메뉴 건너뛰기




Volumn 45, Issue 1, 2017, Pages

ADAR1 restricts LINE-1 retrotransposition

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DEAMINASE; ADENOSINE DEAMINASE ACTING ON RNA 1; BINDING PROTEIN; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG; ADAR1 PROTEIN, HUMAN; HEAT SHOCK PROTEIN; PROTEIN BINDING; RETROPOSON; RNA BINDING PROTEIN;

EID: 85014834160     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkw834     Document Type: Article
Times cited : (57)

References (69)
  • 1
    • 84902143592 scopus 로고    scopus 로고
    • An RNA editor, adenosine deaminase acting on double-stranded RNA (ADAR1)
    • George, C.X., John, L. and Samuel, C.E. (2014) An RNA editor, adenosine deaminase acting on double-stranded RNA (ADAR1). J. Interferon Cytokine Res., 34, 437-446.
    • (2014) J. Interferon Cytokine Res. , vol.34 , pp. 437-446
    • George, C.X.1    John, L.2    Samuel, C.E.3
  • 2
    • 85012078057 scopus 로고    scopus 로고
    • New insights into the biological role of mammalian ADARS; The RNA editing proteins
    • Mannion, N., Arieti, F., Gallo, A., Keegan, L.P. and O'Connell, M.A. (2015) New Insights into the Biological Role of Mammalian ADARs; the RNA Editing Proteins. Biomolecules, 5, 2338-2362.
    • (2015) Biomolecules , vol.5 , pp. 2338-2362
    • Mannion, N.1    Arieti, F.2    Gallo, A.3    Keegan, L.P.4    O'Connell, M.A.5
  • 3
    • 0029164692 scopus 로고
    • Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: Evidence for two forms of the deaminase
    • Patterson, J.B. and Samuel, C.E. (1995) Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase. Mol. Cell. Biol., 15, 5376-5388.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5376-5388
    • Patterson, J.B.1    Samuel, C.E.2
  • 5
    • 79952069367 scopus 로고    scopus 로고
    • Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral
    • Samuel, C.E. (2011) Adenosine deaminases acting on RNA (ADARs) are both antiviral and proviral. Virology, 411, 180-193.
    • (2011) Virology , vol.411 , pp. 180-193
    • Samuel, C.E.1
  • 6
    • 33846073016 scopus 로고    scopus 로고
    • Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus infection
    • Nie, Y., Hammond, G.L. and Yang, J.H. (2007) Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus infection. J Virol., 81, 917-923.
    • (2007) J Virol. , vol.81 , pp. 917-923
    • Nie, Y.1    Hammond, G.L.2    Yang, J.H.3
  • 7
    • 70749147276 scopus 로고    scopus 로고
    • RNA adenosine deaminase ADAR1 deficiency leads to increased activation of protein kinase PKR and reduced vesicular stomatitis virus growth following interferon treatment
    • Li, Z., Wolff, K.C. and Samuel, C.E. (2010) RNA adenosine deaminase ADAR1 deficiency leads to increased activation of protein kinase PKR and reduced vesicular stomatitis virus growth following interferon treatment. Virology, 396, 316-322.
    • (2010) Virology , vol.396 , pp. 316-322
    • Li, Z.1    Wolff, K.C.2    Samuel, C.E.3
  • 8
    • 33748101596 scopus 로고    scopus 로고
    • RNA editing in hepatitis delta virus
    • Casey, J.L. (2006) RNA editing in hepatitis delta virus. Curr. Top. Microbiol. Immunol., 307, 67-89.
    • (2006) Curr. Top. Microbiol. Immunol. , vol.307 , pp. 67-89
    • Casey, J.L.1
  • 11
    • 33846092075 scopus 로고    scopus 로고
    • A-to-G hypermutation in the genome of lymphocytic choriomeningitis virus
    • Zahn, R.C., Schelp, I., Utermohlen, O. and von Laer, D. (2007) A-to-G hypermutation in the genome of lymphocytic choriomeningitis virus. J. Virol., 81, 457-464.
    • (2007) J. Virol. , vol.81 , pp. 457-464
    • Zahn, R.C.1    Schelp, I.2    Utermohlen, O.3    Von Laer, D.4
  • 12
    • 84903558577 scopus 로고    scopus 로고
    • Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR)
    • Mohamed, Y.M., Bangphoomi, N., Yamane, D., Suda, Y., Kato, K., Horimoto, T. and Akashi, H. (2014) Physical interaction between bovine viral diarrhea virus nonstructural protein 4A and adenosine deaminase acting on RNA (ADAR). Arch. Virol., 159, 1735-1741.
