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Volumn 8, Issue 2, 2011, Pages

Identification of protein partners of the human immunodeficiency virus 1 tat/rev exon 3 leads to the discovery of a new HIV-1 splicing regulator, protein hnRNP K

Author keywords

hnRNP K; Mass spectrometry; Nucleolin; RNP affinity chromatography; Splicing regulation; Virus HIV 1

Indexed keywords

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; DNA BINDING PROTEIN; DNA TOPOISOMERASE (ATP HYDROLYSING); ELONGATION FACTOR 1ALPHA; GLYCOGEN PHOSPHORYLASE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A3; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D0; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN Q; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U; HNRNP A1; HNRNP K PROTEIN; INTERLEUKIN ENHANCER BINDING FACTOR 2; INTERLEUKIN ENHANCER BINDING FACTOR 3; KARYOPHERIN; NEF PROTEIN; NUCLEOLIN; NUCLEOPHOSMIN; RAN PROTEIN; REV PROTEIN; RNA HELICASE; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UNINDEXED DRUG; VIRUS PROTEIN; VIRUS RNA; PHOSPHOPROTEIN; RNA BINDING PROTEIN; RNA PRECURSOR;

EID: 79954475530     PISSN: 15476286     EISSN: 15558584     Source Type: Journal    
DOI: 10.4161/rna/8.2.13984     Document Type: Article
Times cited : (37)

References (72)
  • 1
    • 0027494083 scopus 로고
    • Alternative splicing of human immunodeficiency virus type 1 mRNA modulates viral protein expression, replication, and infectivity
    • Purcell DF, Martin MA. Alternative splicing of human immunodeficiency virus type 1 mRNA modulates viral protein expression, replication and infectivity. J Virol 1993; 67:6365-78. (Pubitemid 23309100)
    • (1993) Journal of Virology , vol.67 , Issue.11 , pp. 6365-6378
    • Purcell, D.F.J.1    Martin, M.A.2
  • 2
    • 68649095173 scopus 로고    scopus 로고
    • Chapter 1. Regulation of HIV-1 alternative RNA splicing and its role in virus replication
    • Stoltzfus MC. Chapter 1. Regulation of HIV-1 alternative RNA splicing and its role in virus replication. Adv Virus Res 2009; 74:1-40.
    • (2009) Adv Virus Res , vol.74 , pp. 1-40
    • Stoltzfus, M.C.1
  • 3
    • 34848881569 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional regulation of HIV-1 gene expression: Role of cellular factors for Tat and Rev
    • Nekhai S, Jeang KT. Transcriptional and post-transcriptional regulation of HIV-1 gene expression: role of cellular factors for Tat and Rev. Future Microbiol 2006; 1:417-26.
    • (2006) Future Microbiol , vol.1 , pp. 417-426
    • Nekhai, S.1    Jeang, K.T.2
  • 4
    • 0032577444 scopus 로고    scopus 로고
    • HIV-1 auxiliary proteins: Making connections in a dying cell
    • DOI 10.1016/S0092-8674(00)81431-2
    • Cullen BR. HIV-1 auxiliary proteins: making connections in a dying cell. Cell 1998; 93:685-92. (Pubitemid 28257576)
    • (1998) Cell , vol.93 , Issue.5 , pp. 685-692
    • Cullen, B.R.1
  • 5
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: Insights from virology
    • DOI 10.1016/S0968-0004(03)00142-7
    • Cullen BR. Nuclear mRNA export: insights from virology. Trends Biochem Sci 2003; 28:419-24. (Pubitemid 36976744)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.8 , pp. 419-424
    • Cullen, B.R.1
  • 6
    • 0029062573 scopus 로고
    • Induction of apoptosis in uninfected lymphocytes by HIV-1 Tat protein
    • Li CJ, Friedman DJ, Wang C, Metelev V, Pardee AB. Induction of apoptosis in uninfected lymphocytes by HIV-1 Tat protein. Science 1995; 268:429-31.
