메뉴 건너뛰기




Volumn 12, Issue 11, 2016, Pages 2145-2166

Ehrlichia secretes Etf-1 to induce autophagy and capture nutrients for its growth through RAB5 and class III phosphatidylinositol 3-kinase

Author keywords

ATG5; autophagy; BECN1; class III PtdIns3K; Ehrlichia chaffeensis; endosome; Etf 1; infection; LC3; RAB5; type IV secretion effector

Indexed keywords

AMINO ACID; AUTOPHAGY PROTEIN 5; BACTERIAL PROTEIN; BECLIN 1; ETF 1 PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HUNTINGTIN; PHOSPHATIDYLINOSITOL 3 KINASE; RAB PROTEIN; RAPAMYCIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; 3-METHYLADENINE; ADENINE; ATG5 PROTEIN, MOUSE; AUTOPHAGY RELATED PROTEIN 5; GLUTAMIC ACID; GLUTAMINE; GUANOSINE TRIPHOSPHATE; MUTANT PROTEIN; PROTEIN BINDING;

EID: 84988416865     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.1080/15548627.2016.1217369     Document Type: Article
Times cited : (57)

References (132)
  • 2
    • 0025789921 scopus 로고
    • Ehrlichia chaffeensis, a new species associated with human ehrlichiosis
    • 1757557
    • B.E.Anderson, J.E.Dawson, D.C.Jones, K.H.Wilson. Ehrlichia chaffeensis, a new species associated with human ehrlichiosis. J Clin Microbiol 1991; 29:2838–42; PMID:1757557
    • (1991) J Clin Microbiol , vol.29 , pp. 2838-2842
    • Anderson, B.E.1    Dawson, J.E.2    Jones, D.C.3    Wilson, K.H.4
  • 3
    • 0023097769 scopus 로고
    • Human infection with Ehrlichia canis, a leukocytic rickettsia
    • 3029590
    • K.Maeda, N.Markowitz, R.C.Hawley, M.Ristic, D.Cox, J.E.McDade. Human infection with Ehrlichia canis, a leukocytic rickettsia. N Engl J Med 1987; 316:853–6; PMID:3029590; http://dx.doi.org/10.1056/NEJM198704023161406
    • (1987) N Engl J Med , vol.316 , pp. 853-856
    • Maeda, K.1    Markowitz, N.2    Hawley, R.C.3    Ristic, M.4    Cox, D.5    McDade, J.E.6
  • 4
    • 0037240533 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis: a prototypical emerging pathogen
    • 12525424
    • C.D.Paddock, J.E.Childs. Ehrlichia chaffeensis:a prototypical emerging pathogen. Clin Microbiol Rev 2003; 16:37–64; PMID:12525424; http://dx.doi.org/10.1128/CMR.16.1.37-64.2003
    • (2003) Clin Microbiol Rev , vol.16 , pp. 37-64
    • Paddock, C.D.1    Childs, J.E.2
  • 6
    • 84877829941 scopus 로고    scopus 로고
    • Microbial quest for food in vivo: 'nutritional virulence' as an emerging paradigm
    • 23490329
    • Y.Abu Kwaik, D.Bumann. Microbial quest for food in vivo:'nutritional virulence' as an emerging paradigm. Cell Microbiol 2013; 15:882–90; PMID:23490329; http://dx.doi.org/10.1111/cmi.12138
    • (2013) Cell Microbiol , vol.15 , pp. 882-890
    • Abu Kwaik, Y.1    Bumann, D.2
  • 7
    • 84945255271 scopus 로고    scopus 로고
    • Molecular pathogenesis of Ehrlichia chaffeensis infection
    • 26488275
    • Y.Rikihisa. Molecular pathogenesis of Ehrlichia chaffeensis infection. Annu Rev Microbiol 2015; 69:283–304; PMID:26488275; http://dx.doi.org/10.1146/annurev-micro-091014-104411
    • (2015) Annu Rev Microbiol , vol.69 , pp. 283-304
    • Rikihisa, Y.1
  • 8
    • 0030959591 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis inclusions are early endosomes which selectively accumulate transferrin receptor
    • 9119487
    • R.E.Barnewall, Y.Rikihisa, E.H.Lee. Ehrlichia chaffeensis inclusions are early endosomes which selectively accumulate transferrin receptor. Infect Immun 1997; 65:1455–61; PMID:9119487
    • (1997) Infect Immun , vol.65 , pp. 1455-1461
    • Barnewall, R.E.1    Rikihisa, Y.2    Lee, E.H.3
  • 9
    • 0033009747 scopus 로고    scopus 로고
    • Human granulocytic ehrlichiosis agent and Ehrlichia chaffeensis reside in different cytoplasmic compartments in HL-60 cells
    • 10024584
    • J.Mott, R.E.Barnewall, Y.Rikihisa. Human granulocytic ehrlichiosis agent and Ehrlichia chaffeensis reside in different cytoplasmic compartments in HL-60 cells. Infect Immun 1999; 67:1368–78; PMID:10024584
    • (1999) Infect Immun , vol.67 , pp. 1368-1378
    • Mott, J.1    Barnewall, R.E.2    Rikihisa, Y.3
  • 10
    • 33947101530 scopus 로고    scopus 로고
    • Degradation of p22phox and inhibition of superoxide generation by Ehrlichia chaffeensis in human monocytes
    • 17087735
    • M.Lin, Y.Rikihisa. Degradation of p22phox and inhibition of superoxide generation by Ehrlichia chaffeensis in human monocytes. Cell Microbiol 2007; 9:861–74; PMID:17087735; http://dx.doi.org/10.1111/j.1462-5822.2006.00835.x
    • (2007) Cell Microbiol , vol.9 , pp. 861-874
    • Lin, M.1    Rikihisa, Y.2
  • 12
    • 0013865801 scopus 로고
    • Functions of lysosomes
    • 5322983
    • C.De Duve, R.Wattiaux. Functions of lysosomes. Annu Rev Physiol 1966; 28:435–92; PMID:5322983; http://dx.doi.org/10.1146/annurev.ph.28.030166.002251
    • (1966) Annu Rev Physiol , vol.28 , pp. 435-492
    • De Duve, C.1    Wattiaux, R.2
  • 13
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: a history of macroautophagy
    • 20811353
    • Z.Yang, D.J.Klionsky. Eaten alive:a history of macroautophagy. Nat?Cell Biol 2010; 12:814–22; PMID:20811353; http://dx.doi.org/10.1038/ncb0910-814
    • (2010) Nat?Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 14
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: renovation of cells and tissues
    • 22078875
    • N.Mizushima, M.Komatsu. Autophagy:renovation of cells and tissues. Cell 2011; 147:728–41; PMID:22078875; http://dx.doi.org/10.1016/j.cell.2011.10.026
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 15
    • 84888380983 scopus 로고    scopus 로고
    • The autophagosome: origins unknown, biogenesis complex
    • C.A.Lamb, T.Yoshimori, S.A.Tooze. The autophagosome:origins unknown, biogenesis complex. Nat Rev Mol Cell Biol 2013; 14:759–74; PMID:24201109; http://dx.doi.org/10.1038/nrm3696
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 1109-1174
    • Lamb, C.A.1    Yoshimori, T.2    Tooze, S.A.3
  • 16
    • 80054025654 scopus 로고    scopus 로고
    • The role of atg proteins in autophagosome formation
    • 21801009
    • N.Mizushima, T.Yoshimori, Y.Ohsumi. The role of atg proteins in autophagosome formation. Annu Rev Cell Dev Biol 2011; 27:107–32; PMID:21801009; http://dx.doi.org/10.1146/annurev-cellbio-092910-154005
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 17
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • 18843052
