메뉴 건너뛰기




Volumn 7, Issue 1, 2016, Pages 105-112

Roles for SUMO in pre-mRNA processing

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RNA POLYMERASE II; SUMO PROTEIN; CYSTEINE PROTEINASE; RNA PRECURSOR; SENP2 PROTEIN, HUMAN; TRANSCRIPTOME;

EID: 84955693735     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1318     Document Type: Review
Times cited : (13)

References (70)
  • 1
    • 0342813068 scopus 로고    scopus 로고
    • SUMO-1: wrestling with a new ubiquitin-related modifier
    • Saitoh H, Pu RT, Dasso M. SUMO-1: wrestling with a new ubiquitin-related modifier. Trends Biochem Sci 1997, 22:374-376.
    • (1997) Trends Biochem Sci , vol.22 , pp. 374-376
    • Saitoh, H.1    Pu, R.T.2    Dasso, M.3
  • 3
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p
    • Johnson ES, Blobel G. Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J Biol Chem 1997, 272:26799-26802.
    • (1997) J Biol Chem , vol.272 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 4
    • 34347265174 scopus 로고    scopus 로고
    • Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins
    • Dye BT, Schulman BA. Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins. Annu Rev Biophys Biomol Struct 2007, 36:131-150.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 131-150
    • Dye, B.T.1    Schulman, B.A.2
  • 5
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis MJ, Coutavas E, Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 1996, 135:1457-1470.
    • (1996) J Cell Biol , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 6
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • Mahajan R, Gerace L, Melchior F. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J Cell Biol 1998, 140:259-270.
    • (1998) J Cell Biol , vol.140 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 7
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • Psakhye I, Jentsch S. Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell 2012, 151:807-820.
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 8
    • 72449175818 scopus 로고    scopus 로고
    • Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks
    • Galanty Y, Belotserkovskaya R, Coates J, Polo S, Miller KM, Jackson SP. Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks. Nature 2009, 462:935-939.
    • (2009) Nature , vol.462 , pp. 935-939
    • Galanty, Y.1    Belotserkovskaya, R.2    Coates, J.3    Polo, S.4    Miller, K.M.5    Jackson, S.P.6
  • 10
    • 23344442009 scopus 로고    scopus 로고
    • Human MMS21/NSE2 is a SUMO ligase required for DNA repair
    • Potts PR, Yu H. Human MMS21/NSE2 is a SUMO ligase required for DNA repair. Mol Cell Biol 2005, 25:7021-7032.
    • (2005) Mol Cell Biol , vol.25 , pp. 7021-7032
    • Potts, P.R.1    Yu, H.2
  • 11
    • 84905370092 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) isoforms and conjugation-independent function in DNA double-strand break repair pathways
    • Hu Y, Parvin JD. Small ubiquitin-like modifier (SUMO) isoforms and conjugation-independent function in DNA double-strand break repair pathways. J Biol Chem 2014, 289:21289-21295.
    • (2014) J Biol Chem , vol.289 , pp. 21289-21295
    • Hu, Y.1    Parvin, J.D.2
  • 12
    • 1542380494 scopus 로고    scopus 로고
    • Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission
    • Harder Z, Zunino R, McBride H. Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr Biol 2004, 14:340-345.
    • (2004) Curr Biol , vol.14 , pp. 340-345
    • Harder, Z.1    Zunino, R.2    McBride, H.3
  • 13
    • 34249046463 scopus 로고    scopus 로고
    • SUMOylation regulates kainate-receptor-mediated synaptic transmission
    • Martin S, Nishimune A, Mellor JR, Henley JM. SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature 2007, 447:321-325.
    • (2007) Nature , vol.447 , pp. 321-325
    • Martin, S.1    Nishimune, A.2    Mellor, J.R.3    Henley, J.M.4
  • 15
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson ES, Blobel G. Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J Cell Biol 1999, 147:981-994.
    • (1999) J Cell Biol , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 16
    • 66349136233 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3
    • Guo B, Sharrocks AD. Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3. Mol Cell Biol 2009, 29:3204-3218.