    • (2014) Arch. Virol. , vol.159 , pp. 1735-1741
    • Mohamed, Y.M.1    Bangphoomi, N.2    Yamane, D.3    Suda, Y.4    Kato, K.5    Horimoto, T.6    Akashi, H.7
  • 13
    • 18144401994 scopus 로고    scopus 로고
    • New antiviral pathway that mediates hepatitis C virus replicon interferon sensitivity through ADAR1
    • Taylor, D.R., Puig, M., Darnell, M.E., Mihalik, K. and Feinstone, S.M. (2005) New antiviral pathway that mediates hepatitis C virus replicon interferon sensitivity through ADAR1. J. Virol., 79, 6291-6298.
    • (2005) J. Virol. , vol.79 , pp. 6291-6298
    • Taylor, D.R.1    Puig, M.2    Darnell, M.E.3    Mihalik, K.4    Feinstone, S.M.5
  • 15
    • 79551705342 scopus 로고    scopus 로고
    • Double-stranded RNA adenosine deaminase ADAR-1-induced hypermutated genomes among inactivated seasonal influenza and live attenuated measles virus vaccines
    • Suspene, R., Petit, V., Puyraimond-Zemmour, D., Aynaud, M.M., Henry, M., Guetard, D., Rusniok, C., Wain-Hobson, S. and Vartanian, J.P. (2011 Double-stranded RNA adenosine deaminase ADAR-1-induced hypermutated genomes among inactivated seasonal influenza and live attenuated measles virus vaccines. J. Virol., 85, 2458-2462.
    • (2011) J Virol. , vol.85 , pp. 2458-2462
    • Suspene, R.1    Petit, V.2    Puyraimond-Zemmour, D.3    Aynaud, M.M.4    Henry, M.5    Guetard, D.6    Rusniok, C.7    Wain-Hobson, S.8    Vartanian, J.P.9
  • 16
    • 55249089269 scopus 로고    scopus 로고
    • Double-stranded RNA adenosine deaminases enhance expression of human immunodeficiency virus type 1 proteins
    • Phuphuakrat, A., Kraiwong, R., Boonarkart, C., Lauhakirti, D., Lee, T.H. and Auewarakul, P. (2008) Double-stranded RNA adenosine deaminases enhance expression of human immunodeficiency virus type 1 proteins. J. Virol., 82, 10864-10872.
    • (2008) J. Virol. , vol.82 , pp. 10864-10872
    • Phuphuakrat, A.1    Kraiwong, R.2    Boonarkart, C.3    Lauhakirti, D.4    Lee, T.H.5    Auewarakul, P.6
  • 17
    • 70749142026 scopus 로고    scopus 로고
    • Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates viral infection
    • Doria, M., Neri, F., Gallo, A., Farace, M.G. and Michienzi, A. (2009) Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates viral infection. Nucleic Acids Res., 37, 5848-5858.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5848-5858
    • Doria, M.1    Neri, F.2    Gallo, A.3    Farace, M.G.4    Michienzi, A.5
  • 18
    • 70349283034 scopus 로고    scopus 로고
    • ADAR1 interacts with PKR during human immunodeficiency virus infection of lymphocytes and contributes to viral replication
    • Clerzius, G., Gelinas, J.F., Daher, A., Bonnet, M., Meurs, E.F. and Gatignol, A. (2009) ADAR1 interacts with PKR during human immunodeficiency virus infection of lymphocytes and contributes to viral replication. J. Virol., 83, 10119-10128.
    • (2009) J. Virol. , vol.83 , pp. 10119-10128
    • Clerzius, G.1    Gelinas, J.F.2    Daher, A.3    Bonnet, M.4    Meurs, E.F.5    Gatignol, A.6
  • 20
    • 84920926965 scopus 로고    scopus 로고
    • Double-stranded RNA-specific adenosine deaminase 1 (ADAR1) promotes EIAV replication and infectivity
    • Tang, Y.D., Na, L., Fu, L.H., Yang, F., Zhu, C.H., Tang, L., Li, Q., Wang, J.Y., Li, Z., Wang, X.F. et al. (2015) Double-stranded RNA-specific adenosine deaminase 1 (ADAR1) promotes EIAV replication and infectivity. Virology, 476, 364-371.
