메뉴 건너뛰기




Volumn 352, Issue 2, 2014, Pages 152-159

Emerging roles of heterogeneous nuclear ribonucleoprotein K (hnRNP K) in cancer progression

Author keywords

Carcinogenesis; Heterogeneous nuclear ribonucleoprotein K; Prognostic biomarker

Indexed keywords

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; MESSENGER RNA; UNTRANSLATED RNA;

EID: 84906054100     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2014.06.019     Document Type: Review
Times cited : (89)

References (103)
  • 1
    • 0028216121 scopus 로고
    • Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing
    • Dejgaard K., Leffers H., Rasmussen H.H., Madsen P., Kruse T.A., Gesser B., Nielsen H., Celis J.E. Identification, molecular cloning, expression and chromosome mapping of a family of transformation upregulated hnRNP-K proteins derived by alternative splicing. J. Mol. Biol. 1994, 236:33-48.
    • (1994) J. Mol. Biol. , vol.236 , pp. 33-48
    • Dejgaard, K.1    Leffers, H.2    Rasmussen, H.H.3    Madsen, P.4    Kruse, T.A.5    Gesser, B.6    Nielsen, H.7    Celis, J.E.8
  • 3
    • 0023955859 scopus 로고
    • Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins
    • Piñol-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
    • Piñol-Roma, S.1    Choi, Y.D.2    Matunis, M.J.3    Dreyfuss, G.4
  • 4
    • 0024009108 scopus 로고
    • Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities
    • Swanson M.S., Dreyfuss G. Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol. Cell. Biol. 1988, 8:2237-2241.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2237-2241
    • Swanson, M.S.1    Dreyfuss, G.2
  • 5
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
    • Siomi H., Matunis M.J., Michael W.M., Dreyfuss G. The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res. 1993, 21:1193-1198.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 6
    • 0036223676 scopus 로고    scopus 로고
    • The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms
    • Makeyev A.V., Liebhaber S.A. The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms. RNA 2002, 8:265-278.
    • (2002) RNA , vol.8 , pp. 265-278
    • Makeyev, A.V.1    Liebhaber, S.A.2
  • 7
    • 0242637418 scopus 로고    scopus 로고
    • A novel set of nuclear localization signals determine distributions of the αCP RNA-binding proteins
    • Chkheidze A.N., Liebhaber S.A. A novel set of nuclear localization signals determine distributions of the αCP RNA-binding proteins. Mol. Cell. Biol. 2003, 23:8405-8415.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8405-8415
    • Chkheidze, A.N.1    Liebhaber, S.A.2
  • 8
    • 0030978415 scopus 로고    scopus 로고
    • The K nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP K protein
    • Michael W.M., Eder P.S., Dreyfuss G. The K nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J. 1997, 16:3587-3598.
    • (1997) EMBO J. , vol.16 , pp. 3587-3598
    • Michael, W.M.1    Eder, P.S.2    Dreyfuss, G.3
  • 10
    • 34547739089 scopus 로고    scopus 로고
    • Sequence and transcriptional study of HNRPK pseudogenes, and expression and molecular modeling analysis of hnRNP K isoforms
    • Leopoldino A.M., Carregaro F., Silva C.H., Feitosa O., Mancini U.M., Freitas J.M., Tajara E.H. Sequence and transcriptional study of HNRPK pseudogenes, and expression and molecular modeling analysis of hnRNP K isoforms. Genome 2007, 50:451-462.
    • (2007) Genome , vol.50 , pp. 451-462
    • Leopoldino, A.M.1    Carregaro, F.2    Silva, C.H.3    Feitosa, O.4    Mancini, U.M.5    Freitas, J.M.6    Tajara, E.H.7
  • 11
    • 78049353667 scopus 로고    scopus 로고
    • Characterization of multiple alternative forms of heterogeneous nuclear ribonucleoprotein K by phosphate-affinity electrophoresis
    • Kimura Y., Nagata K., Suzuki N., Yokoyama R., Yamanaka Y., Kitamura H., Hirano H., Ohara O. Characterization of multiple alternative forms of heterogeneous nuclear ribonucleoprotein K by phosphate-affinity electrophoresis. Proteomics 2010, 10:3884-3895.
    • (2010) Proteomics , vol.10 , pp. 3884-3895
    • Kimura, Y.1    Nagata, K.2    Suzuki, N.3    Yokoyama, R.4    Yamanaka, Y.5    Kitamura, H.6    Hirano, H.7    Ohara, O.8
  • 12
    • 33744948703 scopus 로고    scopus 로고
    • Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src
    • Ostareck-Lederer A., Ostareck D.H., Rucknagel K.P., Schierhorn A., Moritz B., Huttelmaier S., Flach N., Handoko L., Wahle E. Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src. J. Biol. Chem. 2006, 281:11115-11125.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11115-11125
    • Ostareck-Lederer, A.1    Ostareck, D.H.2    Rucknagel, K.P.3    Schierhorn, A.4    Moritz, B.5    Huttelmaier, S.6    Flach, N.7    Handoko, L.8    Wahle, E.9
  • 13
    • 33947235787 scopus 로고    scopus 로고
    • Direct mass-spectrometric identification of Arg296 and Arg299 as the methylation sites of hnRNP K protein for methyltransferase PRMT1
    • Chiou Y.Y., Lin W.J., Fu S.L., Lin C.H. Direct mass-spectrometric identification of Arg296 and Arg299 as the methylation sites of hnRNP K protein for methyltransferase PRMT1. Protein J. 2007, 26:87-93.