    • E.Itakura, C.Kishi, K.Inoue, N.Mizushima. Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol Biol Cell 2008; 19:5360–72; PMID:18843052; http://dx.doi.org/10.1091/mbc.E08-01-0080
    • (2008) Mol Biol Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 18
    • 0032545292 scopus 로고    scopus 로고
    • A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy
    • 9852036
    • N.Mizushima, H.Sugita, T.Yoshimori, Y.Ohsumi. A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy. J Biol Chem 1998; 273:33889–92; PMID:9852036; http://dx.doi.org/10.1074/jbc.273.51.33889
    • (1998) J Biol Chem , vol.273 , pp. 33889-33892
    • Mizushima, N.1    Sugita, H.2    Yoshimori, T.3    Ohsumi, Y.4
  • 19
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • 11060023
    • Y.Kabeya, N.Mizushima, T.Ueno, A.Yamamoto, T.Kirisako, T.Noda, E.Kominami, Y.Ohsumi, T.Yoshimori. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19:5720–8; PMID:11060023; http://dx.doi.org/10.1093/emboj/19.21.5720
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6    Kominami, E.7    Ohsumi, Y.8    Yoshimori, T.9
  • 20
    • 0025363276 scopus 로고
    • Studies on the mechanisms of autophagy: formation of the autophagic vacuole
    • 2351689
    • W.A.Dunn, Jr. Studies on the mechanisms of autophagy:formation of the autophagic vacuole. J Cell Biol 1990; 110:1923–33; PMID:2351689; http://dx.doi.org/10.1083/jcb.110.6.1923
    • (1990) J Cell Biol , vol.110 , pp. 1923-1933
    • Dunn, W.A.1
  • 21
    • 0032555641 scopus 로고    scopus 로고
    • Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes
    • 9705327
    • T.O.Berg, M.Fengsrud, P.E.Stromhaug, T.Berg, P.O.Seglen. Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes. J Biol Chem 1998; 273:21883–92; PMID:9705327; http://dx.doi.org/10.1074/jbc.273.34.21883
    • (1998) J Biol Chem , vol.273 , pp. 21883-21892
    • Berg, T.O.1    Fengsrud, M.2    Stromhaug, P.E.3    Berg, T.4    Seglen, P.O.5
  • 22
    • 0031031041 scopus 로고    scopus 로고
    • The autophagic and endocytic pathways converge at the nascent autophagic vacuoles
    • 9008703
    • W.Liou, H.J.Geuze, M.J.Geelen, J.W.Slot. The autophagic and endocytic pathways converge at the nascent autophagic vacuoles. J Cell Biol 1997; 136:61–70; PMID:9008703; http://dx.doi.org/10.1083/jcb.136.1.61
    • (1997) J Cell Biol , vol.136 , pp. 61-70
    • Liou, W.1    Geuze, H.J.2    Geelen, M.J.3    Slot, J.W.4
  • 23
    • 0020402944 scopus 로고
    • Uptake and degradation of proteins by isolated rat liver lysosomes. Suggestion of a microautophagic pathway of proteolysis
    • 6755063
    • J.Ahlberg, L.Marzella, H.Glaumann. Uptake and degradation of proteins by isolated rat liver lysosomes. Suggestion of a microautophagic pathway of proteolysis. Lab Invest 1982; 47:523–32; PMID:6755063
    • (1982) Lab Invest , vol.47 , pp. 523-532
    • Ahlberg, J.1    Marzella, L.2    Glaumann, H.3
  • 24
    • 67650258765 scopus 로고    scopus 로고
    • In vitro reconstitution of fusion between immature ?autophagosomes and endosomes
    • 19337031
    • J.Morvan, R.Kochl, R.Watson, L.M.Collinson, H.B.Jefferies, S.A.Tooze?. In vitro reconstitution of fusion between immature ?autophagosomes and endosomes. Autophagy 2009; 5:676–89; PMID:19337031; http://dx.doi.org/10.4161/auto.5.5.8378
    • (2009) Autophagy , vol.5 , pp. 676-689
    • Morvan, J.1    Kochl, R.2    Watson, R.3    Collinson, L.M.4    Jefferies, H.B.5    Tooze, S.A.6
  • 25
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • 17909521
    • Z.Xie, D.J.Klionsky. Autophagosome formation:core machinery and adaptations. Nat Cell Biol 2007; 9:1102–9; PMID:17909521; http://dx.doi.org/10.1038/ncb1007-1102
    • (2007) Nat Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 26
    • 84898611787 scopus 로고    scopus 로고
    • Autophagosomes, phagosomes, autolysosomes, phagolysosomes, autophagolysosomes … wait, I'm confused
    • 24657946
    • D.J.Klionsky, E.L.Eskelinen, V.Deretic. Autophagosomes, phagosomes, autolysosomes, phagolysosomes, autophagolysosomes … wait, I'm confused. Autophagy 2014; 10:549–51; PMID:24657946; http://dx.doi.org/10.4161/auto.28448
    • (2014) Autophagy , vol.10 , pp. 549-551
    • Klionsky, D.J.1    Eskelinen, E.L.2    Deretic, V.3
  • 27
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • 19820708
    • T.L.Thurston, G.Ryzhakov, S.Bloor, N.von Muhlinen, F.Randow. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat Immunol 2009; 10:1215–21; PMID:19820708; http://dx.doi.org/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
  • 29
    • 68349143052 scopus 로고    scopus 로고
    • Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy
    • 19683680
    • N.Dupont, S.Lacas-Gervais, J.Bertout, I.Paz, B.Freche, G.T.Van Nhieu, F.G.Van Der Goot, P.J.Sansonetti, F.Lafont. Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy. Cell Host Microbe 2009; 6:137–49; PMID:19683680; http://dx.doi.org/10.1016/j.chom.2009.07.005
    • (2009) Cell Host Microbe , vol.6 , pp. 137-149
    • Dupont, N.1    Lacas-Gervais, S.2    Bertout, J.3    Paz, I.4    Freche, B.5    Van Nhieu, G.T.6    Van Der Goot, F.G.7    Sansonetti, P.J.8    Lafont, F.9
  • 30
    • 74049126112 scopus 로고    scopus 로고
    • The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway
    • 19812211
    • Y.T.Zheng, S.Shahnazari, A.Brech, T.Lamark, T.Johansen, J.H.Brumell. The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway. J Immunol 2009; 183:5909–16; PMID:19812211; http://dx.doi.org/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
  • 31
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • 15607973
    • M.G.Gutierrez, S.S.Master, S.B.Singh, G.A.Taylor, M.I.Colombo, V.Deretic. Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 2004; 119:753–66; PMID:15607973; http://dx.doi.org/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
  • 32
    • 21344472825 scopus 로고    scopus 로고
    • Autophagy induction favours the generation and maturation of the Coxiella-replicative vacuoles
    • 15953030
    • M.G.Gutierrez, C.L.Vazquez, D.B.Munafo, F.C.Zoppino, W.Beron, M.Rabinovitch, M.I.Colombo. Autophagy induction favours the generation and maturation of the Coxiella-replicative vacuoles. Cell Microbiol 2005; 7:981–93; PMID:15953030; http://dx.doi.org/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    Colombo, M.I.7