    • (2015) Virology , vol.476 , pp. 364-371
    • Tang, Y.D.1    Na, L.2    Fu, L.H.3    Yang, F.4    Zhu, C.H.5    Tang, L.6    Li, Q.7    Wang, J.Y.8    Li, Z.9    Wang, X.F.10
  • 21
    • 84862507347 scopus 로고    scopus 로고
    • Active human retrotransposons: Variation and disease
    • Hancks, D.C. and Kazazian, H.H. Jr (2012) Active human retrotransposons: variation and disease. Curr. Opin. Genet. Dev., 22, 191-203.
    • (2012) Curr. Opin. Genet. Dev. , vol.22 , pp. 191-203
    • Hancks, D.C.1    Kazazian, H.H.2
  • 22
    • 58849089283 scopus 로고    scopus 로고
    • Non-LTR retrotransposons encode non canonical RRM domains in their first open reading frame
    • Khazina, E. and Weichenrieder, O. (2009) Non-LTR retrotransposons encode non canonical RRM domains in their first open reading frame. Proc. Natl. Acad. Sci. U.S.A., 106, 731-736.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 731-736
    • Khazina, E.1    Weichenrieder, O.2
  • 23
    • 0009969062 scopus 로고    scopus 로고
    • Human L1 retrotransposon encodes a conserved endonuclease required for retrotransposition
    • Feng, Q., Moran, J.V., Kazazian, H.H. Jr and Boeke, J.D. (1996) Human L1 retrotransposon encodes a conserved endonuclease required for retrotransposition. Cell, 87, 905-916.
    • (1996) Cell , vol.87 , pp. 905-916
    • Feng, Q.1    Moran, J.V.2    Kazazian, H.H.3    Boeke, J.D.4
  • 24
    • 0026428975 scopus 로고
    • Reverse transcriptase encoded by a human transposable element
    • Mathias, S.L., Scott, A.F., Kazazian, H.H. Jr, Boeke, J.D. and Gabriel, A. (1991) Reverse transcriptase encoded by a human transposable element. Science, 254, 1808-1810.
    • (1991) Science , vol.254 , pp. 1808-1810
    • Mathias, S.L.1    Scott, A.F.2    Kazazian, H.H.3    Boeke, J.D.4    Gabriel, A.5
  • 26
    • 84951275519 scopus 로고    scopus 로고
    • A 3′Poly(A) Tract Is Required for LINE-1 Retrotransposition
    • Doucet, A.J., Wilusz, J.E., Miyoshi, T., Liu, Y. and Moran, J.V. (2015) A 3′Poly(A) Tract Is Required for LINE-1 Retrotransposition. Mol Cell., 60, 728-741.
    • (2015) Mol Cell. , vol.60 , pp. 728-741
    • Doucet, A.J.1    Wilusz, J.E.2    Miyoshi, T.3    Liu, Y.4    Moran, J.V.5
  • 29
    • 57049092878 scopus 로고    scopus 로고
    • The take and give between retrotransposable elements and their hosts
    • Beauregard, A., Curcio, M.J. and Belfort, M. (2008) The take and give between retrotransposable elements and their hosts. Annu. Rev. Genet., 42, 587-617.
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 587-617
    • Beauregard, A.1    Curcio, M.J.2    Belfort, M.3
  • 30
    • 84883589001 scopus 로고    scopus 로고
    • Mapping the LINE1 ORF1 protein interactome reveals associated inhibitors of human retrotransposition
    • Goodier, J.L., Cheung, L.E. and Kazazian, H.H. Jr (2013) Mapping the LINE1 ORF1 protein interactome reveals associated inhibitors of human retrotransposition. Nucleic Acids Res., 41, 7401-7419.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 7401-7419
    • Goodier, J.L.1    Cheung, L.E.2    Kazazian, H.H.3
  • 31
    • 84889600606 scopus 로고    scopus 로고
    • Affinity proteomics reveals human host factors implicated in discrete stages of LINE-1 retrotransposition
    • Taylor, M.S., Lacava, J., Mita, P., Molloy, K.R., Huang, C.R., Li, D., Adney, E.M., Jiang, H., Burns, K.H. et al. (2013) Affinity proteomics reveals human host factors implicated in discrete stages of LINE-1 retrotransposition. Cell, 155, 1034-1048.
    • (2013) Cell , vol.155 , pp. 1034-1048
    • Taylor, M.S.1    Lacava, J.2    Mita, P.3    Molloy, K.R.4    Huang, C.R.5    Li, D.6    Adney, E.M.7    Jiang, H.8    Burns, K.H.9
  • 32
    • 84930817295 scopus 로고    scopus 로고
    • The zinc-finger antiviral protein zap inhibits line and alu retrotransposition
    • Moldovan, J.B. and Moran, J.V. (2015) The Zinc-Finger Antiviral Protein ZAP Inhibits LINE and Alu Retrotransposition. PLoS Genet., 11, e1005121.
