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Volumn 287, Issue 22, 2012, Pages 18130-18141

Tudor staphylococcal nuclease (Tudor-SN) participates in small ribonucleoprotein (snRNP) assembly via interacting with symmetrically dimethylated Sm proteins

Author keywords

[No Author keywords available]

Indexed keywords

CORE COMPLEX; CORE PROTEINS; DIMETHYLARGININE; IN-VIVO; METHYL GROUP; METHYLTRANSFERASES; MOLECULAR BASIS; MUTAGENESIS EXPERIMENT; NUCLEAR RIBONUCLEOPROTEIN; RIBONUCLEOPROTEINS; SPLICEOSOMES; STAPHYLOCOCCAL NUCLEASE; TANDEM REPEATS; TUDOR DOMAINS;

EID: 84861561394     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.311852     Document Type: Article
Times cited : (49)

References (56)
  • 1
    • 23044512471 scopus 로고    scopus 로고
    • The p100 EBNA-2 coactivator: A highly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle
    • DOI 10.1016/j.bbaexp.2004.10.009, PII S0167478104002386
    • Broadhurst, M. K., Lee, R. S., Hawkins, S., and Wheeler, T. T. (2005) The p100 EBNA-2 co-activator.Ahighly conserved protein found in a range of exocrine and endocrine cells and tissues in cattle. Biochim. Biophys. Acta 1681, 126-133 (Pubitemid 41071385)
    • (2005) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1681 , Issue.2-3 , pp. 126-133
    • Broadhurst, M.K.1    Lee, R.S.-F.2    Hawkins, S.3    Wheeler, T.T.4
  • 2
    • 33947221468 scopus 로고    scopus 로고
    • NF-Y and Sp1 are involved in transcriptional regulation of rat SND p102 gene
    • Rodríguez, L., Ochoa, B., and Martínez, M. J. (2007) NF-Y and Sp1 are involved in transcriptional regulation of rat SND p102 gene. Biochem. Biophys. Res. Commun. 356, 226-232
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 226-232
    • Rodríguez, L.1    Ochoa, B.2    Martínez, M.J.3
  • 3
    • 0038393032 scopus 로고    scopus 로고
    • Two variants of zebrafish p100 are expressed during embryogenesis and regulated by Nodal signaling
    • DOI 10.1016/S0014-5793(03)00445-9
    • Zhao, C. T., Shi, K. H., Su, Y., Liang, L. Y., Yan, Y., Postlethwait, J., and Meng, A.M. (2003) Two variants of zebrafish p100 are expressed during embryogenesis and regulated by Nodal signaling. FEBS Lett. 543, 190-195 (Pubitemid 36577253)
    • (2003) FEBS Letters , vol.543 , Issue.1-3 , pp. 190-195
    • Zhao, C.T.1    Shi, K.H.2    Su, Y.3    Liang, L.Y.4    Yan, Y.5    Postlethwait, J.6    Meng, A.M.7
  • 4
    • 35348881050 scopus 로고    scopus 로고
    • Tudor nuclease genes and programmed DNA rearrangements in Tetrahymena thermophila
    • DOI 10.1128/EC.00192-07
    • Howard-Till, R. A., and Yao, M. C. (2007) Tudor nuclease genes and programmed DNA rearrangements in Tetrahymena thermophila. Eukaryot. Cell 6, 1795-1804 (Pubitemid 47585569)
    • (2007) Eukaryotic Cell , vol.6 , Issue.10 , pp. 1795-1804
    • Howard-Till, R.A.1    Yao, M.-C.2
  • 5
    • 0034961722 scopus 로고    scopus 로고
    • Identification of a cytoskeleton-associated 120 kDa RNA-binding protein in developing rice seeds
    • DOI 10.1023/A:1010643209402
    • Sami-Subbu, R., Choi, S. B., Wu, Y., Wang, C., and Okita, T. W. (2001) Identification of a cytoskeleton-associated 120-kDa RNA-binding protein in developing rice seeds. Plant Mol. Biol. 46, 79-88 (Pubitemid 32595982)
    • (2001) Plant Molecular Biology , vol.46 , Issue.1 , pp. 79-88
    • Sami-Subbu, R.1    Choi, S.-B.2    Wu, Y.3    Wang, C.4    Okita, T.W.5
  • 6
    • 0037337719 scopus 로고    scopus 로고
    • A Tudor protein with multiple SNc domains from pea seedlings: Cellular localization, partial characterization, sequence analysis, and phylogenetic relationships
    • DOI 10.1093/jxb/erg096
    • Abe, S., Sakai, M., Yagi, K., Hagino, T., Ochi, K., Shibata, K., and Davies, E. (2003) A Tudor protein with multiple SNc domains from pea seedlings. Cellular localization, partial characterization, sequence analysis, and phylogenetic relationships. J. Exp. Bot. 54, 971-983 (Pubitemid 36317411)
