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Volumn 7, Issue , 2016, Pages

The T300A Crohn's disease risk polymorphism impairs function of the WD40 domain of ATG16L1

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; MEMBRANE PROTEIN; TMEM59 PROTEIN; UNCLASSIFIED DRUG; ATG16L1 PROTEIN, HUMAN; ATG16L1 PROTEIN, MOUSE; AUTOPHAGY RELATED PROTEIN; CARRIER PROTEIN; CASPASE 3; DCF1 PROTEIN, HUMAN; NERVE PROTEIN; PEPTIDE; PROTEIN BINDING;

EID: 84976416752     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms11821     Document Type: Article
Times cited : (55)

References (64)
  • 1
    • 33745775434 scopus 로고    scopus 로고
    • Mechanisms of disease: Pathogenesis of Crohn's disease and ulcerative colitis
    • Sartor, R. B. Mechanisms of disease: pathogenesis of Crohn's disease and ulcerative colitis. Nat. Clin. Pract. Gastroenterol. Hepatol. 3, 390-407 (2006).
    • (2006) Nat. Clin. Pract. Gastroenterol. Hepatol , vol.3 , pp. 390-407
    • Sartor, R.B.1
  • 2
    • 70949107842 scopus 로고    scopus 로고
    • Inflammatory bowel disease
    • Abraham, C. & Cho, J. H. Inflammatory bowel disease. N. Engl. J. Med. 361, 2066-2078 (2009).
    • (2009) N. Engl. J. Med , vol.361 , pp. 2066-2078
    • Abraham, C.1    Cho, J.H.2
  • 3
    • 79959216005 scopus 로고    scopus 로고
    • Genetics and pathogenesis of inflammatory bowel disease
    • Khor, B., Gardet, A. & Xavier, R. J. Genetics and pathogenesis of inflammatory bowel disease. Nature 474, 307-317 (2011).
    • (2011) Nature , vol.474 , pp. 307-317
    • Khor, B.1    Gardet, A.2    Xavier, R.J.3
  • 4
    • 78650430453 scopus 로고    scopus 로고
    • Crohn disease: A current perspective on genetics, autophagy and immunity
    • Stappenbeck, T. S. et al. Crohn disease: a current perspective on genetics, autophagy and immunity. Autophagy 7, 355-374 (2011).
    • (2011) Autophagy , vol.7 , pp. 355-374
    • Stappenbeck, T.S.1
  • 5
    • 0037043658 scopus 로고    scopus 로고
    • Inflammatory bowel disease
    • Podolsky, D. K. Inflammatory bowel disease. N. Engl. J. Med. 347, 417-429 (2002).
    • (2002) N. Engl. J. Med , vol.347 , pp. 417-429
    • Podolsky, D.K.1
  • 6
    • 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. et al. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nat. Genet. 39, 596-604 (2007).
    • (2007) Nat. Genet , vol.39 , pp. 596-604
    • Rioux, J.D.1
  • 7
    • 33846627302 scopus 로고    scopus 로고
    • A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1
    • Hampe, J. et al. A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1. Nat. Genet. 39, 207-211 (2007).
    • (2007) Nat. Genet , vol.39 , pp. 207-211
    • Hampe, J.1
  • 8
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • Hugot, J. P. et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature 411, 599-603 (2001).
    • (2001) Nature , vol.411 , pp. 599-603
    • Hugot, J.P.1
  • 9
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in nod2 associated with susceptibility to Crohn's disease
    • Ogura, Y. et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411, 603-606 (2001).
    • (2001) Nature , vol.411 , pp. 603-606
    • Ogura, Y.1
  • 10
    • 33845340501 scopus 로고    scopus 로고
    • A genome-wide association study identifies IL23R as an inflammatory bowel disease gene
    • Duerr, R. H. et al. A genome-wide association study identifies IL23R as an inflammatory bowel disease gene. Science 314, 1461-1463 (2006).
    • (2006) Science , vol.314 , pp. 1461-1463
    • Duerr, R.H.1
  • 12
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • Mizushima, N. & Komatsu, M. Autophagy: renovation of cells and tissues. Cell 147, 728-741 (2011).
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 13
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G., Marino, G. & Levine, B. Autophagy and the integrated stress response. Mol. Cell 40, 280-293 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 14
    • 84891747382 scopus 로고    scopus 로고
    • The machinery of macroautophagy
    • Feng, Y., He, D., Yao, Z. & Klionsky, D. J. The machinery of macroautophagy. Cell Res. 24, 24-41 (2014).
