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Volumn 472, Issue 1, 2015, Pages 83-95

Global translation variations in host cells upon attack of lytic and sublytic Staphylococcus aureus α-haemolysin1

Author keywords

Bacterial toxins; HuR; Polysomal profiling; Pore forming toxins; RNA binding protein; Transcriptome; Translational control; Translatome

Indexed keywords

ALPHA HEMOLYSIN; MESSENGER RNA; RNA BINDING PROTEIN; TRANSCRIPTOME; UNTRANSLATED RNA; BACTERIAL TOXIN; ELAV LIKE PROTEIN 1; ELAVL1 PROTEIN, HUMAN; HEMOLYSIN; STAPHYLOCOCCAL ALPHA-TOXIN;

EID: 84945924164     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150284     Document Type: Article
Times cited : (3)

References (90)
  • 1
    • 27944495724 scopus 로고    scopus 로고
    • Virulence determinants in Staphylococcus aureus and their involvement in clinical syndromes
    • CrossRef PubMed
    • Ferry, T., Perpoint, T., Vandenesch, F. and Etienne, J. (2005) Virulence determinants in Staphylococcus aureus and their involvement in clinical syndromes. Curr. Infect. Dis. Rep. 7, 420-428 CrossRef PubMed
    • (2005) Curr. Infect. Dis. Rep. , vol.7 , pp. 420-428
    • Ferry, T.1    Perpoint, T.2    Vandenesch, F.3    Etienne, J.4
  • 2
    • 60549112375 scopus 로고    scopus 로고
    • Staphylococcus aureus and squamous cell carcinoma of the skin
    • CrossRef PubMed
    • Kullander, J., Forslund, O. and Dillner, J. (2009) Staphylococcus aureus and squamous cell carcinoma of the skin. Cancer Epidemiol. Biomarkers Prev. 18, 472-478 CrossRef PubMed
    • (2009) Cancer Epidemiol. Biomarkers Prev. , vol.18 , pp. 472-478
    • Kullander, J.1    Forslund, O.2    Dillner, J.3
  • 3
    • 45449117125 scopus 로고    scopus 로고
    • Pore formation: An ancient yet complex form of attack
    • CrossRef PubMed
    • Iacovache, I., van der Goot, F.G. and Pernot, L. (2008) Pore formation: an ancient yet complex form of attack. Biochim. Biophys. Acta 1778, 1611-1623 CrossRef PubMed
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1611-1623
    • Iacovache, I.1    Van Der Goot, F.G.2    Pernot, L.3
  • 5
    • 84856910671 scopus 로고    scopus 로고
    • Staphylococcus aureus a-hemolysin mediates virulence in a murine model of severe pneumonia through activation of the NLRP3 inflammasome
    • CrossRef PubMed
    • Kebaier, C., Chamberland, R.R., Allen, I.C., Gao, X., Broglie, P.M., Hall, J.D., Jania, C., Doerschuk, C.M., Tilley, S.L. and Duncan, J.A. (2012) Staphylococcus aureus a-hemolysin mediates virulence in a murine model of severe pneumonia through activation of the NLRP3 inflammasome. J. Infect. Dis. 205, 807-817 CrossRef PubMed
    • (2012) J. Infect. Dis. , vol.205 , pp. 807-817
    • Kebaier, C.1    Chamberland, R.R.2    Allen, I.C.3    Gao, X.4    Broglie, P.M.5    Hall, J.D.6    Jania, C.7    Doerschuk, C.M.8    Tilley, S.L.9    Duncan, J.A.10
  • 7
    • 81155159184 scopus 로고    scopus 로고
    • Staphylococcal a-toxin induces a higher T cell proliferation and interleukin-31 in atopic dermatitis
    • CrossRef PubMed
    • Niebuhr, M., Mamerow, D., Heratizadeh, A., Satzger, I. and Werfel, T. (2011) Staphylococcal a-toxin induces a higher T cell proliferation and interleukin-31 in atopic dermatitis. Int. Arch. Allergy Immunol. 156, 412-425 CrossRef PubMed
    • (2011) Int. Arch. Allergy Immunol. , vol.156 , pp. 412-425
    • Niebuhr, M.1    Mamerow, D.2    Heratizadeh, A.3    Satzger, I.4    Werfel, T.5
  • 8
    • 84855998874 scopus 로고    scopus 로고
    • The UPEC pore-forming toxin a-hemolysin triggers proteolysis of host proteins to disrupt cell adhesion, inflammatory, and survival pathways
    • CrossRef PubMed
    • Dhakal, B.K. and Mulvey, M.A. (2012) The UPEC pore-forming toxin a-hemolysin triggers proteolysis of host proteins to disrupt cell adhesion, inflammatory, and survival pathways. Cell Host Microbe 11, 58-69 CrossRef PubMed
    • (2012) Cell Host Microbe , vol.11 , pp. 58-69
    • Dhakal, B.K.1    Mulvey, M.A.2
  • 9
    • 84863922855 scopus 로고    scopus 로고
    • ADAM10 mediates vascular injury induced by Staphylococcus aureus a-hemolysin
    • CrossRef PubMed