    • (2009) Mol Cell Biol , vol.29 , pp. 3204-3218
    • Guo, B.1    Sharrocks, A.D.2
  • 17
    • 64749093273 scopus 로고    scopus 로고
    • Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex
    • Ouyang J, Shi Y, Valin A, Xuan Y, Gill G. Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex. Mol Cell 2009, 34:145-154.
    • (2009) Mol Cell , vol.34 , pp. 145-154
    • Ouyang, J.1    Shi, Y.2    Valin, A.3    Xuan, Y.4    Gill, G.5
  • 19
    • 73449092854 scopus 로고    scopus 로고
    • SUMO engages multiple corepressors to regulate chromatin structure and transcription
    • Ouyang J, Gill G. SUMO engages multiple corepressors to regulate chromatin structure and transcription. Epigenetics 2009, 4:440-444.
    • (2009) Epigenetics , vol.4 , pp. 440-444
    • Ouyang, J.1    Gill, G.2
  • 20
    • 0344824404 scopus 로고    scopus 로고
    • Histone sumoylation is associated with transcriptional repression
    • Shiio Y, Eisenman RN. Histone sumoylation is associated with transcriptional repression. Proc Natl Acad Sci USA 2003, 100:13225-13230.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13225-13230
    • Shiio, Y.1    Eisenman, R.N.2
  • 21
    • 0037930875 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins are negatively regulated through SUMO-1 modification independent of the ubiquitin/26 S proteasome pathway
    • Hirano Y, Murata S, Tanaka K, Shimizu M, Sato R. Sterol regulatory element-binding proteins are negatively regulated through SUMO-1 modification independent of the ubiquitin/26 S proteasome pathway. J Biol Chem 2003, 278:16809-16819.
    • (2003) J Biol Chem , vol.278 , pp. 16809-16819
    • Hirano, Y.1    Murata, S.2    Tanaka, K.3    Shimizu, M.4    Sato, R.5
  • 22
    • 0037064083 scopus 로고    scopus 로고
    • Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation
    • Kim J, Cantwell CA, Johnson PF, Pfarr CM, Williams SC. Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation. J Biol Chem 2002, 277:38037-38044.
    • (2002) J Biol Chem , vol.277 , pp. 38037-38044
    • Kim, J.1    Cantwell, C.A.2    Johnson, P.F.3    Pfarr, C.M.4    Williams, S.C.5
  • 25
    • 0041669469 scopus 로고    scopus 로고
    • Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity
    • Yang SH, Jaffray E, Hay RT, Sharrocks AD. Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity. Mol Cell 2003, 12:63-74.
    • (2003) Mol Cell , vol.12 , pp. 63-74
    • Yang, S.H.1    Jaffray, E.2    Hay, R.T.3    Sharrocks, A.D.4
  • 27
    • 0035947677 scopus 로고    scopus 로고
    • Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor
    • Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD. Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor. J Biol Chem 2001, 276:18513-18518.
    • (2001) J Biol Chem , vol.276 , pp. 18513-18518
    • Goodson, M.L.1    Hong, Y.2    Rogers, R.3    Matunis, M.J.4    Park-Sarge, O.K.5    Sarge, K.D.6
  • 29
    • 0038558190 scopus 로고    scopus 로고
    • Sumoylation is involved in β-catenin-dependent activation of Tcf-4
    • Yamamoto H, Ihara M, Matsuura Y, Kikuchi A. Sumoylation is involved in β-catenin-dependent activation of Tcf-4. EMBO J 2003, 22:2047-2059.
    • (2003) EMBO J , vol.22 , pp. 2047-2059
    • Yamamoto, H.1    Ihara, M.2    Matsuura, Y.3    Kikuchi, A.4
  • 31
    • 59649124496 scopus 로고    scopus 로고
    • Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break
    • Kalocsay M, Hiller NJ, Jentsch S. Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break. Mol Cell 2009, 33:335-343.