    • (2014) Cell Res , Issue.24 , pp. 24-41
    • Feng, Y.1    He, D.2    Yao, Z.3    Klionsky, D.J.4
  • 15
    • 77956180361 scopus 로고    scopus 로고
    • Autophagy and innate immunity: Triggering, targeting and tuning
    • Sumpter, Jr R. & Levine, B. Autophagy and innate immunity: triggering, targeting and tuning. Semin. Cell Dev. Biol. 21, 699-711 (2010).
    • (2010) Semin. Cell Dev. Biol , vol.21 , pp. 699-711
    • Sumpter, R.1    Levine, B.2
  • 16
    • 71049130205 scopus 로고    scopus 로고
    • Molecular basis of canonical and bactericidal autophagy
    • Noda, T. & Yoshimori, T. Molecular basis of canonical and bactericidal autophagy. Int. Immunol. 21, 1199-1204 (2009).
    • (2009) Int. Immunol , vol.21 , pp. 1199-1204
    • Noda, T.1    Yoshimori, T.2
  • 17
    • 84896992565 scopus 로고    scopus 로고
    • Selective autophagy against membranous compartments: Canonical and unconventional purposes and mechanisms
    • Pimentel-Muinos, F. X. & Boada-Romero, E. Selective autophagy against membranous compartments: canonical and unconventional purposes and mechanisms. Autophagy 10, 397-407 (2014).
    • (2014) Autophagy , vol.10 , pp. 397-407
    • Pimentel-Muinos, F.X.1    Boada-Romero, E.2
  • 18
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine, B., Mizushima, N. & Virgin, H. W. Autophagy in immunity and inflammation. Nature 469, 323-335 (2011).
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 19
    • 84899131967 scopus 로고    scopus 로고
    • Autophagy in antimicrobial immunity
    • Gomes, L. C. & Dikic, I. Autophagy in antimicrobial immunity. Mol. Cell 54, 224-233 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 224-233
    • Gomes, L.C.1    Dikic, I.2
  • 20
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic, V. & Levine, B. Autophagy, immunity, and microbial adaptations. Cell Host Microbe 5, 527-549 (2009).
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 21
    • 84918535219 scopus 로고    scopus 로고
    • NOD1 and NOD2: Signaling, host defense, and inflammatory disease
    • Caruso, R., Warner, N., Inohara, N. & Nunez, G. NOD1 and NOD2: signaling, host defense, and inflammatory disease. Immunity 41, 898-908 (2014).
    • (2014) Immunity , vol.41 , pp. 898-908
    • Caruso, R.1    Warner, N.2    Inohara, N.3    Nunez, G.4
  • 24
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita, N. et al. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell 19, 2092-2100 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1
  • 25
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C. & Klionsky, D. J. Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43, 67-93 (2009).
    • (2009) Annu. Rev. Genet , Issue.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 26
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • Hanada, T. et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J. Biol. Chem. 282, 37298-37302 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 37298-37302
    • Hanada, T.1
  • 27
    • 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. et al. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J. Cell Sci. 116, 1679-1688 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 1679-1688
    • Mizushima, N.1
  • 28
    • 84874646724 scopus 로고    scopus 로고
    • FIP200 regulates targeting of Atg16L1 to the isolation membrane
    • Nishimura, T. et al. FIP200 regulates targeting of Atg16L1 to the isolation membrane. EMBO. Rep. 14, 284-291 (2013).
    • (2013) EMBO. Rep , vol.14 , pp. 284-291
    • Nishimura, T.1
  • 29
    • 84873569898 scopus 로고    scopus 로고
    • Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-dependent and -independent autophagy
    • Gammoh, N., Florey, O., Overholtzer, M. & Jiang, X. Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-dependent and -independent autophagy. Nat. Struct. Mol. Biol. 20, 144-149 (2013).
