메뉴 건너뛰기




Volumn 2, Issue APR, 2011, Pages

Effector glycosyltransferases in Legionella

Author keywords

eEF1A; Glycosyltransferase; Legionella; Protein synthesis; Virulence factor

Indexed keywords


EID: 84055202984     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2011.00076     Document Type: Article
Times cited : (20)

References (92)
  • 1
    • 0030587932 scopus 로고    scopus 로고
    • An alpha to beta conformational switch in EF-Tu
    • Abel, K., Yoder, M. D., Hilgenfeld, R., and Jurnak, F. (1996). An alpha to beta conformational switch in EF-Tu. Structure 4, 1153-1159.
    • (1996) Structure , vol.4 , pp. 1153-1159
    • Abel, K.1    Yoder, M.D.2    Hilgenfeld, R.3    Jurnak, F.4
  • 3
    • 0033638335 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha
    • Andersen, G. R., Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T. G., Kjeldgaard, M., and Nyborg, J. (2000). Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Mol. Cell 6, 1261-1266.
    • (2000) Mol. Cell , vol.6 , pp. 1261-1266
    • Andersen, G.R.1    Pedersen, L.2    Valente, L.3    Chatterjee, I.4    Kinzy, T.G.5    Kjeldgaard, M.6    Nyborg, J.7
  • 4
    • 34247618762 scopus 로고    scopus 로고
    • Legionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein family
    • Banga, S., Gao, P., Shen, X., Fiscus, V., Zong, W. X., Chen, L., and Luo, Z. Q. (2007). Legionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein family. Proc. Natl. Acad. Sci. U.S.A. 104, 5121-5126.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5121-5126
    • Banga, S.1    Gao, P.2    Shen, X.3    Fiscus, V.4    Zong, W.X.5    Chen, L.6    Luo, Z.Q.7
  • 6
    • 0037222925 scopus 로고    scopus 로고
    • Purification and characterization of a UDP-glucosyltransferase produced by Legionella pneumophila
    • Belyi, I., Popoff, M. R., and Cianciotto, N. P. (2003). Purification and characterization of a UDP-glucosyltransferase produced by Legionella pneumophila. Infect. Immun. 71, 181-186.
    • (2003) Infect. Immun. , vol.71 , pp. 181-186
    • Belyi, I.1    Popoff, M.R.2    Cianciotto, N.P.3
  • 7
    • 77949284319 scopus 로고    scopus 로고
    • Bacterial toxin and effector glycosyltransferases
    • Belyi, Y., and Aktories, K. (2010). Bacterial toxin and effector glycosyltransferases. Biochim. Biophys. Acta 1800, 134-143.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 134-143
    • Belyi, Y.1    Aktories, K.2
  • 9
    • 67749124468 scopus 로고    scopus 로고
    • Region of elongation factor 1A1 involved in substrate recognition by Legionella pneumophila glucosyltransferase Lgt1: identification of Lgt1 as a retaining glucosyltransferase
    • Belyi, Y., Stahl, M., Sovkova, I., Kaden, P., Luy, B., and Aktories, K. (2009). Region of elongation factor 1A1 involved in substrate recognition by Legionella pneumophila glucosyltransferase Lgt1: identification of Lgt1 as a retaining glucosyltransferase. J. Biol. Chem. 284, 20167-20174.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20167-20174
    • Belyi, Y.1    Stahl, M.2    Sovkova, I.3    Kaden, P.4    Luy, B.5    Aktories, K.6
  • 10
    • 41949084350 scopus 로고    scopus 로고
    • Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila
    • Belyi, Y., Tabakova, I., Stahl, M., and Aktories, K. (2008). Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila. J. Bacteriol. 190, 3026-3035.
    • (2008) J. Bacteriol. , vol.190 , pp. 3026-3035
    • Belyi, Y.1    Tabakova, I.2    Stahl, M.3    Aktories, K.4
  • 14
    • 0031841662 scopus 로고    scopus 로고
    • Expression of Legionella pneumophila virulence traits in response to growth conditions
    • Byrne, B., and Swanson, M. S. (1998). Expression of Legionella pneumophila virulence traits in response to growth conditions. Infect. Immun. 66, 3029-3034.
    • (1998) Infect. Immun. , vol.66 , pp. 3029-3034
    • Byrne, B.1    Swanson, M.S.2
  • 16
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
    • Charnock, S. J., and Davies, G. J. (1999). Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry 38, 6380-6385.