    • Powers, M.E., Kim, H.K., Wang, Y. and Bubeck Wardenburg, J. (2012) ADAM10 mediates vascular injury induced by Staphylococcus aureus a-hemolysin. J. Infect. Dis. 206, 352-356 CrossRef PubMed
    • (2012) J. Infect. Dis. , vol.206 , pp. 352-356
    • Powers, M.E.1    Kim, H.K.2    Wang, Y.3    Bubeck Wardenburg, J.4
  • 10
    • 0029556445 scopus 로고
    • Bacterial hemolysins and leukotoxins affect target cells by forming large exogenous pores into their plasma membrane: Escherichia coli hemolysin a as a case example
    • CrossRef PubMed
    • Menestrina, G., Dalla Serra, M., Pederzolli, C., Bregante, M. and Gambale, F. (1995) Bacterial hemolysins and leukotoxins affect target cells by forming large exogenous pores into their plasma membrane: Escherichia coli hemolysin a as a case example. Biosci. Rep. 15, 543-551 CrossRef PubMed
    • (1995) Biosci. Rep. , vol.15 , pp. 543-551
    • Menestrina, G.1    Dalla Serra, M.2    Pederzolli, C.3    Bregante, M.4    Gambale, F.5
  • 11
    • 33846829776 scopus 로고    scopus 로고
    • Pore-forming toxins and cellular non-immune defenses (CNIDs)
    • CrossRef PubMed
    • Aroian, R. and van der Goot, F.G. (2007) Pore-forming toxins and cellular non-immune defenses (CNIDs). Curr. Opin. Microbiol. 10, 57-61 CrossRef PubMed
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 57-61
    • Aroian, R.1    Van Der Goot, F.G.2
  • 12
    • 0035853082 scopus 로고    scopus 로고
    • Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O
    • CrossRef PubMed
    • Walev, I., Bhakdi, S.C., Hofmann, F., Djonder, N., Valeva, A., Aktories, K. and Bhakdi, S. (2001) Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O. Proc. Natl. Acad. Sci. U.S.A. 98, 3185-3190 CrossRef PubMed
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3185-3190
    • Walev, I.1    Bhakdi, S.C.2    Hofmann, F.3    Djonder, N.4    Valeva, A.5    Aktories, K.6    Bhakdi, S.7
  • 13
    • 79951622570 scopus 로고    scopus 로고
    • RAB-5-and RAB-11-dependent vesicle-trafficking pathways are required for plasma membrane repair after attack by bacterial pore-forming toxin
    • CrossRef PubMed
    • Los, F.C. O., Kao, C.-Y., Smitham, J., McDonald, K.L., Ha, C., Peixoto, C.A. and Aroian, R.V. (2011) RAB-5-and RAB-11-dependent vesicle-trafficking pathways are required for plasma membrane repair after attack by bacterial pore-forming toxin. Cell Host Microbe 9, 147-157 CrossRef PubMed
    • (2011) Cell Host Microbe , vol.9 , pp. 147-157
    • Los, F.C.O.1    Kao, C.-Y.2    Smitham, J.3    McDonald, K.L.4    Ha, C.5    Peixoto, C.A.6    Aroian, R.V.7
  • 15
    • 44949119547 scopus 로고    scopus 로고
    • Inactivation of host Akt/protein kinase B signaling by bacterial pore-forming toxins
    • CrossRef PubMed
    • Wiles, T.J., Dhakal, B.K., Eto, D.S. and Mulvey, M.A. (2008) Inactivation of host Akt/protein kinase B signaling by bacterial pore-forming toxins. Mol. Biol. Cell 19, 1427-1438 CrossRef PubMed
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1427-1438
    • Wiles, T.J.1    Dhakal, B.K.2    Eto, D.S.3    Mulvey, M.A.4
  • 20
    • 33646166722 scopus 로고    scopus 로고
    • Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. Aureus alpha-toxin or streptolysin O. Biochem
    • CrossRef PubMed
    • Husmann, M., Dersch, K., Bobkiewicz, W., Beckmann, E., Veerachato, G. and Bhakdi, S. (2006) Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O. Biochem. Biophys. Res. Commun. 344, 1128-1134 CrossRef PubMed
    • (2006) Biophys. Res. Commun. , vol.344 , pp. 1128-1134
    • Husmann, M.1    Dersch, K.2    Bobkiewicz, W.3    Beckmann, E.4    Veerachato, G.5    Bhakdi, S.6
  • 21
    • 84865188660 scopus 로고    scopus 로고
    • Infection-induced host translational blockage inhibits immune responses and epithelial renewal in the Drosophila gut
    • CrossRef PubMed
    • Chakrabarti, S., Liehl, P., Buchon, N. and Lemaitre, B. (2012) Infection-induced host translational blockage inhibits immune responses and epithelial renewal in the Drosophila gut. Cell Host Microbe 12, 60-70 CrossRef PubMed
    • (2012) Cell Host Microbe , vol.12 , pp. 60-70
    • Chakrabarti, S.1    Liehl, P.2    Buchon, N.3    Lemaitre, B.4
  • 22
