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Volumn 10, Issue 10, 2014, Pages 1787-1800

A role of autophagy in PTP4A3-driven cancer progression

Author keywords

BECN1; Cancer progression; Mammalian autophagy regulation; PIK3C3; Prognosis marker; PTP4A3

Indexed keywords

CHLOROQUINE; PEPTIDES AND PROTEINS; PROTEIN KINASE B; PROTEIN PTP4A3; PROTEIN SQSTM1; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; LIGHT CHAIN 3, HUMAN; MEMBRANE PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; PROTEIN TYROSINE PHOSPHATASE; PTP4A1 PROTEIN, HUMAN; PTP4A3 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SQSTM1 PROTEIN, HUMAN; TUMOR PROTEIN;

EID: 84907886748     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.29989     Document Type: Article
Times cited : (43)

References (49)
  • 1
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • PMID:18006683
    • Mizushima N. Autophagy: process and function. Genes Dev 2007; 21:2861-73; PMID:18006683; http://dx.doi.org/10.1101/gad.1599207
    • (2007) Genes Dev , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 2
    • 0029582765 scopus 로고
    • Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-kinase essential for normal cell growth and vacuole morphology
    • PMID:8719881
    • Takegawa K, DeWald DB, Emr SD. Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-kinase essential for normal cell growth and vacuole morphology. J Cell Sci 1995; 108:3745-56; PMID:8719881
    • (1995) J Cell Sci , vol.108 , pp. 3745-3756
    • Takegawa, K.1    DeWald, D.B.2    Emr, S.D.3
  • 3
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • PMID:10625637
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P. Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 2000; 275:992-8; PMID:10625637; http://dx.doi.org/10.1074/jbc.275.2.992
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 4
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • PMID:20097051
    • He C, Levine B. The Beclin 1 interactome. Curr Opin Cell Biol 2010; 22:140-9; PMID:20097051; http://dx.doi.org/10.1016/j.ceb.2010.01.001
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 140-149
    • He, C.1    Levine, B.2
  • 5
    • 79954544250 scopus 로고    scopus 로고
    • LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis
    • PMID:21497758
    • Weidberg H, Shpilka T, Shvets E, Abada A, Shimron F, Elazar Z. LC3 and GATE-16 N termini mediate membrane fusion processes required for autophagosome biogenesis. Dev Cell 2011; 20:444-54; PMID:21497758; http://dx.doi.org/10.1016/j.devcel.2011.02.006
    • (2011) Dev Cell , vol.20 , pp. 444-454
    • Weidberg, H.1    Shpilka, T.2    Shvets, E.3    Abada, A.4    Shimron, F.5    Elazar, Z.6
  • 6
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • PMID:17986448
    • Hanada T, Noda NN, Satomi Y, Ichimura Y, Fujioka Y, Takao T, Inagaki F, Ohsumi Y. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 2007; 282:37298-302; PMID:17986448; http://dx.doi.org/10.1074/jbc.C700195200
    • (2007) J Biol Chem , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5    Takao, T.6    Inagaki, F.7    Ohsumi, Y.8
  • 7
    • 84355162283 scopus 로고    scopus 로고
    • Canonical and non-canonical autophagy: Variations on a common theme of self-eating?