    • (2007) Protein J. , vol.26 , pp. 87-93
    • Chiou, Y.Y.1    Lin, W.J.2    Fu, S.L.3    Lin, C.H.4
  • 14
    • 78751607537 scopus 로고    scopus 로고
    • Identification of the methylation preference region in heterogeneous nuclear ribonucleoprotein K by protein arginine methyltransferase 1 and its implication in regulating nuclear/cytoplasmic distribution
    • Chang Y.I., Hsu S.C., Chau G.Y., Huang C.Y., Sung J.S., Hua W.K., Lin W.J. Identification of the methylation preference region in heterogeneous nuclear ribonucleoprotein K by protein arginine methyltransferase 1 and its implication in regulating nuclear/cytoplasmic distribution. Biochem. Biophys. Res. Commun. 2011, 404:865-869.
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 865-869
    • Chang, Y.I.1    Hsu, S.C.2    Chau, G.Y.3    Huang, C.Y.4    Sung, J.S.5    Hua, W.K.6    Lin, W.J.7
  • 15
    • 43549088269 scopus 로고    scopus 로고
    • Arginine methylation of hnRNP K enhances p53 transcriptional activity
    • Chen Y., Zhou X., Liu N., Wang C., Zhang L., Mo W., Hu G. Arginine methylation of hnRNP K enhances p53 transcriptional activity. FEBS Lett. 2008, 582:1761-1765.
    • (2008) FEBS Lett. , vol.582 , pp. 1761-1765
    • Chen, Y.1    Zhou, X.2    Liu, N.3    Wang, C.4    Zhang, L.5    Mo, W.6    Hu, G.7
  • 16
    • 84865714994 scopus 로고    scopus 로고
    • DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation
    • Pelisch F., Pozzi B., Risso G., Muñoz M.J., Srebrow A. DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation regulates p53 transcriptional activation. J. Biol. Chem. 2012, 287:30789-30799.
    • (2012) J. Biol. Chem. , vol.287 , pp. 30789-30799
    • Pelisch, F.1    Pozzi, B.2    Risso, G.3    Muñoz, M.J.4    Srebrow, A.5
  • 17
    • 85027948730 scopus 로고    scopus 로고
    • SUMOylation of hnRNP-K is required for p53-mediated cell-cycle arrest in response to DNA damage
    • Lee S.W., Lee M.H., Park J.H., Kang S.H., Yoo H.M., Ka S.H., Oh Y.M., Jeon Y.J., Chung C.H. SUMOylation of hnRNP-K is required for p53-mediated cell-cycle arrest in response to DNA damage. EMBO J. 2012, 31:4441-4452.
    • (2012) EMBO J. , vol.31 , pp. 4441-4452
    • Lee, S.W.1    Lee, M.H.2    Park, J.H.3    Kang, S.H.4    Yoo, H.M.5    Ka, S.H.6    Oh, Y.M.7    Jeon, Y.J.8    Chung, C.H.9
  • 18
    • 0028834524 scopus 로고
    • The K protein domain that recruits the interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites. Implications that K protein acts as a docking platform
    • Van Seuningen I., Ostrowski J., Bustelo X.R., Sleath P.R., Bomsztyk K. The K protein domain that recruits the interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites. Implications that K protein acts as a docking platform. J. Biol. Chem. 1995, 270:26976-26985.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26976-26985
    • Van Seuningen, I.1    Ostrowski, J.2    Bustelo, X.R.3    Sleath, P.R.4    Bomsztyk, K.5
  • 20
    • 0034603039 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in the regulation of the interaction of heterogenous nuclear ribonucleoprotein K protein with its protein and RNA partners
    • Ostrowski J., Schullery D.S., Denisenko O.N., Higaki Y., Watts J., Aebersold R., Stempka L., Gschwendt M., Bomsztyk K. Role of tyrosine phosphorylation in the regulation of the interaction of heterogenous nuclear ribonucleoprotein K protein with its protein and RNA partners. J. Biol. Chem. 2000, 275:3619-3628.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3619-3628
    • Ostrowski, J.1    Schullery, D.S.2    Denisenko, O.N.3    Higaki, Y.4    Watts, J.5    Aebersold, R.6    Stempka, L.7    Gschwendt, M.8    Bomsztyk, K.9
  • 21
    • 2942623743 scopus 로고    scopus 로고
    • HnRNP K: one protein multiple processes
    • Bomsztyk K., Denisenko O., Ostrowski J. HnRNP K: one protein multiple processes. BioEssays 2004, 26:629-638.
    • (2004) BioEssays , vol.26 , pp. 629-638
    • Bomsztyk, K.1    Denisenko, O.2    Ostrowski, J.3
  • 23
    • 0035947671 scopus 로고    scopus 로고
    • Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue
    • Habelhah H., Shah K., Huang L., Burlingame A.L., Shokat K.M., Ronai Z. Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue. J. Biol. Chem. 2001, 276:18090-18095.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18090-18095
    • Habelhah, H.1    Shah, K.2    Huang, L.3    Burlingame, A.L.4    Shokat, K.M.5    Ronai, Z.6
  • 26
    • 0242490528 scopus 로고    scopus 로고
    • Nuclear shift of hnRNP K protein in neoplasms and other states of enhanced cell proliferation
    • Ostrowski J., Bomsztyk K. Nuclear shift of hnRNP K protein in neoplasms and other states of enhanced cell proliferation. Br. J. Cancer 2003, 89:1493-1501.