    • (1999) Biochemistry , vol.38 , pp. 6380-6385
    • Charnock, S.J.1    Davies, G.J.2
  • 17
    • 70350461453 scopus 로고    scopus 로고
    • The purified and recombinant Legionella pneumophila chaperonin alters mitochondrial trafficking and microfilament organization
    • Chong, A., Lima, C. A., Allan, D. S., Nasrallah, G. K., and Garduno, R. A. (2009). The purified and recombinant Legionella pneumophila chaperonin alters mitochondrial trafficking and microfilament organization. Infect. Immun. 77, 4724-4739.
    • (2009) Infect. Immun. , vol.77 , pp. 4724-4739
    • Chong, A.1    Lima, C.A.2    Allan, D.S.3    Nasrallah, G.K.4    Garduno, R.A.5
  • 18
    • 11144342006 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A
    • Chuang, S. M., Chen, L., Lambertson, D., Anand, M., Kinzy, T. G., and Madura, K. (2005). Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol. Cell. Biol. 25, 403-413.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 403-413
    • Chuang, S.M.1    Chen, L.2    Lambertson, D.3    Anand, M.4    Kinzy, T.G.5    Madura, K.6
  • 19
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho, P. M., Deleury, E., Davies, G. J., and Henrissat, B. (2003). An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328, 307-317.
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 21
    • 50849115482 scopus 로고    scopus 로고
    • Legionella eukaryotic-like type IV substrates interfere with organelle trafficking
    • doi: 10.1371/journal.ppat.1000117
    • de Felipe, K. S., Glover, R. T., Charpentier, X., Anderson, O. R., Reyes, M., Pericone, C. D., and Shuman, H. A. (2008). Legionella eukaryotic-like type IV substrates interfere with organelle trafficking. PLoS Pathog. 4, e1000117. doi: 10.1371/journal.ppat.1000117
    • (2008) PLoS Pathog , vol.4
    • de Felipe, K.S.1    Glover, R.T.2    Charpentier, X.3    Anderson, O.R.4    Reyes, M.5    Pericone, C.D.6    Shuman, H.A.7
  • 22
    • 27744546297 scopus 로고    scopus 로고
    • Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer
    • de Felipe, K. S., Pampou, S., Jovanovic, O. S., Pericone, C. D., Ye, S. F., Kalachikov, S., and Shuman, H. A. (2005). Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer. J. Bacteriol. 187, 7716-7726.
    • (2005) J. Bacteriol. , vol.187 , pp. 7716-7726
    • de Felipe, K.S.1    Pampou, S.2    Jovanovic, O.S.3    Pericone, C.D.4    Ye, S.F.5    Kalachikov, S.6    Shuman, H.A.7
  • 23
    • 37149000256 scopus 로고    scopus 로고
    • Legionella spp. and Legionnaires' disease
    • Diederen, B. M. (2008). Legionella spp. and Legionnaires' disease. J. Infect. 56, 1-12.
    • (2008) J. Infect. , vol.56 , pp. 1-12
    • Diederen, B.M.1
  • 24
    • 33645277360 scopus 로고    scopus 로고
    • Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation
    • Doma, M. K., and Parker, R. (2006). Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 440, 561-564.
    • (2006) Nature , vol.440 , pp. 561-564
    • Doma, M.K.1    Parker, R.2
  • 25
    • 0036359281 scopus 로고    scopus 로고
    • Moonlighting functions of polypeptide elongation factor 1 from actin bundling to zinc finger protein R1-associated nuclear localization
    • Ejiri, S. (2002). Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization. Biosci. Biotechnol. Biochem. 66, 1-21.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1-21
    • Ejiri, S.1
  • 26
    • 59849094765 scopus 로고    scopus 로고
    • Legionella pneumophila Dot/ Icm translocated substrates: a sum of parts
    • Ensminger, A. W., and Isberg, R. R. (2009). Legionella pneumophila Dot/ Icm translocated substrates: a sum of parts. Curr. Opin. Microbiol. 12, 67-73.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 67-73
    • Ensminger, A.W.1    Isberg, R.R.2
  • 28
    • 70350716934 scopus 로고    scopus 로고
    • The perplexing functions and surprising origins of Legionella pneumophila type IV secretion effectors
    • Franco, I. S., Shuman, H. A., and Charpentier, X. (2009). The perplexing functions and surprising origins of Legionella pneumophila type IV secretion effectors. Cell. Microbiol. 11, 1435-1443.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1435-1443
    • Franco, I.S.1    Shuman, H.A.2    Charpentier, X.3
  • 29
    • 0035865381 scopus 로고    scopus 로고
    • Bovine alpha1 3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases
    • Gastinel, L. N., Bignon, C., Misra, A. K., Hindsgaul, O., Shaper, J. H., and Joziasse, D. H. (2001). Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases. EMBO J. 20, 638-649.