    • 84866418820 scopus 로고    scopus 로고
    • Pathogenic pore-forming proteins: Function and host response
    • CrossRef PubMed
    • Bischofberger, M., Iacovache, I. and van der Goot, F.G. (2012) Pathogenic pore-forming proteins: function and host response. Cell Host Microbe 12, 266-275 CrossRef PubMed
    • (2012) Cell Host Microbe , vol.12 , pp. 266-275
    • Bischofberger, M.1    Iacovache, I.2    Van Der Goot, F.G.3
  • 24
    • 0035085993 scopus 로고    scopus 로고
    • Subcytocidal attack by staphylococcal alpha-toxin activates NF-kappaB and induces interleukin-8 production
    • CrossRef PubMed
    • Dragneva, Y., Anuradha, C.D., Valeva, A., Hoffmann, A., Bhakdi, S. and Husmann, M. (2001) Subcytocidal attack by staphylococcal alpha-toxin activates NF-kappaB and induces interleukin-8 production. Infect. Immun. 69, 2630-2635 CrossRef PubMed
    • (2001) Infect. Immun. , vol.69 , pp. 2630-2635
    • Dragneva, Y.1    Anuradha, C.D.2    Valeva, A.3    Hoffmann, A.4    Bhakdi, S.5    Husmann, M.6
  • 26
    • 48849105158 scopus 로고    scopus 로고
    • Histone modifications and chromatin remodeling during bacterial infections
    • CrossRef PubMed
    • Hamon, M.A. and Cossart, P. (2008) Histone modifications and chromatin remodeling during bacterial infections. Cell Host Microbe. 4, 100-109 CrossRef PubMed
    • (2008) Cell Host Microbe. , vol.4 , pp. 100-109
    • Hamon, M.A.1    Cossart, P.2
  • 30
    • 84861798070 scopus 로고    scopus 로고
    • Widespread uncoupling between transcriptome and translatome variations after a stimulus in mammalian cells
    • CrossRef PubMed
    • Tebaldi, T., Re, A., Viero, G., Pegoretti, I., Passerini, A., Blanzieri, E. and Quattrone, A. (2012) Widespread uncoupling between transcriptome and translatome variations after a stimulus in mammalian cells. BMC Genomics 13, 220 CrossRef PubMed
    • (2012) BMC Genomics , vol.13 , pp. 220
    • Tebaldi, T.1    Re, A.2    Viero, G.3    Pegoretti, I.4    Passerini, A.5    Blanzieri, E.6    Quattrone, A.7
  • 31
    • 41349095905 scopus 로고    scopus 로고
    • Genome-wide identification and characterization of transcripts translationally regulated by bacterial lipopolysaccharide in macrophage-like J774.1 cells
    • CrossRef PubMed
    • Kitamura, H., Ito, M., Yuasa, T., Kikuguchi, C., Hijikata, A., Takayama, M., Kimura, Y., Yokoyama, R., Kaji, T. and Ohara, O. (2008) Genome-wide identification and characterization of transcripts translationally regulated by bacterial lipopolysaccharide in macrophage-like J774.1 cells. Physiol. Genomics 33, 121-132 CrossRef PubMed
    • (2008) Physiol. Genomics , vol.33 , pp. 121-132
    • Kitamura, H.1    Ito, M.2    Yuasa, T.3    Kikuguchi, C.4    Hijikata, A.5    Takayama, M.6    Kimura, Y.7    Yokoyama, R.8    Kaji, T.9    Ohara, O.10
  • 34
    • 0032508971 scopus 로고    scopus 로고
    • The interaction of Staphylococcus aureus bi-component gamma-hemolysins and leucocidins with cells and lipid membranes
    • CrossRef PubMed
    • Ferreras, M., Höper, F., Dalla Serra, M., Colin, D.A., Prévost, G. and Menestrina, G. (1998) The interaction of Staphylococcus aureus bi-component gamma-hemolysins and leucocidins with cells and lipid membranes. Biochim. Biophys. Acta 1414, 108-126 CrossRef PubMed
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 108-126
    • Ferreras, M.1    Höper, F.2    Dalla Serra, M.3    Colin, D.A.4    Prévost, G.5    Menestrina, G.6
  • 35
    • 77954602645 scopus 로고    scopus 로고
    • Analysis of single nucleic acid molecules with protein nanopores
    • CrossRef PubMed
    • Maglia, G., Heron, A.J., Stoddart, D., Japrung, D. and Bayley, H. (2010) Analysis of single nucleic acid molecules with protein nanopores. Methods Enzymol. 475, 591-623 CrossRef PubMed
    • (2010) Methods Enzymol. , vol.475 , pp. 591-623
    • Maglia, G.1    Heron, A.J.2    Stoddart, D.3    Japrung, D.4    Bayley, H.5
  • 36
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • PubMed
    • Pfaffl, M.W. (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29, e45 PubMed
    • (2001) Nucleic Acids Res. , vol.29 , pp. e45
    • Pfaffl, M.W.1
  • 37
    • 84892739582 scopus 로고    scopus 로고