  • 33
    • 84856010816 scopus 로고    scopus 로고
    • Selective subversion of autophagy complexes facilitates completion of the Brucella intracellular cycle
    • 22264511
    • T.Starr, R.Child, T.D.Wehrly, B.Hansen, S.Hwang, C.Lopez-Otin, H.W.Virgin, J.Celli. Selective subversion of autophagy complexes facilitates completion of the Brucella intracellular cycle. Cell Host Microbe 2012; 11:33–45; PMID:22264511; http://dx.doi.org/10.1016/j.chom.2011.12.002
    • (2012) Cell Host Microbe , vol.11 , pp. 33-45
    • Starr, T.1    Child, R.2    Wehrly, T.D.3    Hansen, B.4    Hwang, S.5    Lopez-Otin, C.6    Virgin, H.W.7    Celli, J.8
  • 34
    • 84883401064 scopus 로고    scopus 로고
    • Francisella tularensis harvests nutrients derived via ATG5-independent autophagy to support intracellular growth
    • 23966861
    • S.Steele, J.Brunton, B.Ziehr, S.Taft-Benz, N.Moorman, T.Kawula. Francisella tularensis harvests nutrients derived via ATG5-independent autophagy to support intracellular growth. PLoS Pathog 2013; 9:e1003562; PMID:23966861; http://dx.doi.org/10.1371/journal.ppat.1003562
    • (2013) PLoS Pathog
    • Steele, S.1    Brunton, J.2    Ziehr, B.3    Taft-Benz, S.4    Moorman, N.5    Kawula, T.6
  • 35
    • 38849200959 scopus 로고    scopus 로고
    • Subversion of cellular autophagy by Anaplasma phagocytophilum
    • 17979984
    • H.Niu, M.Yamaguchi, Y.Rikihisa. Subversion of cellular autophagy by Anaplasma phagocytophilum. Cell Microbiol 2008; 10:593–605; PMID:17979984; http://dx.doi.org/10.1111/j.1462-5822.2007.01068.x
    • (2008) Cell Microbiol , vol.10 , pp. 593-605
    • Niu, H.1    Yamaguchi, M.2    Rikihisa, Y.3
  • 36
    • 84877317415 scopus 로고    scopus 로고
    • Ats-1: a novel bacterial molecule that links ?autophagy to bacterial nutrition
    • 23388398
    • H.Niu, Y.Rikihisa. Ats-1:a novel bacterial molecule that links ?autophagy to bacterial nutrition. Autophagy 2013; 9:787–8; PMID:23388398; http://dx.doi.org/10.4161/auto.23693
    • (2013) Autophagy , vol.9 , pp. 787-788
    • Niu, H.1    Rikihisa, Y.2
  • 37
    • 84871385890 scopus 로고    scopus 로고
    • Autophagosomes induced by a bacterial Beclin 1 binding protein facilitate obligatory intracellular infection
    • 23197835
    • H.Niu, Q.Xiong, A.Yamamoto, M.Hayashi-Nishino, Y.Rikihisa. Autophagosomes induced by a bacterial Beclin 1 binding protein facilitate obligatory intracellular infection. Proc Natl Acad Sci U S A 2012; 109:20800–7; PMID:23197835; http://dx.doi.org/10.1073/pnas.1218674109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 20800-20807
    • Niu, H.1    Xiong, Q.2    Yamamoto, A.3    Hayashi-Nishino, M.4    Rikihisa, Y.5
  • 38
    • 0036126936 scopus 로고    scopus 로고
    • Characterization and transcriptional analysis of gene clusters for a type IV secretion machinery in human granulocytic and monocytic ehrlichiosis agents
    • 11895979
    • N.Ohashi, N.Zhi, Q.Lin, Y.Rikihisa. Characterization and transcriptional analysis of gene clusters for a type IV secretion machinery in human granulocytic and monocytic ehrlichiosis agents. Infect Immun 2002; 70:2128–38; PMID:11895979; http://dx.doi.org/10.1128/IAI.70.4.2128-2138.2002
    • (2002) Infect Immun , vol.70 , pp. 2128-2138
    • Ohashi, N.1    Zhi, N.2    Lin, Q.3    Rikihisa, Y.4
  • 39
    • 40449139085 scopus 로고    scopus 로고
    • Regulation of type IV secretion apparatus genes during Ehrlichia chaffeensis intracellular development by a previously unidentified protein
    • 18192398
    • Z.Cheng, X.Wang, Y.Rikihisa. Regulation of type IV secretion apparatus genes during Ehrlichia chaffeensis intracellular development by a previously unidentified protein. J Bacteriol 2008; 190:2096–105; PMID:18192398; http://dx.doi.org/10.1128/JB.01813-07
    • (2008) J Bacteriol , vol.190 , pp. 2096-2105
    • Cheng, Z.1    Wang, X.2    Rikihisa, Y.3
  • 40
    • 58149490639 scopus 로고    scopus 로고
    • Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles
    • 18952796
    • W.Bao, Y.Kumagai, H.Niu, M.Yamaguchi, K.Miura, Y.Rikihisa. Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles. J Bacteriol 2009; 191:278–86; PMID:18952796; http://dx.doi.org/10.1128/JB.01031-08
    • (2009) J Bacteriol , vol.191 , pp. 278-286
    • Bao, W.1    Kumagai, Y.2    Niu, H.3    Yamaguchi, M.4    Miura, K.5    Rikihisa, Y.6
  • 41
    • 75249092539 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum and Ehrlichia chaffeensis type IV secretion and Ank proteins
    • 20053580
    • Y.Rikihisa, M.Lin. Anaplasma phagocytophilum and Ehrlichia chaffeensis type IV secretion and Ank proteins. Curr Opin Microbiol 2010; 13:59–66; PMID:20053580; http://dx.doi.org/10.1016/j.mib.2009.12.008
    • (2010) Curr Opin Microbiol , vol.13 , pp. 59-66
    • Rikihisa, Y.1    Lin, M.2
  • 42
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • 16529981
    • S.Backert, T.F.Meyer. Type IV secretion systems and their effectors in bacterial pathogenesis. Curr Opin Microbiol 2006; 9:207–17; PMID:16529981; http://dx.doi.org/10.1016/j.mib.2006.02.008
    • (2006) Curr Opin Microbiol , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 43
    • 84862804099 scopus 로고    scopus 로고
    • Ehrlichia type IV secretion effector ECH0825 is translocated to mitochondria and curbs ROS and apoptosis by upregulating host MnSOD
    • 22348527
    • H.Liu, W.Bao, M.Lin, H.Niu, Y.Rikihisa. Ehrlichia type IV secretion effector ECH0825 is translocated to mitochondria and curbs ROS and apoptosis by upregulating host MnSOD. Cell Microbiol 2012; 14:1037–50; PMID:22348527; http://dx.doi.org/10.1111/j.1462-5822.2012.01775.x
    • (2012) Cell Microbiol , vol.14 , pp. 1037-1050
    • Liu, H.1    Bao, W.2    Lin, M.3    Niu, H.4    Rikihisa, Y.5
  • 46
    • 0030873250 scopus 로고    scopus 로고
    • Identification of an early endosomal protein regulated by phosphatidylinositol 3-kinase
    • V.Patki, J.Virbasius, W.S.Lane, B.H.Toh, H.S.Shpetner, S.Corvera. Identification of an early endosomal protein regulated by phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A 1997; 94:7326–30; PMID:9207090; http://dx.doi.org/10.1073/pnas.94.14.7326
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7326-7330
    • Patki, V.1    Virbasius, J.2    Lane, W.S.3    Toh, B.H.4    Shpetner, H.S.5    Corvera, S.6
