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Volumn 229, Issue , 2013, Pages 71-76

Identification in the rat brain of a set of nuclear proteins interacting with H1° mRNA

Author keywords

CSD C2; H1 mRNA; PIPPin; Post transcriptional gene regulation; RNA binding proteins

Indexed keywords

ALDOLASE A PROTEIN; ALDOLASE C PROTEIN; BETA TUBULIN 2A PROTEIN; BETA TUBULIN 3 PROTEIN; CHAPERONE; COLD SHOCK DOMAIN CONTAINING PROTEIN 2; GLUTAMATE DEHYDROGENASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK COGNATE PROTEIN 70; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN B1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; HISTONE H1; MESSENGER RNA; NUCLEAR PROTEIN; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; Y BOX BINDING PROTEIN 1;

EID: 84870805245     PISSN: 03064522     EISSN: 18737544     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2012.10.072     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R., Goodlett D.R. Mass spectrometry in proteomics. Chem Rev 2001, 101:269-295.
    • (2001) Chem Rev , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 2
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly
    • Ahmad K., Henikoff S. The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol Cell 2002, 9:1191-1200.
    • (2002) Mol Cell , vol.9 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 3
    • 33646806458 scopus 로고    scopus 로고
    • Cell-type-specific and developmental regulation of heterogeneous nuclear ribonucleoprotein K mRNA in the rat nervous system
    • Blanchette A.R., Fuentes Medel Y.F., Gardner P.D. Cell-type-specific and developmental regulation of heterogeneous nuclear ribonucleoprotein K mRNA in the rat nervous system. Gene Expr Patterns 2006, 6:596-606.
    • (2006) Gene Expr Patterns , vol.6 , pp. 596-606
    • Blanchette, A.R.1    Fuentes Medel, Y.F.2    Gardner, P.D.3
  • 4
    • 33845868270 scopus 로고    scopus 로고
    • Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPPin in developing rat brain and in cultured neurons
    • Bono E., Compagno V., Proia P., Raimondi L., Schiera G., Favaloro V., Campo V., Donatelli M., Di Liegro I. Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPPin in developing rat brain and in cultured neurons. Endocrinology 2007, 148:252-257.
    • (2007) Endocrinology , vol.148 , pp. 252-257
    • Bono, E.1    Compagno, V.2    Proia, P.3    Raimondi, L.4    Schiera, G.5    Favaloro, V.6    Campo, V.7    Donatelli, M.8    Di Liegro, I.9
  • 5
    • 0028826921 scopus 로고
    • Changes in core histone variant composition in differentiating neurons: the roles of differential turnover and synthesis rates
    • Bosch A., Suau P. Changes in core histone variant composition in differentiating neurons: the roles of differential turnover and synthesis rates. Eur J Cell Biol 1995, 68:220-225.
    • (1995) Eur J Cell Biol , vol.68 , pp. 220-225
    • Bosch, A.1    Suau, P.2
  • 9
    • 0022381517 scopus 로고
    • Formulation of a novel synthetic medium for selectively culturing rat CNS neurons
    • Cestelli A., Savettieri G., Ferraro D., Vitale F. Formulation of a novel synthetic medium for selectively culturing rat CNS neurons. Dev Brain Res 1985, 22:219-227.
    • (1985) Dev Brain Res , vol.22 , pp. 219-227
    • Cestelli, A.1    Savettieri, G.2    Ferraro, D.3    Vitale, F.4
  • 10
    • 0026596190 scopus 로고
    • Qualitative differences in nuclear proteins correlate with neuronal terminal differentiation
    • Cestelli A., Castiglia D., Di Liegro C.M., Di Liegro I. Qualitative differences in nuclear proteins correlate with neuronal terminal differentiation. Cell Mol Neurobiol 1992, 12:33-43.
    • (1992) Cell Mol Neurobiol , vol.12 , pp. 33-43
    • Cestelli, A.1    Castiglia, D.2    Di Liegro, C.M.3    Di Liegro, I.4
  • 11
    • 33645220015 scopus 로고    scopus 로고
    • Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?
    • Ciesla J. Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?. Acta Biochim Pol 2006, 53:11-32.
    • (2006) Acta Biochim Pol , vol.53 , pp. 11-32
    • Ciesla, J.1
  • 12
    • 0034133037 scopus 로고    scopus 로고
    • RNA-protein interactions in the control of stability and localization of messenger RNA
    • (review)
    • Derrigo M., Cestelli A., Savettieri G., Di Liegro I. RNA-protein interactions in the control of stability and localization of messenger RNA. Int J Mol Med 2000, 5:111-123. (review).