    • (1995) Science , vol.268 , pp. 429-431
    • Li, C.J.1    Friedman, D.J.2    Wang, C.3    Metelev, V.4    Pardee, A.B.5
  • 7
    • 0035798607 scopus 로고    scopus 로고
    • A second exon splicing silencer within human immunodeficiency virus type 1 tat exon 2 represses splicing of Tat mRNA and binds protein hnRNP H
    • Jacquenet S, Mereau A, Bilodeau PS, Damier L, Stoltzfus CM, Branlant C. A second exon splicing silencer within human immunodeficiency virus type 1 tat exon 2 represses splicing of Tat mRNA and binds protein hnRNP H. J Biol Chem 2001; 276:40464-75.
    • (2001) J Biol Chem , vol.276 , pp. 40464-40475
    • Jacquenet, S.1    Mereau, A.2    Bilodeau, P.S.3    Damier, L.4    Stoltzfus, C.M.5    Branlant, C.6
  • 8
    • 0036974666 scopus 로고    scopus 로고
    • A Janus splicing regulatory element modulates HIV-1 tat and rev mRNA production by coordination of hnRNP A1 cooperative binding
    • DOI 10.1016/S0022-2836(02)00967-1
    • Marchand V, Mereau A, Jacquenet S, Thomas D, Mougin A, Gattoni R, et al. A Janus splicing regulatory element modulates HIV-1 tat and rev mRNA production by coordination of hnRNP A1 cooperative binding. J Mol Biol 2002; 323:629-52. (Pubitemid 36160221)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.4 , pp. 629-652
    • Marchand, V.1    Mereau, A.2    Jacquenet, S.3    Thomas, D.4    Mougin, A.5    Gattoni, R.6    Stevenin, J.7    Branlant, C.8
  • 9
    • 33845993932 scopus 로고    scopus 로고
    • Biochemical and NMR study on the competition between proteins SC35, SRp40, and heterogeneous nuclear ribonucleoprotein A1 at the HIV-1 Tat exon 2 splicing site
    • DOI 10.1074/jbc.M603864200
    • Hallay H, Locker N, Ayadi L, Ropers D, Guittet E, Branlant C. Biochemical and NMR study on the competition between proteins SC35, SRp40 and heterogeneous nuclear ribonucleoprotein A1 at the HIV-1 Tat exon 2 splicing site. J Biol Chem 2006; 281:37159-74. (Pubitemid 46042186)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 37159-37174
    • Hallay, H.1    Locker, N.2    Ayadi, L.3    Ropers, D.4    Guittet, E.5    Branlant, C.6
  • 10
    • 0028999992 scopus 로고
    • Identification of positive and negative splicing regulatory elements within the terminal tat-rev exon of human immunodeficiency virus type 1
    • Staffa A, Cochrane A. Identification of positive and negative splicing regulatory elements within the terminal tat-rev exon of human immunodeficiency virus type 1. Mol Cell Biol 1995; 15:4597-605.
