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Volumn 21, Issue 11, 2009, Pages 1199-1204

Molecular basis of canonical and bactericidal autophagy

Author keywords

Atg14; Atg16L; LC3; PI3P; Xenophagy

Indexed keywords

CELL PROTEIN; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PROTEIN LC3; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 71049130205     PISSN: 09538178     EISSN: 14602377     Source Type: Journal    
DOI: 10.1093/intimm/dxp088     Document Type: Review
Times cited : (37)

References (53)
  • 1
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky, D. J. and Emr, S. D. 2000. Autophagy as a regulated pathway of cellular degradation. Science 290:1717.
    • (2000) Science , vol.290 , pp. 1717
    • Klionsky, D.J.1    Emr, S.D.2
  • 2
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • Noda, T. and Ohsumi, Y. 1998. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273: 3963.
    • (1998) J. Biol. Chem , vol.273 , pp. 3963
    • Noda, T.1    Ohsumi, Y.2
  • 3
    • 47149103494 scopus 로고    scopus 로고
    • Toward unraveling membrane biogenesis in mammalian autophagy
    • Yoshimori, T. and Noda, T. 2008. Toward unraveling membrane biogenesis in mammalian autophagy. Curr. Opin. Cell Biol. 20: 401.
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 401
    • Yoshimori, T.1    Noda, T.2
  • 4
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes
    • Kimura, S., Noda, T. and Yoshimori, T. 2008. Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell Struct. Funct. 33:109.
    • (2008) Cell Struct. Funct , vol.33 , pp. 109
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 6
    • 33745357459 scopus 로고    scopus 로고
    • Autophagy as an immune defense mechanism
    • Deretic, V. 2006. Autophagy as an immune defense mechanism. Curr. Opin. Immunol. 18:375.
    • (2006) Curr. Opin. Immunol , vol.18 , pp. 375
    • Deretic, V.1
  • 7
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya, Y., Mizushima, N., Ueno, T. et al. 2000. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 19:5720.
    • (2000) EMBO J , vol.19 , pp. 5720
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3
  • 8
    • 0032126632 scopus 로고    scopus 로고
    • Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole
    • Lang, T., Schaeffeler, E., Bernreuther, D., Bredschneider, M., Wolf, D. H. and Thumm, M. 1998. Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole. EMBO J. 17:3597.
    • (1998) EMBO J , vol.17 , pp. 3597
    • Lang, T.1    Schaeffeler, E.2    Bernreuther, D.3    Bredschneider, M.4    Wolf, D.H.5    Thumm, M.6
  • 9
    • 33646690504 scopus 로고    scopus 로고
    • Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3
    • Tanida, I., Sou, Y. S., Minematsu-Ikeguchi, N., Ueno, T. and Kominami, E. 2006. Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3. FEBS J. 273:2553.
    • (2006) FEBS J , vol.273 , pp. 2553
    • Tanida, I.1    Sou, Y.S.2    Minematsu-Ikeguchi, N.3    Ueno, T.4    Kominami, E.5
  • 11
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • Kirisako, T., Ichimura, Y., Okada, H. et al. 2000. The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J. Cell Biol. 151:263.
    • (2000) J. Cell Biol , vol.151 , pp. 263
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3
  • 12
    • 0034707036 scopus 로고    scopus 로고
    • A ubiquitin-like system mediates protein lipidation
    • Ichimura, Y., Kirisako, T., Takao, T. et al. 2000. A ubiquitin-like system mediates protein lipidation. Nature 408:488.
    • (2000) Nature , vol.408 , pp. 488
    • Ichimura, Y.1    Kirisako, T.2    Takao, T.3
  • 13
    • 0034050457 scopus 로고    scopus 로고
    • The itinerary of a vesicle component, Aut7p/Cvt5p, terminates in the yeast vacuole via the autophagy/Cvt pathways
    • Huang, W. P., Scott, S. V., Kim, J. and Klionsky, D. J. 2000. The itinerary of a vesicle component, Aut7p/Cvt5p, terminates in the yeast vacuole via the autophagy/Cvt pathways. J. Biol. Chem. 275:5845.
    • (2000) J. Biol. Chem , vol.275 , pp. 5845