    • PMID:22166994
    • Codogno P, Mehrpour M, Proikas-Cezanne T. Canonical and non-canonical autophagy: variations on a common theme of self-eating? Nat Rev Mol Cell Biol 2012; 13:7-12; PMID:22166994
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 7-12
    • Codogno, P.1    Mehrpour, M.2    Proikas-Cezanne, T.3
  • 8
    • 84872231223 scopus 로고    scopus 로고
    • The PI3K, metabolic, and autophagy networks: Interactive partners in cellular health and disease
    • PMID:23294306
    • Shanware NP, Bray K, Abraham RT. The PI3K, metabolic, and autophagy networks: interactive partners in cellular health and disease. Annu Rev Pharmacol Toxicol 2013; 53:89-106; PMID:23294306; http://dx.doi.org/10.1146/annurev-pharmtox-010611-134717
    • (2013) Annu Rev Pharmacol Toxicol , vol.53 , pp. 89-106
    • Shanware, N.P.1    Bray, K.2    Abraham, R.T.3
  • 9
    • 80052227050 scopus 로고    scopus 로고
    • Autophagy as a target for anticancer therapy. Nature reviews
    • Janku F, McConkey DJ, Hong DS, Kurzrock R. Autophagy as a target for anticancer therapy. Nature reviews. Clin Oncol 2011; 8:528-39
    • (2011) Clin Oncol , vol.8 , pp. 528-539
    • Janku, F.1    McConkey, D.J.2    Hong, D.S.3    Kurzrock, R.4
  • 10
    • 0032539752 scopus 로고    scopus 로고
    • Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1
    • PMID:9514946
    • Zeng Q, Hong W, Tan YH. Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1. Biochem Biophys Res Commun 1998; 244:421-7; PMID:9514946; http://dx.doi.org/10.1006/bbrc.1998.8291
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 421-427
    • Zeng, Q.1    Hong, W.2    Tan, Y.H.3
  • 11
    • 78649878760 scopus 로고    scopus 로고
    • PRL-3 phosphatase and cancer metastasis
    • PMID:21053359
    • Al-Aidaroos AQO, Zeng Q. PRL-3 phosphatase and cancer metastasis. J Cell Biochem 2010; 111:1087-98; PMID:21053359; http://dx.doi.org/10.1002/jcb.22913
    • (2010) J Cell Biochem , vol.111 , pp. 1087-1098
    • Al-Aidaroos, A.Q.O.1    Zeng, Q.2
  • 14
    • 34248155345 scopus 로고    scopus 로고
    • PRL-3 down-regulates PTEN expression and signals through PI3K to promote epithelial-mesenchymal transition
    • PMID:17409395
    • Wang H, Quah SY, Dong JM, Manser E, Tang JP, Zeng Q. PRL-3 down-regulates PTEN expression and signals through PI3K to promote epithelial-mesenchymal transition. Cancer Res 2007; 67:2922-6; PMID:17409395; http://dx.doi.org/10.1158/0008-5472.CAN-06-3598
    • (2007) Cancer Res , vol.67 , pp. 2922-2926
    • Wang, H.1    Quah, S.Y.2    Dong, J.M.3    Manser, E.4    Tang, J.P.5    Zeng, Q.6
  • 15
    • 33645516549 scopus 로고    scopus 로고
    • PRL tyrosine phosphatases regulate rho family GTPases to promote invasion and motility
    • PMID:16540666
    • Fiordalisi JJ, Keller PJ, Cox AD. PRL tyrosine phosphatases regulate rho family GTPases to promote invasion and motility. Cancer Res 2006; 66:3153-61; PMID:16540666; http://dx.doi.org/10.1158/0008-5472.CAN-05-3116
    • (2006) Cancer Res , vol.66 , pp. 3153-3161
    • Fiordalisi, J.J.1    Keller, P.J.2    Cox, A.D.3
  • 17
    • 33750359173 scopus 로고    scopus 로고
    • PRL-3 initiates tumor angiogenesis by recruiting endothelial cells in vitro and in vivo
    • PMID:17018620