    • (2003) Journal of Experimental Botany , vol.54 , Issue.384 , pp. 971-983
    • Abe, S.1    Sakai, M.2    Yagi, K.3    Hagino, T.4    Ochi, K.5    Shibata, K.6    Davies, E.7
  • 7
    • 46349107531 scopus 로고    scopus 로고
    • Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing
    • Li, C. L., Yang, W. Z., Chen, Y. P., and Yuan, H. S. (2008) Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing. Nucleic Acids Res. 36, 3579-3589
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3579-3589
    • Li, C.L.1    Yang, W.Z.2    Chen, Y.P.3    Yuan, H.S.4
  • 13
    • 34547829272 scopus 로고    scopus 로고
    • Transcriptional co-activator protein p100 interacts with snRNP proteins and facilitates the assembly of the spliceosome
    • DOI 10.1093/nar/gkm470
    • Yang, J., Välineva, T., Hong, J., Bu, T., Yao, Z., Jensen, O. N., Frilander, M. J., and Silvennoinen, O. (2007) Transcriptional co-activator protein p100 interacts with snRNP proteins and facilitates the assembly of the spliceosome. Nucleic Acids Res. 35, 4485-4494 (Pubitemid 47244599)
    • (2007) Nucleic Acids Research , vol.35 , Issue.13 , pp. 4485-4494
    • Yang, J.1    Valineva, T.2    Hong, J.3    Bu, T.4    Yao, Z.5    Jensen, O.N.6    Frilander, M.J.7    Silvennoinen, O.8
  • 14
    • 17644374227 scopus 로고    scopus 로고
    • The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6
    • DOI 10.1074/jbc.M410465200
    • Välineva, T., Yang, J., Palovuori, R., and Silvennoinen, O. (2005) The transcriptional co-activator protein p100 recruits histone acetyltransferase activity to STAT6 and mediates interaction between the CREB-binding protein and STAT6. J. Biol. Chem. 280, 14989-14996 (Pubitemid 40562851)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14989-14996
    • Valineva, T.1    Yang, J.2    Palovuori, R.3    Silvennoinen, O.4
  • 16
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • DOI 10.1016/S0955-0674(00)00211-8
    • Will, C. L., and Lührmann, R. (2001) Spliceosomal UsnRNP biogenesis, structure, and function. Curr. Opin. Cell Biol. 13, 290-301 (Pubitemid 32429493)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.3 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 17
    • 0033117879 scopus 로고    scopus 로고
    • Structure and assembly of the spliceosomal small nuclear ribonucleoprotein particles
    • DOI 10.1016/S0959-440X(99)80032-3
    • Kambach, C., Walke, S., and Nagai, K. (1999) Structure and assembly of the spliceosomal small nuclear ribonucleoprotein particles. Curr. Opin. Struct Biol. 9, 222-230 (Pubitemid 29452902)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.2 , pp. 222-230
    • Kambach, C.1    Walke, S.2    Nagai, K.3
  • 18
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: Awash in a sea of proteins
    • DOI 10.1016/S1097-2765(03)00270-3
    • Jurica, M. S., and Moore, M. J. (2003) Pre-mRNA splicing. Awash in a sea of proteins. Mol. Cell 12, 5-14 (Pubitemid 36945033)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 21
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • DOI 10.1016/S0092-8674(00)80550-4
    • Kambach, C., Walke, S., Young, R., Avis, J. M., de la Fortelle, E., Raker, V.A., Lührmann, R., Li, J., and Nagai, K. (1999) Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell 96, 375-387 (Pubitemid 29077591)
    • (1999) Cell , vol.96 , Issue.3 , pp. 375-387
    • Kambach, C.1    Walke, S.2    Young, R.3    Avis, J.M.4    De La, F.E.5    Raker, V.A.6    Luhrmann, R.7    Li, J.8    Nagai, K.9
  • 22
    • 0035945611 scopus 로고    scopus 로고
    • Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle
    • DOI 10.1038/35054102