    • (2001) EMBO J , vol.20 , pp. 638-649
    • Gastinel, L.N.1    Bignon, C.2    Misra, A.K.3    Hindsgaul, O.4    Shaper, J.H.5    Joziasse, D.H.6
  • 30
    • 69549133937 scopus 로고    scopus 로고
    • A Legionella type IV effector activates the NF-kappaB pathway by phosphorylating the IkappaB family of inhibitors
    • Ge, J., Xu, H., Li, T., Zhou, Y., Zhang, Z., Li, S., Liu, L., and Shao, F. (2009). A Legionella type IV effector activates the NF-kappaB pathway by phosphorylating the IkappaB family of inhibitors. Proc. Natl. Acad. Sci. U.S.A. 106, 13725-13730.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13725-13730
    • Ge, J.1    Xu, H.2    Li, T.3    Zhou, Y.4    Zhang, Z.5    Li, S.6    Liu, L.7    Shao, F.8
  • 31
    • 0345826092 scopus 로고    scopus 로고
    • The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution
    • Gibson, R. P., Tarling, C. A., Roberts, S., Withers, S. G., and Davies, G. J. (2004). The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution. J. Biol. Chem. 279, 1950-1955.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1950-1955
    • Gibson, R.P.1    Tarling, C.A.2    Roberts, S.3    Withers, S.G.4    Davies, G.J.5
  • 32
    • 33745246850 scopus 로고    scopus 로고
    • X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues
    • Gordon, R. D., Sivarajah, P., Satkunarajah, M., Ma, D., Tarling, C. A., Vizitiu, D., Withers, S. G., and Rini, J. M. (2006). X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues. J. Mol. Biol. 360, 67-79.
    • (2006) J. Mol. Biol. , vol.360 , pp. 67-79
    • Gordon, R.D.1    Sivarajah, P.2    Satkunarajah, M.3    Ma, D.4    Tarling, C.A.5    Vizitiu, D.6    Withers, S.G.7    Rini, J.M.8
  • 33
    • 26944487335 scopus 로고    scopus 로고
    • Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology
    • Gross, S. R., and Kinzy, T. G. (2005). Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat. Struct. Mol. Biol. 12, 772-778.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 772-778
    • Gross, S.R.1    Kinzy, T.G.2
  • 34
    • 58349107899 scopus 로고    scopus 로고
    • Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways
    • Heidtman, M., Chen, E. J., Moy, M. Y., and Isberg, R. R. (2009). Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways. Cell. Microbiol. 11, 230-248.
    • (2009) Cell. Microbiol. , vol.11 , pp. 230-248
    • Heidtman, M.1    Chen, E.J.2    Moy, M.Y.3    Isberg, R.R.4
  • 35
    • 0021718023 scopus 로고
    • Legionella pneumophila inhibits acidification of its phagosome in human monocytes
    • Horwitz, M. A., and Maxfield, F. R. (1984). Legionella pneumophila inhibits acidification of its phagosome in human monocytes. J. Cell Biol. 99, 1936-1943.
    • (1984) J. Cell Biol. , vol.99 , pp. 1936-1943
    • Horwitz, M.A.1    Maxfield, F.R.2
  • 37
    • 78049370513 scopus 로고    scopus 로고
    • Modulation of host cell function by Legionella pneumophila type IV effectors
    • Hubber, A., and Roy, C. R. (2010). Modulation of host cell function by Legionella pneumophila type IV effectors. Annu. Rev. Cell Dev. Biol. 26, 261-283.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 261-283
    • Hubber, A.1    Roy, C.R.2
  • 39
    • 36249027095 scopus 로고    scopus 로고
    • Legionella pneumophila proteins that regulate Rab1 membrane cycling
    • Ingmundson, A., Delprato, A., Lambright, D. G., and Roy, C. R. (2007). Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450, 365-369.