  • 48
    • 39749141485 scopus 로고    scopus 로고
    • The regulation and function of Class III PI3Ks: novel roles for Vps34
    • 18215151
    • J.M.Backer. The regulation and function of Class III PI3Ks:novel roles for Vps34. Biochem J 2008; 410:1–17; PMID:18215151; http://dx.doi.org/10.1042/BJ20071427
    • (2008) Biochem J , vol.410 , pp. 1-17
    • Backer, J.M.1
  • 49
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • 10625637
    • A.Petiot, E.Ogier-Denis, E.F.Blommaart, A.J.Meijer, P.Codogno. Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 2000; 275:992–8; PMID:10625637; http://dx.doi.org/10.1074/jbc.275.2.992
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 50
    • 0005677775 scopus 로고
    • 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • P.O.Seglen, P.B.Gordon. 3-Methyladenine:specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc Natl Acad Sci U S A 1982; 79:1889–92; PMID:6952238; http://dx.doi.org/10.1073/pnas.79.6.1889
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 2238-2292
    • Seglen, P.O.1    Gordon, P.B.2
  • 51
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by ?phosphoinositide 3-kinases
    • 16467569
    • K.Lindmo, H.Stenmark. Regulation of membrane traffic by ?phosphoinositide 3-kinases. J Cell Sci 2006; 119:605–14; PMID:16467569; http://dx.doi.org/10.1242/jcs.02855
    • (2006) J Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 52
    • 0031976047 scopus 로고    scopus 로고
    • Immunodominant major outer membrane proteins of Ehrlichia chaffeensis are encoded by a polymorphic multigene family
    • N.Ohashi, N.Zhi, Y.Zhang, Y.Rikihisa. Immunodominant major outer membrane proteins of Ehrlichia chaffeensis are encoded by a polymorphic multigene family. Infect Immun 1998; 66:132–9; PMID:9423849
    • (1998) Infect Immun , vol.66 , pp. 132-139
    • Ohashi, N.1    Zhi, N.2    Zhang, Y.3    Rikihisa, Y.4
  • 53
    • 84920913770 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis proliferation begins with NtrY/NtrX and PutA/GlnA upregulation and CtrA degradation induced by Proline and Glutamine Uptake
    • 25425236
    • Z.Cheng, M.Lin, Y.Rikihisa. Ehrlichia chaffeensis proliferation begins with NtrY/NtrX and PutA/GlnA upregulation and CtrA degradation induced by Proline and Glutamine Uptake. MBio 2014; 5:e02141; PMID:25425236; http://dx.doi.org/10.1128/mBio.02141-14
    • (2014) MBio , pp. 2141
    • Cheng, Z.1    Lin, M.2    Rikihisa, Y.3
  • 54
    • 84887265439 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis uses its surface protein EtpE to bind GPI-anchored protein DNase X and trigger entry into mammalian cells
    • 24098122
    • D.Mohan Kumar, M.Yamaguchi, K.Miura, M.Lin, M.Los, J.F.Coy, Y.Rikihisa. Ehrlichia chaffeensis uses its surface protein EtpE to bind GPI-anchored protein DNase X and trigger entry into mammalian cells. PLoS Pathog 2013; 9:e1003666; PMID:24098122; http://dx.doi.org/10.1371/journal.ppat.1003666
    • (2013) PLoS Pathog , vol.9 , pp. 1003666
    • Mohan Kumar, D.1    Yamaguchi, M.2    Miura, K.3    Lin, M.4    Los, M.5    Coy, J.F.6    Rikihisa, Y.7
  • 57
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • 11306555
    • A.Kihara, Y.Kabeya, Y.Ohsumi, T.Yoshimori. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep 2001; 2:330–5; PMID:11306555; http://dx.doi.org/10.1093/embo-reports/kve061
    • (2001) EMBO Rep , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 58
    • 80053501671 scopus 로고    scopus 로고
    • Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13
    • 21962518
    • J.Liu, H.Xia, M.Kim, L.Xu, Y.Li, L.Zhang, Y.Cai, H.V.Norberg, T.Zhang, T.Furuya, Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13. Cell 2011; 147:223–34; PMID:21962518; http://dx.doi.org/10.1016/j.cell.2011.08.037
    • (2011) Cell , vol.147 , pp. 223-234
    • Liu, J.1    Xia, H.2    Kim, M.3    Xu, L.4    Li, Y.5    Zhang, L.6    Cai, Y.7    Norberg, H.V.8    Zhang, T.9    Furuya, T.10
  • 59
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • J.Heitman, N.R.Movva, M.N.Hall. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science 1991; 253:905–9; PMID:1715094; http://dx.doi.org/10.1126/science.1715094
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 60
    • 77957682295 scopus 로고    scopus 로고
    • ATG16L1 and NOD2 interact in an autophagy-dependent antibacterial pathway implicated in Crohn's disease pathogenesis
    • 41 e1-2, 20637199
    • C.R.Homer, A.L.Richmond, N.A.Rebert, J.P.Achkar, C.McDonald. ATG16L1 and NOD2 interact in an autophagy-dependent antibacterial pathway implicated in Crohn's disease pathogenesis. Gastroenterology 2010; 139;1630–41, 41 e1-2; PMID:20637199; http://dx.doi.org/10.1053/j.gastro.2010.07.006
    • (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
  • 64
    • 55249109400 scopus 로고    scopus 로고
    • Autophagosome-independent essential function for the autophagy protein Atg5 in cellular immunity to intracellular pathogens
    • 18996346
    • Z.Zhao, B.Fux, M.Goodwin, I.R.Dunay, D.Strong, B.C.Miller, K.Cadwell, M.A.Delgado, M.Ponpuak, K.G.Green, Autophagosome-independent essential function for the autophagy protein Atg5 in cellular immunity to intracellular pathogens. Cell Host Microbe 2008; 4:458–69; PMID:18996346; http://dx.doi.org/10.1016/j.chom.2008.10.003
    • (2008) Cell Host Microbe , vol.4 , pp. 458-469
    • Zhao, Z.1    Fux, B.2    Goodwin, M.3    Dunay, I.R.4    Strong, D.5    Miller, B.C.6    Cadwell, K.7    Delgado, M.A.8    Ponpuak, M.9    Green, K.G.10
  • 65
    • 0009785235 scopus 로고
    • Mouse lysozyme M gene: isolation, characterization, and expression studies
    • M.Cross, I.Mangelsdorf, A.Wedel, R.Renkawitz. Mouse lysozyme M gene:isolation, characterization, and expression studies. Proc Natl Acad Sci U S A 1988; 85:6232–6; PMID:3413093; http://dx.doi.org/10.1073/pnas.85.17.6232
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 6232-6236
    • Cross, M.1    Mangelsdorf, I.2    Wedel, A.3    Renkawitz, R.4
  • 67
    • 0034099224 scopus 로고    scopus 로고
    • Apg5p functions in the sequestration step in the cytoplasm-to-vacuole targeting and macroautophagy pathways
    • 10712513
    • M.D.George, M.Baba, S.V.Scott, N.Mizushima, B.S.Garrison, Y.Ohsumi, D.J.Klionsky. Apg5p functions in the sequestration step in the cytoplasm-to-vacuole targeting and macroautophagy pathways. Mol Biol Cell 2000; 11:969–82; PMID:10712513; http://dx.doi.org/10.1091/mbc.11.3.969