    • TRanslatome: An R/Bioconductor package to portray translational control
    • CrossRef PubMed
    • Tebaldi, T., Dassi, E., Kostoska, G., Viero, G. and Quattrone, A. (2014) tRanslatome: an R/Bioconductor package to portray translational control. Bioinformatics 30, 289-291 CrossRef PubMed
    • (2014) Bioinformatics , vol.30 , pp. 289-291
    • Tebaldi, T.1    Dassi, E.2    Kostoska, G.3    Viero, G.4    Quattrone, A.5
  • 38
    • 67849130563 scopus 로고    scopus 로고
    • ToppGene Suite for gene list enrichment analysis and candidate gene prioritization
    • CrossRef PubMed
    • Chen, J., Bardes, E.E., Aronow, B.J. and Jegga, A.G. (2009) ToppGene Suite for gene list enrichment analysis and candidate gene prioritization. Nucleic Acids Res. 37, W305-W311 CrossRef PubMed
    • (2009) Nucleic Acids Res. , vol.37 , pp. W305-W311
    • Chen, J.1    Bardes, E.E.2    Aronow, B.J.3    Jegga, A.G.4
  • 40
    • 0030741317 scopus 로고    scopus 로고
    • The heptameric prepore of a staphylococcal alpha-hemolysin mutant in lipid bilayers imaged by atomic force microscopy
    • CrossRef PubMed
    • Fang, Y., Cheley, S., Bayley, H. and Yang, J. (1997) The heptameric prepore of a staphylococcal alpha-hemolysin mutant in lipid bilayers imaged by atomic force microscopy. Biochemistry 36, 9518-9522 CrossRef PubMed
    • (1997) Biochemistry , vol.36 , pp. 9518-9522
    • Fang, Y.1    Cheley, S.2    Bayley, H.3    Yang, J.4
  • 41
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers
    • CrossRef PubMed
    • Czajkowsky, D.M., Sheng, S. and Shao, Z. (1998) Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers. J. Mol. Biol. 276, 325-330 CrossRef PubMed
    • (1998) J. Mol. Biol. , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 42
    • 0024421764 scopus 로고
    • Release of interleukin-1 beta associated with potent cytocidal action of staphylococcal alpha-toxin on human monocytes
    • PubMed
    • Bhakdi, S., Muhly, M., Korom, S. and Hugo, F. (1989) Release of interleukin-1 beta associated with potent cytocidal action of staphylococcal alpha-toxin on human monocytes. Infect. Immun. 57, 3512-3519 PubMed
    • (1989) Infect. Immun. , vol.57 , pp. 3512-3519
    • Bhakdi, S.1    Muhly, M.2    Korom, S.3    Hugo, F.4
  • 43
    • 0042335651 scopus 로고    scopus 로고
    • Ion channels and bacterial infection: The case of beta-barrel pore-forming protein toxins of Staphylococcus aureus
    • CrossRef PubMed
    • Menestrina, G., Dalla Serra, M., Comai, M., Coraiola, M., Viero, G., Werner, S., Colin, D.A., Monteil, H. and Prévost, G. (2003) Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus. FEBS Lett. 552, 54-60 CrossRef PubMed
    • (2003) FEBS Lett. , vol.552 , pp. 54-60
    • Menestrina, G.1    Dalla Serra, M.2    Comai, M.3    Coraiola, M.4    Viero, G.5    Werner, S.6    Colin, D.A.7    Monteil, H.8    Prévost, G.9
  • 45
    • 0037407011 scopus 로고    scopus 로고
    • Arresting and releasing staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds
    • CrossRef PubMed
    • Kawate, T. and Gouaux, E. (2003) Arresting and releasing staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds. Protein Sci. 12, 997-1006 CrossRef PubMed
    • (2003) Protein Sci. , vol.12 , pp. 997-1006
    • Kawate, T.1    Gouaux, E.2
  • 46
    • 82955206472 scopus 로고    scopus 로고
    • Rapid assembly of a multimeric membrane protein pore
    • CrossRef PubMed
    • Thompson, J.R., Cronin, B., Bayley, H. and Wallace, M.I. (2011) Rapid assembly of a multimeric membrane protein pore. Biophys. J. 101, 2679-2683 CrossRef PubMed
    • (2011) Biophys. J. , vol.101 , pp. 2679-2683
    • Thompson, J.R.1    Cronin, B.2    Bayley, H.3    Wallace, M.I.4
  • 47
    • 0024399624 scopus 로고
    • Staphylococcal alpha-toxin increases the permeability of lipid vesicles by cholesterol-and pH-dependent assembly of oligomeric channels
    • CrossRef PubMed
    • Forti, S. and Menestrina, G. (1989) Staphylococcal alpha-toxin increases the permeability of lipid vesicles by cholesterol-and pH-dependent assembly of oligomeric channels. Eur. J. Biochem. 181, 767-773 CrossRef PubMed
    • (1989) Eur. J. Biochem. , vol.181 , pp. 767-773