    • (2009) Mol Cell , vol.33 , pp. 335-343
    • Kalocsay, M.1    Hiller, N.J.2    Jentsch, S.3
  • 32
    • 79961029209 scopus 로고    scopus 로고
    • SUMOylation regulates telomere length homeostasis by targeting Cdc13
    • Hang LE, Liu X, Cheung I, Yang Y, Zhao X. SUMOylation regulates telomere length homeostasis by targeting Cdc13. Nat Struct Mol Biol 2011, 18:920-926.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 920-926
    • Hang, L.E.1    Liu, X.2    Cheung, I.3    Yang, Y.4    Zhao, X.5
  • 33
    • 6344254386 scopus 로고    scopus 로고
    • Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance
    • Xhemalce B, Seeler JS, Thon G, Dejean A, Arcangioli B. Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance. EMBO J 2004, 23:3844-3853.
    • (2004) EMBO J , vol.23 , pp. 3844-3853
    • Xhemalce, B.1    Seeler, J.S.2    Thon, G.3    Dejean, A.4    Arcangioli, B.5
  • 34
    • 56749132295 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO)-1, SUMO-2/3 and SUMOylation are involved with centromeric heterochromatin of chromosomes 9 and 1 and proteins of the synaptonemal complex during meiosis in men
    • Brown PW, Hwang K, Schlegel PN, Morris PL. Small ubiquitin-related modifier (SUMO)-1, SUMO-2/3 and SUMOylation are involved with centromeric heterochromatin of chromosomes 9 and 1 and proteins of the synaptonemal complex during meiosis in men. Hum Reprod 2008, 23:2850-2857.
    • (2008) Hum Reprod , vol.23 , pp. 2850-2857
    • Brown, P.W.1    Hwang, K.2    Schlegel, P.N.3    Morris, P.L.4
  • 35
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis
    • Zhang XD, Goeres J, Zhang H, Yen TJ, Porter AC, Matunis MJ. SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol Cell 2008, 29:729-741.
    • (2008) Mol Cell , vol.29 , pp. 729-741
    • Zhang, X.D.1    Goeres, J.2    Zhang, H.3    Yen, T.J.4    Porter, A.C.5    Matunis, M.J.6
  • 37
    • 0029883163 scopus 로고    scopus 로고
    • Gene expression: increasing evidence for a transcriptosome
    • Halle JP, Meisterernst M. Gene expression: increasing evidence for a transcriptosome. Trends Genet 1996, 12:161-163.
    • (1996) Trends Genet , vol.12 , pp. 161-163
    • Halle, J.P.1    Meisterernst, M.2
  • 38
    • 0032192116 scopus 로고    scopus 로고
    • Regulatory targets in the RNA polymerase II holoenzyme
    • Parvin JD, Young RA. Regulatory targets in the RNA polymerase II holoenzyme. Curr Opin Genet Dev 1998, 8:565-570.
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 565-570
    • Parvin, J.D.1    Young, R.A.2
  • 39
    • 0032740248 scopus 로고    scopus 로고
    • Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes
    • Gall JG, Bellini M, Wu Z, Murphy C. Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes. Mol Biol Cell 1999, 10:4385-4402.
    • (1999) Mol Biol Cell , vol.10 , pp. 4385-4402
    • Gall, J.G.1    Bellini, M.2    Wu, Z.3    Murphy, C.4
  • 40
    • 84894318075 scopus 로고    scopus 로고
    • Coupling mRNA processing with transcription in time and space
    • Bentley DL. Coupling mRNA processing with transcription in time and space. Nat Rev Genet 2014, 15:163-175.
    • (2014) Nat Rev Genet , vol.15 , pp. 163-175
    • Bentley, D.L.1
  • 41
    • 84875429298 scopus 로고    scopus 로고
    • Reflections on the history of pre-mRNA processing and highlights of current knowledge: a unified picture
    • Darnell JE Jr. Reflections on the history of pre-mRNA processing and highlights of current knowledge: a unified picture. RNA 2013, 19:443-460.
