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Volumn 214, Issue 4, 2017, Pages 919-929

ZMP STE24 defends against influenza and other pathogenic viruses

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; METALLOPROTEINASE; UNCLASSIFIED DRUG; ZINC METALLOPEPTIDASE STE24; CYTOKINE; DIFFERENTIATION ANTIGEN; LEU-13 ANTIGEN; ZMPSTE24 PROTEIN, HUMAN; ZMPSTE24 PROTEIN, MOUSE;

EID: 85021942862     PISSN: 00221007     EISSN: 15409538     Source Type: Journal    
DOI: 10.1084/jem.20161270     Document Type: Article
Times cited : (59)

References (28)
  • 1
    • 84954305090 scopus 로고    scopus 로고
    • The protease Ste24 clears clogged translocons
    • Ast, T., S. Michaelis, and M. Schuldiner. 2016. The protease Ste24 clears clogged translocons. Cell. 164:103-114. http ://dx .doi .org/10 .1016/j .cell .2015 .11 .053
    • (2016) Cell , vol.164 , pp. 103-114
    • Ast, T.1    Michaelis, S.2    Schuldiner, M.3
  • 2
    • 85017002818 scopus 로고    scopus 로고
    • IFI TM-family proteins: The cell's first line of antiviral defense
    • Bailey, C.C., G. Zhong, I.C. Huang, and M. Farzan. 2014. IFI TM-family proteins: The cell's first line of antiviral defense. Annu. Rev. Virol. 1:261-283. http ://dx .doi .org/10 .1146/annurev-virology-031413-085537
    • (2014) Annu. Rev. Virol , vol.1 , pp. 261-283
    • Bailey, C.C.1    Zhong, G.2    Huang, I.C.3    Farzan, M.4
  • 3
    • 84865768730 scopus 로고    scopus 로고
    • Human ZMP STE24 disease mutations: Residual proteolytic activity correlates with disease severity
    • Barrowman, J., P.A. Wiley, S.E. Hudon-Miller, C.A. Hrycyna, and S. Michaelis. 2012. Human ZMP STE24 disease mutations: Residual proteolytic activity correlates with disease severity. Hum. Mol. Genet. 21:4084-4093. http ://dx .doi .org/10 .1093/hmg/dds233
    • (2012) Hum. Mol. Genet , vol.21 , pp. 4084-4093
    • Barrowman, J.1    Wiley, P.A.2    Hudon-Miller, S.E.3    Hrycyna, C.A.4    Michaelis, S.5
  • 4
    • 0036791026 scopus 로고    scopus 로고
    • Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect
    • Bergo, M.O., B. Gavino, J. Ross, W.K. Schmidt, C. Hong, L.V. Kendall, A. Mohr, M. Meta, H. Genant, Y. Jiang, et al. 2002. Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect. Proc. Natl. Acad. Sci. USA. 99:13049-13054. http ://dx .doi .org/10 .1073/pnas .192460799
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13049-13054
    • Bergo, M.O.1    Gavino, B.2    Ross, J.3    Schmidt, W.K.4    Hong, C.5    Kendall, L.V.6    Mohr, A.7    Meta, M.8    Genant, H.9    Jiang, Y.10
  • 5
    • 72549116887 scopus 로고    scopus 로고
    • The IFI TM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus
    • Brass, A.L., I.C. Huang, Y. Benita, S.P. John, M.N. Krishnan, E.M. Feeley, B.J. Ryan, J.L. Weyer, L. van der Weyden, E. Fikrig, et al. 2009. The IFI TM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus. Cell. 139:1243-1254. http ://dx .doi .org/10 .1016/j .cell .2009 .12 .017
    • (2009) Cell , vol.139 , pp. 1243-1254
    • Brass, A.L.1    Huang, I.C.2    Benita, Y.3    John, S.P.4    Krishnan, M.N.5    Feeley, E.M.6    Ryan, B.J.7    Weyer, J.L.8    van der Weyden, L.9    Fikrig, E.10
