메뉴 건너뛰기




Volumn 14, Issue 11, 2014, Pages 1357-1366

Proteomic analyses of genes regulated by heterogeneous nuclear ribonucleoproteins A/B in Jurkat cells

Author keywords

Cell proliferation; HnRNP A1, A2 B1, A3; Jurkat cells; Quantitative proteomics

Indexed keywords

CRK LIKE PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A2; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A3; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN B; PROTEOME; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; SMALL INTERFERING RNA;

EID: 84901841454     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201300549     Document Type: Article
Times cited : (12)

References (30)
  • 2
    • 0023955859 scopus 로고
    • Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins
    • Pinol-Roma, S., Choi, Y. D., Matunis, M. J., Dreyfuss, G., Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins. Genes Dev. 1988, 2, 215-227.
    • (1988) Genes Dev. , vol.2 , pp. 215-227
    • Pinol-Roma, S.1    Choi, Y.D.2    Matunis, M.J.3    Dreyfuss, G.4
  • 3
    • 63449132795 scopus 로고    scopus 로고
    • Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B
    • He, Y., Smith, R., Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B. Cell. Mol. Life Sci. 2009, 66, 1239-1256.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1239-1256
    • He, Y.1    Smith, R.2
  • 4
    • 0022636245 scopus 로고
    • Identification of proliferation-sensitive human proteins amongst components of the 40 S hnRNP particles. Identity of hnRNP core proteins in the HeLa protein catalogue
    • Celis, J. E., Bravo, R., Arenstorf, H. P., LeStourgeon, W. M., Identification of proliferation-sensitive human proteins amongst components of the 40 S hnRNP particles. Identity of hnRNP core proteins in the HeLa protein catalogue. FEBS Lett. 1986, 194, 101-109.
    • (1986) FEBS Lett. , vol.194 , pp. 101-109
    • Celis, J.E.1    Bravo, R.2    Arenstorf, H.P.3    LeStourgeon, W.M.4
  • 5
    • 0017628745 scopus 로고
    • The packaging proteins of core hnRNP particles and the maintenance of proliferative cell states
    • LeStourgeon, W. M., Beyer, A. L., Christensen, M. E., Walker, B. W. et al., The packaging proteins of core hnRNP particles and the maintenance of proliferative cell states. Cold Spring Harb. Symp. Quant. Biol. 1978, 42(Pt 2), 885-898.
    • (1978) Cold Spring Harb. Symp. Quant. Biol. , vol.42 , Issue.PART 2 , pp. 885-898
    • LeStourgeon, W.M.1    Beyer, A.L.2    Christensen, M.E.3    Walker, B.W.4
  • 6
    • 23844489788 scopus 로고    scopus 로고
    • Roles of heterogeneous nuclear ribonucleoproteins A and B in cell proliferation
    • He, Y., Brown, M. A., Rothnagel, J. A., Saunders, N. A., Smith, R., Roles of heterogeneous nuclear ribonucleoproteins A and B in cell proliferation. J. Cell Sci. 2005, 118, 3173-3183.
    • (2005) J. Cell Sci. , vol.118 , pp. 3173-3183
    • He, Y.1    Brown, M.A.2    Rothnagel, J.A.3    Saunders, N.A.4    Smith, R.5
  • 7
    • 0345275873 scopus 로고    scopus 로고
    • Small interfering RNA-mediated reduction in heterogeneous nuclear ribonucleoparticule A1/A2 proteins induces apoptosis in human cancer cells but not in normal mortal cell lines
    • Patry, C., Bouchard, L., Labrecque, P., Gendron, D. et al., Small interfering RNA-mediated reduction in heterogeneous nuclear ribonucleoparticule A1/A2 proteins induces apoptosis in human cancer cells but not in normal mortal cell lines. Cancer Res. 2003, 63, 7679-7688.
    • (2003) Cancer Res. , vol.63 , pp. 7679-7688
    • Patry, C.1    Bouchard, L.2    Labrecque, P.3    Gendron, D.4
  • 8
    • 38349076683 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A3 binds single-stranded telomeric DNA and inhibits telomerase extension in vitro
    • Huang, P. R., Tsai, S. T., Hsieh, K. H., Wang, T. C., Heterogeneous nuclear ribonucleoprotein A3 binds single-stranded telomeric DNA and inhibits telomerase extension in vitro. Biochim. Biophys. Acta 2008, 1783, 193-202.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 193-202
    • Huang, P.R.1    Tsai, S.T.2    Hsieh, K.H.3    Wang, T.C.4
  • 9
    • 67651249577 scopus 로고    scopus 로고
    • Proteomic analysis of the differential protein expression reveals nuclear GAPDH in activated T lymphocytes
    • Sheng, W. Y., Wang, T. C., Proteomic analysis of the differential protein expression reveals nuclear GAPDH in activated T lymphocytes. PloS One 2009, 4, e6322.
    • (2009) PloS One , vol.4
    • Sheng, W.Y.1    Wang, T.C.2
  • 10
    • 0035870912 scopus 로고    scopus 로고