    • Huang, W.P.1    Scott, S.V.2    Kim, J.3    Klionsky, D.J.4
  • 14
    • 58149290220 scopus 로고    scopus 로고
    • An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure
    • Fujita, N., Hayashi-Nishino, M., Fukumoto, H. et al. 2008. An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure. Mol. Biol. Cell 19:4651.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4651
    • Fujita, N.1    Hayashi-Nishino, M.2    Fukumoto, H.3
  • 15
    • 57549094368 scopus 로고    scopus 로고
    • The Atg8 conjugation system is indispensable for proper development of autophagic isolation membranes in mice
    • Sou, Y. S., Waguri, S., Iwata, J. et al. 2008. The Atg8 conjugation system is indispensable for proper development of autophagic isolation membranes in mice. Mol. Biol. Cell 19:4762.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4762
    • Sou, Y.S.1    Waguri, S.2    Iwata, J.3
  • 16
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion
    • Nakatogawa, H., Ichimura, Y. and Ohsumi, Y. 2007. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell 130:165.
    • (2007) Cell , vol.130 , pp. 165
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 17
    • 67549132527 scopus 로고    scopus 로고
    • The late stages of autophagy: How does the end begin?
    • Noda, T., Fujita, N. and Yoshimori, T. 2009. The late stages of autophagy: How does the end begin? Cell Death Differ. 16: 984.
    • (2009) Cell Death Differ , vol.16 , pp. 984
    • Noda, T.1    Fujita, N.2    Yoshimori, T.3
  • 18
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • 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.
    • (2004) Cell , vol.119 , pp. 753
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 19
    • 8344247016 scopus 로고    scopus 로고
    • Autophagy defends cells against invading group A Streptococcus
    • Nakagawa, I., Amano, A., Mizushima, N. et al. 2004. Autophagy defends cells against invading group A Streptococcus. Science 306:1037.
    • (2004) Science , vol.306 , pp. 1037
    • Nakagawa, I.1    Amano, A.2    Mizushima, N.3
  • 21
    • 33744958258 scopus 로고    scopus 로고
    • Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole
    • Birmingham, C. L., Smith, A. C., Bakowski, M. A., Yoshimori, T. and Brumell, J. H. 2006. Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole. J. Biol. Chem. 281:11374.
    • (2006) J. Biol. Chem , vol.281 , pp. 11374
    • Birmingham, C.L.1    Smith, A.C.2    Bakowski, M.A.3    Yoshimori, T.4    Brumell, J.H.5
  • 22
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser, M. 2009. Origin and function of ubiquitin-like proteins. Nature 458:422.
    • (2009) Nature , vol.458 , pp. 422
    • Hochstrasser, M.1
  • 23
    • 0034682843 scopus 로고    scopus 로고
    • Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p
    • Paz, Y., Elazar, Z. and Fass, D. 2000. Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p. J. Biol. Chem. 275:25445.
    • (2000) J. Biol. Chem , vol.275 , pp. 25445
    • Paz, Y.1    Elazar, Z.2    Fass, D.3
  • 24
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • Mizushima, N., Noda, T., Yoshimori, T. et al. 1998. A protein conjugation system essential for autophagy. Nature 395: 395.
    • (1998) Nature , vol.395 , pp. 395
    • Mizushima, N.1    Noda, T.2    Yoshimori, T.3
  • 25
    • 33644590635 scopus 로고    scopus 로고
    • The crystal structure of plant ATG12 and its biological implication in autophagy
    • Suzuki, N. N., Yoshimoto, K., Fujioka, Y., Ohsumi, Y. and Inagaki, F. 2005. The crystal structure of plant ATG12 and its biological implication in autophagy. Autophagy 1:119.
    • (2005) Autophagy , vol.1 , pp. 119
    • Suzuki, N.N.1    Yoshimoto, K.2    Fujioka, Y.3    Ohsumi, Y.4    Inagaki, F.5
  • 27
    • 0033565655 scopus 로고    scopus 로고
    • Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway
    • Mizushima, N., Noda, T. and Ohsumi, Y. 1999. Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. EMBO J. 18:3888.