    • (2015) PLoS Genet. , vol.11 , pp. e1005121
    • Moldovan, J.B.1    Moran, J.V.2
  • 36
    • 79951559175 scopus 로고    scopus 로고
    • Characterization of L1 retrotransposition with high-throughput dual-luciferase assays
    • Xie, Y., Rosser, J.M., Thompson, T.L., Boeke, J.D. and An, W. (2011) Characterization of L1 retrotransposition with high-throughput dual-luciferase assays. Nucleic Acids Res., 39, e16.
    • (2011) Nucleic Acids Res. , vol.39 , pp. e16
    • Xie, Y.1    Rosser, J.M.2    Thompson, T.L.3    Boeke, J.D.4    An, W.5
  • 37
    • 33846926262 scopus 로고    scopus 로고
    • Characterization of Saccharomyces cerevisiae Npa2p (Urb2p) reveals a low-molecular-mass complex containing Dbp6p, Npa1p (Urb1p), Nop8p, and Rsa3p involved in early steps of 60S ribosomal subunit biogenesis
    • Rosado, I.V., Dez, C., Lebaron, S., Caizergues-Ferrer, M., Henry, Y. and de la Cruz, J. (2007) Characterization of Saccharomyces cerevisiae Npa2p (Urb2p) reveals a low-molecular-mass complex containing Dbp6p, Npa1p (Urb1p), Nop8p, and Rsa3p involved in early steps of 60S ribosomal subunit biogenesis. Mol. Cell. Biol., 27, 1207-1221.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1207-1221
    • Rosado, I.V.1    Dez, C.2    Lebaron, S.3    Caizergues-Ferrer, M.4    Henry, Y.5    De La Cruz, J.6
  • 39
    • 84857834641 scopus 로고    scopus 로고
    • Assignment of protein interactions from affinity purification/mass spectrometry data
    • Pardo, M. and Choudhary, J.S. (2012) Assignment of protein interactions from affinity purification/mass spectrometry data. J. Proteome Res., 11, 1462-1474.
    • (2012) J. Proteome Res. , vol.11 , pp. 1462-1474
    • Pardo, M.1    Choudhary, J.S.2
  • 41
    • 42749093007 scopus 로고    scopus 로고
    • Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing activity inhibits cell migration and proliferation
    • Cenci, C., Barzotti, R., Galeano, F., Corbelli, S., Rota, R., Massimi, L., Di Rocco, C., O'Connell, M.A. and Gallo, A. (2008) Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing activity inhibits cell migration and proliferation. J. Biol. Chem., 283, 7251-7260.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7251-7260
    • Cenci, C.1    Barzotti, R.2    Galeano, F.3    Corbelli, S.4    Rota, R.5    Massimi, L.6    Di Rocco, C.7    O'Connell, M.A.8    Gallo, A.9
  • 42
    • 84879745156 scopus 로고    scopus 로고
    • STAU1 binding 3′ UTR IRAlus complements nuclear retention to protect cells from PKR-mediated translational shutdown
    • Elbarbary, R.A., Li, W., Tian, B. and Maquat, L.E. (2013) STAU1 binding 3′ UTR IRAlus complements nuclear retention to protect cells from PKR-mediated translational shutdown. Genes Dev., 27, 1495-1510.
    • (2013) Genes Dev. , vol.27 , pp. 1495-1510
    • Elbarbary, R.A.1    Li, W.2    Tian, B.3    Maquat, L.E.4
  • 43
    • 84871740038 scopus 로고    scopus 로고
    • HnRNPL and nucleolin bind LINE-1 RNA and function as host factors to modulate retrotransposition
    • Peddigari, S., Li, P.W., Rabe, J.L. and Martin, S.L. (2013). hnRNPL and nucleolin bind LINE-1 RNA and function as host factors to modulate retrotransposition. Nucleic Acids Res., 41, 575-585.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 575-585
    • Peddigari, S.1    Li, P.W.2    Rabe, J.L.3    Martin, S.L.4
  • 44
    • 84868694699 scopus 로고    scopus 로고
    • Poly(A) binding protein C1 is essential for efficient L1 retrotransposition and affects L1 RNP formation
    • Dai, L., Taylor, M.S., O'Donnell, K.A. and Boeke, J.D. (2012) Poly(A) binding protein C1 is essential for efficient L1 retrotransposition and affects L1 RNP formation. Mol. Cell. Biol., 32, 4323-4336.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4323-4336
    • Dai, L.1    Taylor, M.S.2    O'Donnell, K.A.3    Boeke, J.D.4
  • 45
    • 70349843062 scopus 로고    scopus 로고
    • Adenosine deaminase ADAR1 increases gene expression at the translational level by decreasing protein kinase PKR-dependent eIF-2alpha phosphorylation
    • Wang, Y. and Samuel, C.E. (2009) Adenosine deaminase ADAR1 increases gene expression at the translational level by decreasing protein kinase PKR-dependent eIF-2alpha phosphorylation. J. Mol. Biol., 393, 777-787.