    • (2013) Nat. Struct. Mol. Biol , Issue.20 , pp. 144-149
    • Gammoh, N.1    Florey, O.2    Overholtzer, M.3    Jiang, X.4
  • 30
    • 70450248450 scopus 로고    scopus 로고
    • Differential involvement of Atg16L1 in Crohn disease and canonical autophagy: Analysis of the organization of the Atg16L1 complex in fibroblasts
    • Fujita, N. et al. Differential involvement of Atg16L1 in Crohn disease and canonical autophagy: analysis of the organization of the Atg16L1 complex in fibroblasts. J. Biol. Chem. 284, 32602-32609 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 32602-32609
    • Fujita, N.1
  • 31
    • 84902829671 scopus 로고    scopus 로고
    • The parasitophorous vacuole membrane of Toxoplasma gondii is targeted for disruption by ubiquitin-like conjugation systems of autophagy
    • Choi, J. et al. The parasitophorous vacuole membrane of Toxoplasma gondii is targeted for disruption by ubiquitin-like conjugation systems of autophagy. Immunity 40, 924-935 (2014).
    • (2014) Immunity , vol.40 , pp. 924-935
    • Choi, J.1
  • 32
    • 84904575441 scopus 로고    scopus 로고
    • WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1
    • Dooley, H. C. et al. WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and pathogen clearance by recruiting Atg12-5-16L1. Mol. Cell 55, 238-252 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 238-252
    • Dooley, H.C.1
  • 33
    • 50249098491 scopus 로고    scopus 로고
    • Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation
    • Itoh, T. et al. Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol. Biol. Cell 19, 2916-2925 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2916-2925
    • Itoh, T.1
  • 34
    • 84887524897 scopus 로고    scopus 로고
    • The protein ATG16L1 suppresses inflammatory cytokines induced by the intracellular sensors Nod1 and Nod2 in an autophagy-independent manner
    • Sorbara, M. T. et al. The protein ATG16L1 suppresses inflammatory cytokines induced by the intracellular sensors Nod1 and Nod2 in an autophagy-independent manner. Immunity 39, 858-873 (2013).
    • (2013) Immunity , vol.39 , pp. 858-873
    • Sorbara, M.T.1
  • 35
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • Saitoh, T. et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature 456, 264-268 (2008).
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1
  • 36
    • 84888223618 scopus 로고    scopus 로고
    • Atg16l1 is required for autophagy in intestinal epithelial cells and protection of mice from Salmonella infection
    • Conway, K. L. et al. Atg16l1 is required for autophagy in intestinal epithelial cells and protection of mice from Salmonella infection. Gastroenterology 145, 1347-1357 (2013).
    • (2013) Gastroenterology , vol.145 , pp. 1347-1357
    • Conway, K.L.1
  • 37
    • 77953904042 scopus 로고    scopus 로고
    • Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine
    • Cadwell, K. et al. Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine. Cell 141, 1135-1145 (2010).
    • (2010) Cell , vol.141 , pp. 1135-1145
    • Cadwell, K.1
  • 38
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • Cadwell, K. et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 456, 259-263 (2008).
    • (2008) Nature , vol.456 , pp. 259-263
    • Cadwell, K.1
  • 39
    • 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. & Xavier, R. J. Impaired autophagy of an intracellular pathogen induced by a Crohn's disease associated ATG16L1 variant. PLoS ONE 3, e3391 (2008).
    • (2008) PLoS ONE , vol.3 , pp. e3391
    • Kuballa, P.1    Huett, A.2    Rioux, J.D.3    Daly, M.J.4    Xavier, R.J.5
  • 40
    • 73849121209 scopus 로고    scopus 로고
    • Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry
    • Travassos, L. H. et al. Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry. Nat. Immunol. 11, 55-62 (2010).
    • (2010) Nat. Immunol , vol.11 , pp. 55-62
    • Travassos, L.H.1
  • 41
    • 84875214777 scopus 로고    scopus 로고
    • TMEM59 defines a novel ATG16L1-binding motif that promotes local activation of LC3
    • Boada-Romero, E. et al. TMEM59 defines a novel ATG16L1-binding motif that promotes local activation of LC3. EMBO J. 32, 566-582 (2013).
    • (2013) EMBO J , vol.32 , pp. 566-582
    • Boada-Romero, E.1
  • 42
    • 77954223054 scopus 로고    scopus 로고
    • The novel membrane protein TMEM59 modulates complex glycosylation, cell surface expression, and secretion of the amyloid precursor protein
    • Ullrich, S. et al. The novel membrane protein TMEM59 modulates complex glycosylation, cell surface expression, and secretion of the amyloid precursor protein. J. Biol. Chem. 285, 20664-20674 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 20664-20674
    • Ullrich, S.1
  • 43
    • 84886897936 scopus 로고    scopus 로고
    • Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin
    • Fujita, N. et al. Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin. J. Cell Biol. 203, 115-128 (2013).