    • (1999) EMBO J , vol.18 , pp. 3888
    • Mizushima, N.1    Noda, T.2    Ohsumi, Y.3
  • 28
    • 0038325675 scopus 로고    scopus 로고
    • Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
    • Mizushima, N., Kuma, A., Kobayashi, Y. et al. 2003. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J. Cell Sci. 116:1679.
    • (2003) J. Cell Sci , vol.116 , pp. 1679
    • Mizushima, N.1    Kuma, A.2    Kobayashi, Y.3
  • 29
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima, N., Yamamoto, A., Hatano, M. et al. 2001. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J. Cell Biol. 152:657.
    • (2001) J. Cell Biol , vol.152 , pp. 657
    • Mizushima, N.1    Yamamoto, A.2    Hatano, M.3
  • 30
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita, N., Itoh, T., Omori, H., Fukuda, M., Noda, T. and Yoshimori, T. 2008. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell 19: 2092.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2092
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 31
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • Hanada, T., Noda, N. N., Satomi, Y. et al. 2007. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J. Biol. Chem. 282:37298.
    • (2007) J. Biol. Chem , vol.282 , pp. 37298
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3
  • 32
    • 65249185812 scopus 로고    scopus 로고
    • A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy
    • Huett, A., Ng, A., Cao, Z. et al. 2009. A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy. J. Immunol. 182:4917.
    • (2009) J. Immunol , vol.182 , pp. 4917
    • Huett, A.1    Ng, A.2    Cao, Z.3
  • 33
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • Saitoh, T., Fujita, N., Jang, M. H. et al. 2008. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature 456:264.
    • (2008) Nature , vol.456 , pp. 264
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3
  • 34
    • 33846627302 scopus 로고    scopus 로고
    • A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1
    • Hampe, J., Franke, A., Rosenstiel, P. et al. 2007. A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1. Nat. Genet. 39:207.
    • (2007) Nat. Genet , vol.39 , pp. 207
    • Hampe, J.1    Franke, A.2    Rosenstiel, P.3
  • 35
    • 34247554965 scopus 로고    scopus 로고
    • Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis
    • Rioux, J. D., Xavier, R. J., Taylor, K. D. et al. 2007. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nat. Genet. 39:596.
    • (2007) Nat. Genet , vol.39 , pp. 596
    • Rioux, J.D.1    Xavier, R.J.2    Taylor, K.D.3
  • 36
    • 54849421128 scopus 로고    scopus 로고
    • Impaired autophagy of an intracellular pathogen induced by a Crohn's disease associated ATG16L1 variant
    • Kuballa, P., Huett, A., Rioux, J. D., Daly, M. J. and Xavier, R. J. 2008. Impaired autophagy of an intracellular pathogen induced by a Crohn's disease associated ATG16L1 variant. PLoS One 3:e3391.
    • (2008) PLoS One , vol.3
    • Kuballa, P.1    Huett, A.2    Rioux, J.D.3    Daly, M.J.4    Xavier, R.J.5
  • 37
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • Cadwell, K., Liu, J. Y., Brown, S. L. et al. 2008. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 456:259.
    • (2008) Nature , vol.456 , pp. 259
    • Cadwell, K.1    Liu, J.Y.2    Brown, S.L.3
  • 38
    • 44449115788 scopus 로고    scopus 로고
    • Transport of phosphatidylinositol 3-phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae
    • Obara, K., Noda, T., Niimi, K. and Ohsumi, Y. 2008. Transport of phosphatidylinositol 3-phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae. Genes Cells 13:537.
    • (2008) Genes Cells , vol.13 , pp. 537
    • Obara, K.1    Noda, T.2    Niimi, K.3    Ohsumi, Y.4
  • 39
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae
    • Kihara, A., Noda, T., Ishihara, N. and Ohsumi, Y. 2001. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152:519.
    • (2001) J. Cell Biol , vol.152 , pp. 519
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 40