  • 7
    • 84899743971 scopus 로고    scopus 로고
    • Endocytosis of viruses and bacteria
    • Cossart, P., and A. Helenius. 2014. Endocytosis of viruses and bacteria. Cold Spring Harb. Perspect. Biol. 6:a016972. http ://dx .doi .org/10 .1101/cshperspect .a016972
    • (2014) Cold Spring Harb. Perspect. Biol , vol.6
    • Cossart, P.1    Helenius, A.2
  • 8
    • 84856933595 scopus 로고    scopus 로고
    • Genetic inactivation of COPI coatomer separately inhibits vesicular stomatitis virus entry and gene expression
    • Cureton, D.K., R. Burdeinick-Kerr, and S.P. Whelan. 2012. Genetic inactivation of COPI coatomer separately inhibits vesicular stomatitis virus entry and gene expression. J. Virol. 86:655-666. http ://dx .doi .org/10 .1128/JVI .05810-11
    • (2012) J. Virol , vol.86 , pp. 655-666
    • Cureton, D.K.1    Burdeinick-Kerr, R.2    Whelan, S.P.3
  • 11
    • 84936796837 scopus 로고    scopus 로고
    • TRIM32 senses and restricts influenza A virus by ubiquitination of PB1 polymerase
    • Fu, B., L. Wang, H. Ding, J.C. Schwamborn, S. Li, and M.E. Dorf. 2015. TRIM32 senses and restricts influenza A virus by ubiquitination of PB1 polymerase. PLoS Pathog. 11:e1004960. http ://dx .doi .org/10 .1371/journal .ppat .1004960
    • (2015) PLoS Pathog , vol.11
    • Fu, B.1    Wang, L.2    Ding, H.3    Schwamborn, J.C.4    Li, S.5    Dorf, M.E.6
  • 12
    • 84937761010 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison, S.C. 2015. Viral membrane fusion. Virology. 479-480:498-507. http ://dx .doi .org/10 .1016/j .virol .2015 .03 .043
    • (2015) Virology , vol.479-480 , pp. 498-507
    • Harrison, S.C.1
  • 13
    • 84880617786 scopus 로고    scopus 로고
    • In vivo bioluminescent imaging of influenza A virus infection and characterization of novel cross-protective monoclonal antibodies
    • Heaton, N.S., V.H. Leyva-Grado, G.S. Tan, D. Eggink, R. Hai, and P. Palese. 2013. In vivo bioluminescent imaging of influenza A virus infection and characterization of novel cross-protective monoclonal antibodies. J. Virol. 87:8272-8281. http ://dx .doi .org/10 .1128/JVI .00969-13
    • (2013) J. Virol , vol.87 , pp. 8272-8281
    • Heaton, N.S.1    Leyva-Grado, V.H.2    Tan, G.S.3    Eggink, D.4    Hai, R.5    Palese, P.6
  • 14
    • 84976867203 scopus 로고    scopus 로고
    • Ste24p mediates proteolysis of both isoprenylated and non-prenylated oligopeptides
    • Hildebrandt, E.R., B.T. Arachea, M.C. Wiener, and W.K. Schmidt. 2016. Ste24p mediates proteolysis of both isoprenylated and non-prenylated oligopeptides. J. Biol. Chem. 291:14185-14198. http ://dx .doi .org/10 .1074/jbc .M116 .718197
    • (2016) J. Biol. Chem , vol.291 , pp. 14185-14198
    • Hildebrandt, E.R.1    Arachea, B.T.2    Wiener, M.C.3    Schmidt, W.K.4
  • 15
    • 53349178089 scopus 로고    scopus 로고
    • STI NG is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • Ishikawa, H., and G.N. Barber. 2008. STI NG is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature. 455:674-678. http ://dx .doi .org/10 .1038/nature07317