    • (2007) Nature , vol.450 , pp. 365-369
    • Ingmundson, A.1    Delprato, A.2    Lambright, D.G.3    Roy, C.R.4
  • 40
    • 57649149094 scopus 로고    scopus 로고
    • The Legionella pneumophila replication vacuole: making a cosy niche inside host cells
    • Isberg, R. R., O'Connor, T. J., and Heidtman, M. (2009). The Legionella pneumophila replication vacuole: making a cosy niche inside host cells. Nat. Rev. Microbiol. 7, 13-24.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 13-24
    • Isberg, R.R.1    O'Connor, T.J.2    Heidtman, M.3
  • 41
    • 58349085112 scopus 로고    scopus 로고
    • Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system
    • Ivanov, S. S., and Roy, C. R. (2009). Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system. Cell. Microbiol. 11, 261-278.
    • (2009) Cell. Microbiol. , vol.11 , pp. 261-278
    • Ivanov, S.S.1    Roy, C.R.2
  • 42
    • 36849050145 scopus 로고    scopus 로고
    • Clostridium difficile glucosyltransferase toxin B - essential amino acids for substrate-binding
    • Jank, T., Giesemann, T., and Aktories, K. (2007). Clostridium difficile glucosyltransferase toxin B - essential amino acids for substrate-binding. J. Biol. Chem. 282, 35222-35231.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35222-35231
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 43
    • 44749094191 scopus 로고    scopus 로고
    • Inhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermine
    • Jank, T., Ziegler, M. O., Schulz, G. E., and Aktories, K. (2008). Inhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermine. FEBS Lett. 582, 2277-2282.
    • (2008) FEBS Lett , vol.582 , pp. 2277-2282
    • Jank, T.1    Ziegler, M.O.2    Schulz, G.E.3    Aktories, K.4
  • 44
    • 34249887901 scopus 로고    scopus 로고
    • Legionella pneumophila adaptation to intracellular life and the host response: clues from genomics and transcriptomics
    • Jules, M., and Buchrieser, C. (2007). Legionella pneumophila adaptation to intracellular life and the host response: clues from genomics and transcriptomics. FEBS Lett. 581, 2829-2838.
    • (2007) FEBS Lett , vol.581 , pp. 2829-2838
    • Jules, M.1    Buchrieser, C.2
  • 46
    • 59449087670 scopus 로고    scopus 로고
    • eEF1A is a novel component of the mammalian nuclear protein export machinery
    • Khacho, M., Mekhail, K., Pilon-Larose, K., Pause, A., Cote, J., and Lee, S. (2008). eEF1A is a novel component of the mammalian nuclear protein export machinery. Mol. Biol. Cell 19, 5296-5308.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5296-5308
    • Khacho, M.1    Mekhail, K.2    Pilon-Larose, K.3    Pause, A.4    Cote, J.5    Lee, S.6
  • 47
    • 0029958571 scopus 로고    scopus 로고
    • The GTP binding motif: variations on a theme
    • Kjeldgaard, M., Nyborg, J., and Clark, B. F. C. (1996). The GTP binding motif: variations on a theme. FASEB J. 10, 1347-1368.
    • (1996) FASEB J , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.C.3
  • 48
    • 75749083323 scopus 로고    scopus 로고
    • Virulence factors encoded by Legionella longbeachae identified on the basis of the genome sequence analysis of clinical isolate D-4968
    • Kozak, N. A., Buss, M., Lucas, C. E., Frace, M., Govil, D., Travis, T., Olsen-Rasmussen, M., Benson, R. F., and Fields, B. S. (2010). Virulence factors encoded by Legionella longbeachae identified on the basis of the genome sequence analysis of clinical isolate D-4968. J. Bacteriol. 192, 1030-1044.
    • (2010) J. Bacteriol. , vol.192 , pp. 1030-1044
    • Kozak, N.A.1    Buss, M.2    Lucas, C.E.3    Frace, M.4    Govil, D.5    Travis, T.6    Olsen-Rasmussen, M.7    Benson, R.F.8    Fields, B.S.9
  • 49
    • 39849096721 scopus 로고    scopus 로고
    • Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions
    • Kubori, T., Hyakutake, A., and Nagai, H. (2008). Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions. Mol. Microbiol. 67, 1307-1319.
    • (2008) Mol. Microbiol. , vol.67 , pp. 1307-1319
    • Kubori, T.1    Hyakutake, A.2    Nagai, H.3
  • 50
    • 33646795021 scopus 로고    scopus 로고
    • Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)
    • Kubota, T., Shiba, T., Sugioka, S., Furukawa, S., Sawaki, H., Kato, R., Wakatsuki, S., and Narimatsu, H. (2006). Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J. Mol. Biol. 359, 708-727.