    • Guo K, Li J, Wang H, Osato M, Tang JP, Quah SY, Gan BQ, Zeng Q. PRL-3 initiates tumor angiogenesis by recruiting endothelial cells in vitro and in vivo. Cancer Res 2006; 66:9625-35; PMID:17018620; http://dx.doi.org/10.1158/0008-5472.CAN-06-0726
    • (2006) Cancer Res , vol.66 , pp. 9625-9635
    • Guo, K.1    Li, J.2    Wang, H.3    Osato, M.4    Tang, J.P.5    Quah, S.Y.6    Gan, B.Q.7    Zeng, Q.8
  • 18
    • 42949121716 scopus 로고    scopus 로고
    • The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation
    • PMID:18471976
    • Basak S, Jacobs SBR, Krieg AJ, Pathak N, Zeng Q, Kaldis P, Giaccia AJ, Attardi LD. The metastasis-associated gene Prl-3 is a p53 target involved in cell-cycle regulation. Mol Cell 2008; 30:303-14; PMID:18471976; http://dx.doi.org/10.1016/j.molcel.2008.04.002
    • (2008) Mol Cell , vol.30 , pp. 303-314
    • Basak, S.1    Jacobs, S.B.R.2    Krieg, A.J.3    Pathak, N.4    Zeng, Q.5    Kaldis, P.6    Giaccia, A.J.7    Attardi, L.D.8
  • 19
    • 33746904684 scopus 로고    scopus 로고
    • Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer
    • PMID:16832410
    • Radke I, Götte M, Kersting C, Mattsson B, Kiesel L, Wülfing P. Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer. Br J Cancer 2006; 95:347-54; PMID:16832410; http://dx.doi.org/10.1038/sj.bjc.6603261
    • (2006) Br J Cancer , vol.95 , pp. 347-354
    • Radke, I.1    Götte, M.2    Kersting, C.3    Mattsson, B.4    Kiesel, L.5    Wülfing, P.6
  • 20
    • 62449336307 scopus 로고    scopus 로고
    • Over-expression of phosphatase of regenerating liver-3 correlates with tumor progression and poor prognosis in nasopharyngeal carcinoma
    • PMID:19101992
    • Zhou J, Wang S, Lu J, Li J, Ding Y. Over-expression of phosphatase of regenerating liver-3 correlates with tumor progression and poor prognosis in nasopharyngeal carcinoma. Int J Cancer 2009; 124:1879-86; PMID:19101992; http://dx.doi.org/10.1002/ijc.24096
    • (2009) Int J Cancer , vol.124 , pp. 1879-1886
    • Zhou, J.1    Wang, S.2    Lu, J.3    Li, J.4    Ding, Y.5
  • 21
    • 65349155174 scopus 로고    scopus 로고
    • Early endosomes and endosomal coatomer are required for autophagy
    • PMID:19364919
    • Razi M, Chan EYW, Tooze SA. Early endosomes and endosomal coatomer are required for autophagy. J Cell Biol 2009; 185:305-21; PMID:19364919; http://dx.doi.org/10.1083/jcb.200810098
    • (2009) J Cell Biol , vol.185 , pp. 305-321
    • Razi, M.1    Chan, E.Y.W.2    Tooze, S.A.3
  • 22
    • 79957850849 scopus 로고    scopus 로고
    • Following autophagy step by step
    • PMID:21635796
    • Hansen TE, Johansen T. Following autophagy step by step. BMC Biol 2011; 9:39; PMID:21635796; http://dx.doi.org/10.1186/1741-7007-9-39
    • (2011) BMC Biol , vol.9 , pp. 39
    • Hansen, T.E.1    Johansen, T.2
  • 23
    • 77957325618 scopus 로고    scopus 로고
    • Snapin-regulated late endosomal transport is critical for efficient autophagy-lysosomal function in neurons
    • PMID:20920792
    • Cai Q, Lu L, Tian JH, Zhu YB, Qiao H, Sheng ZH. Snapin-regulated late endosomal transport is critical for efficient autophagy-lysosomal function in neurons. Neuron 2010; 68:73-86; PMID:20920792; http://dx.doi.org/10.1016/j.neuron.2010.09.022
    • (2010) Neuron , vol.68 , pp. 73-86
    • Cai, Q.1    Lu, L.2    Tian, J.H.3    Zhu, Y.B.4    Qiao, H.5    Sheng, Z.H.6
  • 24
    • 0034647510 scopus 로고    scopus 로고
    • Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome
    • PMID:10747914
    • Zeng Q, Si X, Horstmann H, Xu Y, Hong W, Pallen CJ. Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. J Biol Chem 2000; 275:21444-52; PMID:10747914; http://dx.doi.org/10.1074/jbc.M000453200
    • (2000) J Biol Chem , vol.275 , pp. 21444-21452
    • Zeng, Q.1    Si, X.2    Horstmann, H.3    Xu, Y.4    Hong, W.5    Pallen, C.J.6
  • 25
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • PMID:9639028
    • Yamamoto A, Tagawa Y, Yoshimori T, Moriyama Y, Masaki R, Tashiro Y. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct 1998; 23:33-42; PMID:9639028; http://dx.doi.org/10.1247/csf.23.33
    • (1998) Cell Struct Funct , vol.23 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 26
    • 0032555641 scopus 로고    scopus 로고
    • Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes
    • PMID:9705327
    • Berg TO, Fengsrud M, Strømhaug PE, Berg T, Seglen PO. Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes. J Biol Chem 1998; 273:21883-92; PMID:9705327; http://dx.doi.org/10.1074/jbc.273.34.21883
    • (1998) J Biol Chem , vol.273 , pp. 21883-21892
    • Berg, T.O.1    Fengsrud, M.2    Strømhaug, P.E.3    Berg, T.4    Seglen, P.O.5
  • 27
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • PMID:11060023
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, Kominami E, Ohsumi Y, Yoshimori T. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19:5720-8; PMID:11060023; http://dx.doi.org/10.1093/emboj/19.21.5720
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6    Kominami, E.7    Ohsumi, Y.8    Yoshimori, T.9
  • 29
    • 77950501014 scopus 로고    scopus 로고
    • mTOR regulation of autophagy
    • PMID:20083114
    • Jung CH, Ro SH, Cao J, Otto NM, Kim DH. mTOR regulation of autophagy. FEBS Lett 2010; 584:1287-95; PMID:20083114; http://dx.doi.org/10.1016/j.febslet.2010.01.017
    • (2010) FEBS Lett , vol.584 , pp. 1287-1295
    • Jung, C.H.1    Ro, S.H.2    Cao, J.3    Otto, N.M.4    Kim, D.H.5
  • 30
    • 77953543377 scopus 로고    scopus 로고
    • The Beclin 1-VPS34 complex - At the crossroads of autophagy and beyond
    • PMID:20356743
    • Funderburk SF, Wang QJ, Yue Z. The Beclin 1-VPS34 complex - at the crossroads of autophagy and beyond. Trends Cell Biol 2010; 20:355-62; PMID:20356743; http://dx.doi.org/10.1016/j.tcb.2010.03.002
    • (2010) Trends Cell Biol , vol.20 , pp. 355-362
    • Funderburk, S.F.1    Wang, Q.J.2    Yue, Z.3
  • 31
    • 4344595626 scopus 로고    scopus 로고
    • Regulation and role of autophagy in mammalian cells
    • PMID:15325584
    • Meijer AJ, Codogno P. Regulation and role of autophagy in mammalian cells. Int J Biochem Cell Biol 2004; 36:2445-62; PMID:15325584; http://dx.doi.org/10.1016/j.biocel.2004.02.002
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2445-2462
    • Meijer, A.J.1    Codogno, P.2
  • 32
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • PMID:11038174
    • Kirisako T, Ichimura Y, Okada H, Kabeya Y, Mizushima N, Yoshimori T, Ohsumi M, Takao T, Noda T, Ohsumi Y. The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J Cell Biol 2000; 151:263-76; PMID:11038174; http://dx.doi.org/10.1083/jcb.151.2.263
    • (2000) J Cell Biol , vol.151 , pp. 263-276
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3    Kabeya, Y.4    Mizushima, N.5    Yoshimori, T.6    Ohsumi, M.7    Takao, T.8    Noda, T.9    Ohsumi, Y.10