    • (1995) Mol Cell Biol , vol.15 , pp. 4597-4605
    • Staffa, A.1    Cochrane, A.2
  • 11
    • 0031841948 scopus 로고    scopus 로고
    • The exon splicing silencer in human immunodeficiency virus type 1 tat exon 3 is bipartite and acts early in spliceosome assembly
    • Si ZH, Rauch D, Stoltzfus CM. The exon splicing silencer in human immunodeficiency virus type 1 Tat exon 3 is bipartite and acts early in spliceosome assembly. Mol Cell Biol 1998; 18:5404-13. (Pubitemid 28388123)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.9 , pp. 5404-5413
    • Si, Z.-H.1    Rauch, D.2    Martin, S.C.3
  • 12
    • 0036849108 scopus 로고    scopus 로고
    • HnRNP A1 controls HIV-1 mRNA splicing through cooperative binding to intron and exon splicing silencers in the context of a conserved secondary structure
    • DOI 10.1017/S1355838202023075
    • Damgaard CK, Tange TO, Kjems J. hnRNP A1 controls HIV-1 mRNA splicing through cooperative binding to intron and exon splicing silencers in the context of a conserved secondary structure. RNA 2002; 8:1401-15. (Pubitemid 35332964)
    • (2002) RNA , vol.8 , Issue.11 , pp. 1401-1415
    • Damgaard, C.K.1    Tange, T.O.2    Kjems, J.3
  • 13
    • 0035886048 scopus 로고    scopus 로고
    • The hnRNP A1 protein regulates HIV-1 tat splicing via a novel intron silencer element
    • DOI 10.1093/emboj/20.20.5748
    • Tange TO, Damgaard CK, Guth S, Valcarcel J, Kjems J. The hnRNP A1 protein regulates HIV-1 tat splicing via a novel intron silencer element. EMBO J 2001; 20:5748-58. (Pubitemid 33014352)
    • (2001) EMBO Journal , vol.20 , Issue.20 , pp. 5748-5758
    • Tange, T.O.1    Damgaard, C.K.2    Guth, S.3    Valcarcel, J.4    Kjems, J.5
  • 14
    • 0033565285 scopus 로고    scopus 로고
    • HnRNP A/B proteins are required for inhibition of HIV-1 pre-mRNA splicing
    • DOI 10.1093/emboj/18.14.4060
    • Caputi M, Mayeda A, Krainer AR, Zahler AM. hnRNP A/B proteins are required for inhibition of HIV-1 premRNA splicing. EMBO J 1999; 18:4060-7. (Pubitemid 29335858)
    • (1999) EMBO Journal , vol.18 , Issue.14 , pp. 4060-4067
    • Caputi, M.1    Mayeda, A.2    Krainer, A.R.3    Zahler, A.M.4
  • 15
    • 0035691667 scopus 로고    scopus 로고
    • Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins
    • DOI 10.1016/S1097-2765(01)00409-9
    • Zhu J, Mayeda A, Krainer AR. Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins. Mol Cell 2001; 8:1351-61. (Pubitemid 34086947)
    • (2001) Molecular Cell , vol.8 , Issue.6 , pp. 1351-1361
    • Zhu, J.1    Mayeda, A.2    Krainer, A.R.3
  • 16
    • 58149502545 scopus 로고    scopus 로고
    • Role of cellular RNA processing factors in human immunodeficiency virus type 1 mRNA metabolism, replication and infectivity
    • Jablonski JA, Caputi M. Role of cellular RNA processing factors in human immunodeficiency virus type 1 mRNA metabolism, replication and infectivity. J Virol 2009; 83:981-92.
    • (2009) J Virol , vol.83 , pp. 981-992
    • Jablonski, J.A.1    Caputi, M.2
  • 18
    • 0035965130 scopus 로고    scopus 로고
    • SF2/ASF binds to a splicing enhancer in the third HIV-1 tat exon and stimulates U2AF binding independently of the RS domain
    • DOI 10.1006/jmbi.2001.4971
    • Tange TO, Kjems J. SF2/ASF binds to a splicing enhancer in the third HIV-1 tat exon and stimulates U2AF binding independently of the RS domain. J Mol Biol 2001; 312:649-62. (Pubitemid 33120935)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.4 , pp. 649-662
    • Tange, T.O.1    Kjems, J.2
  • 19
    • 0033013977 scopus 로고    scopus 로고
    • Substrate specificities of SR proteins in constitutive splicing are determined by their RNA recognition motifs and composite pre-mRNA exonic elements
    • Mayeda A, Screaton GR, Chandler SD, Fu XD, Krainer AR. Substrate specificities of SR proteins in constitutive splicing are determined by their RNA recognition motifs and composite pre-mRNA exonic elements. Mol Cell Biol 1999; 19:1853-63.
