메뉴 건너뛰기




Volumn 288, Issue 2, 2013, Pages 938-946

ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, laboratory of genetics and physiology 2 (LGP2)

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; ATP-HYDROLYSIS ACTIVITY; BIOCHEMICAL ASSAY; BIOLOGICAL RESPONSE; ENZYMATIC ACTIVITIES; ENZYMATIC PROPERTIES; HYDROLYSIS ACTIVITY; IN-VIVO; MOLECULAR SIGNATURES; PATTERN RECOGNITION RECEPTORS; RNA INTERACTION; RNA RECOGNITION; SINGLE-MOLECULE ANALYSIS; VIRUS INFECTION;

EID: 84872348735     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.424416     Document Type: Article
Times cited : (78)

References (27)
  • 1
    • 58049217490 scopus 로고    scopus 로고
    • RNA recognition and signal transduction by RIG-I-like receptors
    • Yoneyama, M., and Fujita, T. (2009) RNA recognition and signal transduction by RIG-I-like receptors. Immunol. Rev. 227, 54-65
    • (2009) Immunol. Rev. , vol.227 , pp. 54-65
    • Yoneyama, M.1    Fujita, T.2
  • 2
    • 84857393830 scopus 로고    scopus 로고
    • Activation of RIG-I-like receptor signal transduction
    • Bruns, A. M., and Horvath, C. M. (2012) Activation of RIG-I-like receptor signal transduction. Crit. Rev. Biochem. Mol. Biol. 47, 194-206
    • (2012) Crit. Rev. Biochem. Mol. Biol. , vol.47 , pp. 194-206
    • Bruns, A.M.1    Horvath, C.M.2
  • 4
    • 33845431988 scopus 로고    scopus 로고
    • RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2
    • DOI 10.1128/JVI.01325-06
    • Komuro, A., and Horvath, C. M. (2006) RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2. J. Virol. 80, 12332-12342 (Pubitemid 44904383)
    • (2006) Journal of Virology , vol.80 , Issue.24 , pp. 12332-12342
    • Komuro, A.1    Horvath, C.M.2
  • 7
    • 79954989343 scopus 로고    scopus 로고
    • Impaired cellular responses to cytosolic DNA or infection with Listeria monocytogenes and vaccinia virus in the absence of the murine LGP2 protein
    • Pollpeter, D., Komuro, A., Barber, G. N., and Horvath, C. M. (2011) Impaired cellular responses to cytosolic DNA or infection with Listeria monocytogenes and vaccinia virus in the absence of the murine LGP2 protein. PLoS ONE 6, e18842
    • (2011) PLoS ONE , vol.6
    • Pollpeter, D.1    Komuro, A.2    Barber, G.N.3    Horvath, C.M.4
  • 13
    • 60749124538 scopus 로고    scopus 로고
    • Cytosolic viral sensor RIG-I is a 5′-triphosphate-dependent translocase on double-stranded RNA
    • Myong, S., Cui, S., Cornish, P. V., Kirchhofer, A., Gack, M. U., Jung, J. U., Hopfner, K. P., and Ha, T. (2009) Cytosolic viral sensor RIG-I is a 5′-triphosphate-dependent translocase on double-stranded RNA. Science 323, 1070-1074
    • (2009) Science , vol.323 , pp. 1070-1074
    • Myong, S.1    Cui, S.2    Cornish, P.V.3    Kirchhofer, A.4    Gack, M.U.5    Jung, J.U.6    Hopfner, K.P.7    Ha, T.8
  • 14
    • 77749322591 scopus 로고    scopus 로고
    • Stepwise translocation of nucleic acid motors
    • Myong, S., and Ha, T. (2010) Stepwise translocation of nucleic acid motors. Curr. Opin. Struct. Biol. 20, 121-127
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 121-127
    • Myong, S.1    Ha, T.2
  • 15
    • 79956335271 scopus 로고    scopus 로고
    • Protein induced fluorescence enhancement as a single molecule assay with short distance sensitivity
    • Hwang, H., Kim, H., and Myong, S. (2011) Protein induced fluorescence enhancement as a single molecule assay with short distance sensitivity. Proc. Natl. Acad. Sci. U.S.A. 108, 7414-7418
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 7414-7418
    • Hwang, H.1    Kim, H.2    Myong, S.3
  • 16
    • 65649083024 scopus 로고    scopus 로고
    • Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2
    • Bamming, D., and Horvath, C. M. (2009) Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J. Biol. Chem. 284, 9700-9712
    • (2009) J. Biol. Chem. , vol.284 , pp. 9700-9712
    • Bamming, D.1    Horvath, C.M.2
  • 17
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • DOI 10.1038/ni1087
    • Yoneyama, M., Kikuchi, M., Natsukawa, T., Shinobu, N., Imaizumi, T., Miyagishi, M., Taira, K., Akira, S., and Fujita, T. (2004) The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat. Immunol. 5, 730-737 (Pubitemid 39023305)
    • (2004) Nature Immunology , vol.5 , Issue.7 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3    Shinobu, N.4    Imaizumi, T.5    Miyagishi, M.6    Taira, K.7    Akira, S.8    Fujita, T.9
  • 18
  • 21
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • Kowalinski, E., Lunardi, T., McCarthy, A. A., Louber, J., Brunel, J., Grigorov, B., Gerlier, D., and Cusack, S. (2011) Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 147, 423-435
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1    Lunardi, T.2    McCarthy, A.A.3    Louber, J.4    Brunel, J.5    Grigorov, B.6    Gerlier, D.7    Cusack, S.8
  • 25
    • 77649221014 scopus 로고    scopus 로고
    • Melanoma differentiation-associated gene 5 (MDA5) is involved in the innate immune response to Paramyxoviridae infection in vivo
    • Gitlin, L., Benoit, L., Song, C., Cella, M., Gilfillan, S., Holtzman, M. J., and Colonna, M. (2010) Melanoma differentiation-associated gene 5 (MDA5) is involved in the innate immune response to Paramyxoviridae infection in vivo. PLoS Pathog. 6, e1000734
    • (2010) PLoS Pathog. , vol.6
    • Gitlin, L.1    Benoit, L.2    Song, C.3    Cella, M.4    Gilfillan, S.5    Holtzman, M.J.6    Colonna, M.7
  • 26
    • 79960765634 scopus 로고    scopus 로고
    • Sensing of viral nucleic acids by RIG-I. From translocation to translation
    • Schmidt, A., Rothenfusser, S., and Hopfner, K. P. (2012) Sensing of viral nucleic acids by RIG-I. From translocation to translation. Eur. J. Cell Biol. 91, 78-85
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 78-85
    • Schmidt, A.1    Rothenfusser, S.2    Hopfner, K.P.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.