    • Stark, H., Dube, P., Lührmann, R., and Kastner, B. (2001) Arrangement of RNAand proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle. Nature 409, 539-542 (Pubitemid 32144362)
    • (2001) Nature , vol.409 , Issue.6819 , pp. 539-542
    • Stark, H.1    Dube, P.2    Luhrmann, R.3    Kastner, B.4
  • 23
    • 33645607060 scopus 로고    scopus 로고
    • Protein interfaces in signaling regulated by arginine methylation
    • Boisvert, F. M., Chénard, C. A., and Richard, S. (2005) Protein interfaces in signaling regulated by arginine methylation. Sci. STKE 2005, re2
    • (2005) Sci. STKE , vol.2005
    • Boisvert, F.M.1    Chénard, C.A.2    Richard, S.3
  • 25
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • DOI 10.1016/S0960-9822(01)00592-9
    • Meister, G., Eggert, C., Bühler, D., Brahms, H., Kambach, C., and Fischer, U. (2001) Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr. Biol. 11, 1990-1994 (Pubitemid 33146428)
    • (2001) Current Biology , vol.11 , Issue.24 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5    Fischer, U.6
  • 26
    • 33846001366 scopus 로고    scopus 로고
    • The Arginine Methyltransferase CARM1 Regulates the Coupling of Transcription and mRNA Processing
    • DOI 10.1016/j.molcel.2006.11.019, PII S1097276506007908
    • Cheng, D., Côté, J., Shaaban, S., and Bedford, M. T. (2007) The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol. Cell 25, 71-83 (Pubitemid 46049059)
    • (2007) Molecular Cell , vol.25 , Issue.1 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 27
    • 34548356376 scopus 로고    scopus 로고
    • Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins
    • DOI 10.1083/jcb.200702147
    • Gonsalvez, G. B., Tian, L., Ospina, J. K., Boisvert, F. M., Lamond, A. I., and Matera, A. G. (2007) Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J. Cell Biol. 178, 733-740 (Pubitemid 47347358)
    • (2007) Journal of Cell Biology , vol.178 , Issue.5 , pp. 733-740
    • Gonsalvez, G.B.1    Tian, L.2    Ospina, J.K.3    Boisvert, F.-M.4    Lamond, A.I.5    Matera, A.G.6
  • 29
    • 0037459239 scopus 로고    scopus 로고
    • High-resolution X-ray and NMR structures of the SMN Tudor domain: Conformational variation in the binding site for symmetrically dimethylated arginine residues
    • DOI 10.1016/S0022-2836(03)00148-7
    • Sprangers, R., Groves, M. R., Sinning, I., and Sattler, M. (2003) High resolution x-ray andNMRstructures of theSMNTudor domain. Conformational variation in the binding site for symmetrically dimethylated arginine residues. J. Mol. Biol. 327, 507-520 (Pubitemid 36298718)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.2 , pp. 507-520
    • Sprangers, R.1    Groves, M.R.2    Sinning, I.3    Sattler, M.4
  • 30
    • 23344444863 scopus 로고    scopus 로고
    • Tudor domains bind symmetrical dimethylated arginines
    • DOI 10.1074/jbc.M414328200
    • Côté, J., and Richard, S. (2005) Tudor domains bind symmetrical dimethylated arginines. J. Biol. Chem. 280, 28476-28483 (Pubitemid 41105747)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28476-28483
    • Cote, J.1    Richard, S.2
  • 32
    • 34548152119 scopus 로고    scopus 로고
    • Molecular functions of the SMN complex
    • DOI 10.1177/0883073807305666
    • Kolb, S. J., Battle, D. J., and Dreyfuss, G. (2007) Molecular functions of the SMN complex. J. Child Neurol. 22, 990-994 (Pubitemid 47308313)
    • (2007) Journal of Child Neurology , vol.22 , Issue.8 , pp. 990-994
    • Kolb, S.J.1    Battle, D.J.2    Dreyfuss, G.3
  • 33
    • 0242683460 scopus 로고    scopus 로고
    • Essential role for the Tudor domain of SMN in spliceosomal U snRNP assembly. Implications for spinal muscular atrophy
    • Bühler, D., Raker, V., Lührmann, R., and Fischer, U. (1999) Essential role for the Tudor domain of SMN in spliceosomal U snRNP assembly. Implications for spinal muscular atrophy. Hum. Mol. Genet. 8, 2351-2357
