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Volumn 11, Issue 4, 2012, Pages

Host cell interactome of HIV-1 Rev includes RNA helicases involved in multiple facets of virus production

Author keywords

[No Author keywords available]

Indexed keywords

DEAD BOX PROTEIN; DEAD BOX PROTEIN DDX1; DEAD BOX PROTEIN DDX17; DEAD BOX PROTEIN DDX24; DEAD BOX PROTEIN DDX3X; DEAD BOX PROTEIN DDX47; DEAD BOX PROTEIN DDX5; DEAD BOX PROTEIN DHX36; DEAD BOX PROTEIN DHX9; MESSENGER RNA; REV PROTEIN; RNA HELICASE; UNCLASSIFIED DRUG; REV PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; REV PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS-1; SMALL INTERFERING RNA;

EID: 84859867090     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.015313     Document Type: Article
Times cited : (112)

References (56)
  • 1
    • 1642289565 scopus 로고    scopus 로고
    • HIV-1 and the host cell: An intimate association
    • Freed, E. O. (2004) HIV-1 and the host cell: an intimate association. Trends Microbiol. 12, 170-177
    • (2004) Trends Microbiol. , vol.12 , pp. 170-177
    • Freed, E.O.1
  • 2
    • 79851486019 scopus 로고    scopus 로고
    • Insights into cellular factors that regulate HIV-1 replication in human cells
    • Lever, A. M., and Jeang, K. T. (2011) Insights into cellular factors that regulate HIV-1 replication in human cells. Biochemistry 50, 920-931
    • (2011) Biochemistry , vol.50 , pp. 920-931
    • Lever, A.M.1    Jeang, K.T.2
  • 3
    • 79959211941 scopus 로고    scopus 로고
    • Host factors involved in retroviral budding and release
    • Martin-Serrano, J., and Neil, S. J. (2011) Host factors involved in retroviral budding and release. Nat. Rev. Microbiol. 9, 519-531
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 519-531
    • Martin-Serrano, J.1    Neil, S.J.2
  • 4
    • 0031711593 scopus 로고    scopus 로고
    • HIV-1: Fifteen proteins and an RNA
    • DOI 10.1146/annurev.biochem.67.1.1
    • Frankel, A. D., and Young, J. A. (1998) HIV-1: fifteen proteins and an RNA. Annu. Rev. Biochem. 67, 1-25 (Pubitemid 28411121)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 1-25
    • Frankel, A.D.1    Young, J.A.T.2
  • 5
    • 0031757472 scopus 로고    scopus 로고
    • The HIV-1 Rev protein
    • DOI 10.1146/annurev.micro.52.1.491
    • Pollard, V. W., and Malim, M. H. (1998) The HIV-1 Rev protein. Annu. Rev. Microbiol. 52, 491-532 (Pubitemid 28481200)
    • (1998) Annual Review of Microbiology , vol.52 , pp. 491-532
    • Pollard, V.W.1    Malim, M.H.2
  • 6
    • 0028108364 scopus 로고
    • A molecular rheostat. Co-operative rev binding to stem I of the rev-response element modulates human immunodeficiency virus type-1 late gene expression
    • Mann, D. A., Mikaelian, I., Zemmel, R. W., Green, S. M., Lowe, A. D., Kimura, T., Singh, M., Butler, P. J., Gait, M. J., and Karn, J. (1994) A molecular rheostat. Co-operative rev binding to stem I of the rev-response element modulates human immunodeficiency virus type-1 late gene expression. J. Mol. Biol. 241, 193-207
    • (1994) J. Mol. Biol. , vol.241 , pp. 193-207
    • Mann, D.A.1    Mikaelian, I.2    Zemmel, R.W.3    Green, S.M.4    Lowe, A.D.5    Kimura, T.6    Singh, M.7    Butler, P.J.8    Gait, M.J.9    Karn, J.10
  • 7
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook, A., Bono, F., Jinek, M., and Conti, E. (2007) Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76, 647-671
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 8
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin-beta proteins
    • Xu, D., Farmer, A., and Chook, Y. M. (2010) Recognition of nuclear targeting signals by Karyopherin-beta proteins. Curr. Opin. Struct. Biol. 20, 782-790