    • Telomerase is regulated by protein kinase C-zeta in human nasopharyngeal cancer cells
    • Yu, C. C., Lo, S. C., Wang, T. C., Telomerase is regulated by protein kinase C-zeta in human nasopharyngeal cancer cells. Biochem. J. 2001, 355, 459-464.
    • (2001) Biochem. J. , vol.355 , pp. 459-464
    • Yu, C.C.1    Lo, S.C.2    Wang, T.C.3
  • 11
    • 79961220477 scopus 로고    scopus 로고
    • Identification of guanylate-binding protein 1 as a potential oral cancer marker involved in cell invasion using omics-based analysis
    • Yu, C. J., Chang, K. P., Chang, Y. J., Hsu, C. W. et al., Identification of guanylate-binding protein 1 as a potential oral cancer marker involved in cell invasion using omics-based analysis. J. Proteome Res. 2011, 10, 3778-3788.
    • (2011) J. Proteome Res. , vol.10 , pp. 3778-3788
    • Yu, C.J.1    Chang, K.P.2    Chang, Y.J.3    Hsu, C.W.4
  • 12
    • 84865135805 scopus 로고    scopus 로고
    • N-(1-Pyrenyl) maleimide inhibits telomerase activity in a cell free system and induces apoptosis in Jurkat cells
    • Huang, P. R., Yeh, Y. M., Pao, C. C., Chen, C. Y., Wang, T. C., N-(1-Pyrenyl) maleimide inhibits telomerase activity in a cell free system and induces apoptosis in Jurkat cells. Mol. Biol. Rep. 2012, 39, 8899-8905.
    • (2012) Mol. Biol. Rep. , vol.39 , pp. 8899-8905
    • Huang, P.R.1    Yeh, Y.M.2    Pao, C.C.3    Chen, C.Y.4    Wang, T.C.5
  • 13
    • 84879987276 scopus 로고    scopus 로고
    • Proteome-wide dysregulation by glucose-6-phosphate dehydrogenase (G6PD) reveals a novel protective role for G6PD in aflatoxin B(1)-mediated cytotoxicity
    • Lin, H. R., Wu, C. C., Wu, Y. H., Hsu, C. W. et al., Proteome-wide dysregulation by glucose-6-phosphate dehydrogenase (G6PD) reveals a novel protective role for G6PD in aflatoxin B(1)-mediated cytotoxicity. J. Proteome Res. 2013, 12, 3434-3448.
    • (2013) J. Proteome Res. , vol.12 , pp. 3434-3448
    • Lin, H.R.1    Wu, C.C.2    Wu, Y.H.3    Hsu, C.W.4
  • 14
    • 79953171559 scopus 로고    scopus 로고
    • Proteome-wide dysregulation by PRA1 depletion delineates a role of PRA1 in lipid transport and cell migration
    • M900641-MCP900200
    • Liu, H. P., Wu, C. C., Kao, H. Y., Huang, Y. C. et al., Proteome-wide dysregulation by PRA1 depletion delineates a role of PRA1 in lipid transport and cell migration. Mol. Cell. Proteomics 2011, 10, M900641-MCP900200.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Liu, H.P.1    Wu, C.C.2    Kao, H.Y.3    Huang, Y.C.4
  • 15
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • Olsen, J. V., de Godoy, L. M., Li, G., Macek, B. et al., Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol. Cell. Proteomics 2005, 4, 2010-2021.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.2    Li, G.3    Macek, B.4
  • 16
    • 52649098504 scopus 로고    scopus 로고
    • Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometer
    • Bantscheff, M., Boesche, M., Eberhard, D., Matthieson, T. et al., Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometer. Mol. Cell. Proteomics 2008, 7, 1702-1713.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1702-1713
    • Bantscheff, M.1    Boesche, M.2    Eberhard, D.3    Matthieson, T.4
  • 17
    • 36348987990 scopus 로고    scopus 로고
    • iTRAQ reagent-based quantitative proteomic analysis on a linear ion trap mass spectrometer
    • Griffin, T. J., Xie, H., Bandhakavi, S., Popko, J. et al., iTRAQ reagent-based quantitative proteomic analysis on a linear ion trap mass spectrometer. J. Proteome Res. 2007, 6, 4200-4209.
    • (2007) J. Proteome Res. , vol.6 , pp. 4200-4209
    • Griffin, T.J.1    Xie, H.2    Bandhakavi, S.3    Popko, J.4
  • 18
    • 76649106744 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of prostate cancer reveals a role for miR-128 in prostate cancer
    • Khan, A. P., Poisson, L. M., Bhat, V. B., Fermin, D. et al., Quantitative proteomic profiling of prostate cancer reveals a role for miR-128 in prostate cancer. Mol. Cell. Proteomics 2010, 9, 298-312.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 298-312
    • Khan, A.P.1    Poisson, L.M.2    Bhat, V.B.3    Fermin, D.4
  • 19
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • Mueller, L. N., Brusniak, M. Y., Mani, D. R., Aebersold, R., An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. J. Proteome Res. 2008, 7, 51-61.
    • (2008) J. Proteome Res. , vol.7 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.Y.2    Mani, D.R.3    Aebersold, R.4
  • 20
    • 79953293308 scopus 로고    scopus 로고