  • 33
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • PMID:16286508
    • Bjørkøy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, Stenmark H, Johansen T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005; 171:603-14; PMID:16286508; http://dx.doi.org/10.1083/jcb.200507002
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 34
    • 34548259958 scopus 로고    scopus 로고
    • p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • PMID:17580304
    • Pankiv S, Clausen TH, Lamark T, Brech A, Bruun JA, Outzen H, Øvervatn A, Bjørkøy G, Johansen T. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282:24131-45; PMID:17580304; http://dx.doi.org/10.1074/jbc.M702824200
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5    Outzen, H.6    Øvervatn, A.7    Bjørkøy, G.8    Johansen, T.9
  • 37
    • 84857368699 scopus 로고    scopus 로고
    • NAC1 modulates sensitivity of ovarian cancer cells to cisplatin by altering the HMGB1-mediated autophagic response
    • PMID:21743489
    • Zhang Y, Cheng Y, Ren X, Zhang L, Yap KL, Wu H, Patel R, Liu D, Qin ZH, Shih IM, et al. NAC1 modulates sensitivity of ovarian cancer cells to cisplatin by altering the HMGB1-mediated autophagic response. Oncogene 2012; 31:1055-64; PMID:21743489; http://dx.doi.org/10.1038/onc.2011.290
    • (2012) Oncogene , vol.31 , pp. 1055-1064
    • Zhang, Y.1    Cheng, Y.2    Ren, X.3    Zhang, L.4    Yap, K.L.5    Wu, H.6    Patel, R.7    Liu, D.8    Qin, Z.H.9    Shih, I.M.10
  • 38
    • 77954288770 scopus 로고    scopus 로고
    • PCBP1 suppresses the translation of metastasis-associated PRL-3 phosphatase
    • PMID:20609352
    • Wang H, Vardy LA, Tan CP, Loo JM, Guo K, Li J, Lim SG, Zhou J, Chng WJ, Ng SB, et al. PCBP1 suppresses the translation of metastasis-associated PRL-3 phosphatase. Cancer Cell 2010; 18:52-62; PMID:20609352; http://dx.doi.org/10.1016/j.ccr.2010.04.028
    • (2010) Cancer Cell , vol.18 , pp. 52-62
    • Wang, H.1    Vardy, L.A.2    Tan, C.P.3    Loo, J.M.4    Guo, K.5    Li, J.6    Lim, S.G.7    Zhou, J.8    Chng, W.J.9    Ng, S.B.10
  • 39
    • 78651396985 scopus 로고    scopus 로고
    • Phosphatase PRL-3 is a direct regulatory target of TGFbeta in colon cancer metastasis
    • PMID:21084277
    • Jiang Y, Liu XQ, Rajput A, Geng L, Ongchin M, Zeng Q, Taylor GS, Wang J. Phosphatase PRL-3 is a direct regulatory target of TGFbeta in colon cancer metastasis. Cancer Res 2011; 71:234-44; PMID:21084277; http://dx.doi.org/10.1158/0008-5472.CAN-10-1487
    • (2011) Cancer Res , vol.71 , pp. 234-244
    • Jiang, Y.1    Liu, X.Q.2    Rajput, A.3    Geng, L.4    Ongchin, M.5    Zeng, Q.6    Taylor, G.S.7    Wang, J.8
  • 41
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • PMID:11121744
    • Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000; 10:524-30; PMID:11121744; http://dx.doi.org/10.1016/S0962-8924(00)01852-3
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 42
    • 80052697287 scopus 로고    scopus 로고
    • The role of autophagy in cancer: Therapeutic implications
    • PMID:21878654
    • Yang ZJ, Chee CE, Huang S, Sinicrope FA. The role of autophagy in cancer: therapeutic implications. Mol Cancer Ther 2011; 10:1533-41; PMID:21878654; http://dx.doi.org/10.1158/1535-7163.MCT-11-0047