    • (2000) Mol Biol Cell , vol.11 , pp. 969-982
    • George, M.D.1    Baba, M.2    Scott, S.V.3    Mizushima, N.4    Garrison, B.S.5    Ohsumi, Y.6    Klionsky, D.J.7
  • 68
    • 84904678420 scopus 로고    scopus 로고
    • The general amino acid control pathway regulates mTOR and autophagy during serum/glutamine starvation
    • 25049270
    • R.Chen, Y.Zou, D.Mao, D.Sun, G.Gao, J.Shi, X.Liu, C.Zhu, M.Yang, W.Ye, The general amino acid control pathway regulates mTOR and autophagy during serum/glutamine starvation. J Cell Biol 2014; 206:173–82; PMID:25049270; http://dx.doi.org/10.1083/jcb.201403009
    • (2014) J Cell Biol , vol.206 , pp. 173-182
    • Chen, R.1    Zou, Y.2    Mao, D.3    Sun, D.4    Gao, G.5    Shi, J.6    Liu, X.7    Zhu, C.8    Yang, M.9    Ye, W.10
  • 69
    • 84899102098 scopus 로고    scopus 로고
    • Targeted metabolomics of Physaria fendleri, an industrial crop producing hydroxy fatty acids
    • 24443498
    • J.C.Cocuron, B.Anderson, A.Boyd, A.P.Alonso. Targeted metabolomics of Physaria fendleri, an industrial crop producing hydroxy fatty acids. Plant Cell Physiol 2014; 55:620–33; PMID:24443498; http://dx.doi.org/10.1093/pcp/pcu011
    • (2014) Plant Cell Physiol , vol.55 , pp. 620-633
    • Cocuron, J.C.1    Anderson, B.2    Boyd, A.3    Alonso, A.P.4
  • 70
    • 34250802413 scopus 로고    scopus 로고
    • Comigration of two autophagosome-associated dehydrogenases on two-dimensional polyacrylamide gels
    • 16874067
    • M.L.Sneve, A.Overbye, M.Fengsrud, P.O.Seglen. Comigration of two autophagosome-associated dehydrogenases on two-dimensional polyacrylamide gels. Autophagy 2005; 1:157–62; PMID:16874067; http://dx.doi.org/10.4161/auto.1.3.2037
    • (2005) Autophagy , vol.1 , pp. 157-162
    • Sneve, M.L.1    Overbye, A.2    Fengsrud, M.3    Seglen, P.O.4
  • 71
    • 34547640142 scopus 로고    scopus 로고
    • Surface-exposed proteins of Ehrlichia chaffeensis
    • 17517859
    • Y.Ge, Y.Rikihisa. Surface-exposed proteins of Ehrlichia chaffeensis. Infect Immun 2007; 75:3833–41; PMID:17517859; http://dx.doi.org/10.1128/IAI.00188-07
    • (2007) Infect Immun , vol.75 , pp. 3833-3841
    • Ge, Y.1    Rikihisa, Y.2
  • 72
    • 77955953184 scopus 로고    scopus 로고
    • Cyclic di-GMP signaling regulates invasion of Ehrlichia chaffeensis into human monocytes
    • 20562302
    • Y.Kumagai, J.Matsuo, Y.Hayakawa, Y.Rikihisa. Cyclic di-GMP signaling regulates invasion of Ehrlichia chaffeensis into human monocytes. J Bacteriol 2010; 192:4122–33; PMID:20562302; http://dx.doi.org/10.1128/JB.00132-10
    • (2010) J Bacteriol , vol.192 , pp. 4122-4133
    • Kumagai, Y.1    Matsuo, J.2    Hayakawa, Y.3    Rikihisa, Y.4
  • 74
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • 21258367
    • J.Kim, M.Kundu, B.Viollet, K.L.Guan. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 2011; 13:132–41; PMID:21258367; http://dx.doi.org/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
  • 75
    • 0025837327 scopus 로고
    • Mitogen-activated 70K S6 kinase. Identification of in vitro 40 S ribosomal S6 phosphorylation sites
    • S.Ferrari, H.R.Bandi, J.Hofsteenge, B.M.Bussian, G.Thomas. Mitogen-activated 70K S6 kinase. Identification of in vitro 40 S ribosomal S6 phosphorylation sites. J Biol Chem 1991; 266:22770–5; PMID:1939282
    • (1991) J Biol Chem , vol.266 , pp. 22770-22775
    • Ferrari, S.1    Bandi, H.R.2    Hofsteenge, J.3    Bussian, B.M.4    Thomas, G.5
  • 76
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
    • S.A.Hawley, M.Davison, A.Woods, S.P.Davies, R.K.Beri, D.Carling, D.G.Hardie. Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J Biol Chem 1996; 271:27879–87; PMID:8910387; http://dx.doi.org/10.1074/jbc.271.44.27879
    • (1996) J Biol Chem , vol.271 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 77
    • 65549145048 scopus 로고    scopus 로고
    • An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1
    • 19150980
    • C.C.Thoreen, S.A.Kang, J.W.Chang, Q.Liu, J.Zhang, Y.Gao, L.J.Reichling, T.Sim, D.M.Sabatini, N.S.Gray. An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1. J Biol Chem 2009; 284:8023–32; PMID:19150980; http://dx.doi.org/10.1074/jbc.M900301200
    • (2009) J Biol Chem , vol.284 , pp. 8023-8032
    • Thoreen, C.C.1    Kang, S.A.2    Chang, J.W.3    Liu, Q.4    Zhang, J.5    Gao, Y.6    Reichling, L.J.7    Sim, T.8    Sabatini, D.M.9    Gray, N.S.10
  • 78
    • 58549084167 scopus 로고    scopus 로고
    • Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
    • 19074260
    • P.K.Kim, D.W.Hailey, R.T.Mullen, J.Lippincott-Schwartz. Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes. Proc Natl Acad Sci U S A 2008; 105:20567–74; PMID:19074260; http://dx.doi.org/10.1073/pnas.0810611105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20567-20574
    • Kim, P.K.1    Hailey, D.W.2    Mullen, R.T.3    Lippincott-Schwartz, J.4
  • 79
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • 17580304
    • S.Pankiv, T.H.Clausen, T.Lamark, A.Brech, J.A.Bruun, H.Outzen, A.Øvervatn, G.Bjørkøy, T.Johansen. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282:24131–45; PMID:17580304; http://dx.doi.org/10.1074/jbc.M702824200
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5    Outzen, H.6    Øvervatn, A.7    Bjørkøy, G.8    Johansen, T.9
  • 82
    • 34250802980 scopus 로고    scopus 로고
    • Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy
    • 17389386
    • S.Alonso, K.Pethe, D.G.Russell, G.E.Purdy. Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy. Proc Natl Acad Sci U S A 2007; 104:6031–6; PMID:17389386; http://dx.doi.org/10.1073/pnas.0700036104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 6031-6036
    • Alonso, S.1    Pethe, K.2    Russell, D.G.3    Purdy, G.E.4
  • 83
    • 34250899749 scopus 로고    scopus 로고
    • Ubiquitin trafficking to the lysosome: keeping the house tidy and getting rid of unwanted guests
    • 17457035
    • G.E.Purdy, D.G.Russell. Ubiquitin trafficking to the lysosome:keeping the house tidy and getting rid of unwanted guests. Autophagy 2007; 3:399–401; PMID:17457035; http://dx.doi.org/10.4161/auto.4272
    • (2007) Autophagy , vol.3 , pp. 399-401
    • Purdy, G.E.1    Russell, D.G.2