    • (2003) Br. J. Cancer , vol.89 , pp. 1493-1501
    • Ostrowski, J.1    Bomsztyk, K.2
  • 28
    • 0030855478 scopus 로고    scopus 로고
    • The product of the murine homolog of the Drosophila extra sex combs gene displays transcriptional repressor activity
    • Denisenko O.N., Bomsztyk K. The product of the murine homolog of the Drosophila extra sex combs gene displays transcriptional repressor activity. Mol. Cell. Biol. 1997, 17:4707-4717.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4707-4717
    • Denisenko, O.N.1    Bomsztyk, K.2
  • 29
    • 0034686029 scopus 로고    scopus 로고
    • Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein
    • Shnyreva M., Schullery D.S., Suzuki H., Higaki Y., Bomsztyk K. Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein. J. Biol. Chem. 2000, 275:15498-15503.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15498-15503
    • Shnyreva, M.1    Schullery, D.S.2    Suzuki, H.3    Higaki, Y.4    Bomsztyk, K.5
  • 30
    • 0032527924 scopus 로고    scopus 로고
    • In situ cross-linking by cisplatin of nuclear matrix-bound transcription factors to nuclear DNA of human breast cancer cells
    • Samuel S.K., Spencer V.A., Bajno L., Sun J.M., Holth L.T., Oesterreich S., Davie J.R. In situ cross-linking by cisplatin of nuclear matrix-bound transcription factors to nuclear DNA of human breast cancer cells. Cancer Res. 1998, 58:3004-3008.
    • (1998) Cancer Res. , vol.58 , pp. 3004-3008
    • Samuel, S.K.1    Spencer, V.A.2    Bajno, L.3    Sun, J.M.4    Holth, L.T.5    Oesterreich, S.6    Davie, J.R.7
  • 31
    • 0036403836 scopus 로고    scopus 로고
    • Unraveling the organization of the internal nuclear matrix: RNA-dependent anchoring of NuMA to a lamin scaffold
    • Barboro P., D'Arrigo C., Diaspro A., Mormino M., Alberti I., Parodi S., Patrone E., Balbi C. Unraveling the organization of the internal nuclear matrix: RNA-dependent anchoring of NuMA to a lamin scaffold. Exp. Cell Res. 2002, 279:202-218.
    • (2002) Exp. Cell Res. , vol.279 , pp. 202-218
    • Barboro, P.1    D'Arrigo, C.2    Diaspro, A.3    Mormino, M.4    Alberti, I.5    Parodi, S.6    Patrone, E.7    Balbi, C.8
  • 33
    • 57749204774 scopus 로고    scopus 로고
    • Proteomic analysis of the nuclear matrix in the early stages of rat liver carcinogenesis: identification of differentially expressed and MAR-binding proteins
    • Barboro P., D'Arrigo C., Repaci E., Bagnasco L., Orecchia P., Carnemolla B., Patrone E., Balbi C. Proteomic analysis of the nuclear matrix in the early stages of rat liver carcinogenesis: identification of differentially expressed and MAR-binding proteins. Exp. Cell Res. 2009, 315:226-239.
    • (2009) Exp. Cell Res. , vol.315 , pp. 226-239
    • Barboro, P.1    D'Arrigo, C.2    Repaci, E.3    Bagnasco, L.4    Orecchia, P.5    Carnemolla, B.6    Patrone, E.7    Balbi, C.8
  • 34
    • 84863814698 scopus 로고    scopus 로고
    • The role of nuclear matrix proteins binding to matrix attachment regions (MARs) in prostate cancer cell differentiation
    • Barboro P., Repaci E., D'Arrigo C., Balbi C. The role of nuclear matrix proteins binding to matrix attachment regions (MARs) in prostate cancer cell differentiation. PLoS ONE 2012, 7:e40617.
    • (2012) PLoS ONE , vol.7
    • Barboro, P.1    Repaci, E.2    D'Arrigo, C.3    Balbi, C.4
  • 36
    • 33847205083 scopus 로고    scopus 로고
    • What are the molecular ties that maintain genomic loops?
    • Marenduzzo D., Faro-Trindade I., Cook P.R. What are the molecular ties that maintain genomic loops?. Trends Genet. 2007, 23:126-133.