    • Forti, S.1    Menestrina, G.2
  • 48
    • 33847298089 scopus 로고    scopus 로고
    • Cholesterol-dependent actin remodeling via RhoA and Rac1 activation by the Streptococcus pneumoniae toxin pneumolysin
    • CrossRef PubMed
    • Iliev, A.I., Djannatian, J.R., Nau, R., Mitchell, T.J. and Wouters, F.S. (2007) Cholesterol-dependent actin remodeling via RhoA and Rac1 activation by the Streptococcus pneumoniae toxin pneumolysin. Proc. Natl. Acad. Sci. U.S.A. 104, 2897-2902 CrossRef PubMed
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2897-2902
    • Iliev, A.I.1    Djannatian, J.R.2    Nau, R.3    Mitchell, T.J.4    Wouters, F.S.5
  • 49
    • 0028209773 scopus 로고
    • Sequestration of muscarinic cholinergic receptors in permeabilized neuroblastoma cells
    • CrossRef PubMed
    • Slowiejko, D.M., Levey, A.I. and Fisher, S.K. (1994) Sequestration of muscarinic cholinergic receptors in permeabilized neuroblastoma cells. J. Neurochem. 62, 1795-1803 CrossRef PubMed
    • (1994) J. Neurochem. , vol.62 , pp. 1795-1803
    • Slowiejko, D.M.1    Levey, A.I.2    Fisher, S.K.3
  • 50
    • 77955783248 scopus 로고    scopus 로고
    • Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus alpha-hemolysin-mediated cellular injury
    • CrossRef PubMed
    • Wilke, G.A. and Bubeck Wardenburg, J. (2010) Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus alpha-hemolysin-mediated cellular injury. Proc. Natl. Acad. Sci. U.S.A. 107, 13473-13478 CrossRef PubMed
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13473-13478
    • Wilke, G.A.1    Bubeck Wardenburg, J.2
  • 51
    • 70349295148 scopus 로고    scopus 로고
    • Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein
    • CrossRef PubMed
    • Harris, B., Pereira, I. and Parkin, E. (2009) Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein. Brain Res. 1296, 203-215 CrossRef PubMed
    • (2009) Brain Res. , vol.1296 , pp. 203-215
    • Harris, B.1    Pereira, I.2    Parkin, E.3
  • 52
    • 0037388094 scopus 로고    scopus 로고
    • Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae
    • CrossRef PubMed
    • Arava, Y., Wang, Y., Storey, J.D., Liu, C.L., Brown, P.O. and Herschlag, D. (2003) Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 100, 3889-3894 CrossRef PubMed
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3889-3894
    • Arava, Y.1    Wang, Y.2    Storey, J.D.3    Liu, C.L.4    Brown, P.O.5    Herschlag, D.6
  • 53
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • CrossRef PubMed
    • Sonenberg, N. and Hinnebusch, A.G. (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136, 731-745 CrossRef PubMed
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 54
    • 84868600748 scopus 로고    scopus 로고
    • Regulation of mRNA translation by signaling pathways
    • CrossRef PubMed
    • Roux, P.P. and Topisirovic, I. (2012) Regulation of mRNA translation by signaling pathways. Cold Spring Harb. Perspect. Biol. 4, a012252 CrossRef PubMed
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. a012252
    • Roux, P.P.1    Topisirovic, I.2
  • 55
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • CrossRef PubMed
    • Ma, X.M. and Blenis, J. (2009) Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. Mol. Cell Biol. 10, 307-318 CrossRef PubMed
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 57
    • 0023726116 scopus 로고
    • Identification of the 40 S ribosomal protein S6 phosphorylation sites induced by cycloheximide
    • PubMed
    • Krieg, J., Hofsteenge, J. and Thomas, G. (1988) Identification of the 40 S ribosomal protein S6 phosphorylation sites induced by cycloheximide. J. Biol. Chem. 263, 11473-11477 PubMed
    • (1988) J. Biol. Chem. , vol.263 , pp. 11473-11477
    • Krieg, J.1    Hofsteenge, J.2    Thomas, G.3
  • 59
    • 34249064912 scopus 로고    scopus 로고
    • Use of cyclodextrins to manipulate plasma membrane cholesterol content: Evidence, misconceptions and control strategies
    • CrossRef PubMed
    • Zidovetzki, R. and Levitan, I. (2007) Use of cyclodextrins to manipulate plasma membrane cholesterol content: evidence, misconceptions and control strategies. Biochim. Biophys. Acta 1768, 1311-1324 CrossRef PubMed