    • (2013) J. Cell Biol , vol.203 , pp. 115-128
    • Fujita, N.1
  • 44
    • 78149456945 scopus 로고    scopus 로고
    • WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins
    • Pashkova, N. et al. WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol. Cell 40, 433-443 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 433-443
    • Pashkova, N.1
  • 45
    • 84878756142 scopus 로고    scopus 로고
    • The Crohn's disease: Associated ATG16L1 variant and Salmonella invasion
    • Messer, J. S. et al. The Crohn's disease: associated ATG16L1 variant and Salmonella invasion. BMJ Open 3, e002790 (2013).
    • (2013) BMJ Open , vol.3 , pp. e002790
    • Messer, J.S.1
  • 46
    • 84901660514 scopus 로고    scopus 로고
    • Atg16L1 T300A variant decreases selective autophagy resulting in altered cytokine signaling and decreased antibacterial defense
    • Lassen, K. G. et al. Atg16L1 T300A variant decreases selective autophagy resulting in altered cytokine signaling and decreased antibacterial defense. Proc. Natl Acad. Sci. USA 111, 7741-7746 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7741-7746
    • Lassen, K.G.1
  • 47
    • 84896730900 scopus 로고    scopus 로고
    • A Crohn's disease variant in Atg16l1 enhances its degradation by caspase 3
    • Murthy, A. et al. A Crohn's disease variant in Atg16l1 enhances its degradation by caspase 3. Nature 506, 456-462 (2014).
    • (2014) Nature , vol.506 , pp. 456-462
    • Murthy, A.1
  • 48
    • 77957682295 scopus 로고    scopus 로고
    • ATG16L1 and NOD2 interact in an autophagy-dependent antibacterial pathway implicated in Crohn's disease pathogenesis
    • Homer, C. R., Richmond, A. L., Rebert, N. A., Achkar, J. P. & McDonald, C. ATG16L1 and NOD2 interact in an autophagy-dependent antibacterial pathway implicated in Crohn's disease pathogenesis. Gastroenterology 139, 1630-1641 1641 e1-2 (2010).
    • (2010) Gastroenterology , vol.139 , pp. 1630-1641
    • Homer, C.R.1    Richmond, A.L.2    Rebert, N.A.3    Achkar, J.P.4    McDonald, C.5
  • 49
    • 73849151394 scopus 로고    scopus 로고
    • NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation
    • Cooney, R. et al. NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation. Nat. Med. 16, 90-97 (2010).
    • (2010) Nat. Med , vol.16 , pp. 90-97
    • Cooney, R.1
  • 50
    • 84898757170 scopus 로고    scopus 로고
    • Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins
    • Klionsky, D. J. & Schulman, B. A. Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins. Nat. Struct. Mol. Biol. 21, 336-345 (2014).
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 336-345
    • Klionsky, D.J.1    Schulman, B.A.2
  • 51
    • 80051550866 scopus 로고    scopus 로고
    • Crohn's disease-associated ATG16L1 polymorphism modulates pro-inflammatory cytokine responses selectively upon activation of NOD2
    • Plantinga, T. S. et al. Crohn's disease-associated ATG16L1 polymorphism modulates pro-inflammatory cytokine responses selectively upon activation of NOD2. Gut 60, 1229-1235 (2011).
    • (2011) Gut , vol.60 , pp. 1229-1235
    • Plantinga, T.S.1
  • 52
    • 0142138688 scopus 로고    scopus 로고
    • T3JAM, a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK
    • Dadgostar, H., Doyle, S. E., Shahangian, A., Garcia, D. E. & Cheng, G. T3JAM, a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK(1). FEBS Lett. 553, 403-407 (2003).
    • (2003) FEBS Lett , vol.553 , pp. 403-407
    • Dadgostar, H.1    Doyle, S.E.2    Shahangian, A.3    Garcia, D.E.4    Cheng, G.5
  • 53
    • 0036510367 scopus 로고    scopus 로고
    • Identification and characterization of DEDD2, a death effector domaincontaining protein
    • Roth, W., Stenner-Liewen, F., Pawlowski, K., Godzik, A. & Reed, J. C. Identification and characterization of DEDD2, a death effector domaincontaining protein. J. Biol. Chem. 277, 7501-7508 (2002).