    • (2006) J. Mol. Biol. , vol.359 , pp. 708-727
    • Kubota, T.1    Shiba, T.2    Sugioka, S.3    Furukawa, S.4    Sawaki, H.5    Kato, R.6    Wakatsuki, S.7    Narimatsu, H.8
  • 51
    • 33845511552 scopus 로고    scopus 로고
    • A Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell death
    • Laguna, R. K., Creasey, E. A., Li, Z., Valtz, N., and Isberg, R. R. (2006). A Legionella pneumophila-translocated substrate that is required for growth within macrophages and protection from host cell death. Proc. Natl. Acad. Sci. U.S.A. 103, 18745-18750.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18745-18750
    • Laguna, R.K.1    Creasey, E.A.2    Li, Z.3    Valtz, N.4    Isberg, R.R.5
  • 52
    • 3142615417 scopus 로고    scopus 로고
    • Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue
    • Lairson, L. L., Chiu, C. P., Ly, H. D., He, S., Wakarchuk, W. W., Strynadka, N. C., and Withers, S. G. (2004). Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue. J. Biol. Chem. 279, 28339-28344.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28339-28344
    • Lairson, L.L.1    Chiu, C.P.2    Ly, H.D.3    He, S.4    Wakarchuk, W.W.5    Strynadka, N.C.6    Withers, S.G.7
  • 56
    • 77957137443 scopus 로고    scopus 로고
    • LnaB: a Legionella pneumophila activator of NF-kappaB
    • Losick, V. P., Haenssler, E., Moy, M. Y., and Isberg, R. R. (2010). LnaB: a Legionella pneumophila activator of NF-kappaB. Cell. Microbiol. 12, 1083-1097.
    • (2010) Cell. Microbiol. , vol.12 , pp. 1083-1097
    • Losick, V.P.1    Haenssler, E.2    Moy, M.Y.3    Isberg, R.R.4
  • 58
    • 84889234826 scopus 로고    scopus 로고
    • Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila
    • Machner, M. P., and Isberg, R. R. (2006). Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev. Cell 11, 47-56.
    • (2006) Dev. Cell , vol.11 , pp. 47-56
    • Machner, M.P.1    Isberg, R.R.2
  • 59
    • 84889234796 scopus 로고    scopus 로고
    • A bifunctional bacterial protein links GDI displacement to Rab1 activation
    • Machner, M. P., and Isberg, R. R. (2007). A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318, 974-977.
    • (2007) Science , vol.318 , pp. 974-977
    • Machner, M.P.1    Isberg, R.R.2
  • 60
    • 77954377942 scopus 로고    scopus 로고
    • eEF1A: thinking outside the ribosome
    • Mateyak, M. K., and Kinzy, T. G. (2010). eEF1A: thinking outside the ribosome. J. Biol. Chem. 285, 21209-21213.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21209-21213
    • Mateyak, M.K.1    Kinzy, T.G.2
  • 61
    • 1642317212 scopus 로고    scopus 로고
    • eEF1A binding to aminoacylated viral RNA represses minus strand synthesis by TYMV RNA-dependent RNA polymerase
    • Matsuda, D., Yoshinari, S., and Dreher, T. W. (2004). eEF1A binding to aminoacylated viral RNA represses minus strand synthesis by TYMV RNA-dependent RNA polymerase. Virology 321, 47-56.
    • (2004) Virology , vol.321 , pp. 47-56
    • Matsuda, D.1    Yoshinari, S.2    Dreher, T.W.3
  • 62
    • 9644272497 scopus 로고    scopus 로고
    • A phosphatidylserine-binding site in the cytosolic fragment of Clostridium sordellii lethal toxin facilitates glucosylation of membrane-bound Rac and is required for cytotoxicity
    • Mesmin, B., Robbe, K., Geny, B., Luton, F., Brandolin, G., Popoff, M. R., and Antonny, B. (2004). A phosphatidylserine-binding site in the cytosolic fragment of Clostridium sordellii lethal toxin facilitates glucosylation of membrane-bound Rac and is required for cytotoxicity. J. Biol. Chem. 279, 49876-49882.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49876-49882
    • Mesmin, B.1    Robbe, K.2    Geny, B.3    Luton, F.4    Brandolin, G.5    Popoff, M.R.6    Antonny, B.7
  • 63
    • 77950421915 scopus 로고    scopus 로고
    • Genome analysis of microorganisms living in amoebae reveals a melting pot of evolution
    • Moliner, C., Fournier, P. E., and Raoult, D. (2010). Genome analysis of microorganisms living in amoebae reveals a melting pot of evolution. FEMS Microbiol. Rev. 34, 281-294.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 281-294
    • Moliner, C.1    Fournier, P.E.2    Raoult, D.3
  • 64
    • 0030843867 scopus 로고    scopus 로고
    • Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme
    • Mosi, R., He, S., Uitdehaag, J., Dijkstra, B. W., and Withers, S. G. (1997). Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme. Biochemistry 36, 9927-9934.
