of Rab7 with RILP contributing to inhibition of phagosome maturation. J. Leukoc. Biol. 82, 1437-1445. doi: 10.1189/jlb.0507289
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 1437-1445
    • Sun, J.1    Deghmane, A.E.2    Soualhine, H.3    Hong, T.4    Bucci, C.5    Solodkin, A.6
  • 135
    • 0029155737 scopus 로고
    • Association of Legionella pneumophila with the macrophage endoplasmic reticulum
    • Swanson, M. S., and Isberg, R. R. (1995). Association of Legionella pneumophila with the macrophage endoplasmic reticulum. Infect. Immun. 63, 3609-3620.
    • (1995) Infect. Immun. , vol.63 , pp. 3609-3620
    • Swanson, M.S.1    Isberg, R.R.2
  • 136
    • 84964872341 scopus 로고    scopus 로고
    • The bacterial and cellular determinants controlling the recruitment of mTOR to the Salmonella-containing vacuole
    • doi: 10.1242/bio.20122840
    • Tattoli, I., Philpott, D. J., and Girardin, S. E. (2012). The bacterial and cellular determinants controlling the recruitment of mTOR to the Salmonella-containing vacuole. Biol. Open 1, 1215-1225. doi: 10.1242/bio.20122840
    • (2012) Biol. Open , vol.1 , pp. 1215-1225
    • Tattoli, I.1    Philpott, D.J.2    Girardin, S.E.3
  • 137
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • doi: 10.1038/ni.1800
    • Thurston, T. L., Ryzhakov, G., Bloor, S., von, M. N., and Randow, F. (2009). The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat. Immunol. 10, 1215-1221. doi: 10.1038/ni.1800
    • (2009) Nat. Immunol. , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    von Muhlinen, N.4    Randow, F.5
  • 138
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • doi: 10.1038/nature10744
    • Thurston, T. L., Wandel, M. P., von, M. N., Foeglein, A., and Randow, F. (2012). Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature 482, 414-418. doi: 10.1038/nature10744
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.1    Wandel, M.P.2    von Muhlinen, N.3    Foeglein, A.4    Randow, F.5
  • 139
    • 38849105061 scopus 로고    scopus 로고
    • A picky eater: exploring the mechanisms of selective autophagy in human pathologies
    • doi: 10.1111/j.1600-0854.2007.00674.x
    • van der Vaart, A., Mari, M., and Reggiori, F. (2008). A picky eater: exploring the mechanisms of selective autophagy in human pathologies. Traffic 9, 281-289. doi: 10.1111/j.1600-0854.2007.00674.x
    • (2008) Traffic , vol.9 , pp. 281-289
    • van der Vaart, A.1    Mari, M.2    Reggiori, F.3
  • 140
    • 34250716965 scopus 로고    scopus 로고
    • M. tuberculosis and M. leprae translocate from the phagolysosome to the cytosol in myeloid cells
    • doi: 10.1016/j.cell.2007.05.059
    • van der Wel, N., Hava, D., Houben, D., Fluitsma, D., van, Z. M., Pierson, J., et al. (2007). M. tuberculosis and M. leprae translocate from the phagolysosome to the cytosol in myeloid cells. Cell 129, 1287-1298. doi: 10.1016/j.cell.2007.05.059
    • (2007) Cell , vol.129 , pp. 1287-1298
    • van der Wel, N.1    Hava, D.2    Houben, D.3    Fluitsma, D.4    van Zon, M.5    Pierson, J.6
  • 141
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: more than just a road to PKB
    • doi: 10.1042/0264-6021:3460561
    • Vanhaesebroeck, B., and Alessi, D. R. (2000). The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J. 346(Pt 3), 561-576. doi: 10.1042/0264-6021:3460561
    • (2000) Biochem. J. , vol.346 , Issue.PART 3 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 142
    • 84872466790 scopus 로고    scopus 로고
    • Eat-me: autophagy, phagocytosis, and reactive oxygen species signaling. Antioxid
    • doi: 10.1089/ars.2012.4810
    • Vernon, P. J., and Tang, D. (2013). Eat-me: autophagy, phagocytosis, and reactive oxygen species signaling. Antioxid. Redox Signal. 18, 677-691. doi: 10.1089/ars.2012.4810