    • (2009) J. Mol. Biol. , vol.393 , pp. 777-787
    • Wang, Y.1    Samuel, C.E.2
  • 46
    • 84898947864 scopus 로고    scopus 로고
    • Tandem immunoprecipitation approach to identify HIV-1 Gag associated host factors
    • Gao, W., Li, M. and Zhang, J. (2014) Tandem immunoprecipitation approach to identify HIV-1 Gag associated host factors. J. Virol. Methods, 203, 116-119.
    • (2014) J. Virol. Methods , vol.203 , pp. 116-119
    • Gao, W.1    Li, M.2    Zhang, J.3
  • 48
    • 80255140478 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Nef suppresses Hsp70-mediated Tat activation
    • Sugiyama, R., Naganumam, H., Nishitsujim, H. and Takakum, H. (2011). Human immunodeficiency virus-1 Nef suppresses Hsp70-mediated Tat activation. FEBS Lett., 585, 3367-3371.
    • (2011) FEBS Lett. , vol.585 , pp. 3367-3371
    • Sugiyama, R.1    Naganumam, H.2    Nishitsujim, H.3    Takakum, H.4
  • 49
    • 0034614455 scopus 로고    scopus 로고
    • Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription
    • O'Keeffe, B., Fong, Y., Chen, D., Zhou, S. and Zhou, Q. (2000) Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. J Biol Chem., 275, 279-287.
    • (2000) J Biol Chem. , vol.275 , pp. 279-287
    • O'Keeffe, B.1    Fong, Y.2    Chen, D.3    Zhou, S.4    Zhou, Q.5
  • 50
    • 0036227658 scopus 로고    scopus 로고
    • Specific incorporation of heat shock protein 70 family members into primate lentiviral virions
    • Gurer, C., Cimarelli, A. and Luban, J. (2002) Specific incorporation of heat shock protein 70 family members into primate lentiviral virions. J Virol., 76, 4666-4670.
    • (2002) J Virol. , vol.76 , pp. 4666-4670
    • Gurer, C.1    Cimarelli, A.2    Luban, J.3
  • 53
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • Buchan, J.R. and Parker, R. (2009) Eukaryotic stress granules: The ins and outs of translation. Mol. Cell., 36, 932-941.
    • (2009) Mol. Cell. , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 54
    • 84907425731 scopus 로고    scopus 로고
    • 1st inteRNAtional symposium on stress-associated RNA granules in human disease and viral infection
    • Banfield, B.W., Mouland, A.J. and McCormick, C. (2014) 1st International Symposium on Stress-associated RNA Granules in Human Disease and Viral Infection. Viruses, 6, 3500-3513.
    • (2014) Viruses , vol.6 , pp. 3500-3513
    • Banfield, B.W.1    Mouland, A.J.2    McCormick, C.3
  • 56
    • 23344449390 scopus 로고    scopus 로고
    • ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing
    • Nie, Y., Ding, L., Kao, P.N., Braun, R. and Yang, J.H. (2005) ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing. Mol. Cell. Biol., 25, 6956-6963.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6956-6963
    • Nie, Y.1    Ding, L.2    Kao, P.N.3    Braun, R.4    Yang, J.H.5
  • 57
    • 84887617987 scopus 로고    scopus 로고
    • ADAR regulates RNA editing, transcript stability, and gene expression
    • Wang, I.X., So, E., Devlin, J.L., Zhao, Y., Wu, M. and Cheung, V.G. (2013) ADAR regulates RNA editing, transcript stability, and gene expression. Cell Rep., 5, 849-860.