    • (1997) Biochemistry , vol.36 , pp. 9927-9934
    • Mosi, R.1    He, S.2    Uitdehaag, J.3    Dijkstra, B.W.4    Withers, S.G.5
  • 65
    • 0037108389 scopus 로고    scopus 로고
    • Infection due to Legionella species other than L. pneumophila
    • Muder, R. R., and Yu, V. L. (2002). Infection due to Legionella species other than L. pneumophila. Clin. Infect. Dis. 35, 990-998.
    • (2002) Clin. Infect. Dis. , vol.35 , pp. 990-998
    • Muder, R.R.1    Yu, V.L.2
  • 66
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • Muller, M. P., Peters, H., Blumer, J., Blankenfeldt, W., Goody, R. S., and Itzen, A. (2010). The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329, 946-949.
    • (2010) Science , vol.329 , pp. 946-949
    • Muller, M.P.1    Peters, H.2    Blumer, J.3    Blankenfeldt, W.4    Goody, R.S.5    Itzen, A.6
  • 67
    • 33748172869 scopus 로고    scopus 로고
    • The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor
    • Murata, T., Delprato, A., Ingmundson, A., Toomre, D. K., Lambright, D. G., and Roy, C. R. (2006). The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nat. Cell Biol. 8, 971-977.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 971-977
    • Murata, T.1    Delprato, A.2    Ingmundson, A.3    Toomre, D.K.4    Lambright, D.G.5    Roy, C.R.6
  • 68
    • 0037169078 scopus 로고    scopus 로고
    • A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes
    • Nagai, H., Kagan, J. C., Zhu, X., Kahn, R. A., and Roy, C. R. (2002). A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science 295, 679-682.
    • (2002) Science , vol.295 , pp. 679-682
    • Nagai, H.1    Kagan, J.C.2    Zhu, X.3    Kahn, R.A.4    Roy, C.R.5
  • 69
    • 0037418741 scopus 로고    scopus 로고
    • Glucosaminylglycan biosynthesis: what we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2
    • Negishi, M., Dong, J., Darden, T. A., Pedersen, L. G., and Pedersen, L. C. (2003). Glucosaminylglycan biosynthesis: what we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2. Biochem. Biophys. Res. Commun. 303, 393-398.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 393-398
    • Negishi, M.1    Dong, J.2    Darden, T.A.3    Pedersen, L.G.4    Pedersen, L.C.5
  • 70
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • Nelson, R. J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M., and Craig, E. A. (1992). The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71, 97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 71
    • 34547217380 scopus 로고    scopus 로고
    • Effector proteins translocated by Legionella pneumophila: strength in numbers
    • Ninio, S., and Roy, C. R. (2007). Effector proteins translocated by Legionella pneumophila: strength in numbers. Trends Microbiol. 15, 372-380.
    • (2007) Trends Microbiol , vol.15 , pp. 372-380
    • Ninio, S.1    Roy, C.R.2
  • 72
    • 0032496097 scopus 로고    scopus 로고
    • Interactions between bacterial toxins and intestinal cells
    • Popoff, M. R. (1998). Interactions between bacterial toxins and intestinal cells. Toxicon 36, 665-685.
    • (1998) Toxicon , vol.36 , pp. 665-685
    • Popoff, M.R.1
  • 73
    • 77951220224 scopus 로고    scopus 로고
    • Indispensable role for the eukaryotic-like ankyrin domains of the ankyrin B effector of Legionella pneumophila within macrophages and amoebae
    • Price, C. T., Al-Khodor, S., Al-Quadan, T., and Abu, K. Y. (2010). Indispensable role for the eukaryotic-like ankyrin domains of the ankyrin B effector of Legionella pneumophila within macrophages and amoebae. Infect. Immun. 78, 2079-2088.