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • 2:330
    • Kihara, A., Kabeya, Y., Ohsumi, Y. and Yoshimori, T. 2001. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2:330.
    • (2001) EMBO Rep
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 41
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • Yue, Z., Jin, S., Yang, C., Levine, A. J. and Heintz, N. 2003. Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc. Natl Acad. Sci. USA. 100:15077.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15077
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 42
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • 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.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5360
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 43
    • 64049086758 scopus 로고    scopus 로고
    • Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
    • Matsunaga, K., Saitoh, T., Tabata, K. et al. 2009. Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat. Cell Biol. 11:385.
    • (2009) Nat. Cell Biol , vol.11 , pp. 385
    • Matsunaga, K.1    Saitoh, T.2    Tabata, K.3
  • 44
    • 58049192897 scopus 로고    scopus 로고
    • Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase
    • Sun, Q., Fan, W., Chen, K., Ding, X., Chen, S. and Zhong, Q. 2008. Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc. Natl Acad. Sci. USA 105:19211.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 19211
    • Sun, Q.1    Fan, W.2    Chen, K.3    Ding, X.4    Chen, S.5    Zhong, Q.6
  • 45
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • Zhong, Y., Wang, Q. J., Li, X. et al. 2009. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat. Cell Biol. 11:468.
    • (2009) Nat. Cell Biol , vol.11 , pp. 468
    • Zhong, Y.1    Wang, Q.J.2    Li, X.3
  • 47
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe, E. L., Walker, S. A., Manifava, M. 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.
    • (2008) J. Cell Biol , vol.182 , pp. 685
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3
  • 49
    • 0036259995 scopus 로고    scopus 로고
    • Disruption of the Salmonella-containing vacuole leads to increased replication of Salmonella enterica serovar typhimurium in the cytosol of epithelial cells
    • Brumell, J. H., Tang, P., Zaharik, M. L. and Finlay, B. B. 2002. Disruption of the Salmonella-containing vacuole leads to increased replication of Salmonella enterica serovar typhimurium in the cytosol of epithelial cells. Infect. Immun. 70:3264.
    • (2002) Infect. Immun , vol.70 , pp. 3264
    • Brumell, J.H.1    Tang, P.2    Zaharik, M.L.3    Finlay, B.B.4
  • 50
    • 65549094988 scopus 로고    scopus 로고
    • Activation of antibacterial autophagy by NADPH oxidases
    • Huang, J., Canadien, V., Lam, G. Y. et al. 2009. Activation of antibacterial autophagy by NADPH oxidases. Proc. Natl Acad. Sci. USA 106:6226.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 6226
    • Huang, J.1    Canadien, V.2    Lam, G.Y.3
  • 51
    • 50249176472 scopus 로고    scopus 로고
    • SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34
    • Mallo, G. V., Espina, M., Smith, A. C. et al. 2008. SopB promotes phosphatidylinositol 3-phosphate formation on Salmonella vacuoles by recruiting Rab5 and Vps34. J. Cell Biol. 182: 741.
    • (2008) J. Cell Biol , vol.182 , pp. 741
    • Mallo, G.V.1    Espina, M.2    Smith, A.C.3
  • 52
    • 47649095818 scopus 로고    scopus 로고
    • Sorting nexin-1 defines an early phase of Salmonella-containing vacuole-remodeling during Salmonella infection
    • Bujny, M. V., Ewels, P. A., Humphrey, S., Attar, N., Jepson, M. A. and Cullen, P. J. 2008. Sorting nexin-1 defines an early phase of Salmonella-containing vacuole-remodeling during Salmonella infection. J. Cell Sci. 121:2027.
    • (2008) J. Cell Sci , vol.121 , pp. 2027
    • Bujny, M.V.1    Ewels, P.A.2    Humphrey, S.3    Attar, N.4    Jepson, M.A.5    Cullen, P.J.6


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