    • (1999) Mol Cell Biol , vol.19 , pp. 1853-1863
    • Mayeda, A.1    Screaton, G.R.2    Chandler, S.D.3    Fu, X.D.4    Krainer, A.R.5
  • 20
    • 70350433635 scopus 로고    scopus 로고
    • Cooperative-binding and splicing-repressive properties of hnRNP A1
    • Okunola HL, Krainer AR. Cooperative-binding and splicing-repressive properties of hnRNP A1. Mol Cell Biol 2009; 29:5620-31.
    • (2009) Mol Cell Biol , vol.29 , pp. 5620-5631
    • Okunola, H.L.1    Krainer, A.R.2
  • 21
    • 34248212743 scopus 로고    scopus 로고
    • hnRNP E1 and E2 have distinct roles in modulating HIV-1 gene expression
    • Woolaway K, Asai K, Emili A, Cochrane A. hnRNP E1 and E2 have distinct roles in modulating HIV-1 gene expression. Retrovirology 2007; 4:28.
    • (2007) Retrovirology , vol.4 , pp. 28
    • Woolaway, K.1    Asai, K.2    Emili, A.3    Cochrane, A.4
  • 24
    • 0036242097 scopus 로고    scopus 로고
    • Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis
    • DOI 10.1017/S1355838202021088
    • Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ. Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA 2002; 8:426-39. (Pubitemid 34437714)
    • (2002) RNA , vol.8 , Issue.4 , pp. 426-439
    • Jurica, M.S.1    Licklider, L.J.2    Gygi, S.P.3    Grigorieff, N.4    Moore, M.J.5
  • 26
    • 0032512419 scopus 로고    scopus 로고
    • Minimal RNA constructs that specifically bind aminoglycoside antibiotics with high affinities
    • DOI 10.1021/bi971095t
    • Hamasaki K, Killian J, Cho J, Rando RR. Minimal RNA constructs that specifically bind aminoglycoside antibiotics with high affinities. Biochemistry 1998; 37:656-63. (Pubitemid 28123799)
    • (1998) Biochemistry , vol.37 , Issue.2 , pp. 656-663
    • Hamasaki, K.1    Killian, J.2    Cho, J.3    Rando, R.R.4
  • 27
    • 33846681638 scopus 로고    scopus 로고
    • Nucleolin: A multiFACeTed protein
    • DOI 10.1016/j.tcb.2006.11.010, PII S0962892406003370
    • Mongelard F, Bouvet P. Nucleolin: a multiFACeTed protein. Trends Cell Biol 2007; 17:80-6. (Pubitemid 46199181)
    • (2007) Trends in Cell Biology , vol.17 , Issue.2 , pp. 80-86
    • Mongelard, F.1    Bouvet, P.2
  • 28
    • 0034672094 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin
    • DOI 10.1093/emboj/19.24.6870
    • Allain FH, Bouvet P, Dieckmann T, Feigon J. Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin. EMBO J 2000; 19:6870-81. (Pubitemid 32011680)
    • (2000) EMBO Journal , vol.19 , Issue.24 , pp. 6870-6881
    • Allain, F.H.-T.1    Bouvet, P.2    Dieckmann, T.3    Feigon, J.4
  • 29
    • 2942623743 scopus 로고    scopus 로고
    • HnRNP K: One protein multiple processes
    • DOI 10.1002/bies.20048
    • Bomsztyk K, Denisenko O, Ostrowski J. hnRNP K: one protein multiple processes. Bioessays 2004; 26:629-38. (Pubitemid 38758340)
    • (2004) BioEssays , vol.26 , Issue.6 , pp. 629-638
    • Bomsztyk, K.1    Denisenko, O.2    Ostrowski, J.3
  • 30
  • 31
    • 34250313662 scopus 로고    scopus 로고
    • Members of the heterogeneous nuclear ribonucleoprotein H family activate splicing of an HIV-1 splicing substrate by promoting formation of ATP-dependent spliceosomal complexes
    • DOI 10.1074/jbc.M700774200
    • Schaub MC, Lopez SR, Caputi M. Members of the heterogeneous nuclear ribonucleoprotein H family activate splicing of an HIV-1 splicing substrate by promoting formation of ATP-dependent spliceosomal complexes. J Biol Chem 2007; 282:13617-26. (Pubitemid 47100498)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.18 , pp. 13617-13626
    • Schaub, M.C.1    Lopez, S.R.2    Caputi, M.3
  • 33
  • 34
    • 0035957922 scopus 로고    scopus 로고
    • Two different combinations of RNA-binding domains determine the RNA binding specificity of nucleolin
    • Ginisty H, Amalric F, Bouvet P. Two different combinations of RNA-binding domains determine the RNA binding specificity of nucleolin. J Biol Chem 2001; 276:14338-43.