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1311-1324
    • Zidovetzki, R.1    Levitan, I.2
  • 60
    • 0028365388 scopus 로고
    • Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation
    • PubMed
    • Jursch, R., Hildebrand, A., Hobom, G., Tranum-Jensen, J., Ward, R., Kehoe, M. and Bhakdi, S. (1994) Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation. Infect. Immun. 62, 2249-2256 PubMed
    • (1994) Infect. Immun. , vol.62 , pp. 2249-2256
    • Jursch, R.1    Hildebrand, A.2    Hobom, G.3    Tranum-Jensen, J.4    Ward, R.5    Kehoe, M.6    Bhakdi, S.7
  • 61
    • 0029126941 scopus 로고
    • Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis
    • CrossRef PubMed
    • Panchal, R.G. and Bayley, H. (1995) Interactions between residues in staphylococcal alpha-hemolysin revealed by reversion mutagenesis. J. Biol. Chem. 270, 23072-23076 CrossRef PubMed
    • (1995) J. Biol. Chem. , vol.270 , pp. 23072-23076
    • Panchal, R.G.1    Bayley, H.2
  • 62
    • 67651240325 scopus 로고    scopus 로고
    • Membrane bound monomer of staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway
    • CrossRef PubMed
    • Srivastava, S.S., Pany, S., Sneh, A., Ahmed, N., Rahman, A. and Musti, K.V. (2009) Membrane bound monomer of staphylococcal alpha-hemolysin induces caspase activation and apoptotic cell death despite initiation of membrane repair pathway. PLoS One 4, e6293 CrossRef PubMed
    • (2009) PLoS One , vol.4
    • Srivastava, S.S.1    Pany, S.2    Sneh, A.3    Ahmed, N.4    Rahman, A.5    Musti, K.V.6
  • 63
    • 0035969249 scopus 로고    scopus 로고
    • Alpha-Toxin is a mediator of Staphylococcus aureus-induced cell death and activates caspases via the intrinsic death pathway independently of death receptor signaling
    • CrossRef PubMed
    • Bantel, H., Sinha, B., Domschke, W., Peters, G., Schulze-Osthoff, K. and Jänicke, R.U. (2001) alpha-Toxin is a mediator of Staphylococcus aureus-induced cell death and activates caspases via the intrinsic death pathway independently of death receptor signaling. J. Cell Biol. 155, 637-648 CrossRef PubMed
    • (2001) J. Cell Biol. , vol.155 , pp. 637-648
    • Bantel, H.1    Sinha, B.2    Domschke, W.3    Peters, G.4    Schulze-Osthoff, K.5    Jänicke, R.U.6
  • 64
    • 77955902024 scopus 로고    scopus 로고
    • The widespread regulation of microRNA biogenesis, function and decay
    • PubMed
    • Krol, J., Loedige, I. and Filipowicz, W. (2010) The widespread regulation of microRNA biogenesis, function and decay. Nat. Rev. Genet. 11, 597-610 PubMed
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 597-610
    • Krol, J.1    Loedige, I.2    Filipowicz, W.3
  • 65
    • 84872775027 scopus 로고    scopus 로고
    • Translational control by 3'-UTR-binding proteins
    • CrossRef PubMed
    • Szostak, E. and Gebauer, F. (2013) Translational control by 3'-UTR-binding proteins. Brief Funct. Genomics 12, 58-65 CrossRef PubMed
    • (2013) Brief Funct. Genomics , vol.12 , pp. 58-65
    • Szostak, E.1    Gebauer, F.2
  • 66
    • 74249123570 scopus 로고    scopus 로고
    • The miR-34 family in cancer and apoptosis
    • CrossRef PubMed
    • Hermeking, H. (2010) The miR-34 family in cancer and apoptosis. Cell Death Differ. 17, 193-199 CrossRef PubMed
    • (2010) Cell Death Differ. , vol.17 , pp. 193-199
    • Hermeking, H.1
  • 67
    • 68949161769 scopus 로고    scopus 로고
    • P38 Mitogen-activated protein kinase-and HuR-dependent stabilization of p21(Cip1) mRNA mediates the G(1)/S checkpoint
    • CrossRef PubMed
    • Lafarga, V., Cuadrado, A., Lopez de Silanes, I., Bengoechea, R., Fernandez-Capetillo, O. and Nebreda, A.R. (2009) p38 Mitogen-activated protein kinase-and HuR-dependent stabilization of p21(Cip1) mRNA mediates the G(1)/S checkpoint. Mol. Cell. Biol. 29, 4341-4351 CrossRef PubMed
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4341-4351
    • Lafarga, V.1    Cuadrado, A.2    Lopez De Silanes, I.3    Bengoechea, R.4    Fernandez-Capetillo, O.5    Nebreda, A.R.6
  • 68
    • 84884816943 scopus 로고    scopus 로고
    • ELAV proteins along evolution: Back to the nucleus?