    • (2013) Redox Signal , vol.18 , pp. 677-691
    • Vernon, P.J.1    Tang, D.2
  • 143
    • 84877792258 scopus 로고    scopus 로고
    • Targeting the intracellular environment in cystic fibrosis: restoring autophagy as a novel strategy to circumvent the CFTR defect
    • doi: 10.3389/fphar.2013.00001
    • Villella, V. R., Esposito, S., Bruscia, E. M., Maiuri, M. C., Raia, V., Kroemer, G., et al. (2013). Targeting the intracellular environment in cystic fibrosis: restoring autophagy as a novel strategy to circumvent the CFTR defect. Front. Pharmacol. 4:1. doi: 10.3389/fphar.2013.00001
    • (2013) Front. Pharmacol. , vol.4 , pp. 1
    • Villella, V.R.1    Esposito, S.2    Bruscia, E.M.3    Maiuri, M.C.4    Raia, V.5    Kroemer, G.6
  • 144
    • 33947141939 scopus 로고    scopus 로고
    • Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii
    • doi: 10.1111/j.1462-5822.2007.00901.x
    • Voth, D. E., and Heinzen, R. A. (2007). Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii. Cell. Microbiol. 9, 829-840. doi: 10.1111/j.1462-5822.2007.00901.x
    • (2007) Cell. Microbiol. , vol.9 , pp. 829-840
    • Voth, D.E.1    Heinzen, R.A.2
  • 145
    • 84865220380 scopus 로고    scopus 로고
    • Extracellular, M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway
    • doi: 10.1016/j.cell.2012.06.040
    • Watson, R. O., Manzanillo, P. S., and Cox, J. S. (2012). Extracellular, M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway. Cell 150, 803-815. doi: 10.1016/j.cell.2012.06.040
    • (2012) Cell , vol.150 , pp. 803-815
    • Watson, R.O.1    Manzanillo, P.S.2    Cox, J.S.3
  • 146
    • 66749093481 scopus 로고    scopus 로고
    • Intracellular biology and virulence determinants of Francisella tularensis revealed by transcriptional profiling inside macrophages
    • doi: 10.1111/j.1462-5822.2009.01316.x
    • Wehrly, T. D., Farhan, H., McEwan, D. G., Wagner, S., Rogov, V. V., Brady, N. R., et al. (2009). Intracellular biology and virulence determinants of Francisella tularensis revealed by transcriptional profiling inside macrophages. Cell. Microbiol. 11, 1128-1150. doi: 10.1111/j.1462-5822.2009.01316.x
    • (2009) Cell. Microbiol. , vol.11 , pp. 1128-1150
    • Wehrly, T.D.1    Farhan, H.2    McEwan, D.G.3    Wagner, S.4    Rogov, V.V.5    Brady, N.R.6
  • 147
    • 80052197913 scopus 로고    scopus 로고
    • TBK1 mediates crosstalk between the innate immune response and autophagy
    • doi: 10.1126/scisignal.2002355
    • Weidberg, H., and Elazar, Z. (2011). TBK1 mediates crosstalk between the innate immune response and autophagy. Sci. Signal. 4:e39. doi: 10.1126/scisignal.2002355
    • (2011) Sci. Signal. , vol.4
    • Weidberg, H.1    Elazar, Z.2
  • 148
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • doi: 10.1126/science.1205405
    • Wild, P., Farhan, H., McEwan, D. G., Wagner, S., Rogov, V. V., Brady, N. R., et al. (2011). Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333, 228-233. doi: 10.1126/science.1205405
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1    Farhan, H.2    McEwan, D.G.3    Wagner, S.4    Rogov, V.V.5    Brady, N.R.6
  • 149
    • 35448965809 scopus 로고    scopus 로고
    • A unique Mycobacterium ESX-1 protein co-secretes with CFP-10/ESAT-6 and is necessary for inhibiting phagosome maturation
    • doi: 10.1111/j.1365-2958.2007.05959.x
    • Xu, J., Laine, O., Masciocchi, M., Manoranjan, J., Smith, J., Du, S. J., et al. (2007). A unique Mycobacterium ESX-1 protein co-secretes with CFP-10/ESAT-6 and is necessary for inhibiting phagosome maturation. Mol. Microbiol. 66, 787-800. doi: 10.1111/j.1365-2958.2007.05959.x
    • (2007) Mol. Microbiol. , vol.66 , pp. 787-800