    • (2007) Trends Genet. , vol.23 , pp. 126-133
    • Marenduzzo, D.1    Faro-Trindade, I.2    Cook, P.R.3
  • 39
    • 0029926495 scopus 로고    scopus 로고
    • Zik1, a transcriptional repressor that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein
    • Denisenko O.N., O'Neill B., Ostrowski J., Van Seuningen I., Bomsztyk K. Zik1, a transcriptional repressor that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein. J. Biol. Chem. 1996, 271:27701-27706.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27701-27706
    • Denisenko, O.N.1    O'Neill, B.2    Ostrowski, J.3    Van Seuningen, I.4    Bomsztyk, K.5
  • 40
    • 50249099734 scopus 로고    scopus 로고
    • A proteomics approach for identification of single strand DNA-binding proteins involved in transcriptional regulation of mouse μ opioid receptor gene
    • Choi H.S., Song K.Y., Hwang C.K., Kim C.S., Law P.Y., Wei L.N., Loh H.H. A proteomics approach for identification of single strand DNA-binding proteins involved in transcriptional regulation of mouse μ opioid receptor gene. Mol. Cell. Proteomics 2008, 7:1517-1529.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1517-1529
    • Choi, H.S.1    Song, K.Y.2    Hwang, C.K.3    Kim, C.S.4    Law, P.Y.5    Wei, L.N.6    Loh, H.H.7
  • 41
    • 22544464680 scopus 로고    scopus 로고
    • HnRNP K binds a core polypyrimidine element in the eukaryotic translation initiation factor 4E (eIF4E) promoter, and its regulation of eIF4E contributes to neoplastic transformation
    • Lynch M., Chen L., Ravitz M.J., Mehtani S., Korenblat K., Pazin M.J., Schmidt E.V. HnRNP K binds a core polypyrimidine element in the eukaryotic translation initiation factor 4E (eIF4E) promoter, and its regulation of eIF4E contributes to neoplastic transformation. Mol. Cell. Biol. 2005, 25:6436-6453.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6436-6453
    • Lynch, M.1    Chen, L.2    Ravitz, M.J.3    Mehtani, S.4    Korenblat, K.5    Pazin, M.J.6    Schmidt, E.V.7
  • 42
    • 0032584731 scopus 로고    scopus 로고
    • Differential effects of heterogeneous nuclear ribonucleoprotein K on Sp1- and Sp3-mediated transcriptional activation of a neuronal nicotinic acetylcholine receptor promoter
    • Du Q., Melnikova I.N., Gardner P.D. Differential effects of heterogeneous nuclear ribonucleoprotein K on Sp1- and Sp3-mediated transcriptional activation of a neuronal nicotinic acetylcholine receptor promoter. J. Biol. Chem. 1998, 273:19877-19883.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19877-19883
    • Du, Q.1    Melnikova, I.N.2    Gardner, P.D.3
  • 43
    • 0034618358 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins as regulators of gene expression through interactions with the human thymidine kinase promoter
    • Lau J.S., Baumeister P., Kim E., Roy B., Hsieh T.Y., Lai M., Lee A.S. Heterogeneous nuclear ribonucleoproteins as regulators of gene expression through interactions with the human thymidine kinase promoter. J. Cell. Biochem. 2000, 79:395-406.
    • (2000) J. Cell. Biochem. , vol.79 , pp. 395-406
    • Lau, J.S.1    Baumeister, P.2    Kim, E.3    Roy, B.4    Hsieh, T.Y.5    Lai, M.6    Lee, A.S.7
  • 44
    • 0037111632 scopus 로고    scopus 로고
    • HnRNP-K and Purα act together to repress the transcriptional activity of the CD43 gene promoter
    • Da Silva N., Bharti A., Shelley C.S. HnRNP-K and Purα act together to repress the transcriptional activity of the CD43 gene promoter. Blood 2002, 100:3536-3544.
    • (2002) Blood , vol.100 , pp. 3536-3544
    • Da Silva, N.1    Bharti, A.2    Shelley, C.S.3
  • 45
    • 0037423817 scopus 로고    scopus 로고
    • Posttranscriptional control of renin synthesis: identification of proteins interacting with renin mRNA 3'-untranslated region
    • Skalweit A., Doller A., Huth A., Kähne T., Persson P.B., Thiele B.J. Posttranscriptional control of renin synthesis: identification of proteins interacting with renin mRNA 3'-untranslated region. Circ. Res. 2003, 92:419-427.
    • (2003) Circ. Res. , vol.92 , pp. 419-427
    • Skalweit, A.1    Doller, A.2    Huth, A.3    Kähne, T.4    Persson, P.B.5    Thiele, B.J.6
  • 46
    • 0037053297 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken β-tropomyosin pre-mRNA
    • Expert-Bezançon A., Le Caer J.P., Marie J. Heterogeneous nuclear ribonucleoprotein (hnRNP) K is a component of an intronic splicing enhancer complex that activates the splicing of the alternative exon 6A from chicken β-tropomyosin pre-mRNA. J. Biol. Chem. 2002, 277:16614-16623.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16614-16623
    • Expert-Bezançon, A.1    Le Caer, J.P.2    Marie, J.3
  • 47
    • 84870509497 scopus 로고    scopus 로고
    • Control of alternative splicing by forskolin through hnRNP K during neuronal differentiation
    • Cao W., Razanau A., Feng D., Lobo V.G., Xie J. Control of alternative splicing by forskolin through hnRNP K during neuronal differentiation. Nucleic Acids Res. 2012, 40:8059-8071.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8059-8071
    • Cao, W.1    Razanau, A.2    Feng, D.3    Lobo, V.G.4    Xie, J.5
  • 50
    • 84878871506 scopus 로고
    • Starvation actively inhibits splicing of glucose-6-phosphate dehydrogenase mRNA via a bifunctional ESE/ESS element bound by hnRNP K
    • Cyphert T.J., Suchanek A.L., Griffith B.N., Salati L.M. Starvation actively inhibits splicing of glucose-6-phosphate dehydrogenase mRNA via a bifunctional ESE/ESS element bound by hnRNP K. Biochim. Biophys. Acta 1829, 2013:905-915.
    • (1829) Biochim. Biophys. Acta , vol.2013 , pp. 905-915
    • Cyphert, T.J.1    Suchanek, A.L.2    Griffith, B.N.3    Salati, L.M.4
  • 52
    • 0345549480 scopus 로고    scopus 로고
    • Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo
    • Evans J.R., Mitchell S.A., Spriggs K.A., Ostrowski J., Bomsztyk K., Ostarek D., Willis A.E. Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo. Oncogene 2003, 22:8012-8020.