    • (2000) Int J Mol Med , vol.5 , pp. 111-123
    • Derrigo, M.1    Cestelli, A.2    Savettieri, G.3    Di Liegro, I.4
  • 13
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J.D., Lebovitz R.M., Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res 1983, 11:1475-1489.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 16
    • 0031912139 scopus 로고    scopus 로고
    • Messenger RNAs in dendrites: localization, stability, and implications for neuronal function
    • Gao F.B. Messenger RNAs in dendrites: localization, stability, and implications for neuronal function. BioEssays 1998, 20:70-78.
    • (1998) BioEssays , vol.20 , pp. 70-78
    • Gao, F.B.1
  • 17
    • 47849125619 scopus 로고    scopus 로고
    • Multiplexed dendritic targeting of alpha calcium calmodulin-dependent protein kinase II, neurogranin, and activity-regulated cytoskeleton-associated protein RNAs by the A2 pathway
    • Gao Y., Tatavarty V., Korza G., Levin M.K., Carson J.H. Multiplexed dendritic targeting of alpha calcium calmodulin-dependent protein kinase II, neurogranin, and activity-regulated cytoskeleton-associated protein RNAs by the A2 pathway. Mol Biol Cell 2008, 19:2311-2327.
    • (2008) Mol Biol Cell , vol.19 , pp. 2311-2327
    • Gao, Y.1    Tatavarty, V.2    Korza, G.3    Levin, M.K.4    Carson, J.H.5
  • 20
    • 0036289532 scopus 로고    scopus 로고
    • Eukaryotic mRNPs may represent posttranscriptional operons
    • Keene J.D., Tenenbaum S.A. Eukaryotic mRNPs may represent posttranscriptional operons. Mol Cell 2002, 9:1161-1167.
    • (2002) Mol Cell , vol.9 , pp. 1161-1167
    • Keene, J.D.1    Tenenbaum, S.A.2
  • 21
    • 23444446940 scopus 로고    scopus 로고
    • Post-transcriptional operons and regulons co-ordinating gene expression
    • Keene J.D., Lager P.J. Post-transcriptional operons and regulons co-ordinating gene expression. Chromosome Res 2005, 13:327-337.
    • (2005) Chromosome Res , vol.13 , pp. 327-337
    • Keene, J.D.1    Lager, P.J.2
  • 22
    • 0036403312 scopus 로고    scopus 로고
    • RNA-protein interactions of the 3' untranslated regions of myosin heavy chain transcripts
    • Kiri A., Goldspink G. RNA-protein interactions of the 3' untranslated regions of myosin heavy chain transcripts. J Muscle Res Cell Motil 2002, 23:119-129.
    • (2002) J Muscle Res Cell Motil , vol.23 , pp. 119-129
    • Kiri, A.1    Goldspink, G.2
  • 23
    • 0032191130 scopus 로고    scopus 로고
    • Dendritic localization of mRNAs
    • Kuhl D., Skehel P. Dendritic localization of mRNAs. Curr Opin Neurobiol 1998, 8:600-606.
    • (1998) Curr Opin Neurobiol , vol.8 , pp. 600-606
    • Kuhl, D.1    Skehel, P.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 79952412205 scopus 로고    scopus 로고
    • Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K
    • Laursen L.S., Chan C.W., Ffrench-Constant C. Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K. J Cell Biol 2011, 192:797-811.
    • (2011) J Cell Biol , vol.192 , pp. 797-811
    • Laursen, L.S.1    Chan, C.W.2    Ffrench-Constant, C.3
  • 26
    • 79959425165 scopus 로고    scopus 로고
    • HnRNP K post-transcriptionally co-regulates multiple cytoskeletal genes needed for axonogenesis
    • Liu Y., Szaro B.G. HnRNP K post-transcriptionally co-regulates multiple cytoskeletal genes needed for axonogenesis. Development 2011, 138:3079-3090.
    • (2011) Development , vol.138 , pp. 3079-3090
    • Liu, Y.1    Szaro, B.G.2
  • 28
    • 33845965024 scopus 로고    scopus 로고
    • Cytokines direct the regulation of Bim mRNA stability by heat-shock cognate protein 70
    • Matsui H., Asou H., Inaba T. Cytokines direct the regulation of Bim mRNA stability by heat-shock cognate protein 70. Mol Cell 2007, 25:99-112.
    • (2007) Mol Cell , vol.25 , pp. 99-112
    • Matsui, H.1    Asou, H.2    Inaba, T.3
  • 30
    • 0033588085 scopus 로고    scopus 로고
    • PIPPin/CSD-C2 is a brain-specific protein that contains a cold-shock domain and binds specifically to H1° and H3.3 mRNAs
    • Nastasi T., Scaturro M., Bellafiore M., Raimondi L., Beccari S., Cestelli A., Di Liegro I. PIPPin/CSD-C2 is a brain-specific protein that contains a cold-shock domain and binds specifically to H1° and H3.3 mRNAs. J Biol Chem 1999, 274:24087-24093.
    • (1999) J Biol Chem , vol.274 , pp. 24087-24093