    • Xu, J.1    Laine, O.2    Masciocchi, M.3    Manoranjan, J.4    Smith, J.5    Du, S.J.6
  • 150
    • 73449109492 scopus 로고    scopus 로고
    • Listeria monocytogenes ActA is a key player in evading autophagic recognition
    • doi: 10.4161/auto.5.8.10177
    • Yoshikawa, Y., Ogawa, M., Hain, T., Chakraborty, T., and Sasakawa, C. (2009a). Listeria monocytogenes ActA is a key player in evading autophagic recognition. Autophagy 5, 1220-1221. doi: 10.4161/auto.5.8.10177
    • (2009) Autophagy , vol.5 , pp. 1220-1221
    • Yoshikawa, Y.1    Ogawa, M.2    Hain, T.3    Chakraborty, T.4    Sasakawa, C.5
  • 151
    • 70349652310 scopus 로고    scopus 로고
    • Listeria monocytogenes ActA-mediated escape from autophagic recognition
    • doi: 10.1038/ncb1967
    • Yoshikawa, Y., Ogawa, M., Hain, T., Yoshida, M., Fukumatsu, M., Kim, M., et al. (2009b). Listeria monocytogenes ActA-mediated escape from autophagic recognition. Nat. Cell Biol. 11, 1233-1240. doi: 10.1038/ncb1967
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1233-1240
    • Yoshikawa, Y.1    Ogawa, M.2    Hain, T.3    Yoshida, M.4    Fukumatsu, M.5    Kim, M.6
  • 152
    • 0347626252 scopus 로고    scopus 로고
    • Autophagy: a regulated bulk degradation process inside cells. Biochem. Biophys
    • doi: 10.1016/j.bbrc.2003.07.023
    • Yoshimori, T. (2004). Autophagy: a regulated bulk degradation process inside cells. Biochem. Biophys. Res. Commun. 313, 453-458. doi: 10.1016/j.bbrc.2003.07.023
    • (2004) Res. Commun. , vol.313 , pp. 453-458
    • Yoshimori, T.1
  • 153
    • 33749162486 scopus 로고    scopus 로고
    • Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis
    • doi: 10.1038/ncb1482
    • Yousefi, S., Perozzo, R., Schmid, I., Ziemiecki, A., Schaffner, T., Scapozza, L., et al. (2006). Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis. Nat. Cell Biol. 8, 1124-1132. doi: 10.1038/ncb1482
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1124-1132
    • Yousefi, S.1    Perozzo, R.2    Schmid, I.3    Ziemiecki, A.4    Schaffner, T.5    Scapozza, L.6
  • 154
    • 79954557629 scopus 로고    scopus 로고
    • Interleukin-10 polymorphisms and tuberculosis susceptibility: a meta-analysis
    • doi: 10.5588/ijtld.09.0703
    • Zhang, J., Chen, Y., Nie, X. B., Wu, W. H., Zhang, H., Zhang, M., et al. (2011). Interleukin-10 polymorphisms and tuberculosis susceptibility: a meta-analysis. Int. J. Tuberc. Lung Dis. 15, 594-601. doi: 10.5588/ijtld.09.0703
    • (2011) Int. J. Tuberc. Lung Dis. , vol.15 , pp. 594-601
    • Zhang, J.1    Chen, Y.2    Nie, X.B.3    Wu, W.H.4    Zhang, H.5    Zhang, M.6
  • 155
    • 74049126112 scopus 로고    scopus 로고
    • The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway
    • doi: 10.4049/jimmunol.0900441
    • Zheng, Y. T., Shahnazari, S., Brech, A., Lamark, T., Johansen, T., and Brumell, J. H. (2009). The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway. J. Immunol. 183, 5909-5916. doi: 10.4049/jimmunol.0900441
    • (2009) J. Immunol. , vol.183 , pp. 5909-5916
    • Zheng, Y.T.1    Shahnazari, S.2    Brech, A.3    Lamark, T.4    Johansen, T.5    Brumell, J.H.6
  • 156
    • 77955239270 scopus 로고    scopus 로고
    • Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites
    • doi: 10.1111/j.1600-0854.2010.01086.x
    • Zoppino, F. C., Militello, R. D., Slavin, I., Alvarez, C., and Colombo, M. I. (2010). Autophagosome formation depends on the small GTPase Rab1 and functional ER exit sites. Traffic 11, 1246-1261. doi: 10.1111/j.1600-0854.2010.01086.x
    • (2010) Traffic , vol.11 , pp. 1246-1261
    • Zoppino, F.C.1    Militello, R.D.2    Slavin, I.3    Alvarez, C.4    Colombo, M.I.5


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