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Volumn 40, Issue 9, 2012, Pages 4025-4039

C6 pyridinium ceramide influences alternative pre-mRNA splicing by inhibiting protein phosphatase-1

Author keywords

[No Author keywords available]

Indexed keywords

CERAMIDE DERIVATIVE; DEXTRO 2 N [6' (1 PYRIDINIUM)HEXANOYL]SPHINGOSINE BROMIDE; PHOSPHOPROTEIN PHOSPHATASE 1; PYRIDINIUM DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84861372934     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr1289     Document Type: Article
Times cited : (22)

References (49)
  • 1
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Pan, Q., Shai, O., Lee, L.J., Frey, B.J. and Blencowe, B.J. (2008) Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nat. Genet., 40, 1413-1415.
    • (2008) Nat. Genet. , vol.40 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 4
    • 0035159666 scopus 로고    scopus 로고
    • Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions
    • Shav-Tal, Y., Cohen, M., Lapter, S., Dye, B., Patton, J.G., Vandekerckhove, J. and Zipori, D. (2001) Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions. Mol. Biol. Cell, 12, 2328-2340. (Pubitemid 33051959)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2328-2340
    • Shav-Tal, Y.1    Cohen, M.2    Lapter, S.3    Dye, B.4    Patton, J.G.5    Vandekerckhove, J.6    Zipori, D.7
  • 5
    • 1142310938 scopus 로고    scopus 로고
    • Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock
    • DOI 10.1038/nature02288
    • Shin, C., Feng, Y. and Manley, J.L. (2004) Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock. Nature, 427, 553-558. (Pubitemid 38209114)
    • (2004) Nature , vol.427 , Issue.6974 , pp. 553-558
    • Shin, C.1    Feng, Y.2    Manley, J.L.3
  • 6
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao, S.H. and Manley, J.L. (1997) Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev., 11, 334-344. (Pubitemid 27079911)
    • (1997) Genes and Development , vol.11 , Issue.3 , pp. 334-344
    • Xiao, S.-H.1    Manley, J.L.2
  • 7
    • 0037066727 scopus 로고    scopus 로고
    • De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1
    • DOI 10.1074/jbc.M112010200
    • Chalfant, C.E., Rathman, K., Pinkerman, R.L., Wood, R.E., Obeid, L.M., Ogretmen, B. and Hannun, Y.A. (2002) De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1. J. Biol. Chem., 277, 12587-12595. (Pubitemid 34952617)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 12587-12595
    • Chalfant, C.E.1    Rathman, K.2    Pinkerman, R.L.3    Wood, R.E.4    Obeid, L.M.5    Ogretmen, B.6    Hannun, Y.A.7
  • 8
    • 33847036385 scopus 로고    scopus 로고
    • Ceramide-activated protein phosphatase involvement in insulin resistance via Akt, serine/arginine-rich protein 40, and ribonucleic acid splicing in L6 skeletal muscle cells
    • Ghosh, N., Patel, N., Jiang, K., Watson, J.E., Cheng, J., Chalfant, C.E. and Cooper, D.R. (2007) Ceramide-activated protein phosphatase involvement in insulin resistance via Akt, serine/arginine-rich protein 40, and ribonucleic acid splicing in L6 skeletal muscle cells. Endocrinology, 148, 1359-1366.
    • (2007) Endocrinology , vol.148 , pp. 1359-1366
    • Ghosh, N.1    Patel, N.2    Jiang, K.3    Watson, J.E.4    Cheng, J.5    Chalfant, C.E.6    Cooper, D.R.7
  • 9
    • 47649131293 scopus 로고    scopus 로고
    • Nuclear sphingolipids: Metabolism and signaling
    • Ledeen, R.W. and Wu, G. (2008) Nuclear sphingolipids: metabolism and signaling. J. Lipid Res., 49, 1176-1186.