    • Nastasi, T.1    Scaturro, M.2    Bellafiore, M.3    Raimondi, L.4    Beccari, S.5    Cestelli, A.6    Di Liegro, I.7
  • 32
    • 66349087418 scopus 로고    scopus 로고
    • Actin-associated hnRNP proteins as transacting factors in the control of mRNA transport and localization
    • Percipalle P., Raju C.S., Fukuda N. Actin-associated hnRNP proteins as transacting factors in the control of mRNA transport and localization. RNA Biol 2009, 6:171-174.
    • (2009) RNA Biol , vol.6 , pp. 171-174
    • Percipalle, P.1    Raju, C.S.2    Fukuda, N.3
  • 33
    • 73449102588 scopus 로고    scopus 로고
    • Heterochromatin protein 1 (HP1a) positively regulates euchromatic gene expression through RNA transcript association and interaction with hnRNPs in Drosophila
    • Piacentini L., Fanti L., Negri R., Del Vescovo V., Fatica A., Altieri F., Pimpinelli S. Heterochromatin protein 1 (HP1a) positively regulates euchromatic gene expression through RNA transcript association and interaction with hnRNPs in Drosophila. PLoS Genet 2009, 5:e1000670.
    • (2009) PLoS Genet , vol.5
    • Piacentini, L.1    Fanti, L.2    Negri, R.3    Del Vescovo, V.4    Fatica, A.5    Altieri, F.6    Pimpinelli, S.7
  • 34
    • 0023113877 scopus 로고
    • Changes in H1 complement in differentiating rat-brain cortical neurons
    • Pina B., Martinez P., Suau P. Changes in H1 complement in differentiating rat-brain cortical neurons. Eur J Biochem 1987, 164:71-76.
    • (1987) Eur J Biochem , vol.164 , pp. 71-76
    • Pina, B.1    Martinez, P.2    Suau, P.3
  • 35
    • 0023404906 scopus 로고
    • Changes in histones H2A and H3 variant composition in differentiating and mature rat brain cortical neurons
    • Pina B., Suau P. Changes in histones H2A and H3 variant composition in differentiating and mature rat brain cortical neurons. Dev Biol 1987, 123:51-58.
    • (1987) Dev Biol , vol.123 , pp. 51-58
    • Pina, B.1    Suau, P.2
  • 39
    • 0034212951 scopus 로고    scopus 로고
    • Staufen: a common component of mRNA transport in oocytes and neurons?
    • Roegiers F., Jan Y.N. Staufen: a common component of mRNA transport in oocytes and neurons?. Trends Cell Biol 2000, 10:220-224.
    • (2000) Trends Cell Biol , vol.10 , pp. 220-224
    • Roegiers, F.1    Jan, Y.N.2
  • 40
    • 0029117178 scopus 로고
    • Posttranscriptional regulation of H1 zero and H3.3B histone genes in differentiating rat cortical neurons
    • Scaturro M., Cestelli A., Castiglia D., Nastasi T., Di Liegro I. Posttranscriptional regulation of H1 zero and H3.3B histone genes in differentiating rat cortical neurons. Neurochem Res 1995, 20:969-976.
    • (1995) Neurochem Res , vol.20 , pp. 969-976
    • Scaturro, M.1    Cestelli, A.2    Castiglia, D.3    Nastasi, T.4    Di Liegro, I.5
  • 44
    • 33847421038 scopus 로고    scopus 로고
    • Coregulation of light neurofilament mRNA by poly(A)-binding protein and aldolase C: implications for neurodegeneration
    • Stefanizzi I., Cañete-Soler R. Coregulation of light neurofilament mRNA by poly(A)-binding protein and aldolase C: implications for neurodegeneration. Brain Res 2007, 1139:15-28.
    • (2007) Brain Res , vol.1139 , pp. 15-28
    • Stefanizzi, I.1    Cañete-Soler, R.2
  • 46
    • 77949874234 scopus 로고    scopus 로고
    • Histone variants - ancient wrap artists of the epigenome
    • Talbert P.B., Henikoff S. Histone variants - ancient wrap artists of the epigenome. Nat Rev Mol Cell Biol 2010, 11:264-275.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 264-275
    • Talbert, P.B.1    Henikoff, S.2
  • 47
    • 84857108841 scopus 로고    scopus 로고
    • Histone variants and epigenetic inheritance
    • Yuan G., Zhu B. Histone variants and epigenetic inheritance. Biochim Biophys Acta 2012, 1819:222-229.
    • (2012) Biochim Biophys Acta , vol.1819 , pp. 222-229
    • Yuan, G.1    Zhu, B.2
  • 48
    • 79851483839 scopus 로고    scopus 로고
    • Quaking regulates Hnrnpa1 expression through its 3' UTR in oligodendrocyte precursor cells
    • Zearfoss N.R., Clingman C.C., Farley B.M., McCoig L.M., Ryder S.P. Quaking regulates Hnrnpa1 expression through its 3' UTR in oligodendrocyte precursor cells. PLoS Genet 2011, 7:e1001269.
    • (2011) PLoS Genet , vol.7
    • Zearfoss, N.R.1    Clingman, C.C.2    Farley, B.M.3    McCoig, L.M.4    Ryder, S.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.