    • (2003) Oncogene , vol.22 , pp. 8012-8020
    • Evans, J.R.1    Mitchell, S.A.2    Spriggs, K.A.3    Ostrowski, J.4    Bomsztyk, K.5    Ostarek, D.6    Willis, A.E.7
  • 53
    • 0032575526 scopus 로고    scopus 로고
    • Translational inhibition in vitro of human papillomavirus type 16 L2 mRNA mediated through interaction with heterogenous ribonucleoprotein K and poly(rC)-binding proteins 1 and 2
    • Collier B., Goobar-Larsson L., Sokolowski M., Schwartz S. Translational inhibition in vitro of human papillomavirus type 16 L2 mRNA mediated through interaction with heterogenous ribonucleoprotein K and poly(rC)-binding proteins 1 and 2. J. Biol. Chem. 1998, 273:22648-22656.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22648-22656
    • Collier, B.1    Goobar-Larsson, L.2    Sokolowski, M.3    Schwartz, S.4
  • 54
    • 16844370540 scopus 로고    scopus 로고
    • Involvement of Hu and heterogeneous nuclear ribonucleoprotein K in neuronal differentiation through p21 mRNA post-transcriptional regulation
    • Yano M., Okano H.J., Okano H. Involvement of Hu and heterogeneous nuclear ribonucleoprotein K in neuronal differentiation through p21 mRNA post-transcriptional regulation. J. Biol. Chem. 2005, 280:12690-12699.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12690-12699
    • Yano, M.1    Okano, H.J.2    Okano, H.3
  • 55
    • 4344575965 scopus 로고    scopus 로고
    • Control of mRNA translation and stability in haematopoietic cells: the function of hnRNPs K and E1/E2
    • Ostareck-Lederer A., Ostareck D.H. Control of mRNA translation and stability in haematopoietic cells: the function of hnRNPs K and E1/E2. Biol. Cell 2004, 96:407-411.
    • (2004) Biol. Cell , vol.96 , pp. 407-411
    • Ostareck-Lederer, A.1    Ostareck, D.H.2
  • 56
    • 0030772963 scopus 로고    scopus 로고
    • MRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end
    • Ostareck D.H., Ostareck-Lederer A., Wilm M., Thiele B.J., Mann M., Hentze M.W. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end. Cell 1997, 89:597-606.
    • (1997) Cell , vol.89 , pp. 597-606
    • Ostareck, D.H.1    Ostareck-Lederer, A.2    Wilm, M.3    Thiele, B.J.4    Mann, M.5    Hentze, M.W.6
  • 57
    • 49649117795 scopus 로고    scopus 로고
    • MRNA silencing in human erythroid cell maturation: heterogeneous nuclear ribonucleoprotein K controls the expression of its regulator c-Src
    • Naarmann I.S., Harnisch C., Flach N., Kremmer E., Kühn H., Ostareck D.H., Ostareck-Lederer A. mRNA silencing in human erythroid cell maturation: heterogeneous nuclear ribonucleoprotein K controls the expression of its regulator c-Src. J. Biol. Chem. 2008, 283:18461-18472.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18461-18472
    • Naarmann, I.S.1    Harnisch, C.2    Flach, N.3    Kremmer, E.4    Kühn, H.5    Ostareck, D.H.6    Ostareck-Lederer, A.7
  • 59
    • 33746353084 scopus 로고    scopus 로고
    • The DICE-binding activity of KH domain 3 of hnRNP K is affected by c-Src-mediated tyrosine phosphorylation
    • Messias A.C., Harnisch C., Ostareck-Lederer A., Sattler M., Ostareck D.H. The DICE-binding activity of KH domain 3 of hnRNP K is affected by c-Src-mediated tyrosine phosphorylation. J. Mol. Biol. 2006, 361:470-481.
    • (2006) J. Mol. Biol. , vol.361 , pp. 470-481
    • Messias, A.C.1    Harnisch, C.2    Ostareck-Lederer, A.3    Sattler, M.4    Ostareck, D.H.5
  • 60
    • 0027182876 scopus 로고
    • Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro
    • Takimoto M., Tomonaga T., Matunis M., Avigan M., Krutzsch H., Dreyfuss G., Levens D. Specific binding of heterogeneous ribonucleoprotein particle protein K to the human c-myc promoter, in vitro. J. Biol. Chem. 1993, 268:18249-18258.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18249-18258
    • Takimoto, M.1    Tomonaga, T.2    Matunis, M.3    Avigan, M.4    Krutzsch, H.5    Dreyfuss, G.6    Levens, D.7
  • 62
    • 1642291861 scopus 로고    scopus 로고
    • Differential protein synthesis and expression levels in normal and neoplastic human prostate cells and their regulation by type I and II interferons
    • Nagano K., Masters J.R., Akpan A., Yang A., Corless S., Wood C., Hastie C., Zvelebil M., Cramer R., Naaby-Hansen S. Differential protein synthesis and expression levels in normal and neoplastic human prostate cells and their regulation by type I and II interferons. Oncogene 2004, 23:1693-1703.
