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Volumn 89, Issue 1, 2015, Pages 863-869

Swine interferon-inducible transmembrane proteins potently inhibit influenza A virus replication

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN INTERFERON INDUCIBLE TRANSMEMBRANE PROTEIN; IFTM1 LIKE PROTEIN; IFTM2; IFTM3; INTERFERON; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 84919418051     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02516-14     Document Type: Article
Times cited : (13)

References (24)
  • 4
    • 84879048489 scopus 로고    scopus 로고
    • Interferoninducible transmembrane protein 3 (IFITM3) restricts reovirus cell entry
    • Anafu AA, Bowen CH, Chin CR, Brass AL, Holm GH. 2013. Interferoninducible transmembrane protein 3 (IFITM3) restricts reovirus cell entry. J Biol Chem 288:17261-17271. http://dx.doi.org/10.1074/jbc.M112.438515.
    • (2013) J Biol Chem , vol.288 , pp. 17261-17271
    • Anafu, A.A.1    Bowen, C.H.2    Chin, C.R.3    Brass, A.L.4    Holm, G.H.5
  • 5
    • 79551715390 scopus 로고    scopus 로고
    • The IFITM proteins inhibit HIV-1 infection
    • Lu J, Pan Q, Rong L, He W, Liu SL, Liang C. 2011. The IFITM proteins inhibit HIV-1 infection. J Virol 85:2126-2137. http://dx.doi.org/10.1128/JVI.01531-10.
    • (2011) J Virol , vol.85 , pp. 2126-2137
    • Lu, J.1    Pan, Q.2    Rong, L.3    He, W.4    Liu, S.L.5    Liang, C.6
  • 10
    • 84901337841 scopus 로고    scopus 로고
    • IFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusion
    • Desai TM, Marin M, Chin CR, Savidis G, Brass AL, Melikyan GB. 2014. IFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusion. PLoS Pathog 10: e1004048. http://dx.doi.org/10.1371/journal.ppat.1004048.
    • (2014) PLoS Pathog , vol.10
    • Desai, T.M.1    Marin, M.2    Chin, C.R.3    Savidis, G.4    Brass, A.L.5    Melikyan, G.B.6
  • 11
    • 84876349734 scopus 로고    scopus 로고
    • The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry
    • Amini-Bavil-Olyaee S, Choi YJ, Lee JH, Shi M, Huang IC, Farzan M, Jung JU. 2013. The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry. Cell Host Microbe 13:452-464. http://dx.doi.org/10.1016/j.chom.2013.03.006.
    • (2013) Cell Host Microbe , vol.13 , pp. 452-464
    • Amini-Bavil-Olyaee, S.1    Choi, Y.J.2    Lee, J.H.3    Shi, M.4    Huang, I.C.5    Farzan, M.6    Jung, J.U.7
  • 12
    • 77955892540 scopus 로고    scopus 로고
    • Palmitoylome profiling reveals S-palmitoylationdependent antiviral activity of IFITM3
    • Yount JS, Moltedo B, Yang YY, Charron G, Moran TM, Lopez CB, Hang HC. 2010. Palmitoylome profiling reveals S-palmitoylationdependent antiviral activity of IFITM3. Nat Chem Biol 6:610-614. http://dx.doi.org/10.1038/nchembio.405.
    • (2010) Nat Chem Biol , vol.6 , pp. 610-614
    • Yount, J.S.1    Moltedo, B.2    Yang, Y.Y.3    Charron, G.4    Moran, T.M.5    Lopez, C.B.6    Hang, H.C.7
  • 14
    • 84861727353 scopus 로고    scopus 로고
    • S-palmitoylation and ubiquitination differentially regulate interferon-induced transmembrane protein 3 (IFITM3)-mediated resistance to influenza virus
    • Yount JS, Karssemeijer RA, Hang HC. 2012. S-palmitoylation and ubiquitination differentially regulate interferon-induced transmembrane protein 3 (IFITM3)-mediated resistance to influenza virus. J Biol Chem 287: 19631-19641. http://dx.doi.org/10.1074/jbc.M112.362095.
    • (2012) J Biol Chem , vol.287 , pp. 19631-19641
    • Yount, J.S.1    Karssemeijer, R.A.2    Hang, H.C.3
  • 15
    • 84899449482 scopus 로고    scopus 로고