    • (2001) J Biol Chem , vol.276 , pp. 14338-14343
    • Ginisty, H.1    Amalric, F.2    Bouvet, P.3
  • 36
    • 0035863847 scopus 로고    scopus 로고
    • Conserved stem-loop structures in the HIV-1 RNA region containing the A3 3′ splice site and its cis-regulatory element: Possible involvement in RNA splicing
    • Jacquenet S, Ropers D, Bilodeau PS, Damier L, Mougin A, Stoltzfus CM, Branlant C. Conserved stem-loop structures in the HIV-1 RNA region containing the A3 3′ splice site and its cis-regulatory element: possible involvement in RNA splicing. Nucl Acids Res 2001; 29:464-78. (Pubitemid 32060933)
    • (2001) Nucleic Acids Research , vol.29 , Issue.2 , pp. 464-478
    • Jacquenet, S.1    Ropers, D.2    Bilodeau, P.S.3    Damier, L.4    Mougin, A.5    Stoltzfus, C.M.6    Branlant, C.7
  • 37
    • 0035941211 scopus 로고    scopus 로고
    • Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H′/F/2H9 family
    • Caputi M, Zahler AM. Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H′/F/2H9 family. J Biol Chem 2001; 276:43850-9.
    • (2001) J Biol Chem , vol.276 , pp. 43850-43859
    • Caputi, M.1    Zahler, A.M.2
  • 38
    • 0037053297 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken beta-tropomyosin pre-mRNA
    • DOI 10.1074/jbc.M201083200
    • Expert-Bezançon A, Le Caer JP, Marie J. Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken beta-tropomyosin pre-mRNA. J Biol Chem 2002; 277:16614-23. (Pubitemid 34967679)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16614-16623
    • Expert-Bezancon, A.1    Caer, J.P.L.2    Marie, J.3
  • 39
    • 3142713701 scopus 로고    scopus 로고
    • Differential effects of the SR proteins 9G8, SC35, ASF/SF2, and SRp40 on the utilization of the A1 to A5 splicing sites of HIV-1 RNA
    • DOI 10.1074/jbc.M404452200
    • Ropers D, Ayadi L, Gattoni R, Jacquenet S, Damier L, Branlant C, Stevenin J. Differential effects of the SR proteins 9G8, SC35, ASF/SF2 and SRp40 on the utilization of the A1 to A5 splicing sites of HIV-1 RNA. J Biol Chem 2004; 279:29963-73. (Pubitemid 38937916)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 29963-29973
    • Ropers, D.1    Ayadi, L.2    Gattoni, R.3    Jacquenet, S.4    Damier, L.5    Branlant, C.6    Stevenin, J.7
  • 40
    • 27444437305 scopus 로고    scopus 로고
    • Dual effect of the SR proteins ASF/SF2, SC35 and 9G8 on HIV-1 RNA splicing and virion production
    • Jacquenet S, Decimo D, Muriaux D, Darlix JL. Dual effect of the SR proteins ASF/SF2, SC35 and 9G8 on HIV-1 RNA splicing and virion production. Retrovirology 2005; 2:33.