    • (2010) Infect. Immun. , vol.78 , pp. 2079-2088
    • Price, C.T.1    Al-Khodor, S.2    Al-Quadan, T.3    Abu, K.Y.4
  • 74
    • 74549200971 scopus 로고    scopus 로고
    • Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa
    • doi: 10.1371/journal. ppat.1000704
    • Price, C. T., Al-Khodor, S., Al-Quadan, T., Santic, M., Habyarimana, F., Kalia, A., and Kwaik, Y. A. (2009). Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa. PLoS Pathog. 5, e1000704. doi: 10.1371/journal. ppat.1000704
    • (2009) PLoS Pathog , vol.5
    • Price, C.T.1    Al-Khodor, S.2    Al-Quadan, T.3    Santic, M.4    Habyarimana, F.5    Kalia, A.6    Kwaik, Y.A.7
  • 75
    • 11844280851 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in glycosyltransferases
    • Qasba, P. K., Ramakrishnan, B., and Boeggeman, E. (2005). Substrate-induced conformational changes in glycosyltransferases. Trends Biochem. Sci. 30, 53-62.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 53-62
    • Qasba, P.K.1    Ramakrishnan, B.2    Boeggeman, E.3
  • 76
    • 33645063702 scopus 로고    scopus 로고
    • Structural snapshots of beta-1 4-galactosyltransferase-I along the kinetic pathway
    • Ramakrishnan, B., Ramasamy, V., and Qasba, P. K. (2006). Structural snapshots of beta-1,4-galactosyltransferase-I along the kinetic pathway. J. Mol. Biol. 357, 1619-1633.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1619-1633
    • Ramakrishnan, B.1    Ramasamy, V.2    Qasba, P.K.3
  • 77
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V. (2002). Ribosome structure and the mechanism of translation. Cell 108, 557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 78
    • 0037085362 scopus 로고    scopus 로고
    • Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis
    • Ruest, L. B., Marcotte, R., and Wang, E. (2002). Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis. J. Biol. Chem. 277, 5418-5425.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5418-5425
    • Ruest, L.B.1    Marcotte, R.2    Wang, E.3
  • 79
    • 0025989349 scopus 로고
    • Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability
    • Sarge, K. D., Zimarino, V., Holm, K., Wu, C., and Morimoto, R. I. (1991). Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability. Genes Dev. 5, 1902-1911.
    • (1991) Genes Dev , vol.5 , pp. 1902-1911
    • Sarge, K.D.1    Zimarino, V.2    Holm, K.3    Wu, C.4    Morimoto, R.I.5
  • 80
  • 81
    • 65549084822 scopus 로고    scopus 로고
    • Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response
    • Shen, X., Banga, S., Liu, Y., Xu, L., Gao, P., Shamovsky, I., Nudler, E., and Luo, Z. Q. (2009). Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response. Cell. Microbiol. 11, 911-926.
    • (2009) Cell. Microbiol. , vol.11 , pp. 911-926
    • Shen, X.1    Banga, S.2    Liu, Y.3    Xu, L.4    Gao, P.5    Shamovsky, I.6    Nudler, E.7    Luo, Z.Q.8
  • 82
    • 77957935294 scopus 로고    scopus 로고
    • Dom34: Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay
    • Shoemaker, C. J., Eyler, D. E., and Green, R. (2010). Dom34: Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 330, 369-372.
    • (2010) Science , vol.330 , pp. 369-372
    • Shoemaker, C.J.1    Eyler, D.E.2    Green, R.3
  • 83
    • 79953884100 scopus 로고    scopus 로고
    • Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases
    • Soya, N., Fang, Y., Palcic, M. M., and Klassen, J. S. (2011). Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases. Glycobiology 21, 547-552.
    • (2011) Glycobiology , vol.21 , pp. 547-552
    • Soya, N.1    Fang, Y.2    Palcic, M.M.3    Klassen, J.S.4
  • 84
    • 4544226530 scopus 로고    scopus 로고
    • Mutation of toxB and a truncated version of the efa-1 gene in Escherichia coli O157: H7 influences the expression and secretion of locus of enterocyte effacement-encoded proteins but not intestinal colonization in calves or sheep
    • Stevens, M. P., Roe, A. J., Vlisidou, I., van Diemen, P. M., La Ragione, R. M., Best, A., Woodward, M. J., Gally, D. L., and Wallis, T. S. (2004). Mutation of toxB and a truncated version of the efa-1 gene in Escherichia coli O157: H7 influences the expression and secretion of locus of enterocyte effacement-encoded proteins but not intestinal colonization in calves or sheep. Infect. Immun. 72, 5402-5411.