  • 87
    • 0021971199 scopus 로고
    • Mechanism of membrane damage by streptolysin-O
    • S.Bhakdi, J.Tranum-Jensen, A.Sziegoleit. Mechanism of membrane damage by streptolysin-O. Infect Immun 1985; 47:52–60; PMID:3880730
    • (1985) Infect Immun , vol.47 , pp. 52-60
    • Bhakdi, S.1    Tranum-Jensen, J.2    Sziegoleit, A.3
  • 88
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • 15068806
    • P.Venkatraman, R.Wetzel, M.Tanaka, N.Nukina, A.L.Goldberg. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 2004; 14:95–104; PMID:15068806; http://dx.doi.org/10.1016/S1097-2765(04)00151-0
    • (2004) Mol Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 89
    • 70350380897 scopus 로고    scopus 로고
    • Mimicking proteasomal release of polyglutamine peptides initiates aggregation and toxicity
    • 19690053
    • M.Raspe, J.Gillis, H.Krol, S.Krom, K.Bosch, H.van Veen, E.Reits. Mimicking proteasomal release of polyglutamine peptides initiates aggregation and toxicity. J Cell Sci 2009; 122:3262–71; PMID:19690053; http://dx.doi.org/10.1242/jcs.045567
    • (2009) J Cell Sci , vol.122 , pp. 3262-3271
    • Raspe, M.1    Gillis, J.2    Krol, H.3    Krom, S.4    Bosch, K.5    van Veen, H.6    Reits, E.7
  • 90
    • 33947164372 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
    • 17318184
    • N.Bhutani, P.Venkatraman, A.L.Goldberg. Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation. EMBO J 2007; 26:1385–96; PMID:17318184; http://dx.doi.org/10.1038/sj.emboj.7601592
    • (2007) EMBO J , vol.26 , pp. 1592-1596
    • Bhutani, N.1    Venkatraman, P.2    Goldberg, A.L.3
  • 92
    • 0028800171 scopus 로고
    • Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
    • T.M.Harding, K.A.Morano, S.V.Scott, D.J.Klionsky. Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J Cell Biol 1995; 131:591–602; PMID:7593182; http://dx.doi.org/10.1083/jcb.131.3.591
    • (1995) J Cell Biol , vol.131 , pp. 1083-1602
    • Harding, T.M.1    Morano, K.A.2    Scott, S.V.3    Klionsky, D.J.4
  • 93
    • 0035185530 scopus 로고    scopus 로고
    • Specific inhibitor of puromycin-sensitive aminopeptidase with a homophthalimide skeleton: identification of the target molecule and a structure-activity relationship study
    • M.Komoda, H.Kakuta, H.Takahashi, Y.Fujimoto, S.Kadoya, F.Kato, Y.Hashimoto. Specific inhibitor of puromycin-sensitive aminopeptidase with a homophthalimide skeleton:identification of the target molecule and a structure-activity relationship study. Bioorg Med Chem 2001; 9:121–31; PMID:11197332; http://dx.doi.org/10.1016/S0968–0896(00)00231–5
    • (2001) Bioorg Med Chem , vol.9 , pp. 231-235
    • Komoda, M.1    Kakuta, H.2    Takahashi, H.3    Fujimoto, Y.4    Kadoya, S.5    Kato, F.6    Hashimoto, Y.7
  • 94
    • 0037421050 scopus 로고    scopus 로고
    • Fluorescent bioprobes for visualization of puromycin-sensitive aminopeptidase in living cells
    • H.Kakuta, Y.Koiso, K.Nagasawa, Y.Hashimoto. Fluorescent bioprobes for visualization of puromycin-sensitive aminopeptidase in living cells. Bioorg Med Chem Lett 2003; 13:83–6; PMID:12467622; http://dx.doi.org/10.1016/S0960–894X(02)00845–4
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 844-845
    • Kakuta, H.1    Koiso, Y.2    Nagasawa, K.3    Hashimoto, Y.4
  • 95
    • 84876086849 scopus 로고    scopus 로고
    • Class IA PI3K p110beta subunit promotes autophagy through Rab5 small GTPase in response to growth factor limitation
    • Z.Dou, J.A.Pan, H.A.Dbouk, L.M.Ballou, J.L.DeLeon, Y.Fan, J.S.Chen, Z.Liang, G.Li, J.M.Backer, Class IA PI3K p110beta subunit promotes autophagy through Rab5 small GTPase in response to growth factor limitation. Mol Cell 2013; 50:29–42; PMID:23434372; http://dx.doi.org/10.1016/j.molcel.2013.01.022
    • (2013) Mol Cell , vol.50 , pp. 1016-1042
    • Dou, Z.1    Pan, J.A.2    Dbouk, H.A.3    Ballou, L.M.4    DeLeon, J.L.5    Fan, Y.6    Chen, J.S.7    Liang, Z.8    Li, G.9    Backer, J.M.10
  • 96
    • 80054978956 scopus 로고    scopus 로고
    • Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy
    • W.C.Su, T.C.Chao, Y.L.Huang, S.C.Weng, K.S.Jeng, M.M.Lai. Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy. J Virol 2011; 85:10561–71; PMID:21835792; http://dx.doi.org/10.1128/JVI.00173–11
    • (2011) J Virol , vol.85 , pp. 111-173
    • Su, W.C.1    Chao, T.C.2    Huang, Y.L.3    Weng, S.C.4    Jeng, K.S.5    Lai, M.M.6
  • 97
    • 46249127490 scopus 로고    scopus 로고
    • Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease
    • B.Ravikumar, S.Imarisio, S.Sarkar, C.J.O'Kane, D.C.Rubinsztein. Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease. J Cell Sci 2008; 121:1649–60; PMID:18430781; http://dx.doi.org/10.1242/jcs.025726
    • (2008) J Cell Sci , vol.121 , pp. 1242-1260
    • Ravikumar, B.1    Imarisio, S.2    Sarkar, S.3    O'Kane, C.J.4    Rubinsztein, D.C.5
  • 99
    • 1942469322 scopus 로고    scopus 로고
    • Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference
    • 14985334
    • F.Huang, A.Khvorova, W.Marshall, A.Sorkin. Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference. J Biol Chem 2004; 279:16657–61; PMID:14985334; http://dx.doi.org/10.1074/jbc.C400046200
    • (2004) J Biol Chem , vol.279 , pp. 16657-16661
    • Huang, F.1    Khvorova, A.2    Marshall, W.3    Sorkin, A.4
  • 100
    • 33748792527 scopus 로고    scopus 로고
    • Insulin-stimulated Interaction between insulin receptor substrate 1 and p85alpha and activation of protein kinase B/Akt require Rab5
    • 16880210
    • X.Su, I.J.Lodhi, A.R.Saltiel, P.D.Stahl. Insulin-stimulated Interaction between insulin receptor substrate 1 and p85alpha and activation of protein kinase B/Akt require Rab5. J Biol Chem 2006; 281:27982–90; PMID:16880210; http://dx.doi.org/10.1074/jbc.M602873200
    • (2006) J Biol Chem , vol.281 , pp. 27982-27990
    • Su, X.1    Lodhi, I.J.2    Saltiel, A.R.3    Stahl, P.D.4
  • 102
    • 0026554965 scopus 로고
    • GTP-binding proteins in intracellular transport
    • 14731525
    • S.R.Pfeffer. GTP-binding proteins in intracellular transport. Trends Cell Biol 1992; 2:41–6; PMID:14731525; http://dx.doi.org/10.1016/0962-8924(92)90161-F
    • (1992) Trends Cell Biol , vol.2 , pp. 41-46
    • Pfeffer, S.R.1
  • 103
    • 0024276910 scopus 로고
    • Do GTPases direct membrane traffic in secretion?