    • (2005) Retrovirology , vol.2 , pp. 33
    • Jacquenet, S.1    Decimo, D.2    Muriaux, D.3    Darlix, J.L.4
  • 41
    • 0034705373 scopus 로고    scopus 로고
    • Interaction of nucleolin with an evolutionarily conserved pre-ribosomal RNA sequence is required for the assembly of the primary processing complex
    • DOI 10.1074/jbc.M002350200
    • Ginisty H, Serin G, Ghisolfi-Nieto L, Roger B, Libante V, Amalric F, Bouvet P. Interaction of nucleolin with an evolutionarily conserved pre-ribosomal RNA sequence is required for the assembly of the primary processing complex. J Biol Chem 2000; 275:18845-50. (Pubitemid 30422847)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 18845-18850
    • Ginisty, H.1    Serin, G.2    Ghisolfi-Nieto, L.3    Roger, B.4    Libante, V.5    Amalric, F.6    Bouvet, P.7
  • 42
    • 2642554747 scopus 로고    scopus 로고
    • Contributions of the RNA-binding and linker domains and RNA structure to the specificity and affinity of the nucleolin RBD12/NRE interaction
    • DOI 10.1021/bi049904d
    • Finger LD, Johansson C, Rinaldi B, Bouvet P, Feigon J. Contributions of the RNA-binding and linker domains and RNA structure to the specificity and affinity of the nucleolin RBD12/NRE interaction. Biochemistry 2004; 43:6937-47. (Pubitemid 38720512)
    • (2004) Biochemistry , vol.43 , Issue.22 , pp. 6937-6947
    • Finger, L.D.1    Johansson, C.2    Rinaldi, B.3    Bouvet, P.4    Feigon, J.5
  • 44
    • 0036354940 scopus 로고    scopus 로고
    • Anchorage of HIV on permissive cells leads to coaggregation of viral particles with surface nucleolin at membrane raft microdomains
    • DOI 10.1006/excr.2002.5522
    • Nisole S, Krust B, Hovanessian AG. Anchorage of HIV on permissive cells leads to coaggregation of viral particles with surface nucleolin at membrane raft microdomains. Exp Cell Res 2002; 276:155-73. (Pubitemid 34969310)
    • (2002) Experimental Cell Research , vol.276 , Issue.2 , pp. 155-173
    • Nisole, S.1    Krust, B.2    Hovanessian, A.G.3
  • 45
    • 0025141758 scopus 로고
    • Identification of sequences important in the nucleolar localization human immunodeficiency virus Rev: Relevance of nucleolar localization to function
    • Cochrane AW, Perkins A, Rosen CA. Identification of sequences important in the nucleolar localization of human immunodeficiency virus Rev: relevance of nucleolar localization to function. J Virol 1990; 64:881-5. (Pubitemid 20032706)
    • (1990) Journal of Virology , vol.64 , Issue.2 , pp. 881-885
    • Cochrane, A.W.1    Perkins, A.2    Rosen, C.A.3
  • 47
    • 0034468319 scopus 로고    scopus 로고
    • The carboxy-terminal fragment of nucleolin interacts with the nucleocapsid domain of retroviral Gag proteins and inhibits virion assembly
    • DOI 10.1128/JVI.74.23.11027-11039.2000
    • Bacharach E, Gonsky J, Alin K, Orlova M, Goff SP. The carboxy-terminal fragment of nucleolin interacts with the nucleocapsid domain of retroviral gag proteins and inhibits virion assembly. J Virol 2000; 74:11027-39. (Pubitemid 32223968)
    • (2000) Journal of Virology , vol.74 , Issue.23 , pp. 11027-11039
    • Bacharach, E.1    Gonsky, J.2    Alin, K.3    Orlova, M.4    Goff, S.P.5
  • 52
    • 77953015118 scopus 로고    scopus 로고
    • Analysis of the RNA helicase p68 (Ddx5) as a transcriptional regulator
    • Nicol SM, Fuller-Pace FV. Analysis of the RNA helicase p68 (Ddx5) as a transcriptional regulator. Methods Mol Biol 2010; 587:265-79.
    • (2010) Methods Mol Biol , vol.587 , pp. 265-279
    • Nicol, S.M.1    Fuller-Pace, F.V.2
  • 53
    • 0034607554 scopus 로고    scopus 로고
    • Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm
    • Kim JH, Hahm B, Kim YK, Choi M, Jang SK. Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm. J Mol Biol 2000; 298:395-405.