    • CrossRef PubMed
    • Colombrita, C., Silani, V. and Ratti, A. (2013) ELAV proteins along evolution: back to the nucleus? Mol. Cell. Neurosci. 56, 447-455 CrossRef PubMed
    • (2013) Mol. Cell. Neurosci. , vol.56 , pp. 447-455
    • Colombrita, C.1    Silani, V.2    Ratti, A.3
  • 73
    • 0033056295 scopus 로고    scopus 로고
    • Proteasome activity is required for anthrax lethal toxin to kill macrophages
    • PubMed
    • Tang, G. and Leppla, S.H. (1999) Proteasome activity is required for anthrax lethal toxin to kill macrophages. Infect. Immun. 67, 3055-3060 PubMed
    • (1999) Infect. Immun. , vol.67 , pp. 3055-3060
    • Tang, G.1    Leppla, S.H.2
  • 74
    • 78249235456 scopus 로고    scopus 로고
    • In vivo accumulation of Helicobacter pylori products, NOD1, ubiquitinated proteins and proteasome in a novel cytoplasmic structure
    • CrossRef PubMed
    • Necchi, V., Sommi, P., Ricci, V. and Solcia, E. (2010) In vivo accumulation of Helicobacter pylori products, NOD1, ubiquitinated proteins and proteasome in a novel cytoplasmic structure. PLoS One 5, e9716 CrossRef PubMed
    • (2010) PLoS One , vol.5
    • Necchi, V.1    Sommi, P.2    Ricci, V.3    Solcia, E.4
  • 75
    • 1642564569 scopus 로고    scopus 로고
    • Regulation of p53 by Mdm2: Fate is in the numbers
    • CrossRef PubMed
    • Shmueli, A. and Oren, M. (2004) Regulation of p53 by Mdm2: fate is in the numbers. Mol. Cell 13, 4-5 CrossRef PubMed
    • (2004) Mol. Cell , vol.13 , pp. 4-5
    • Shmueli, A.1    Oren, M.2
  • 76
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • CrossRef PubMed
    • Minich, W.B., Balasta, M.L., Goss, D.J. and Rhoads, R.E. (1994) Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc. Natl. Acad. Sci. U.S.A. 91, 7668-7672 CrossRef PubMed
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 77
    • 0030454053 scopus 로고    scopus 로고
    • General RNA binding proteins render translation cap dependent
    • PubMed
    • Svitkin, Y.V, Ovchinnikov, L.P., Dreyfuss, G. and Sonenberg, N. (1996) General RNA binding proteins render translation cap dependent. EMBO J. 15, 7147-7155 PubMed
    • (1996) EMBO J. , vol.15 , pp. 7147-7155
    • Svitkin, Y.V.1    Ovchinnikov, L.P.2    Dreyfuss, G.3    Sonenberg, N.4
  • 79
    • 84928748405 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E confers resistance to cellular stress and DNA-damaging agents through an interaction with 4E-T: A rationale for novel therapeutic approaches
    • CrossRef PubMed
    • Martínez, A., Sesé, M., Losa, J.H., Robichaud, N., Sonenberg, N., Aasen, T., Ramón, Y. and Cajal, S. (2015) Phosphorylation of eIF4E confers resistance to cellular stress and DNA-damaging agents through an interaction with 4E-T: A rationale for novel therapeutic approaches. PLoS One 10, e0123352 CrossRef PubMed
    • (2015) PLoS One , vol.10
    • Martínez, A.1    Sesé, M.2    Losa, J.H.3    Robichaud, N.4    Sonenberg, N.5    Aasen, T.6    Ramón, Y.7    Cajal, S.8
  • 80
    • 84861177209 scopus 로고    scopus 로고
    • The Staphylococcus aureus alpha-toxin perturbs the barrier function in Caco-2 epithelial cell monolayers by altering junctional integrity
    • CrossRef PubMed
    • Kwak, Y.-K., Vikström, E., Magnusson, K.-E., Vécsey-Semjén, B., Colque-Navarro, P. and Möllby, R. (2012) The Staphylococcus aureus alpha-toxin perturbs the barrier function in Caco-2 epithelial cell monolayers by altering junctional integrity. Infect. Immun. 80, 1670-1680 CrossRef PubMed
    • (2012) Infect. Immun. , vol.80 , pp. 1670-1680
    • Kwak, Y.-K.1    Vikström, E.2    Magnusson, K.-E.3    Vécsey-Semjén, B.4    Colque-Navarro, P.5    Möllby, R.6
  • 81
    • 79960674990 scopus 로고    scopus 로고
    • Unsaturated fatty acids drive disintegrin and metalloproteinase (ADAM)-dependent cell adhesion, proliferation, and migration by modulating membrane fluidity
    • CrossRef PubMed
    • Reiss, K., Cornelsen, I., Husmann, M., Gimpl, G. and Bhakdi, S. (2011) Unsaturated fatty acids drive disintegrin and metalloproteinase (ADAM)-dependent cell adhesion, proliferation, and migration by modulating membrane fluidity. J. Biol. Chem. 286, 26931-26942 CrossRef PubMed