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 782-790
    • Xu, D.1    Farmer, A.2    Chook, Y.M.3
  • 9
    • 68949187846 scopus 로고    scopus 로고
    • mRNA nuclear export at a glance
    • Carmody, S. R., and Wente, S. R. (2009) mRNA nuclear export at a glance. J. Cell Sci. 122, 1933-1937
    • (2009) J. Cell Sci. , vol.122 , pp. 1933-1937
    • Carmody, S.R.1    Wente, S.R.2
  • 10
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: Insights from virology
    • Cullen, B. R. (2003) Nuclear mRNA export: insights from virology. Trends Biochem. Sci. 28, 419-424
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 419-424
    • Cullen, B.R.1
  • 11
    • 0026591789 scopus 로고
    • The Rev protein of human immunodeficiency virus type 1 promotes polysomal association and translation of gag/pol and vpu/env mRNAs
    • D'Agostino, D. M., Felber, B. K., Harrison, J. E., and Pavlakis, G. N. (1992) The Rev protein of human immunodeficiency virus type 1 promotes polysomal association and translation of gag/pol and vpu/env mRNAs. Mol. Cell Biol. 12, 1375-1386
    • (1992) Mol. Cell Biol. , vol.12 , pp. 1375-1386
    • D'Agostino, D.M.1    Felber, B.K.2    Harrison, J.E.3    Pavlakis, G.N.4
  • 12
    • 67449087214 scopus 로고    scopus 로고
    • Rev regulates translation of human immunodeficiency virus type 1 RNAs
    • Groom, H. C., Anderson, E. C., Dangerfield, J. A., and Lever, A. M. (2009) Rev regulates translation of human immunodeficiency virus type 1 RNAs. J. Gen. Virol. 90, 1141-1147
    • (2009) J. Gen. Virol. , vol.90 , pp. 1141-1147
    • Groom, H.C.1    Anderson, E.C.2    Dangerfield, J.A.3    Lever, A.M.4
  • 15
    • 9644289433 scopus 로고    scopus 로고
    • A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev
    • DOI 10.1016/j.virol.2004.09.039, PII S0042682204006452
    • Fang, J., Kubota, S., Yang, B., Zhou, N., Zhang, H., Godbout, R., and Pomerantz, R. J. (2004) A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev. Virology 330, 471-480 (Pubitemid 39572852)
    • (2004) Virology , vol.330 , Issue.2 , pp. 471-480
    • Fang, J.1    Kubota, S.2    Yang, B.3    Zhou, N.4    Zhang, H.5    Godbout, R.6    Pomerantz, R.J.7
  • 16
    • 7044253474 scopus 로고    scopus 로고
    • Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function
    • DOI 10.1016/j.cell.2004.09.029, PII S0092867404008360
    • Yedavalli, V. S., Neuveut, C., Chi, Y. H., Kleiman, L., and Jeang, K. T. (2004) Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function. Cell 119, 381-392 (Pubitemid 39423840)
    • (2004) Cell , vol.119 , Issue.3 , pp. 381-392
    • Yedavalli, V.S.R.K.1    Neuveut, C.2    Chi, Y.-H.3    Kleiman, L.4    Jeang, K.-T.5
  • 17
    • 34547211817 scopus 로고    scopus 로고
    • The Long Unwinding Road of RNA Helicases
    • DOI 10.1016/j.molcel.2007.07.014, PII S109727650700487X
    • Bleichert, F., and Baserga, S. J. (2007) The long unwinding road of RNA helicases. Mol. Cell 27, 339-352 (Pubitemid 47126943)
    • (2007) Molecular Cell , vol.27 , Issue.3 , pp. 339-352
    • Bleichert, F.1    Baserga, S.J.2
  • 18
    • 78650854687 scopus 로고    scopus 로고
    • RNA helicases at work: Binding and rearranging
    • Jankowsky, E. (2010) RNA helicases at work: binding and rearranging. Trends Biochem. Sci. 36, 19-29
    • (2010) Trends Biochem. Sci. , vol.36 , pp. 19-29
    • Jankowsky, E.1
  • 20
    • 39549100997 scopus 로고    scopus 로고
    • Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes
    • DOI 10.1110/ps.073246608