    • 2836065
    • H.R.Bourne. Do GTPases direct membrane traffic in secretion? Cell 1988; 53:669–71; PMID:2836065; http://dx.doi.org/10.1016/0092-8674(88)90081-5
    • (1988) Cell , vol.53 , pp. 669-671
    • Bourne, H.R.1
  • 104
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • 19603039
    • H.Stenmark. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 2009; 10:513–25; PMID:19603039; http://dx.doi.org/10.1038/nrm2728
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 105
    • 26944460079 scopus 로고    scopus 로고
    • A GTPase-activating protein controls Rab5 function in endocytic trafficking
    • 16086013
    • A.K.Haas, E.Fuchs, R.Kopajtich, F.A.Barr. A GTPase-activating protein controls Rab5 function in endocytic trafficking. Nat Cell Biol 2005; 7:887–93; PMID:16086013; http://dx.doi.org/10.1038/ncb1290
    • (2005) Nat Cell Biol , vol.7 , pp. 887-893
    • Haas, A.K.1    Fuchs, E.2    Kopajtich, R.3    Barr, F.A.4
  • 106
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • 21248839
    • B.Levine, N.Mizushima, H.W.Virgin. Autophagy in immunity and inflammation. Nature 2011; 469:323–35; PMID:21248839; http://dx.doi.org/10.1038/nature09782
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 107
    • 79951910694 scopus 로고    scopus 로고
    • Autophagy in immunity and cell-autonomous defense against intracellular microbes
    • 21349088
    • V.Deretic. Autophagy in immunity and cell-autonomous defense against intracellular microbes. Immunol Rev 2011; 240:92–104; PMID:21349088; http://dx.doi.org/10.1111/j.1600-065X.2010.00995.x
    • (2011) Immunol Rev , vol.240 , pp. 92-104
    • Deretic, V.1
  • 109
    • 0037627408 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis glycosylated phosphatidylinositol causes phagosome maturation arrest
    • 12702770
    • R.A.Fratti, J.Chua, I.Vergne, V.Deretic. Mycobacterium tuberculosis glycosylated phosphatidylinositol causes phagosome maturation arrest. Proc Natl Acad Sci U S A 2003; 100:5437–42; PMID:12702770; http://dx.doi.org/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
  • 110
    • 84880831979 scopus 로고    scopus 로고
    • Secreted acid phosphatase (SapM) of Mycobacterium tuberculosis is indispensable for arresting phagosomal maturation and growth of the pathogen in guinea pig tissues
    • 23923000
    • R.V.Puri, P.V.Reddy, A.K.Tyagi. Secreted acid phosphatase (SapM) of Mycobacterium tuberculosis is indispensable for arresting phagosomal maturation and growth of the pathogen in guinea pig tissues. PLoS One 2013; 8:e70514; PMID:23923000; http://dx.doi.org/10.1371/journal.pone.0070514
    • (2013) PLoS One , vol.8 , pp. 70514
    • Puri, R.V.1    Reddy, P.V.2    Tyagi, A.K.3
  • 112
    • 32644434386 scopus 로고    scopus 로고
    • Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease
    • 16476778
    • A.Pal, F.Severin, B.Lommer, A.Shevchenko, M.Zerial. Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early endosome motility and is up-regulated in Huntington's disease. J Cell Biol 2006; 172:605–18; PMID:16476778; http://dx.doi.org/10.1083/jcb.200509091
    • (2006) J Cell Biol , vol.172 , pp. 605-618
    • Pal, A.1    Severin, F.2    Lommer, B.3    Shevchenko, A.4    Zerial, M.5
  • 113
    • 0025362656 scopus 로고
    • In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome
    • 2166050
    • J.Tooze, M.Hollinshead, T.Ludwig, K.Howell, B.Hoflack, H.Kern. In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome. J Cell Biol 1990; 111:329–45; PMID:2166050; http://dx.doi.org/10.1083/jcb.111.2.329
    • (1990) J Cell Biol , vol.111 , pp. 329-345
    • Tooze, J.1    Hollinshead, M.2    Ludwig, T.3    Howell, K.4    Hoflack, B.5    Kern, H.6
  • 114
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in Mammalian cells
    • 16874026
    • E.L.Eskelinen. Maturation of autophagic vacuoles in Mammalian cells. Autophagy 2005; 1:1–10; PMID:16874026; http://dx.doi.org/10.4161/auto.1.1.1270
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.L.1
  • 115
    • 57649195400 scopus 로고    scopus 로고
    • Autophagy and multivesicular bodies: two closely related partners
    • 19008921
    • C.M.Fader, M.I.Colombo. Autophagy and multivesicular bodies:two closely related partners. Cell Death Differ 2009; 16:70–8; PMID:19008921; http://dx.doi.org/10.1038/cdd.2008.168
    • (2009) Cell Death Differ , vol.16 , pp. 70-78
    • Fader, C.M.1    Colombo, M.I.2
  • 118
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • 9515966
    • T.Kobayashi, E.Stang, K.S.Fang, P.de Moerloose, R.G.Parton, J.?Gruenberg. A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 1998; 392:193–7; PMID:9515966; http://dx.doi.org/10.1038/32440
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    de Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 119
    • 0141433284 scopus 로고    scopus 로고
    • PI3P signaling regulates receptor sorting but not transport in the endosomal pathway
    • 12975344
    • A.Petiot, J.Faure, H.Stenmark, J.Gruenberg. PI3P signaling regulates receptor sorting but not transport in the endosomal pathway. J Cell Biol 2003; 162:971–9; PMID:12975344; http://dx.doi.org/10.1083/jcb.200303018
    • (2003) J Cell Biol , vol.162 , pp. 971-979
    • Petiot, A.1    Faure, J.2    Stenmark, H.3    Gruenberg, J.4
  • 120
    • 0032944031 scopus 로고    scopus 로고
    • Multivesicular body morphogenesis requires phosphatidyl-inositol 3-kinase activity
    • 9889123
    • M.Fernandez-Borja, R.Wubbolts, J.Calafat, H.Janssen, N.Divecha, S.Dusseljee, J.Neefjes. Multivesicular body morphogenesis requires phosphatidyl-inositol 3-kinase activity. Curr Biol 1999; 9:55–8; PMID:9889123; http://dx.doi.org/10.1016/S0960-9822(99)80048-7
    • (1999) Curr Biol , vol.9 , pp. 55-58
    • Fernandez-Borja, M.1    Wubbolts, R.2    Calafat, J.3    Janssen, H.4    Divecha, N.5    Dusseljee, S.6    Neefjes, J.7
  • 121
    • 84862793994 scopus 로고    scopus 로고
    • Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function
    • 22284051