    • (2004) Oncogene , vol.23 , pp. 1693-1703
    • Nagano, K.1    Masters, J.R.2    Akpan, A.3    Yang, A.4    Corless, S.5    Wood, C.6    Hastie, C.7    Zvelebil, M.8    Cramer, R.9    Naaby-Hansen, S.10
  • 65
    • 34250178439 scopus 로고    scopus 로고
    • From mRNA metabolism to cancer therapy: chronic myelogenous leukemia shows the way
    • Perrotti D., Neviani P. From mRNA metabolism to cancer therapy: chronic myelogenous leukemia shows the way. Clin. Cancer Res. 2007, 13:1638-1642.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 1638-1642
    • Perrotti, D.1    Neviani, P.2
  • 66
    • 0026788001 scopus 로고
    • Dominant negative MYC blocks transformation by ABL oncogenes
    • Sawyers C.L., Callahan W., Witte O.N. Dominant negative MYC blocks transformation by ABL oncogenes. Cell 1992, 70:901-910.
    • (1992) Cell , vol.70 , pp. 901-910
    • Sawyers, C.L.1    Callahan, W.2    Witte, O.N.3
  • 67
    • 70349442548 scopus 로고    scopus 로고
    • The first 30 years of p53: growing ever more complex
    • Levine A.J., Oren M. The first 30 years of p53: growing ever more complex. Nat. Rev. Cancer 2009, 9:749-758.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 749-758
    • Levine, A.J.1    Oren, M.2
  • 68
    • 28944446040 scopus 로고    scopus 로고
    • HnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage
    • Moumen A., Masterson P., O'Connor M.J., Jackson S.P. HnRNP K: an HDM2 target and transcriptional coactivator of p53 in response to DNA damage. Cell 2005, 123:1065-1078.
    • (2005) Cell , vol.123 , pp. 1065-1078
    • Moumen, A.1    Masterson, P.2    O'Connor, M.J.3    Jackson, S.P.4
  • 69
    • 84874586389 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of heterogeneous nuclear ribonucleoprotein K promotes p53 transcriptional activation in response to DNA damage
    • Moumen A., Magill C., Dry K.L., Jackson S.P. ATM-dependent phosphorylation of heterogeneous nuclear ribonucleoprotein K promotes p53 transcriptional activation in response to DNA damage. Cell Cycle 2013, 12:698-704.
    • (2013) Cell Cycle , vol.12 , pp. 698-704
    • Moumen, A.1    Magill, C.2    Dry, K.L.3    Jackson, S.P.4
  • 70
    • 84880266961 scopus 로고    scopus 로고
    • HnRNP K suppresses apoptosis independent of p53 status by maintaining high levels of endogenous caspase inhibitor
    • Xiao Z., Ko H.L., Goh E.H., Wang B., Ren E.C. hnRNP K suppresses apoptosis independent of p53 status by maintaining high levels of endogenous caspase inhibitor. Carcinogenesis 2013, 34:1458-1467.
    • (2013) Carcinogenesis , vol.34 , pp. 1458-1467
    • Xiao, Z.1    Ko, H.L.2    Goh, E.H.3    Wang, B.4    Ren, E.C.5
  • 71
    • 84887101163 scopus 로고    scopus 로고
    • MicroRNAs and other non-coding RNAs as targets for anticancer drug development
    • Ling H., Fabbri M., Calin G.A. MicroRNAs and other non-coding RNAs as targets for anticancer drug development. Nat. Rev. Drug. Discov. 2013, 12:847-865.
    • (2013) Nat. Rev. Drug. Discov. , vol.12 , pp. 847-865
    • Ling, H.1    Fabbri, M.2    Calin, G.A.3
  • 73
    • 77955319040 scopus 로고    scopus 로고
    • Noncoding RNAs: the missing "linc" in p53-mediated repression
    • Barsotti A.M., Prives C. Noncoding RNAs: the missing "linc" in p53-mediated repression. Cell 2010, 142:358-360.
    • (2010) Cell , vol.142 , pp. 358-360
    • Barsotti, A.M.1    Prives, C.2
  • 74
    • 44049092769 scopus 로고    scopus 로고
    • Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription
    • Kim K., Choi J., Heo K., Kim H., Levens D., Kohno K., Johnson E.M., Brock H.W., An W. Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription. J. Biol. Chem. 2008, 283:9113-9126.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9113-9126
    • Kim, K.1    Choi, J.2    Heo, K.3    Kim, H.4    Levens, D.5    Kohno, K.6    Johnson, E.M.7    Brock, H.W.8    An, W.9
  • 80
    • 33749370720 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K is over expressed, aberrantly localised and is associated with poor prognosis in colorectal cancer
    • Carpenter B., McKay M., Dundas S.R., Lawrie L.C., Telfer C., Murray G.I. Heterogeneous nuclear ribonucleoprotein K is over expressed, aberrantly localised and is associated with poor prognosis in colorectal cancer. Br. J. Cancer 2006, 95:921-927.
    • (2006) Br. J. Cancer , vol.95 , pp. 921-927
    • Carpenter, B.1    McKay, M.2    Dundas, S.R.3    Lawrie, L.C.4    Telfer, C.5    Murray, G.I.6
  • 81
    • 84872799855 scopus 로고    scopus 로고
    • Immunohistochemical detection of HSP27 and hnRNP K as prognostic and predictive biomarkers for colorectal cancer
    • Wang F., Zhang P., Shi C., Yang Y., Qin H. Immunohistochemical detection of HSP27 and hnRNP K as prognostic and predictive biomarkers for colorectal cancer. Med. Oncol. 2012, 29:1780-1788.
    • (2012) Med. Oncol. , vol.29 , pp. 1780-1788
    • Wang, F.1    Zhang, P.2    Shi, C.3    Yang, Y.4    Qin, H.5
  • 82
    • 34547916791 scopus 로고    scopus 로고
    • Evidence for heterogeneous nuclear ribonucleoprotein K overexpression in oral squamous cell carcinoma
    • Roychoudhury P., Chaudhuri K. Evidence for heterogeneous nuclear ribonucleoprotein K overexpression in oral squamous cell carcinoma. Br. J. Cancer 2007, 97:574-575.