    • (2000) J Mol Biol , vol.298 , pp. 395-405
    • Kim, J.H.1    Hahm, B.2    Kim, Y.K.3    Choi, M.4    Jang, S.K.5
  • 55
    • 69249087295 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-xS splice isoform
    • Revil T, Pelletier J, Toutant J, Cloutier A, Chabot B. Heterogeneous nuclear ribonucleoprotein K represses the production of pro-apoptotic Bcl-xS splice isoform. J Biol Chem 2009; 284:21458-67.
    • (2009) J Biol Chem , vol.284 , pp. 21458-21467
    • Revil, T.1    Pelletier, J.2    Toutant, J.3    Cloutier, A.4    Chabot, B.5
  • 56
    • 53349100912 scopus 로고    scopus 로고
    • HIV Nef enhances Tat-mediated viral transcription through a hnRNP-K-nucleated signaling complex
    • Wolf D, Witte V, Clark P, Blume K, Lichtenheld MG, Baur AS. HIV Nef enhances Tat-mediated viral transcription through a hnRNP-K-nucleated signaling complex. Cell Host Microbe 2008; 4:398-408.
    • (2008) Cell Host Microbe , vol.4 , pp. 398-408
    • Wolf, D.1    Witte, V.2    Clark, P.3    Blume, K.4    Lichtenheld, M.G.5    Baur, A.S.6
  • 57
    • 0037126394 scopus 로고    scopus 로고
    • Functional interaction of Sam68 and heterogeneous nuclear ribonucleoprotein K
    • DOI 10.1038/sj.onc.1205759
    • Yang JP, Reddy TR, Truong KT, Suhasini M, Wong- Staal F. Functional interaction of Sam68 and heterogeneous nuclear ribonucleoprotein K. Oncogene 2002; 21:7187-94. (Pubitemid 35305605)
    • (2002) Oncogene , vol.21 , Issue.47 , pp. 7187-7194
    • Yang, J.-P.1    Reddy, T.R.2    Truong, K.T.3    Suhasini, M.4    Wong-Staal, F.5
  • 59
    • 60349131692 scopus 로고    scopus 로고
    • Mapping of determinants involved in the stimulation of HIV-1 expression by Sam68
    • McLaren M, Cochrane A. Mapping of determinants involved in the stimulation of HIV-1 expression by Sam68. Virology 2009; 385:93-104.
    • (2009) Virology , vol.385 , pp. 93-104
    • McLaren, M.1    Cochrane, A.2
  • 61
    • 0037174860 scopus 로고    scopus 로고
    • An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K
    • Chen HC, Lin WC, Tsay YG, Lee SC, Chang CJ. An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K. J Biol Chem 2002; 277:40403-9.
    • (2002) J Biol Chem , vol.277 , pp. 40403-40409
    • Chen, H.C.1    Lin, W.C.2    Tsay, Y.G.3    Lee, S.C.4    Chang, C.J.5
  • 62
    • 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, Pomerantz RJ. A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev. Virology 2004; 330:471-80. (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
  • 63
    • 1242264341 scopus 로고    scopus 로고
    • DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner
    • DOI 10.1093/nar/gkg933
    • Zhang S, Schlott B, Gorlach M, Grosse F. DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner. Nucl Acids Res 2004; 32:1-10. (Pubitemid 38228598)
    • (2004) Nucleic Acids Research , vol.32 , Issue.1 , pp. 1-10
    • Zhang, S.1    Schlott, B.2    Gorlach, M.3    Grosse, F.4
  • 65
    • 0031914976 scopus 로고    scopus 로고
    • DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45
    • DOI 10.1074/jbc.273.4.2136
    • Ting NS, Kao PN, Chan DW, Lintott LG, Lees-Miller SP. DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. J Biol Chem 1998; 273:2136-45. (Pubitemid 28069263)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 2136-2145
    • Ting, N.S.Y.1    Kao, P.N.2    Chan, D.W.3    Lintott, L.G.4    Lees-Miller, S.P.5
  • 66
    • 75749124997 scopus 로고    scopus 로고
    • 2-D structure of the A region of Xist RNA and its implication for PRC2 association
    • Maenner S, Blaud M, Fouillen L, Savoye A, Marchand V, Dubois A, et al. 2-D structure of the A region of Xist RNA and its implication for PRC2 association. PLoS Biol 2010; 8:1000276.