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2351-2357
    • Bühler, D.1    Raker, V.2    Lührmann, R.3    Fischer, U.4
  • 34
    • 33749261487 scopus 로고    scopus 로고
    • The abundance of the spliceosomal snRNPs is not limiting the splicing of U12-type introns
    • DOI 10.1261/rna.213906
    • Pessa, H. K., Ruokolainen, A., and Frilander, M. J. (2006) The abundance of the spliceosomal snRNPs is not limiting the splicing of U12-type introns. RNA 12, 1883-1892 (Pubitemid 44484261)
    • (2006) RNA , vol.12 , Issue.10 , pp. 1883-1892
    • Pessa, H.K.J.1    Ruokolainen, A.2    Frilander, M.J.3
  • 35
    • 43049168361 scopus 로고    scopus 로고
    • SMN Deficiency Causes Tissue-Specific Perturbations in the Repertoire of snRNAs and Widespread Defects in Splicing
    • DOI 10.1016/j.cell.2008.03.031, PII S0092867408004601
    • Zhang, Z., Lotti, F., Dittmar, K., Younis, I., Wan, L., Kasim, M., and Dreyfuss, G. (2008) SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing. Cell 133, 585-600 (Pubitemid 351636302)
    • (2008) Cell , vol.133 , Issue.4 , pp. 585-600
    • Zhang, Z.1    Lotti, F.2    Dittmar, K.3    Younis, I.4    Wan, L.5    Kasim, M.6    Dreyfuss, G.7
  • 36
    • 0035710746 scopus 로고    scopus 로고
    • -ΔΔCT 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-ΔΔC(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
  • 37
    • 0037066694 scopus 로고    scopus 로고
    • Quantitative assessment of gene targeting in vitro and in vivo by the pancreatic transcription factor, Pdx1. Importance of chromatin structure in directing promoter binding
    • DOI 10.1074/jbc.M111857200
    • Chakrabarti, S. K., James, J. C., and Mirmira, R. G. (2002) Quantitative assessment of gene targeting in vitro and in vivo by the pancreatic transcription factor Pdx1. Importance of chromatin structure in directing promoter binding. J. Biol. Chem. 277, 13286-13293 (Pubitemid 34952700)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13286-13293
    • Chakrabarti, S.K.1    James, J.C.2    Mirmira, R.G.3
  • 38
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • DOI 10.1038/nature01031
    • Zhou, Z., Licklider, L. J., Gygi, S. P., and Reed, R. (2002) Comprehensive proteomic analysis of the human spliceosome. Nature 419, 182-185 (Pubitemid 35025448)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 39
    • 20344369784 scopus 로고    scopus 로고
    • Proximity of the U12 snRNA with both the 5′ splice site and the branch point during early stages of spliceosome assembly
    • DOI 10.1128/MCB.25.12.4813-4825.2005
    • Frilander, M. J., and Meng, X. (2005) Proximity of the U12 snRNA with both the 5′ splice site and the branch point during early stages of spliceosome assembly. Mol. Cell. Biol. 25, 4813-4825 (Pubitemid 40781084)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.12 , pp. 4813-4825
    • Frilander, M.J.1    Meng, X.2
  • 40
    • 0024421742 scopus 로고
    • Direct, sequence-specific binding of the human U1-70K ribonucleoprotein antigen protein to loop I of U1 small nuclear RNA
    • Surowy, C. S., van Santen, V. L., Scheib-Wixted, S. M., and Spritz, R. A. (1989) Direct sequence-specific binding of the human U1-70K ribonucleoprotein antigen protein to loop I of U1 small nuclear RNA. Mol. Cell. Biol. 9, 4179-4186 (Pubitemid 19239585)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.10 , pp. 4179-4186
    • Surowy, C.S.1    Van Santen, V.L.2    Scheib-Wixted, S.M.3    Spritz, R.A.4
  • 41
    • 17844395704 scopus 로고    scopus 로고
    • Prp8 protein: At the heart of the spliceosome
    • DOI 10.1261/rna.2220705
    • Grainger, R. J., and Beggs, J. D. (2005) Prp8 protein: at the heart of the spliceosome. RNA 11, 533-557 (Pubitemid 40594322)