    • Edgcomb, S. P., Aschrafi, A., Kompfner, E., Williamson, J. R., Gerace, L., and Hennig, M. (2008) Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes. Protein Sci. 17, 420-430 (Pubitemid 351281542)
    • (2008) Protein Science , vol.17 , Issue.3 , pp. 420-430
    • Edgcomb, S.P.1    Aschrafi, A.2    Kompfner, E.3    Williamson, J.R.4    Gerace, L.5    Hennig, M.6
  • 21
    • 60349118158 scopus 로고    scopus 로고
    • Reconstitution of nuclear import in permeabilized cells
    • Cassany, A., and Gerace, L. (2009) Reconstitution of nuclear import in permeabilized cells. Methods Mol. Biol. 464, 181-205
    • (2009) Methods Mol. Biol. , vol.464 , pp. 181-205
    • Cassany, A.1    Gerace, L.2
  • 22
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983) Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res.11, 1475-1489
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 23
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn, M. P., Wolters, D., and Yates, J. R., 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 25
    • 0043064042 scopus 로고    scopus 로고
    • A hypergeometric probability model for protein identification and validation using tandem mass spectral data and protein sequence databases
    • DOI 10.1021/ac034157w
    • Sadygov, R. G., and Yates, J. R., 3rd (2003) A hypergeometric probability model for protein identification and validation using tandem mass spectral data and protein sequence databases. Anal. Chem. 75, 3792-3798 (Pubitemid 36962113)
    • (2003) Analytical Chemistry , vol.75 , Issue.15 , pp. 3792-3798
    • Sadygov, R.G.1    Yates III, J.R.2
  • 26
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R., 3rd, Eng, J. K., McCormack, A. L., and Schieltz, D. (1995) Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 67, 1426-1436
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 27
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, W. H., and Yates, J. R., 3rd (2002) DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1, 21-26
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 28
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • DOI 10.1021/ac0498563
    • Liu, H., Sadygov, R. G., and Yates, J. R., 3rd (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201 (Pubitemid 38943698)
    • (2004) Analytical Chemistry , vol.76 , Issue.14 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 30
    • 84890885963 scopus 로고    scopus 로고
    • Modular Toolkit for Data Processing (MDP): A Python Data Processing Framework
    • Zito, T., Wilbert, N., Wiskott, L., and Berkes, P. (2008) Modular Toolkit for Data Processing (MDP): A Python Data Processing Framework. Frontiers Neuroinformatics 2, 8
    • (2008) Frontiers Neuroinformatics , vol.2 , pp. 8
    • Zito, T.1    Wilbert, N.2    Wiskott, L.3    Berkes, P.4
  • 34
    • 0030041884 scopus 로고    scopus 로고
    • Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E
    • DOI 10.1073/pnas.93.3.1065
    • Rousseau, D., Kaspar, R., Rosenwald, I., Gehrke, L., and Sonenberg, N. (1996) Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E. Proc. Natl. Acad. Sci. U. S. A. 93, 1065-1070 (Pubitemid 26054368)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.3 , pp. 1065-1070
    • Rousseau, D.1    Kaspar, R.2    Rosenwald, I.3    Gehrke, L.4    Sonenberg, N.5
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • -DeltaDeltaCT method
    • DOI 10.1006/meth.2001.1262
    • Livak, K. J., and Schmittgen, T. D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25, 402-408 (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 36
    • 52049106911 scopus 로고    scopus 로고
    • A solution to limited genomic capacity: Using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA
    • Daugherty, M. D., D'Orso, I., and Frankel, A. D. (2008) A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. Mol. Cell 31, 824-834
    • (2008) Mol. Cell , vol.31 , pp. 824-834
    • Daugherty, M.D.1    D'Orso, I.2    Frankel, A.D.3
  • 37
    • 0032911885 scopus 로고    scopus 로고
    • The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals
    • Truant, R., and Cullen, B. R. (1999) The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals. Mol. Cell Biol. 19, 1210-1217 (Pubitemid 29046863)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.2 , pp. 1210-1217
    • Truant, R.1    Cullen, B.R.2
  • 38
    • 39349097864 scopus 로고    scopus 로고
    • Identification of host proteins required for HIV infection through a functional genomic screen
    • DOI 10.1126/science.1152725
    • Brass, A. L., Dykxhoorn, D. M., Benita, Y., Yan, N., Engelman, A., Xavier, R. J., Lieberman, J., and Elledge, S. J. (2008) Identification of host proteins required for HIV infection through a functional genomic screen. Science 319, 921-926 (Pubitemid 351263756)
    • (2008) Science , vol.319 , Issue.5865 , pp. 921-926
    • Brass, A.L.1    Dykxhoorn, D.M.2    Benita, Y.3    Yan, N.4    Engelman, A.5    Xavier, R.J.6    Lieberman, J.7    Elledge, S.J.8
  • 39
    • 67749148923 scopus 로고    scopus 로고
    • A genome-wide short hairpin RNA screening of jurkat T-cells for human proteins contributing to productive HIV-1 replication
    • Yeung, M. L., Houzet, L., Yedavalli, V. S., and Jeang, K. T. (2009) A genome-wide short hairpin RNA screening of jurkat T-cells for human proteins contributing to productive HIV-1 replication. J. Biol. Chem. 284, 19463-19473
    • (2009) J. Biol. Chem. , vol.284 , pp. 19463-19473
    • Yeung, M.L.1    Houzet, L.2    Yedavalli, V.S.3    Jeang, K.T.4
  • 42
    • 18144430655 scopus 로고    scopus 로고
    • Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication
    • Krishnan, V., and Zeichner, S. L. (2004) Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication. Retrovirology 1, 42
    • (2004) Retrovirology , vol.1 , pp. 42
    • Krishnan, V.1    Zeichner, S.L.2
  • 43
    • 77950493743 scopus 로고    scopus 로고
    • RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions
    • Bolinger, C., Sharma, A., Singh, D., Yu, L., and Boris-Lawrie, K. (2010) RNA helicase A modulates translation of HIV-1 and infectivity of progeny virions. Nucleic Acids Res. 38, 1686-1696
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1686-1696
    • Bolinger, C.1    Sharma, A.2    Singh, D.3    Yu, L.4    Boris-Lawrie, K.5
  • 44
    • 42749092275 scopus 로고    scopus 로고
    • The requirement of the DEAD-box protein DDX24 for the packaging of human immunodeficiency virus type 1 RNA
    • Ma, J., Rong, L., Zhou, Y., Roy, B. B., Lu, J., Abrahamyan, L., Mouland, A. J., Pan, Q., and Liang, C. (2008) The requirement of the DEAD-box protein DDX24 for the packaging of human immunodeficiency virus type 1 RNA. Virology 375, 253-264
    • (2008) Virology , vol.375 , pp. 253-264
    • Ma, J.1    Rong, L.2    Zhou, Y.3    Roy, B.B.4    Lu, J.5    Abrahamyan, L.6    Mouland, A.J.7    Pan, Q.8    Liang, C.9
  • 45
    • 0034759926 scopus 로고    scopus 로고
    • A new RNA element located in the coding region of a murine endogenous retrovirus can functionally replace the Rev/Rev-responsive element system in human immunodeficiency virus type 1 Gag expression
    • DOI 10.1128/JVI.75.22.10670-10682.2001
    • Wodrich, H., Bohne, J., Gumz, E., Welker, R., and Krausslich, H. G. (2001) A new RNA element located in the coding region of a murine endogenous retrovirus can functionally replace the Rev/Rev-responsive element system in human immunodeficiency virus type 1 Gag expression. J. Virol. 75, 10670-10682 (Pubitemid 33031537)