    • J.Zhang, C.Reiling, J.B.Reinecke, I.Prislan, L.A.Marky, P.L.Sorgen, N.Naslavsky, S.Caplan. Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function. Traffic 2012; 13:745–57; PMID:22284051; http://dx.doi.org/10.1111/j.1600-0854.2012.01334.x
    • (2012) Traffic , vol.13 , pp. 745-757
    • Zhang, J.1    Reiling, C.2    Reinecke, J.B.3    Prislan, I.4    Marky, L.A.5    Sorgen, P.L.6    Naslavsky, N.7    Caplan, S.8
  • 122
    • 0027938009 scopus 로고
    • Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron-transferrin
    • 7927758
    • R.E.Barnewall, Y.Rikihisa. Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron-transferrin. Infect Immun 1994; 62:4804–10; PMID:7927758
    • (1994) Infect Immun , vol.62 , pp. 4804-4810
    • Barnewall, R.E.1    Rikihisa, Y.2
  • 123
    • 0031015273 scopus 로고    scopus 로고
    • Ultrastructural and antigenic characterization of a granulocytic ehrlichiosis agent directly isolated and stably cultivated from a patient in New York state
    • 8985223
    • Y.Rikihisa, N.Zhi, G.P.Wormser, B.Wen, H.W.Horowitz, K.E.Hechemy. Ultrastructural and antigenic characterization of a granulocytic ehrlichiosis agent directly isolated and stably cultivated from a patient in New York state. J Infect Dis 1997; 175:210–3; PMID:8985223; http://dx.doi.org/10.1093/infdis/175.1.210
    • (1997) J Infect Dis , vol.175 , pp. 210-213
    • Rikihisa, Y.1    Zhi, N.2    Wormser, G.P.3    Wen, B.4    Horowitz, H.W.5    Hechemy, K.E.6
  • 124
    • 0031717461 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies to the 44-kgdalton major outer membrane protein of the human granulocytic ehrlichiosis agent
    • 9774579
    • H.Y.Kim, Y.Rikihisa. Characterization of monoclonal antibodies to the 44-kgdalton major outer membrane protein of the human granulocytic ehrlichiosis agent. J Clin Microbiol 1998; 36:3278–84; PMID:9774579
    • (1998) J Clin Microbiol , vol.36 , pp. 3278-3284
    • Kim, H.Y.1    Rikihisa, Y.2
  • 125
    • 0035105295 scopus 로고    scopus 로고
    • The stress-induced MAP kinase p38 regulates endocytic trafficking via the GDI:Rab5 complex
    • 11239470
    • V.Cavalli, F.Vilbois, M.Corti, M.J.Marcote, K.Tamura, M.Karin, S.Arkinstall, J.Gruenberg. The stress-induced MAP kinase p38 regulates endocytic trafficking via the GDI:Rab5 complex. Mol Cell 2001; 7:421–32; PMID:11239470; http://dx.doi.org/10.1016/S1097-2765(01)00189-7
    • (2001) Mol Cell , vol.7 , pp. 421-432
    • Cavalli, V.1    Vilbois, F.2    Corti, M.3    Marcote, M.J.4    Tamura, K.5    Karin, M.6    Arkinstall, S.7    Gruenberg, J.8
  • 126
    • 79955163875 scopus 로고    scopus 로고
    • A practical guide to evaluating colocalization in biological microscopy
    • 21209361
    • K.W.Dunn, M.M.Kamocka, J.H.McDonald. A practical guide to evaluating colocalization in biological microscopy. Am J Physiol Cell Physiol 2011; 300:C723–42; PMID:21209361; http://dx.doi.org/10.1152/ajpcell.00462.2010
    • (2011) Am J Physiol Cell Physiol , vol.300 , pp. C723-C742
    • Dunn, K.W.1    Kamocka, M.M.2    McDonald, J.H.3
  • 127
    • 33745771590 scopus 로고    scopus 로고
    • Intra-leukocyte expression of two-component systems in Ehrlichia chaffeensis and Anaplasma phagocytophilum and effects of the histidine kinase inhibitor closantel
    • 16882029
    • Z.Cheng, Y.Kumagai, M.Lin, C.Zhang, Y.Rikihisa. Intra-leukocyte expression of two-component systems in Ehrlichia chaffeensis and Anaplasma phagocytophilum and effects of the histidine kinase inhibitor closantel. Cell Microbiol 2006; 8:1241–52; PMID:16882029; http://dx.doi.org/10.1111/j.1462-5822.2006.00704.x
    • (2006) Cell Microbiol , vol.8 , pp. 1241-1252
    • Cheng, Z.1    Kumagai, Y.2    Lin, M.3    Zhang, C.4    Rikihisa, Y.5
  • 128
    • 0016683921 scopus 로고
    • Competition between Chlamydia psittaci and L cells for host isoleucine pools: a limiting factor in chlamydial multiplication
    • 1095493
    • T.P.Hatch. Competition between Chlamydia psittaci and L cells for host isoleucine pools:a limiting factor in chlamydial multiplication. Infect Immun 1975; 12:211–20; PMID:1095493
    • (1975) Infect Immun , vol.12 , pp. 211-220
    • Hatch, T.P.1
  • 129
    • 71049118063 scopus 로고    scopus 로고
    • Rab5 isoforms differentially regulate the trafficking and degradation of epidermal growth factor receptors
    • 19723633
    • P.I.Chen, C.Kong, X.Su, P.D.Stahl. Rab5 isoforms differentially regulate the trafficking and degradation of epidermal growth factor receptors. J Biol Chem 2009; 284:30328–38; PMID:19723633; http://dx.doi.org/10.1074/jbc.M109.034546
    • (2009) J Biol Chem , vol.284 , pp. 30328-30338
    • Chen, P.I.1    Kong, C.2    Su, X.3    Stahl, P.D.4
  • 130
    • 58449097407 scopus 로고    scopus 로고
    • Liver transcriptome profiles associated with strain-specific Ehrlichia chaffeensis-induced hepatitis in SCID mice
    • 19001077
    • K.Miura, Y.Rikihisa. Liver transcriptome profiles associated with strain-specific Ehrlichia chaffeensis-induced hepatitis in SCID mice. Infect Immun 2009; 77:245–54; PMID:19001077; http://dx.doi.org/10.1128/IAI.00979-08
    • (2009) Infect Immun , vol.77 , pp. 245-254
    • Miura, K.1    Rikihisa, Y.2
  • 131
    • 33846911072 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli effector EspF interacts with host protein Abcf2
    • 17064289
    • J.P.Nougayrede, G.H.Foster, M.S.Donnenberg. Enteropathogenic Escherichia coli effector EspF interacts with host protein Abcf2. Cell Microbiol 2007; 9:680–93; PMID:17064289; http://dx.doi.org/10.1111/j.1462-5822.2006.00820.x
    • (2007) Cell Microbiol , vol.9 , pp. 680-693
    • Nougayrede, J.P.1    Foster, G.H.2    Donnenberg, M.S.3
  • 132
    • 71649087199 scopus 로고    scopus 로고
    • A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
    • 19898463
    • M.Hayashi-Nishino, N.Fujita, T.Noda, A.Yamaguchi, T.?Yoshimori, A.Yamamoto. A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat Cell Biol 2009; 11:1433–7; PMID:19898463; http://dx.doi.org/10.1038/ncb1991
    • (2009) Nat Cell Biol , vol.11 , pp. 1433-1437
    • Hayashi-Nishino, M.1    Fujita, N.2    Noda, T.3    Yamaguchi, A.4    Yoshimori, T.5    Yamamoto, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.