    • (2010) PLoS Biol , vol.8 , pp. 1000276
    • Maenner, S.1    Blaud, M.2    Fouillen, L.3    Savoye, A.4    Marchand, V.5    Dubois, A.6
  • 67
    • 0032953308 scopus 로고    scopus 로고
    • HnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells
    • Chou MY, Rooke N, Turck CW, Black DL. hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells. Mol Cell Biol 1999; 19:69-77. (Pubitemid 29018410)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 69-77
    • Chou, M.-Y.1    Rooke, N.2    Turck, C.W.3    Black, D.L.4
  • 69
    • 0032740121 scopus 로고    scopus 로고
    • Identification of a bidirectional splicing enhancer: Differential involvement of SR proteins in 5' or 3' splice site activation
    • Bourgeois CF, Popielarz M, Hildwein G, Stevenin J. Identification of a bidirectional splicing enhancer: differential involvement of SR proteins in 5′ or 3′ splice site activation. Mol Cell Biol 1999; 19:7347-56. (Pubitemid 29493398)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.11 , pp. 7347-7356
    • Bourgeois, C.F.1    Popielarz, M.2    Hildwein, G.3    Stevenin, J.4
  • 70
    • 67650345785 scopus 로고    scopus 로고
    • Proteomic analysis of malignant B-cell derived microparticles reveals CD148 as a potentially useful antigenic biomarker for mantle cell lymphoma diagnosis
    • Miguet L, Bechade G, Fornecker L, Zink E, Felden C, Gervais C, et al. Proteomic analysis of malignant B-cell derived microparticles reveals CD148 as a potentially useful antigenic biomarker for mantle cell lymphoma diagnosis. J Proteome Res 2009; 8:3346-54.
    • (2009) J Proteome Res , vol.8 , pp. 3346-3354
    • Miguet, L.1    Bechade, G.2    Fornecker, L.3    Zink, E.4    Felden, C.5    Gervais, C.6
  • 71
    • 34248512719 scopus 로고    scopus 로고
    • Untargeted large-scale plant metabolomics using liquid chromatography coupled to mass spectrometry
    • DOI 10.1038/nprot.2007.95, PII NPROT.2007.95
    • De Vos RC, Moco S, Lommen A, Keurentjes JJ, Bino RJ, Hall RD. Untargeted large-scale plant metabolomics using liquid chromatography coupled to mass spectrometry. Nat Protoc 2007; 2:778-91. (Pubitemid 46745574)
    • (2007) Nature Protocols , vol.2 , Issue.4 , pp. 778-791
    • De Vos, R.C.H.1    Moco, S.2    Lommen, A.3    Keurentjes, J.J.B.4    Bino, R.J.5    Hall, R.D.6
  • 72
    • 0031559580 scopus 로고    scopus 로고
    • The D1-A2 and D2-A2 pairs of splice sites from human immunodeficiency virus type 1 are highly efficient in vitro, in spite of an unusual branch site
    • DOI 10.1006/bbrc.1997.7091
    • Damier L, Domenjoud L, Branlant C. The D1-A2 and D2-A2 pairs of splice sites from human immunodeficiency virus type 1 are highly efficient in vitro, in spite of an unusual branch site. Biochem Biophys Res Commun 1997; 237:182-7. (Pubitemid 27390348)
    • (1997) Biochemical and Biophysical Research Communications , vol.237 , Issue.1 , pp. 182-187
    • Damier, L.1    Domenjoud, L.2    Branlant, C.3


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