    • (2008) J. Lipid Res. , vol.49 , pp. 1176-1186
    • Ledeen, R.W.1    Wu, G.2
  • 10
    • 1942533609 scopus 로고    scopus 로고
    • Identification of Two RNA cis-Elements That Function to Regulate the 5' Splice Site Selection of Bcl-x Pre-mRNA in Response to Ceramide
    • DOI 10.1074/jbc.M313950200
    • Massiello, A., Salas, A., Pinkerman, R.L., Roddy, P., Roesser, J.R. and Chalfant, C.E. (2004) Identification of two RNA cis-elements that function to regulate the 50 splice site selection of Bcl-x pre-mRNA in response to ceramide. J. Biol. Chem., 279, 15799-15804. (Pubitemid 38509266)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 15799-15804
    • Massiello, A.1    Salas, A.2    Pinkerman, R.L.3    Roddy, P.4    Roesser, J.R.5    Chalfant, C.E.6
  • 12
    • 84860515463 scopus 로고    scopus 로고
    • C16-ceramide analog combined with Pc 4 photodynamic therapy evokes enhanced total ceramide accumulation, promotion of DEVDase activation in the absence of apoptosis, and augmented overall cell killing
    • Separovic, D., Saad, Z.H., Edwin, E.A., Bielawski, J., Pierce, J.S., Buren, E.V. and Bielawska, A. (2011) C16-ceramide analog combined with Pc 4 photodynamic therapy evokes enhanced total ceramide accumulation, promotion of DEVDase activation in the absence of apoptosis, and augmented overall cell killing. J. Lipids, 2011, 713867.
    • (2011) J. Lipids , vol.2011 , pp. 713867
    • Separovic, D.1    Saad, Z.H.2    Edwin, E.A.3    Bielawski, J.4    Pierce, J.S.5    Buren, E.V.6    Bielawska, A.7
  • 13
    • 0033575310 scopus 로고    scopus 로고
    • Long chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid
    • Chalfant, C.E., Kishikawa, K., Mumby, M.C., Kamibayashi, C., Bielawska, A. and Hannun, Y.A. (1999) Long chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid. J. Biol. Chem., 274, 20313-20317.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20313-20317
    • Chalfant, C.E.1    Kishikawa, K.2    Mumby, M.C.3    Kamibayashi, C.4    Bielawska, A.5    Hannun, Y.A.6
  • 14
    • 55249116242 scopus 로고    scopus 로고
    • Rapid generation of splicing reporters with pSpliceExpress
    • Kishore, S., Khanna, A. and Stamm, S. (2008) Rapid generation of splicing reporters with pSpliceExpress. Gene, 427, 104-110.
    • (2008) Gene , vol.427 , pp. 104-110
    • Kishore, S.1    Khanna, A.2    Stamm, S.3
  • 15
    • 0026671202 scopus 로고
    • The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei
    • Beullens, M., Van Eynde, A., Stalmans, W. and Bollen, M. (1992) The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei. J. Biol. Chem., 267, 16538-16544.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16538-16544
    • Beullens, M.1    Van Eynde, A.2    Stalmans, W.3    Bollen, M.4
  • 16
    • 41449099770 scopus 로고    scopus 로고
    • Structure-specific, quantitative methods for analysis of sphingolipids by liquid chromatography-tandem mass spectrometry: "inside-out" sphingolipidomics
    • Sullards, M.C., Allegood, J.C., Kelly, S., Wang, E., Haynes, C.A., Park, H., Chen, Y. and Merrill, A.H. Jr (2007) Structure-specific, quantitative methods for analysis of sphingolipids by liquid chromatography-tandem mass spectrometry: "inside-out" sphingolipidomics. Methods Enzymol., 432, 83-115.
    • (2007) Methods Enzymol. , vol.432 , pp. 83-115
    • Sullards, M.C.1    Allegood, J.C.2    Kelly, S.3    Wang, E.4    Haynes, C.A.5    Park, H.6    Chen, Y.7    Merrill Jr., A.H.8
  • 18
    • 33646792573 scopus 로고    scopus 로고
    • SRp30a (ASF/SF2) regulates the alternative splicing of caspase-9 pre-mRNA and is required for ceramide-responsiveness
    • DOI 10.1194/jlr.C600003-JLR200
    • Massiello, A. and Chalfant, C.E. (2006) SRp30a (ASF/SF2) regulates the alternative splicing of caspase-9 pre-mRNA and is required for ceramide-responsiveness. J. Lipid Res., 47, 892-897. (Pubitemid 43764686)
    • (2006) Journal of Lipid Research , vol.47 , Issue.5 , pp. 892-897
    • Massiello, A.1    Chalfant, C.E.2
  • 20
    • 78651240947 scopus 로고    scopus 로고
    • Enhanced tumor cures after Foscan photodynamic therapy combined with the ceramide analog LCL29. Evidence from mouse squamous cell carcinomas for sphingolipids as biomarkers of treatment response
    • Separovic, D., Bielawski, J., Pierce, J.S., Merchant, S., Tarca, A.L., Bhatti, G., Ogretmen, B. and Korbelik, M. (2011) Enhanced tumor cures after Foscan photodynamic therapy combined with the ceramide analog LCL29. Evidence from mouse squamous cell carcinomas for sphingolipids as biomarkers of treatment response. Int. J. Oncol., 38, 521-527.