    • (2004) Infect. Immun. , vol.72 , pp. 5402-5411
    • Stevens, M.P.1    Roe, A.J.2    Vlisidou, I.3    van Diemen, P.M.4    La Ragione, R.M.5    Best, A.6    Woodward, M.J.7    Gally, D.L.8    Wallis, T.S.9
  • 85
    • 79952117045 scopus 로고    scopus 로고
    • Actin re-organization induced by Chlamydia trachomatis serovar D-evidence for a critical role of the effector protein CT166 targeting Rac
    • doi: 10.1371/journal. pone.0009887
    • Thalmann, J., Janik, K., May, M., Sommer, K., Ebeling, J., Hofmann, F., Genth, H., and Klos, A. (2010). Actin re-organization induced by Chlamydia trachomatis serovar D-evidence for a critical role of the effector protein CT166 targeting Rac. PLoS ONE 5, e9887. doi: 10.1371/journal. pone.0009887
    • (2010) PLoS ONE , vol.5
    • Thalmann, J.1    Janik, K.2    May, M.3    Sommer, K.4    Ebeling, J.5    Hofmann, F.6    Genth, H.7    Klos, A.8
  • 86
    • 0032964202 scopus 로고    scopus 로고
    • X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family
    • Uitdehaag, J. C., Mosi, R., Kalk, K. H., van, D. V, Dijkhuizen, L., Withers, S. G., and Dijkstra, B. W. (1999). X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family. Nat. Struct. Biol. 6, 432-436.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 432-436
    • Uitdehaag, J.C.1    Mosi, R.2    Kalk, K.H.3    van, D.V.4    Dijkhuizen, L.5    Withers, S.G.6    Dijkstra, B.W.7
  • 87
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R., and Wittinghofer, A. (2001). The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 88
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo, D. J., Davies, G. J., Laine, R., and Withers, S. G. (2001). Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412, 835-838.
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 89
    • 77950378868 scopus 로고    scopus 로고
    • Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector
    • doi: 10.1371/journal. ppat.1000822
    • Xu, L., Shen, X., Bryan, A., Banga, S., Swanson, M. S., and Luo, Z. Q. (2010). Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector. PLoS Pathog. 6, e1000822. doi: 10.1371/journal. ppat.1000822
    • (2010) PLoS Pathog , vol.6
    • Xu, L.1    Shen, X.2    Bryan, A.3    Banga, S.4    Swanson, M.S.5    Luo, Z.Q.6
  • 90
    • 0036642514 scopus 로고    scopus 로고
    • Distribution of Legionella species and serogroups isolated by culture in patients with sporadic community-acquired legionellosis: an international collaborative survey
    • Yu, V. L., Plouffe, J. F., Pastoris, M. C., Stout, J. E., Schousboe, M., Widmer, A., Summersgill, J., File, T., Heath, C. M., Paterson, D. L., and Chereshsky, A. (2002). Distribution of Legionella species and serogroups isolated by culture in patients with sporadic community-acquired legionellosis: an international collaborative survey. J. Infect. Dis. 186, 127-128.
    • (2002) J. Infect. Dis. , vol.186 , pp. 127-128
    • Yu, V.L.1    Plouffe, J.F.2    Pastoris, M.C.3    Stout, J.E.4    Schousboe, M.5    Widmer, A.6    Summersgill, J.7    File, T.8    Heath, C.M.9    Paterson, D.L.10    Chereshsky, A.11
  • 91
    • 40849117983 scopus 로고    scopus 로고
    • Conformational changes and reaction of clostridial glycosylating toxins
    • Ziegler, M. O., Jank, T., Aktories, K., and Schulz, G. E. (2008). Conformational changes and reaction of clostridial glycosylating toxins. J. Mol. Biol. 377, 1346-1356.
    • (2008) J. Mol. Biol. , vol.377 , pp. 1346-1356
    • Ziegler, M.O.1    Jank, T.2    Aktories, K.3    Schulz, G.E.4
  • 92
    • 33846988979 scopus 로고    scopus 로고
    • The response regulator PmrA is a major regulator of the icm/dot type IV secretion system in Legionella pneumophila and Coxiella burnetii
    • Zusman, T., Aloni, G., Halperin, E., Kotzer, H., Degtyar, E., Feldman, M., and Segal, G. (2007). The response regulator PmrA is a major regulator of the icm/dot type IV secretion system in Legionella pneumophila and Coxiella burnetii. Mol. Microbiol. 63, 1508-1523.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1508-1523
    • Zusman, T.1    Aloni, G.2    Halperin, E.3    Kotzer, H.4    Degtyar, E.5    Feldman, M.6    Segal, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.