    • (2007) Br. J. Cancer , vol.97 , pp. 574-575
    • Roychoudhury, P.1    Chaudhuri, K.2
  • 84
    • 84862800183 scopus 로고    scopus 로고
    • Heterogeneous ribonucleoprotein K and thymidine phosphorylase are independent prognostic and therapeutic markers for oral squamous cell carcinoma
    • Wu C.S., Chang K.P., Chen L.C., Chen C.C., Liang Y., Hseuh C., Chang Y.S. Heterogeneous ribonucleoprotein K and thymidine phosphorylase are independent prognostic and therapeutic markers for oral squamous cell carcinoma. Oral Oncol. 2012, 48:516-522.
    • (2012) Oral Oncol. , vol.48 , pp. 516-522
    • Wu, C.S.1    Chang, K.P.2    Chen, L.C.3    Chen, C.C.4    Liang, Y.5    Hseuh, C.6    Chang, Y.S.7
  • 85
    • 33845587418 scopus 로고    scopus 로고
    • Protein clusters associated with carcinogenesis, histological differentiation and nodal metastasis in esophageal cancer
    • Hatakeyama H., Kondo T., Fujii K., Nakanishi Y., Kato H., Fukuda S., Hirohashi S. Protein clusters associated with carcinogenesis, histological differentiation and nodal metastasis in esophageal cancer. Proteomics 2006, 6:6300-6316.
    • (2006) Proteomics , vol.6 , pp. 6300-6316
    • Hatakeyama, H.1    Kondo, T.2    Fujii, K.3    Nakanishi, Y.4    Kato, H.5    Fukuda, S.6    Hirohashi, S.7
  • 86
    • 52449111395 scopus 로고    scopus 로고
    • Heterogeneous ribonucleoprotein K and thymidine phosphorylase are independent prognostic and therapeutic markers for nasopharyngeal carcinoma
    • Chen L.C., Hsueh C., Tsang N.M., Liang Y., Chang K.P., Hao S.P., Yu J.S., Chang Y.S. Heterogeneous ribonucleoprotein K and thymidine phosphorylase are independent prognostic and therapeutic markers for nasopharyngeal carcinoma. Clin. Cancer Res. 2008, 14:3807-3813.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 3807-3813
    • Chen, L.C.1    Hsueh, C.2    Tsang, N.M.3    Liang, Y.4    Chang, K.P.5    Hao, S.P.6    Yu, J.S.7    Chang, Y.S.8
  • 88
    • 84863227127 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K (hnRNP K) is a tissue biomarker for detection of early hepatocellular carcinoma in patients with cirrhosis
    • Guo Y., Zhao J., Bi J., Wu Q., Wang X., Lai Q. Heterogeneous nuclear ribonucleoprotein K (hnRNP K) is a tissue biomarker for detection of early hepatocellular carcinoma in patients with cirrhosis. J. Hematol. Oncol. 2012, 5:37.
    • (2012) J. Hematol. Oncol. , vol.5 , pp. 37
    • Guo, Y.1    Zhao, J.2    Bi, J.3    Wu, Q.4    Wang, X.5    Lai, Q.6
  • 89
    • 34547458188 scopus 로고    scopus 로고
    • Loss-of-function screening by randomized intracellular antibodies: identification of hnRNP-K as a potential target for metastasis
    • Inoue A., Sawata S.Y., Taira K., Wadhwa R. Loss-of-function screening by randomized intracellular antibodies: identification of hnRNP-K as a potential target for metastasis. Proc. Natl. Acad. Sci. USA 2007, 104:8983-8988.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8983-8988
    • Inoue, A.1    Sawata, S.Y.2    Taira, K.3    Wadhwa, R.4
  • 90
    • 84878221242 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein K (hnRNP-K) promotes tumor metastasis by induction of genes involved in extracellular matrix, cell movement, and angiogenesis
    • Gao R., Yu Y., Inoue A., Widodo N., Kaul S.C., Wadhwa R. Heterogeneous nuclear ribonucleoprotein K (hnRNP-K) promotes tumor metastasis by induction of genes involved in extracellular matrix, cell movement, and angiogenesis. J. Biol. Chem. 2013, 288:15046-15056.
    • (2013) J. Biol. Chem. , vol.288 , pp. 15046-15056
    • Gao, R.1    Yu, Y.2    Inoue, A.3    Widodo, N.4    Kaul, S.C.5    Wadhwa, R.6
  • 91
    • 65649100065 scopus 로고    scopus 로고
    • Novel antivascular efficacy of metronomic docetaxel therapy in prostate cancer: hnRNP K as a player
    • Benelli R., Monteghirfo S., Balbi C., Barboro P., Ferrari N. Novel antivascular efficacy of metronomic docetaxel therapy in prostate cancer: hnRNP K as a player. Int. J. Cancer 2009, 124:2989-2996.