    • Phosphorylation of the antiviral protein IFITM3 dually regulates its endocytosis and ubiquitination
    • Chesarino NM, McMichael TM, Hach JC, Yount JS. 2014. Phosphorylation of the antiviral protein IFITM3 dually regulates its endocytosis and ubiquitination. J Biol Chem 289:11986-11992. http://dx.doi.org/10.1074/jbc.M114.557694.
    • (2014) J Biol Chem , vol.289 , pp. 11986-11992
    • Chesarino, N.M.1    McMichael, T.M.2    Hach, J.C.3    Yount, J.S.4
  • 17
    • 0021707311 scopus 로고
    • Transcriptional and posttranscriptional regulation of interferon-induced gene expression in human cells
    • Friedman RL, Manly SP, McMahon M, Kerr IM, Stark GR. 1984. Transcriptional and posttranscriptional regulation of interferon-induced gene expression in human cells. Cell 38:745-755. http://dx.doi.org/10.1016/0092-8674(84)90270-8.
    • (1984) Cell , vol.38 , pp. 745-755
    • Friedman, R.L.1    Manly, S.P.2    McMahon, M.3    Kerr, I.M.4    Stark, G.R.5
  • 18
    • 84900481101 scopus 로고    scopus 로고
    • Evolutionary characterization of pig interferon-inducible transmembrane gene family and member expression dynamics in tracheobronchial lymph nodes of pigs infected with swine respiratory disease viruses
    • Miller LC, Jiang Z, Sang Y, Harhay GP, Lager KM. 2014. Evolutionary characterization of pig interferon-inducible transmembrane gene family and member expression dynamics in tracheobronchial lymph nodes of pigs infected with swine respiratory disease viruses. Vet Immunol Immunopathol 159:180-191. http://dx.doi.org/10.1016/j.vetimm.2014.02.015.
    • (2014) Vet Immunol Immunopathol , vol.159 , pp. 180-191
    • Miller, L.C.1    Jiang, Z.2    Sang, Y.3    Harhay, G.P.4    Lager, K.M.5
  • 20
    • 84874738791 scopus 로고    scopus 로고
    • Dissecting the role of COPI complexes on influenza virus infection
    • Sun E, He J, Zhuang X. 2013. Dissecting the role of COPI complexes on influenza virus infection. J Virol 87:2673-2685. http://dx.doi.org/10.1128/JVI.02277-12.
    • (2013) J Virol , vol.87 , pp. 2673-2685
    • Sun, E.1    He, J.2    Zhuang, X.3
  • 21
    • 53249140699 scopus 로고    scopus 로고
    • Modulation of influenza virus replication by alteration of sodium ion transport and protein kinase C activity
    • Hoffmann HH, Palese P, Shaw ML. 2008. Modulation of influenza virus replication by alteration of sodium ion transport and protein kinase C activity. Antiviral Res 80:124-134. http://dx.doi.org/10.1016/j.antiviral.2008.05.008.
    • (2008) Antiviral Res , vol.80 , pp. 124-134
    • Hoffmann, H.H.1    Palese, P.2    Shaw, M.L.3
  • 22
    • 84871983533 scopus 로고    scopus 로고
    • Investigation of influenza virus polymerase activity in pig cells
    • Moncorge O, Long JS, Cauldwell AV, Zhou H, Lycett SJ, Barclay WS. 2013. Investigation of influenza virus polymerase activity in pig cells. J Virol 87:384-394. http://dx.doi.org/10.1128/JVI.01633-12.
    • (2013) J Virol , vol.87 , pp. 384-394
    • Moncorge, O.1    Long, J.S.2    Cauldwell, A.V.3    Zhou, H.4    Lycett, S.J.5    Barclay, W.S.6
  • 23
    • 0029026692 scopus 로고
    • Mutational analysis of influenza virus promoter elements in vivo
    • Neumann G, Hobom G. 1995. Mutational analysis of influenza virus promoter elements in vivo. J Gen Virol 76:1709-1717. http://dx.doi.org/10.1099/0022-1317-76-7-1709.
    • (1995) J Gen Virol , vol.76 , pp. 1709-1717
    • Neumann, G.1    Hobom, G.2
  • 24
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl MW. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29:e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.