    • (2011) Int J. Oncol. , vol.38 , pp. 521-527
    • Separovic, D.1    Bielawski, J.2    Pierce, J.S.3    Merchant, S.4    Tarca, A.L.5    Bhatti, G.6    Ogretmen, B.7    Korbelik, M.8
  • 22
    • 0036798006 scopus 로고    scopus 로고
    • Signals and their transduction pathways regulating alternative splicing: A new dimension of the human genome
    • Stamm, S. (2002) Signals and their transduction pathways regulating alternative splicing: a new dimension of the human genome. Hum. Mol. Genet., 11, 2409-2416. (Pubitemid 35174704)
    • (2002) Human Molecular Genetics , vol.11 , Issue.20 , pp. 2409-2416
    • Stamm, S.1
  • 23
    • 10944272640 scopus 로고    scopus 로고
    • Tau gene alternative splicing: Expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases
    • DOI 10.1016/j.bbadis.2004.08.010, PII S0925443904001541
    • Andreadis, A. (2005) Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases. Biochem. Biophys. Acta, 1739, 91-103. (Pubitemid 40018532)
    • (2005) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1739 , Issue.2 , pp. 91-103
    • Andreadis, A.1
  • 24
    • 0035977067 scopus 로고    scopus 로고
    • FAS activation induces dephosphorylation of SR proteins; Dependence on the de novo generation of ceramide and activation of protein phosphatase 1
    • Chalfant, C.E., Ogretmen, B., Galadari, S., Kroesen, B.J., Pettus, B.J. and Hannun, Y.A. (2001) FAS activation induces dephosphorylation of SR proteins; dependence on the de novo generation of ceramide and activation of protein phosphatase 1. J. Biol. Chem., 276, 44848-44855.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44848-44855
    • Chalfant, C.E.1    Ogretmen, B.2    Galadari, S.3    Kroesen, B.J.4    Pettus, B.J.5    Hannun, Y.A.6
  • 25
    • 0037101633 scopus 로고    scopus 로고
    • Ischemia induces a translocation of the splicing factor tra2-β1 and changes alternative splicing patterns in the brain
    • Daoud, R., Mies, G., Smialowska, A., Oláh, L., Hossmann, K. and Stamm, S. (2002) Ischemia induces a translocation of the splicing factor tra2-beta1 and changes alternative splicing patterns in the brain. J. Neurosci., 22, 5889-5899. (Pubitemid 35387633)
    • (2002) Journal of Neuroscience , vol.22 , Issue.14 , pp. 5889-5899
    • Daoud, R.1    Mies, G.2    Smialowska, A.3    Olah, L.4    Hossmann, K.-A.5    Stamm, S.6
  • 27
    • 0034463165 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine P450scc insulin-like growth factor response element
    • DOI 10.1210/me.14.6.774
    • Urban, R.J., Bodenburg, Y., Kurosky, A., Wood, T.G. and Gasic, S. (2000) Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element. Mol. Endocrinol., 14, 774-782. (Pubitemid 32260491)
    • (2000) Molecular Endocrinology , vol.14 , Issue.6 , pp. 774-782
    • Urban, R.J.1    Bodenburg, Y.2    Kurosky, A.3    Wood, T.G.4    Gasic, S.5
  • 28
    • 0034663495 scopus 로고    scopus 로고
    • Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion
    • Akhmedov, A.T. and Lopez, B.S. (2000) Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion. Nucleic Acids Res., 28, 3022-3030. (Pubitemid 30624091)
    • (2000) Nucleic Acids Research , vol.28 , Issue.16 , pp. 3022-3030
    • Akhmedov, A.T.1    Lopez, B.S.2
  • 29
    • 79959849578 scopus 로고    scopus 로고
    • Consensus PP1 binding motifs regulate transcriptional corepression and alternative RNA splicing activities of the steroid receptor coregulators, p54nrb and PSF
    • Liu, L., Xie, N., Rennie, P., Challis, J.R., Gleave, M., Lye, S.J. and Dong, X. (2011) Consensus PP1 binding motifs regulate transcriptional corepression and alternative RNA splicing activities of the steroid receptor coregulators, p54nrb and PSF. Mol. Endocrinol., 25, 1197-1210.