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 18
    • 33748682298 scopus 로고    scopus 로고
    • New low-viscosity overlay medium for viral plaque assays
    • Matrosovich, M., T. Matrosovich, W. Garten, and H.D. Klenk. 2006. New low-viscosity overlay medium for viral plaque assays. Virol. J. 3:63. http ://dx .doi .org/10 .1186/1743-422X-3-63
    • (2006) Virol. J , vol.3 , pp. 63
    • Matrosovich, M.1    Matrosovich, T.2    Garten, W.3    Klenk, H.D.4
  • 19
    • 84865752291 scopus 로고    scopus 로고
    • Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease
    • Michaelis, S., and J. Barrowman. 2012. Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease. Microbiol. Mol. Biol. Rev. 76:626-651. http ://dx .doi .org/10 .1128/MMBR .00010-12
    • (2012) Microbiol. Mol. Biol. Rev , vol.76 , pp. 626-651
    • Michaelis, S.1    Barrowman, J.2
  • 20
    • 70349645266 scopus 로고    scopus 로고
    • Ageing-related chromatin defects through loss of the NURD complex
    • Pegoraro, G., N. Kubben, U. Wickert, H. Göhler, K. Hoffmann, and T. Misteli. 2009. Ageing-related chromatin defects through loss of the NURD complex. Nat. Cell Biol. 11:1261-1267. http ://dx .doi .org/10 .1038/ncb1971
    • (2009) Nat. Cell Biol , vol.11 , pp. 1261-1267
    • Pegoraro, G.1    Kubben, N.2    Wickert, U.3    Göhler, H.4    Hoffmann, K.5    Misteli, T.6
  • 22
    • 84888015374 scopus 로고    scopus 로고
    • IFI TMs restrict the replication of multiple pathogenic viruses
    • Perreira, J.M., C.R. Chin, E.M. Feeley, and A.L. Brass. 2013. IFI TMs restrict the replication of multiple pathogenic viruses. J. Mol. Biol. 425:4937-4955. http ://dx .doi .org/10 .1016/j .jmb .2013 .09 .024
    • (2013) J. Mol. Biol , vol.425 , pp. 4937-4955
    • Perreira, J.M.1    Chin, C.R.2    Feeley, E.M.3    Brass, A.L.4
  • 25
    • 84880666503 scopus 로고    scopus 로고
    • Influenza: Propagation, quantification, and storage
    • Chapter 15 Unit 15G.1
    • Szretter, K.J., A.L. Balish, and J.M. Katz. 2006. Influenza: Propagation, quantification, and storage. Curr. Protoc. Microbiol. Chapter 15:Unit 15G.1. http ://dx .doi .org/https ://10 .1002/0471729256 .mc15g01s3
    • (2006) Curr. Protoc. Microbiol
    • Szretter, K.J.1    Balish, A.L.2    Katz, J.M.3
  • 26
    • 82455172080 scopus 로고    scopus 로고
    • An enzymatic assay for detection of viral entry
    • Chapter 26 Unit 26.12
    • Tscherne, D.M., and A. García-Sastre. 2011. An enzymatic assay for detection of viral entry. Curr. Protoc. Cell Biol. Chapter 26:Unit 26.12. http ://dx .doi .org/https ://10 .1002/0471143030 .cb2612s51
    • (2011) Curr. Protoc. Cell Biol
    • Tscherne, D.M.1    García-Sastre, A.2
  • 28
    • 84904318995 scopus 로고    scopus 로고
    • Nuclear lamins and neurobiology
    • Young, S.G., H.J. Jung, J.M. Lee, and L.G. Fong. 2014. Nuclear lamins and neurobiology. Mol. Cell. Biol. 34:2776-2785. http ://dx .doi .org/10 .1128/MCB .00486-14
    • (2014) Mol. Cell. Biol , vol.34 , pp. 2776-2785
    • Young, S.G.1    Jung, H.J.2    Lee, J.M.3    Fong, L.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.