    • Quantitative plasma proteome analysis reveals aberrant level of blood coagulation-related proteins in nasopharyngeal carcinoma
    • Peng, P. H., Wu, C. C., Liu, S. C., Chang, K. P. et al., Quantitative plasma proteome analysis reveals aberrant level of blood coagulation-related proteins in nasopharyngeal carcinoma. J. Proteomics 2011, 74, 744-757.
    • (2011) J. Proteomics , vol.74 , pp. 744-757
    • Peng, P.H.1    Wu, C.C.2    Liu, S.C.3    Chang, K.P.4
  • 21
    • 84869219269 scopus 로고    scopus 로고
    • Interactome-wide analysis identifies end-binding protein 1 as a crucial component for the speck-like particle formation of activated absence in melanoma 2 (AIM2) inflammasomes
    • Wang, L. J., Hsu, C. W., Chen, C. C., Liang, Y. et al., Interactome-wide analysis identifies end-binding protein 1 as a crucial component for the speck-like particle formation of activated absence in melanoma 2 (AIM2) inflammasomes. Mol. Cell. Proteomics 2012, 11, 1230-1244.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1230-1244
    • Wang, L.J.1    Hsu, C.W.2    Chen, C.C.3    Liang, Y.4
  • 22
    • 77952909304 scopus 로고    scopus 로고
    • Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas
    • Wu, C. C., Hsu, C. W., Chen, C. D., Yu, C. J. et al., Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas. Mol. Cell. Proteomics 2010, 9, 1100-1117.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1100-1117
    • Wu, C.C.1    Hsu, C.W.2    Chen, C.D.3    Yu, C.J.4
  • 23
    • 77949828806 scopus 로고    scopus 로고
    • Crk and CrkL adaptor proteins: networks for physiological and pathological signaling
    • Birge, R. B., Kalodimos, C., Inagaki, F., Tanaka, S., Crk and CrkL adaptor proteins: networks for physiological and pathological signaling. Cell Commun. Signal. 2009, 7, 13.
    • (2009) Cell Commun. Signal. , vol.7 , pp. 13
    • Birge, R.B.1    Kalodimos, C.2    Inagaki, F.3    Tanaka, S.4
  • 24
    • 0033621446 scopus 로고    scopus 로고
    • The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration
    • Uemura, N., Griffin, J. D., The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration. J. Biol. Chem. 1999, 274, 37525-37532.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37525-37532
    • Uemura, N.1    Griffin, J.D.2
  • 25
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., Hall, A., Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995, 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 26
    • 74449089659 scopus 로고    scopus 로고
    • RhoA/ROCK1 signaling regulates stress granule formation and apoptosis
    • Tsai, N. P., Wei, L. N., RhoA/ROCK1 signaling regulates stress granule formation and apoptosis. Cell. Signal. 2010, 22, 668-675.
    • (2010) Cell. Signal. , vol.22 , pp. 668-675
    • Tsai, N.P.1    Wei, L.N.2
  • 27
    • 36849022482 scopus 로고    scopus 로고
    • Plexin-B1 utilizes RhoA and Rho kinase to promote the integrin-dependent activation of Akt and ERK and endothelial cell motility
    • Basile, J. R., Gavard, J., Gutkind, J. S., Plexin-B1 utilizes RhoA and Rho kinase to promote the integrin-dependent activation of Akt and ERK and endothelial cell motility. J. Biol. Chem. 2007, 282, 34888-34895.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34888-34895
    • Basile, J.R.1    Gavard, J.2    Gutkind, J.S.3
  • 28
    • 65549138571 scopus 로고    scopus 로고
    • RhoA regulates G1-S progression of gastric cancer cells by modulation of multiple INK4 family tumor suppressors
    • Zhang, S., Tang, Q., Xu, F., Xue, Y. et al., RhoA regulates G1-S progression of gastric cancer cells by modulation of multiple INK4 family tumor suppressors. Mol. Cancer Res. 2009, 7, 570-580.
    • (2009) Mol. Cancer Res. , vol.7 , pp. 570-580
    • Zhang, S.1    Tang, Q.2    Xu, F.3    Xue, Y.4
  • 29
    • 0036893185 scopus 로고    scopus 로고
    • DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines
    • Nishihara, H., Maeda, M., Oda, A., Tsuda, M. et al., DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines. Blood 2002, 100, 3968-3974.
    • (2002) Blood , vol.100 , pp. 3968-3974
    • Nishihara, H.1    Maeda, M.2    Oda, A.3    Tsuda, M.4
  • 30
    • 74449089659 scopus 로고    scopus 로고
    • RhoA/ROCK1 signaling regulates stress granule formation and apoptosis
    • Tsai, N. P., Wei, L. N., RhoA/ROCK1 signaling regulates stress granule formation and apoptosis. Cell Signal. 2009, 22, 668-675.
    • (2009) Cell Signal. , vol.22 , pp. 668-675
    • Tsai, N.P.1    Wei, L.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.