    • (2013) Cell Rep. , vol.5 , pp. 849-860
    • Wang, I.X.1    So, E.2    Devlin, J.L.3    Zhao, Y.4    Wu, M.5    Cheung, V.G.6
  • 58
    • 84857394407 scopus 로고    scopus 로고
    • Tudor-SN and ADAR1 are components of cytoplasmic stress granules
    • Weissbach, R. and Scadden, A.D. (2012) Tudor-SN and ADAR1 are components of cytoplasmic stress granules. RNA, 18, 462-471.
    • (2012) RNA , vol.18 , pp. 462-471
    • Weissbach, R.1    Scadden, A.D.2
  • 60
    • 23344449390 scopus 로고    scopus 로고
    • ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing
    • Nie, Y., Ding, L., Kao, P.N., Braun, R. and Yang, J.H. (2005) ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing. Mol. Cell. Biol., 25, 6956-6963.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6956-6963
    • Nie, Y.1    Ding, L.2    Kao, P.N.3    Braun, R.4    Yang, J.H.5
  • 61
    • 84918539112 scopus 로고    scopus 로고
    • Unmasking immune sensing of retroviruses: Interplay between innate sensors and host effectors
    • van Montfoort, N., Olagnier, D. and Hiscott, J. (2014) Unmasking immune sensing of retroviruses: interplay between innate sensors and host effectors. Cytokine Growth Factor Rev., 25, 657-668.
    • (2014) Cytokine Growth Factor Rev. , vol.25 , pp. 657-668
    • Van Montfoort, N.1    Olagnier, D.2    Hiscott, J.3
  • 62
    • 77951984369 scopus 로고    scopus 로고
    • Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus replication
    • Wang, X., Han, Y., Dang, Y., Fu, W., Zhou, T., Ptak, R.G. and Zheng, Y.H. (2010) Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus replication. J. Biol. Chem., 285, 14346-14355.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14346-14355
    • Wang, X.1    Han, Y.2    Dang, Y.3    Fu, W.4    Zhou, T.5    Ptak, R.G.6    Zheng, Y.H.7
  • 65
    • 84924352056 scopus 로고    scopus 로고
    • Genomic analysis of ADAR1 binding and its involvement in multiple RNA processing pathways
    • Bahn, J.H., Ahn, J., Lin, X., Zhang, Q., Lee, J.H., Civelek, M. and Xiao, X. (2015) Genomic analysis of ADAR1 binding and its involvement in multiple RNA processing pathways. Nat. Commun., 6, 6355-6368.
    • (2015) Nat. Commun. , vol.6 , pp. 6355-6368
    • Bahn, J.H.1    Ahn, J.2    Lin, X.3    Zhang, Q.4    Lee, J.H.5    Civelek, M.6    Xiao, X.7
  • 66
    • 77952538520 scopus 로고    scopus 로고
    • Discrete subcellular partitioning of human retrotransposon RNAs despite a common mechanism of genome insertion
    • Goodier, J.L., Mandal, P.K., Zhang, L. and Kazazian, H.H. Jr (2010) Discrete subcellular partitioning of human retrotransposon RNAs despite a common mechanism of genome insertion. Hum. Mol. Genet. 19, 1712-1725.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1712-1725
    • Goodier, J.L.1    Mandal, P.K.2    Zhang, L.3    Kazazian, H.H.4
  • 67
    • 84890045060 scopus 로고    scopus 로고
    • Proteins that contain a functional Z-DNA-binding domain localize to cytoplasmic stress granules
    • Ng, S.K., Weissbach, R., Ronson, G.E. and Scadden, A.D. (2013) Proteins that contain a functional Z-DNA-binding domain localize to cytoplasmic stress granules. Nucleic Acids Res., 41, 9786-9799.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 9786-9799
    • Ng, S.K.1    Weissbach, R.2    Ronson, G.E.3    Scadden, A.D.4
  • 68
    • 84938783916 scopus 로고    scopus 로고
    • SAMHD1 inhibits LINE-1 retrotransposition by promoting stress granule formation
    • Hu, S., Li, J., Xu, F., Mei, S., Le Duff, Y., Yin, L., Pang, X., Cen, S., Jin, Q., Liang, C. et al. (2015) SAMHD1 inhibits LINE-1 retrotransposition by promoting stress granule formation. PLoS Genet., 11, e1005367.
    • (2015) PLoS Genet. , vol.11 , pp. e1005367
    • Hu, S.1    Li, J.2    Xu, F.3    Mei, S.4    Le Duff, Y.5    Yin, L.6    Pang, X.7    Cen, S.8    Jin, Q.9    Liang, C.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.