    • (2013) RNA , vol.19 , pp. 443-460
    • Darnell, J.E.1
  • 42
    • 0030670094 scopus 로고    scopus 로고
    • A CTD function linking transcription to splicing
    • Corden JL, Patturajan M. A CTD function linking transcription to splicing. Trends Biochem Sci 1997, 22:413-416.
    • (1997) Trends Biochem Sci , vol.22 , pp. 413-416
    • Corden, J.L.1    Patturajan, M.2
  • 45
    • 77953929082 scopus 로고    scopus 로고
    • SUMO functions in constitutive transcription and during activation of inducible genes in yeast
    • Rosonina E, Duncan SM, Manley JL. SUMO functions in constitutive transcription and during activation of inducible genes in yeast. Genes Dev 2010, 24:1242-1252.
    • (2010) Genes Dev , vol.24 , pp. 1242-1252
    • Rosonina, E.1    Duncan, S.M.2    Manley, J.L.3
  • 46
    • 84930504087 scopus 로고    scopus 로고
    • The chromatin scaffold protein SAFB1 localizes SUMO-1 to the promoters of ribosomal protein genes to facilitate transcription initiation and splicing
    • Liu HW, Banerjee T, Guan X, Freitas MA, Parvin JD. The chromatin scaffold protein SAFB1 localizes SUMO-1 to the promoters of ribosomal protein genes to facilitate transcription initiation and splicing. Nucleic Acids Res 2015, 43:3605-3613.
    • (2015) Nucleic Acids Res , vol.43 , pp. 3605-3613
    • Liu, H.W.1    Banerjee, T.2    Guan, X.3    Freitas, M.A.4    Parvin, J.D.5
  • 47
    • 77952082869 scopus 로고    scopus 로고
    • Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1)
    • Sanchez-Alvarez M, Montes M, Sanchez-Hernandez N, Hernandez-Munain C, Sune C. Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1). J Biol Chem 2010, 285:15220-15233.
    • (2010) J Biol Chem , vol.285 , pp. 15220-15233
    • Sanchez-Alvarez, M.1    Montes, M.2    Sanchez-Hernandez, N.3    Hernandez-Munain, C.4    Sune, C.5
  • 48
    • 36249027156 scopus 로고    scopus 로고
    • Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing
    • Sims RJ 3rd, Millhouse S, Chen CF, Lewis BA, Erdjument-Bromage H, Tempst P, Manley JL, Reinberg D. Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. Mol Cell 2007, 28:665-676.
    • (2007) Mol Cell , vol.28 , pp. 665-676
    • Sims, R.J.1    Millhouse, S.2    Chen, C.F.3    Lewis, B.A.4    Erdjument-Bromage, H.5    Tempst, P.6    Manley, J.L.7    Reinberg, D.8
  • 50
    • 79952364016 scopus 로고    scopus 로고
    • Histone H3 lysine 9 trimethylation and HP1γ favor inclusion of alternative exons
    • Saint-Andre V, Batsche E, Rachez C, Muchardt C. Histone H3 lysine 9 trimethylation and HP1γ favor inclusion of alternative exons. Nat Struct Mol Biol 2011, 18:337-344.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 337-344
    • Saint-Andre, V.1    Batsche, E.2    Rachez, C.3    Muchardt, C.4
  • 52
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley BR. Sorting out the complexity of SR protein functions. RNA 2000, 6:1197-1211.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 53
    • 67649671966 scopus 로고    scopus 로고
    • SR proteins in vertical integration of gene expression from transcription to RNA processing to translation
    • Zhong XY, Wang P, Han J, Rosenfeld MG, Fu XD. SR proteins in vertical integration of gene expression from transcription to RNA processing to translation. Mol Cell 2009, 35:1-10.
    • (2009) Mol Cell , vol.35 , pp. 1-10
    • Zhong, X.Y.1    Wang, P.2    Han, J.3    Rosenfeld, M.G.4    Fu, X.D.5
  • 54
    • 1942422565 scopus 로고    scopus 로고
    • SUMO modification of heterogeneous nuclear ribonucleoproteins
    • Vassileva MT, Matunis MJ. SUMO modification of heterogeneous nuclear ribonucleoproteins. Mol Cell Biol 2004, 24:3623-3632.