    • (2011) Mol Cancer Ther , vol.10 , pp. 1533-1541
    • Yang, Z.J.1    Chee, C.E.2    Huang, S.3    Sinicrope, F.A.4
  • 44
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • PMID:20602996
    • Lemmon MA, Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010; 141:1117-34; PMID:20602996; http://dx.doi.org/10.1016/j.cell.2010.06.011
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 45
    • 84890597499 scopus 로고    scopus 로고
    • Phosphatase of regenerating liver 3 (PRL3) provokes a tyrosine phosphoproteome to drive prometastatic signal transduction
    • PMID:24030100
    • Walls CD, Iliuk A, Bai Y, Wang M, Tao WA, Zhang ZY. Phosphatase of regenerating liver 3 (PRL3) provokes a tyrosine phosphoproteome to drive prometastatic signal transduction. Mol Cell Proteomics 2013; 12:3759-77; PMID:24030100; http://dx.doi.org/10.1074/mcp.M113.028886
    • (2013) Mol Cell Proteomics , vol.12 , pp. 3759-3777
    • Walls, C.D.1    Iliuk, A.2    Bai, Y.3    Wang, M.4    Tao, W.A.5    Zhang, Z.Y.6
  • 46
    • 84881247984 scopus 로고    scopus 로고
    • Metastasis-associated PRL-3 induces EGFR activation and addiction in cancer cells
    • PMID:23867504
    • Al-Aidaroos AQO, Yuen HF, Guo K, Zhang SD, Chung TH, Chng WJ, Zeng Q. Metastasis-associated PRL-3 induces EGFR activation and addiction in cancer cells. J Clin Invest 2013; 123:3459-71; PMID:23867504; http://dx.doi.org/10.1172/JCI66824
    • (2013) J Clin Invest , vol.123 , pp. 3459-3471
    • Al-Aidaroos, A.Q.O.1    Yuen, H.F.2    Guo, K.3    Zhang, S.D.4    Chung, T.H.5    Chng, W.J.6    Zeng, Q.7
  • 47
    • 84859562694 scopus 로고    scopus 로고
    • Targeting autophagy addiction in cancer
    • PMID:22185891
    • Mancias JD, Kimmelman AC. Targeting autophagy addiction in cancer. Oncotarget 2011; 2:1302-6; PMID:22185891
    • (2011) Oncotarget , vol.2 , pp. 1302-1306
    • Mancias, J.D.1    Kimmelman, A.C.2
  • 48
    • 79953767723 scopus 로고    scopus 로고
    • Polyomavirus enhancer activator 3 protein promotes breast cancer metastatic progression through Snail-induced epithelial-mesenchymal transition
    • PMID:21404275
    • Yuen HF, Chan YK, Grills C, McCrudden CM, Gunasekharan V, Shi Z, Wong ASY, Lappin TR, Chan KW, Fennell DA, et al. Polyomavirus enhancer activator 3 protein promotes breast cancer metastatic progression through Snail-induced epithelial-mesenchymal transition. J Pathol 2011; 224:78-89; PMID:21404275; http://dx.doi.org/10.1002/path.2859
    • (2011) J Pathol , vol.224 , pp. 78-89
    • Yuen, H.F.1    Chan, Y.K.2    Grills, C.3    McCrudden, C.M.4    Gunasekharan, V.5    Shi, Z.6    Wong, A.S.Y.7    Lappin, T.R.8    Chan, K.W.9    Fennell, D.A.10
  • 49
    • 16844385230 scopus 로고    scopus 로고
    • Generation of PRL-3- and PRL-1-specific monoclonal antibodies as potential diagnostic markers for cancer metastases
    • PMID:15788667
    • Li J, Guo K, Koh VWC, Tang JP, Gan BQ, Shi H, Li HX, Zeng Q. Generation of PRL-3- and PRL-1-specific monoclonal antibodies as potential diagnostic markers for cancer metastases. Clin Cancer Res 2005; 11:2195-204; PMID:15788667; http://dx.doi.org/10.1158/1078-0432.CCR-04-1984
    • (2005) Clin Cancer Res , vol.11 , pp. 2195-2204
    • Li, J.1    Guo, K.2    Koh, V.W.C.3    Tang, J.P.4    Gan, B.Q.5    Shi, H.6    Li, H.X.7    Zeng, Q.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.