    • (2011) J. Biol. Chem. , vol.286 , pp. 26931-26942
    • Reiss, K.1    Cornelsen, I.2    Husmann, M.3    Gimpl, G.4    Bhakdi, S.5
  • 82
    • 84860369072 scopus 로고    scopus 로고
    • Staphylococcus aureus activation of caspase 1/calpain signaling mediates invasion through human keratinocytes
    • CrossRef PubMed
    • Soong, G., Chun, J., Parker, D. and Prince, A. (2012) Staphylococcus aureus activation of caspase 1/calpain signaling mediates invasion through human keratinocytes. J. Infect. Dis. 205, 1571-1579 CrossRef PubMed
    • (2012) J. Infect. Dis. , vol.205 , pp. 1571-1579
    • Soong, G.1    Chun, J.2    Parker, D.3    Prince, A.4
  • 83
    • 79960929333 scopus 로고    scopus 로고
    • Transcriptome-wide analysis of regulatory interactions of the RNA-binding protein HuR
    • CrossRef PubMed
    • Lebedeva, S., Jens, M., Theil, K., Schwanhäusser, B., Selbach, M., Landthaler, M. and Rajewsky, N. (2011) Transcriptome-wide analysis of regulatory interactions of the RNA-binding protein HuR. Mol. Cell 43, 340-352 CrossRef PubMed
    • (2011) Mol. Cell , vol.43 , pp. 340-352
    • Lebedeva, S.1    Jens, M.2    Theil, K.3    Schwanhäusser, B.4    Selbach, M.5    Landthaler, M.6    Rajewsky, N.7
  • 84
    • 0032526427 scopus 로고    scopus 로고
    • Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs
    • CrossRef PubMed
    • Fan, X.C. and Steitz, J.A. (1998) Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J. 17, 3448-3460 CrossRef PubMed
    • (1998) EMBO J. , vol.17 , pp. 3448-3460
    • Fan, X.C.1    Steitz, J.A.2
  • 86
    • 34250362729 scopus 로고    scopus 로고
    • Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: Implications for posttranscriptional regulation of cyclooxygenase-2
    • CrossRef PubMed
    • Doller, A., Huwiler, A., Müller, R., Radeke, H.H., Pfeilschifter, J. and Eberhardt, W. (2007) Protein kinase C alpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: implications for posttranscriptional regulation of cyclooxygenase-2. Mol. Biol. Cell 18, 2137-2148 CrossRef PubMed
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2137-2148
    • Doller, A.1    Huwiler, A.2    Müller, R.3    Radeke, H.H.4    Pfeilschifter, J.5    Eberhardt, W.6
  • 87
    • 0034907223 scopus 로고    scopus 로고
    • Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase
    • CrossRef PubMed
    • Ming, X.F., Stoecklin, G., Lu, M., Looser, R. and Moroni, C. (2001) Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase. Mol. Cell. Biol. 21, 5778-5789 CrossRef PubMed
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5778-5789
    • Ming, X.F.1    Stoecklin, G.2    Lu, M.3    Looser, R.4    Moroni, C.5
  • 88
    • 84886000339 scopus 로고    scopus 로고
    • RNA-dependent association with myosin IIA promotes F-actin-guided trafficking of the ELAV-like protein HuR to polysomes
    • CrossRef PubMed
    • Doller, A., Schulz, S., Pfeilschifter, J. and Eberhardt, W. (2013) RNA-dependent association with myosin IIA promotes F-actin-guided trafficking of the ELAV-like protein HuR to polysomes. Nucleic Acids Res. 41, 9152-9167 CrossRef PubMed
    • (2013) Nucleic Acids Res. , vol.41 , pp. 9152-9167
    • Doller, A.1    Schulz, S.2    Pfeilschifter, J.3    Eberhardt, W.4
  • 89
    • 33646807832 scopus 로고    scopus 로고
    • The P53 pathway: What questions remain to be explored?
    • CrossRef PubMed
    • Levine, A.J., Hu, W. and Feng, Z. (2006) The P53 pathway: what questions remain to be explored? Cell Death Differ. 13, 1027-1036 CrossRef PubMed
    • (2006) Cell Death Differ , vol.13 , pp. 1027-1036
    • Levine, A.J.1    Hu, W.2    Feng, Z.3
  • 90
    • 34250735674 scopus 로고    scopus 로고
    • RNA regulons: Coordination of post-transcriptional events
    • CrossRef PubMed
    • Keene, J.D. (2007) RNA regulons: coordination of post-transcriptional events. Nat. Rev. Genet. 8, 533-543 CrossRef PubMed
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 533-543
    • Keene, J.D.1


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