    • (2004) Mol Cell Biol , vol.24 , pp. 3623-3632
    • Vassileva, M.T.1    Matunis, M.J.2
  • 59
    • 84889081371 scopus 로고    scopus 로고
    • Chromatin's thread to alternative splicing regulation
    • Iannone C, Valcarcel J. Chromatin's thread to alternative splicing regulation. Chromosoma 2013, 122:465-474.
    • (2013) Chromosoma , vol.122 , pp. 465-474
    • Iannone, C.1    Valcarcel, J.2
  • 60
    • 82955247079 scopus 로고    scopus 로고
    • Nascent-seq indicates widespread cotranscriptional pre-mRNA splicing in Drosophila
    • Khodor YL, Rodriguez J, Abruzzi KC, Tang CH, Marr MT 2nd, Rosbash M. Nascent-seq indicates widespread cotranscriptional pre-mRNA splicing in Drosophila. Genes Dev 2011, 25:2502-2512.
    • (2011) Genes Dev , vol.25 , pp. 2502-2512
    • Khodor, Y.L.1    Rodriguez, J.2    Abruzzi, K.C.3    Tang, C.H.4    Marr, M.T.5    Rosbash, M.6
  • 61
    • 0024762583 scopus 로고
    • Four factors are required for 3'-end cleavage of pre-mRNAs
    • Takagaki Y, Ryner LC, Manley JL. Four factors are required for 3'-end cleavage of pre-mRNAs. Genes Dev 1989, 3:1711-1724.
    • (1989) Genes Dev , vol.3 , pp. 1711-1724
    • Takagaki, Y.1    Ryner, L.C.2    Manley, J.L.3
  • 63
    • 37849036555 scopus 로고    scopus 로고
    • RNA polymerase II pauses and associates with pre-mRNA processing factors at both ends of genes
    • Glover-Cutter K, Kim S, Espinosa J, Bentley DL. RNA polymerase II pauses and associates with pre-mRNA processing factors at both ends of genes. Nat Struct Mol Biol 2008, 15:71-78.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 71-78
    • Glover-Cutter, K.1    Kim, S.2    Espinosa, J.3    Bentley, D.L.4
  • 64
    • 37549012161 scopus 로고    scopus 로고
    • Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex
    • Vethantham V, Rao N, Manley JL. Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex. Mol Cell Biol 2007, 27:8848-8858.
    • (2007) Mol Cell Biol , vol.27 , pp. 8848-8858
    • Vethantham, V.1    Rao, N.2    Manley, J.L.3
  • 65
    • 39449103526 scopus 로고    scopus 로고
    • Sumoylation regulates multiple aspects of mammalian poly(A) polymerase function
    • Vethantham V, Rao N, Manley JL. Sumoylation regulates multiple aspects of mammalian poly(A) polymerase function. Genes Dev 2008, 22:499-511.
    • (2008) Genes Dev , vol.22 , pp. 499-511
    • Vethantham, V.1    Rao, N.2    Manley, J.L.3
  • 66
    • 84929119503 scopus 로고    scopus 로고
    • A novel post-translational modification of nucleolin, SUMOylation at Lys-294, mediates arsenite-induced cell death by regulating gadd45α mRNA stability
    • Zhang D, Liang Y, Xie Q, Gao G, Wei J, Huang H, Li J, Gao J, Huang C. A novel post-translational modification of nucleolin, SUMOylation at Lys-294, mediates arsenite-induced cell death by regulating gadd45α mRNA stability. J Biol Chem 2015, 290:4784-4800.
    • (2015) J Biol Chem , vol.290 , pp. 4784-4800
    • Zhang, D.1    Liang, Y.2    Xie, Q.3    Gao, G.4    Wei, J.5    Huang, H.6    Li, J.7    Gao, J.8    Huang, C.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.