    • (2009) Int. J. Cancer , vol.124 , pp. 2989-2996
    • Benelli, R.1    Monteghirfo, S.2    Balbi, C.3    Barboro, P.4    Ferrari, N.5
  • 95
    • 79959289248 scopus 로고    scopus 로고
    • Androgen receptor and heterogeneous nuclear ribonucleoprotein K colocalize in the nucleoplasm and are modulated by bicalutamide and 4-hydroxy-tamoxifen in prostatic cancer cell lines
    • Barboro P., Repaci E., Ferrari N., Rubagotti A., Boccardo F., Balbi C. Androgen receptor and heterogeneous nuclear ribonucleoprotein K colocalize in the nucleoplasm and are modulated by bicalutamide and 4-hydroxy-tamoxifen in prostatic cancer cell lines. Prostate 2011, 71:1466-1479.
    • (2011) Prostate , vol.71 , pp. 1466-1479
    • Barboro, P.1    Repaci, E.2    Ferrari, N.3    Rubagotti, A.4    Boccardo, F.5    Balbi, C.6
  • 96
    • 84893365879 scopus 로고    scopus 로고
    • Androgen receptor activity is affected by both nuclear matrix localization and the phosphorylation status of the heterogeneous nuclear ribonucleoprotein K in anti-androgen-treated LNCaP cells
    • Barboro P., Borzì L., Repaci E., Ferrari N., Balbi C. Androgen receptor activity is affected by both nuclear matrix localization and the phosphorylation status of the heterogeneous nuclear ribonucleoprotein K in anti-androgen-treated LNCaP cells. PLoS ONE 2013, 8:e79212.
    • (2013) PLoS ONE , vol.8
    • Barboro, P.1    Borzì, L.2    Repaci, E.3    Ferrari, N.4    Balbi, C.5
  • 97
    • 20144374569 scopus 로고    scopus 로고
    • Influence of neuroendocrine tumor cells on proliferation in prostatic carcinoma
    • Grobholz R., Griebe M., Sauer C.G., Michel M.S., Trojan L., Bleyl U. Influence of neuroendocrine tumor cells on proliferation in prostatic carcinoma. Hum. Pathol. 2005, 36:562-570.
    • (2005) Hum. Pathol. , vol.36 , pp. 562-570
    • Grobholz, R.1    Griebe, M.2    Sauer, C.G.3    Michel, M.S.4    Trojan, L.5    Bleyl, U.6
  • 98
    • 84861576558 scopus 로고    scopus 로고
    • Regulation of neuroendocrine differentiation by AKT/hnRNPK/AR/β-catenin signaling in prostate cancer cells
    • Ciarlo M., Benelli R., Barbieri O., Minghelli S., Barboro P., Balbi C., Ferrari N. Regulation of neuroendocrine differentiation by AKT/hnRNPK/AR/β-catenin signaling in prostate cancer cells. Int. J. Cancer 2012, 131:582-590.
    • (2012) Int. J. Cancer , vol.131 , pp. 582-590
    • Ciarlo, M.1    Benelli, R.2    Barbieri, O.3    Minghelli, S.4    Barboro, P.5    Balbi, C.6    Ferrari, N.7
  • 99
    • 0037049762 scopus 로고    scopus 로고
    • Post-transcriptional mechanisms in BCR/ABL leukemogenesis: role of shuttling RNA-binding proteins
    • Perrotti D., Calabretta B. Post-transcriptional mechanisms in BCR/ABL leukemogenesis: role of shuttling RNA-binding proteins. Oncogene 2002, 21:8577-8583.
    • (2002) Oncogene , vol.21 , pp. 8577-8583
    • Perrotti, D.1    Calabretta, B.2
  • 101
    • 67349245198 scopus 로고    scopus 로고
    • Thymidine phosphorylase mRNA stability and protein levels are increased through ERK-mediated cytoplasmic accumulation of hnRNP K in nasopharyngeal carcinoma cells
    • Chen L.C., Liu H.P., Li H.P., Hsueh C., Yu J.S., Liang C.L., Chang Y.S. Thymidine phosphorylase mRNA stability and protein levels are increased through ERK-mediated cytoplasmic accumulation of hnRNP K in nasopharyngeal carcinoma cells. Oncogene 2009, 28:1904-1915.
    • (2009) Oncogene , vol.28 , pp. 1904-1915
    • Chen, L.C.1    Liu, H.P.2    Li, H.P.3    Hsueh, C.4    Yu, J.S.5    Liang, C.L.6    Chang, Y.S.7
  • 102
    • 78549294158 scopus 로고    scopus 로고
    • Autoantibodies specific to hnRNP K: a new diagnostic marker for immune pathophysiology in aplastic anemia
    • Qi Z., Takamatsu H., Espinoza J.L., Lu X., Sugimori N., Yamazaki H., Okawa K., Nakao S. Autoantibodies specific to hnRNP K: a new diagnostic marker for immune pathophysiology in aplastic anemia. Ann. Hematol. 2010, 89:1255-1263.
    • (2010) Ann. Hematol. , vol.89 , pp. 1255-1263
    • Qi, Z.1    Takamatsu, H.2    Espinoza, J.L.3    Lu, X.4    Sugimori, N.5    Yamazaki, H.6    Okawa, K.7    Nakao, S.8
  • 103
    • 79958706584 scopus 로고    scopus 로고
    • Immunoproteomics of HER2-positive and HER2-negative breast cancer patients with positive lymph nodes
    • Mojtahedi Z., Safaei A., Yousefi Z., Ghaderi A. Immunoproteomics of HER2-positive and HER2-negative breast cancer patients with positive lymph nodes. OMICS 2011, 15:409-418.
    • (2011) OMICS , vol.15 , pp. 409-418
    • Mojtahedi, Z.1    Safaei, A.2    Yousefi, Z.3    Ghaderi, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.