    • (2011) Mol. Endocrinol. , vol.25 , pp. 1197-1210
    • Liu, L.1    Xie, N.2    Rennie, P.3    Challis, J.R.4    Gleave, M.5    Lye, S.J.6    Dong, X.7
  • 30
    • 0030199521 scopus 로고    scopus 로고
    • Interaction of protein phosphatase type 1 with a splicing factor
    • DOI 10.1016/0014-5793(96)00577-7
    • Hirano, K., Erdodi, F., Patton, J.G. and Hartshorne, D.J. (1996) Interaction of protein phosphatase type 1 with a splicing factor. FEBS Lett., 389, 191-194. (Pubitemid 26226497)
    • (1996) FEBS Letters , vol.389 , Issue.2 , pp. 191-194
    • Hirano, K.1    Erdodi, F.2    Patton, J.G.3    Hartshorne, D.J.4
  • 31
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey, T.L. and Elkan, C. (1994) Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell. Syst. Mol. Biol., 2, 28-36.
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 32
    • 33747891736 scopus 로고    scopus 로고
    • An increased specificity score matrix for the prediction of SF2/ASF-specific exonic splicing enhancers
    • DOI 10.1093/hmg/ddl171
    • Smith, P.J., Zhang, C., Wang, J., Chew, S.L., Zhang, M.Q. and Krainer, A.R. (2006) An increased specificity score matrix for the prediction of SF2/ASF-specific exonic splicing enhancers. Hum. Mol. Genet., 15, 2490-2508. (Pubitemid 44288702)
    • (2006) Human Molecular Genetics , vol.15 , Issue.16 , pp. 2490-2508
    • Smith, P.J.1    Zhang, C.2    Wang, J.3    Chew, S.L.4    Zhang, M.Q.5    Krainer, A.R.6
  • 33
    • 0034533608 scopus 로고    scopus 로고
    • An alternative-exon database and its statistical analysis
    • DOI 10.1089/104454900750058107
    • Stamm, S., Zhu, J., Nakai, K., Stoilov, P., Stoss, O. and Zhang, M.Q. (2000) An alternative-exon database and its statistical analysis. DNA Cell Biol., 19, 739-756. (Pubitemid 32011938)
    • (2000) DNA and Cell Biology , vol.19 , Issue.12 , pp. 739-756
    • Stamm, S.1    Zhu, J.2    Nakai, K.3    Stoilov, P.4    Stoss, O.5    Zhang, M.Q.6
  • 35
    • 0038819945 scopus 로고    scopus 로고
    • Mutations in tau gene exon 10 associated with FTDP-17 alter the activity of an exonic splicing enhancer to interact with Tra2β
    • DOI 10.1074/jbc.M301800200
    • Jiang, Z., Tang, H., Havlioglu, N., Zhang, X., Stamm, S., Yan, R. and Wu, J.Y. (2003) Mutations in tau gene exon 10 associated with FTDP-17 alter the activity of an exonic splicing enhancer to interact with Tra2 beta. J. Biol. Chem., 278, 18997-19007. (Pubitemid 36799284)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 18997-19007
    • Jiang, Z.1    Tang, H.2    Havlioglu, N.3    Zhang, X.4    Stamm, S.5    Yan, R.6    Wu, J.Y.7
  • 36
    • 80855123708 scopus 로고    scopus 로고
    • PSF suppresses tau Exon 10 inclusion by interacting with a stem-loop structure downstream of exon 10
    • Ray, P., Kar, A., Fushimi, K., Havlioglu, N., Chen, X. and Wu, J.Y. (2011) PSF suppresses tau Exon 10 inclusion by interacting with a stem-loop structure downstream of exon 10. J. Mol. Neurosci., 45, 453-466.