    • (2005) RNA , vol.11 , Issue.5 , pp. 533-557
    • Grainger, R.J.1    Beggs, J.D.2
  • 42
    • 33646173207 scopus 로고    scopus 로고
    • Assembly of Snu114 into U5 snRNP requires Prp8 and a functional GTPase domain
    • Brenner, T. J., and Guthrie, C. (2006) Assembly of Snu114 into U5 snRNP requires Prp8 and a functional GTPase domain. RNA 12, 862-871
    • (2006) RNA , vol.12 , pp. 862-871
    • Brenner, T.J.1    Guthrie, C.2
  • 43
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
    • DOI 10.1017/S135583820101442X
    • Brahms, H., Meheus, L., de Brabandere, V., Fischer, U., and Lührmann, R. (2001) Symmetrical dimethylation of arginine residues in spliceosomalSm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7, 1531-1542 (Pubitemid 33078929)
    • (2001) RNA , vol.7 , Issue.11 , pp. 1531-1542
    • Brahms, H.1    Meheus, L.2    De Brabandere, V.3    Fischer, U.4    Luhrmann, R.5
  • 44
    • 0035691790 scopus 로고    scopus 로고
    • snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN
    • Sleeman, J. E., Ajuh, P., and Lamond, A. I. (2001) snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN. J. Cell Sci. 114, 4407-4419 (Pubitemid 34082861)
    • (2001) Journal of Cell Science , vol.114 , Issue.24 , pp. 4407-4419
    • Sleeman, J.E.1    Ajuh, P.2    Lamond, A.I.3
  • 45
    • 0037164866 scopus 로고    scopus 로고
    • Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing
    • DOI 10.1083/jcb.200207028
    • Boisvert, F. M., Cote, J., Boulanger, M. C., Cleroux, P., Bachand, F., Autexier, C., and Richard, S. (2002) Symmetrical dimethylarginine methylation is required for the localization ofSMNin Cajal bodies and pre-mRNA splicing. J. Cell Biol. 159, 957-969 (Pubitemid 36055751)
    • (2002) Journal of Cell Biology , vol.159 , Issue.6 , pp. 957-969
    • Boisvert, F.-M.1    Cote, J.2    Boulanger, M.-C.3    Cleroux, P.4    Bachand, F.5    Autexier, C.6    Richard, S.7
  • 46
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • DOI 10.1074/jbc.M000300200
    • Brahms, H., Raymackers, J., Union, A., de Keyser, F., Meheus, L., and Lührmann, R. (2000) The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies. J. Biol. Chem. 275, 17122-17129 (Pubitemid 30398957)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 17122-17129
    • Brahms, H.1    Raymackers, J.2    Union, A.3    De Keyser, F.4    Meheus, L.5    Luhrmann, R.6
  • 47
    • 62649142373 scopus 로고    scopus 로고
    • Structure and ligand binding of the extended Tudor domain of D. melanogaster Tudor- SN
    • Friberg, A., Corsini, L., Mourão, A., and Sattler, M. (2009) Structure and ligand binding of the extended Tudor domain of D. melanogaster Tudor- SN. J. Mol. Biol. 387, 921-934
    • (2009) J. Mol. Biol. , vol.387 , pp. 921-934
    • Friberg, A.1    Corsini, L.2    Mourão, A.3    Sattler, M.4
  • 49
    • 0026111471 scopus 로고
    • Assembly and intracellular transport of snrnp particles
    • Andersen, J., and Zieve, G. W. (1991) Assembly and intracellular transport of snRNP particles. BioEssays 13, 57-64 (Pubitemid 121000542)
    • (1991) BioEssays , vol.13 , Issue.2 , pp. 57-64
    • Andersen, J.1    Zieve, G.W.2
  • 52
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double Tudor domain of JMJD2A
    • Huang, Y., Fang, J., Bedford, M. T., Zhang, Y., and Xu, R. M. (2006) Recognition of histone H3 lysine-4 methylation by the double Tudor domain of JMJD2A. Science 312, 748-751
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 55
    • 75349088708 scopus 로고    scopus 로고
    • From the ribosome to the spliceosome and back again
    • Guthrie, C. (2010) From the ribosome to the spliceosome and back again. J. Biol. Chem. 285, 1-12
    • (2010) J. Biol. Chem. , vol.285 , pp. 1-12
    • Guthrie, C.1


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