    • (2002) J. Biol. Chem , Issue.277 , pp. 7501-7508
    • Roth, W.1    Stenner-Liewen, F.2    Pawlowski, K.3    Godzik, A.4    Reed, J.C.5
  • 54
    • 39849098748 scopus 로고    scopus 로고
    • Role of the JNK signal transduction pathway in inflammatory bowel disease
    • Roy, P. K., Rashid, F., Bragg, J. & Ibdah, J. A. Role of the JNK signal transduction pathway in inflammatory bowel disease. World J. Gastroenterol. 14, 200-202 (2008).
    • (2008) World J. Gastroenterol , vol.14 , pp. 200-202
    • Roy, P.K.1    Rashid, F.2    Bragg, J.3    Ibdah, J.A.4
  • 55
    • 80054868923 scopus 로고    scopus 로고
    • How bacteria-induced apoptosis of intestinal epithelial cells contributes to mucosal inflammation
    • Hausmann, M. How bacteria-induced apoptosis of intestinal epithelial cells contributes to mucosal inflammation. Int. J. Inflam. 2010, 574568 (2010).
    • (2010) Int. J. Inflam 2010 , pp. 574568
    • Hausmann, M.1
  • 56
    • 84926656919 scopus 로고    scopus 로고
    • Autophagy mediates tolerance to Staphylococcus aureus alpha-toxin
    • Maurer, K. et al. Autophagy mediates tolerance to Staphylococcus aureus alpha-toxin. Cell Host Microbe 17, 429-440 (2015).
    • (2015) Cell Host Microbe , vol.17 , pp. 429-440
    • Maurer, K.1
  • 57
    • 34047271297 scopus 로고    scopus 로고
    • Staphylococcus aureus subvert autophagy for induction of caspase-independent host cell death
    • Schnaith, A. et al. Staphylococcus aureus subvert autophagy for induction of caspase-independent host cell death. J. Biol. Chem. 282, 2695-2706 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 2695-2706
    • Schnaith, A.1
  • 58
    • 84908137655 scopus 로고    scopus 로고
    • Autophagy gene Atg16L1 prevents lethal T cell alloreactivity mediated by dendritic cells
    • Hubbard-Lucey, V. M. et al. Autophagy gene Atg16L1 prevents lethal T cell alloreactivity mediated by dendritic cells. Immunity 41, 579-591 (2014).
    • (2014) Immunity , vol.41 , pp. 579-591
    • Hubbard-Lucey, V.M.1
  • 59
    • 84960404438 scopus 로고    scopus 로고
    • The Thr300Ala variant in ATG16L1 is associated with improved survival in human colorectal cancer and enhanced production of type i interferon
    • Grimm, W. A. et al. The Thr300Ala variant in ATG16L1 is associated with improved survival in human colorectal cancer and enhanced production of type I interferon. Gut 65, 456-464 (2016).
    • (2016) Gut , vol.65 , pp. 456-464
    • Grimm, W.A.1
  • 60
    • 84961214933 scopus 로고    scopus 로고
    • ATG16L1 t300A polymorphism is correlated with gastric cancer susceptibility
    • Burada, F. et al. ATG16L1 T300A polymorphism is correlated with gastric cancer susceptibility. Pathol. Oncol. Res. 22, 317-322 (2016).
    • (2016) Pathol. Oncol. Res , vol.22 , pp. 317-322
    • Burada, F.1
  • 61
    • 84932615079 scopus 로고    scopus 로고
    • Polymorphisms in autophagy genes are associated with paget disease of bone
    • Usategui-Martin, R. et al. Polymorphisms in autophagy genes are associated with paget disease of bone. PLoS ONE 10, e0128984 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0128984
    • Usategui-Martin, R.1
  • 63
    • 67649547153 scopus 로고    scopus 로고
    • Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular
    • Klee, M., Pallauf, K., Alcala, S., Fleischer, A. & Pimentel-Muinos, F. X. Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular Bak. EMBO J. 28, 1757-1768 (2009).
    • (2009) Bak. EMBO J , Issue.28 , pp. 1757-1768
    • Klee, M.1    Pallauf, K.2    Alcala, S.3    Fleischer, A.4    Pimentel-Muinos, F.X.5
  • 64
    • 0033855915 scopus 로고    scopus 로고
    • Staphylococcus aureus RN6390 replicates and induces apoptosis in a pulmonary epithelial cell line
    • Kahl, B. C. et al. Staphylococcus aureus RN6390 replicates and induces apoptosis in a pulmonary epithelial cell line. Infect. Immun. 68, 5385-5392 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 5385-5392
    • Kahl, B.C.1


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