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 453-466
    • Ray, P.1    Kar, A.2    Fushimi, K.3    Havlioglu, N.4    Chen, X.5    Wu, J.Y.6
  • 37
    • 1542330117 scopus 로고    scopus 로고
    • Tra2β, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA
    • DOI 10.1111/j.1356-9597.2004.00709.x
    • Kondo, S., Yamamoto, N., Murakami, T., Okumura, M., Mayeda, A. and Imaizumi, K. (2004) Tra2 beta, SF2/ASF and SRp30c modulate the function of an exonic splicing enhancer in exon 10 of tau pre-mRNA. Genes Cells, 9, 121-130. (Pubitemid 38312956)
    • (2004) Genes to Cells , vol.9 , Issue.2 , pp. 121-130
    • Kondo, S.1    Yamamoto, N.2    Murakami, T.3    Okumura, M.4    Mayeda, A.5    Imaizumi, K.6
  • 39
    • 1442348429 scopus 로고    scopus 로고
    • Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors
    • DOI 10.1046/j.1471-4159.2003.02232.x
    • Wang, J., Gao, Q.-S., Wang, Y., Lafyatis, R., Stamm, S. and Andreadis, A. (2004) Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of Cis elements and Trans factors. J. Neurochem., 88, 1078-1090. (Pubitemid 38280676)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.5 , pp. 1078-1090
    • Wang, J.1    Gao, Q.-S.2    Wang, Y.3    Lafyatis, R.4    Stamm, S.5    Andreadis, A.6
  • 42
    • 33646352507 scopus 로고    scopus 로고
    • Specific RNA binding to ordered phospholipid bilayers
    • DOI 10.1093/nar/gkl220
    • Janas, T. and Yarus, M. (2006) Specific RNA binding to ordered phospholipid bilayers. Nucleic Acids Res., 34, 2128-2136. (Pubitemid 44314210)
    • (2006) Nucleic Acids Research , vol.34 , Issue.7 , pp. 2128-2136
    • Janas, T.1    Janas, T.2    Yarus, M.3
  • 43
    • 69949131246 scopus 로고    scopus 로고
    • RISC hitches onto endosome trafficking
    • Siomi, H. and Siomi, M.C. (2009) RISC hitches onto endosome trafficking. Nat. Cell Biol., 11, 1049-1051.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1049-1051
    • Siomi, H.1    Siomi, M.C.2
  • 44
    • 69949117622 scopus 로고    scopus 로고
    • Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity
    • Gibbings, D.J., Ciaudo, C., Erhardt, M. and Voinnet, O. (2009) Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity. Nat. Cell Biol., 11, 1143-1149.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1143-1149
    • Gibbings, D.J.1    Ciaudo, C.2    Erhardt, M.3    Voinnet, O.4
  • 45
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • DOI 10.1146/annurev.cellbio.14.1.231
    • Martin, T.F. (1998) Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu. Rev. Cell. Dev. Biol., 14, 231-264. (Pubitemid 29001455)
    • (1998) Annual Review of Cell and Developmental Biology , vol.14 , pp. 231-264
    • Martin, T.F.J.1
  • 46
    • 0026731973 scopus 로고
    • Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing
    • Mermoud, J.E., Cohen, P. and Lamond, A.I. (1992) Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing. Nucleic Acids Res., 20, 5263-5269.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5263-5269
    • Mermoud, J.E.1    Cohen, P.2    Lamond, A.I.3
  • 47
    • 38349085591 scopus 로고    scopus 로고
    • Regulation of alternative splicing by reversible phosphorylation
    • Stamm, S. (2008) Regulation of alternative splicing by reversible phosphorylation. J.Biol. Chem., 283, 1223-1227.
    • (2008) J.Biol. Chem. , vol.283 , pp. 1223-1227
    • Stamm, S.1
  • 48
    • 58149096435 scopus 로고    scopus 로고
    • Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155)
    • Tanuma, N., Kim, S.E., Beullens, M., Tsubaki, Y., Mitsuhashi, S., Nomura, M., Kawamura, T., Isono, K., Koseki, H., Sato, M. et al. (2008) Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155). J. Biol. Chem., 283, 35805-35814.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35805-35814
    • Tanuma, N.1    Kim, S.E.2    Beullens, M.3    Tsubaki, Y.4    Mitsuhashi, S.5    Nomura, M.6    Kawamura, T.7    Isono, K.8    Koseki, H.9    Sato, M.10


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