    • (2001) Journal of Virology , vol.75 , Issue.22 , pp. 10670-10682
    • Wodrich, H.1    Bohne, J.2    Ellen, G.3    Welker, R.4    Krausslich, H.-G.5
  • 47
    • 79959344720 scopus 로고    scopus 로고
    • DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule TRIF to sense dsRNA in dendritic cells
    • Zhang, Z., Kim, T., Bao, M., Facchinetti, V., Jung, S. Y., Ghaffari, A. A., Qin, J., Cheng, G., and Liu, Y. J. (2011) DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule TRIF to sense dsRNA in dendritic cells. Immunity 34, 866-878
    • (2011) Immunity , vol.34 , pp. 866-878
    • Zhang, Z.1    Kim, T.2    Bao, M.3    Facchinetti, V.4    Jung, S.Y.5    Ghaffari, A.A.6    Qin, J.7    Cheng, G.8    Liu, Y.J.9
  • 48
    • 0030836217 scopus 로고    scopus 로고
    • Site-specific phosphorylation of the human immunodeficiency virus type- 1 Rev protein accelerates formation of an efficient RNA-binding conformation
    • DOI 10.1021/bi971551d
    • Fouts, D. E., True, H. L., Cengel, K. A., and Celander, D. W. (1997) Site-specific phosphorylation of the human immunodeficiency virus type-1 Rev protein accelerates formation of an efficient RNA-binding conformation. Biochemistry 36, 13256-13262 (Pubitemid 27473371)
    • (1997) Biochemistry , vol.36 , Issue.43 , pp. 13256-13262
    • Fouts, D.E.1    True, H.L.2    Cengel, K.A.3    Celander, D.W.4
  • 51
    • 49549088852 scopus 로고    scopus 로고
    • Gle1 does double duty
    • Kutay, U., and Panse, V. G. (2008) Gle1 does double duty. Cell 134, 564-566
    • (2008) Cell , vol.134 , pp. 564-566
    • Kutay, U.1    Panse, V.G.2
  • 52
    • 33749134437 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: Multifunctional proteins with important roles in transcriptional regulation
    • Fuller-Pace, F. V. (2006) DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res. 34, 4206-4215
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4206-4215
    • Fuller-Pace, F.V.1
  • 53
    • 69249217936 scopus 로고    scopus 로고
    • Matrix mediates the functional link between human immunodeficiency virus type 1 RNA nuclear export elements and the assembly competency of Gag in murine cells
    • Sherer, N. M., Swanson, C. M., Papaioannou, S., and Malim, M. H. (2009) Matrix mediates the functional link between human immunodeficiency virus type 1 RNA nuclear export elements and the assembly competency of Gag in murine cells. J. Virol. 83, 8525-8535
    • (2009) J. Virol. , vol.83 , pp. 8525-8535
    • Sherer, N.M.1    Swanson, C.M.2    Papaioannou, S.3    Malim, M.H.4
  • 55
    • 71749110698 scopus 로고    scopus 로고
    • P68 RNA helicase is a nucleocytoplasmic shuttling protein
    • Wang, H., Gao, X., Huang, Y., Yang, J., and Liu, Z. R. (2009) P68 RNA helicase is a nucleocytoplasmic shuttling protein. Cell Res. 19, 1388-1400
    • (2009) Cell Res. , vol.19 , pp. 1388-1400
    • Wang, H.1    Gao, X.2    Huang, Y.3    Yang, J.4    Liu, Z.R.5
  • 56
    • 0032910359 scopus 로고    scopus 로고
    • The carboxyl terminus of RNA helicase a contains a bidirectional nuclear transport domain
    • Tang, H., McDonald, D., Middlesworth, T., Hope, T. J., and Wong-Staal, F. (1999) The carboxyl terminus of RNA helicase A contains a bidirectional nuclear transport domain. Mol. Cell. Biol. 19, 3540-3550 (Pubitemid 29193813)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.5 , pp. 3540-3550
    • Tang, H.1    McDonald, D.2    Middlesworth, T.3    Hope, T.J.4    Wong-Staal, F.5


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