Akiyama, T., Matsuda, S., Namba, Y., Saito, T., Toyoshima, K. & Yamamoto, T. (1991) The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain. Mol. Cell. Biol., 11, 833– 842.
Anderson, P. & Kedersha, N. (2006) RNA granules, , J. Cell Biol., 172:803-808.
Anderson, P. & Kedersha, N. (2009) RNA granules: post-transcriptional and epigenetic modulators of gene expression, Nat. Rev. Mol. Cell Biol., 10:430-436.
Arellano, M., Valdivieso, M. H., Calonge, T. M., Coll, P. M., Duran, A. & Perez, P. (1999)Schizosaccharomyces pombe protein kinase C homologues, pck1p and pck2p, are targets of rho1p and rho2p and differentially regulate cell integrity, J. Cell Sci., 112:3569-3578.
Arimoto, K., Fukuda, H., Imajoh-Ohmi, S., Saito, H. & Takekawa, M. (2008) Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways, Nat. Cell Biol., 10:1324-1332.
Arora, D., Köthe, S., Eijnden, M., Huijsduijnen, R., Heidel, F., Fischer, T., Scholl, S., Tölle, B., Böhmer, S., Lennartsson, J., Isken, F., Müller-Tidow, C. & Böhmer, F. (2012) Expression of protein-tyrosine phosphatases in Acute Myeloid Leukemia cells: FLT3 ITD sustains high levels of DUSP6 expression. Cell Communication and Signaling, 10, 19.
Bahler, J., Wu, J.-Q., Longtine, M. S., Shah, N. G., McKenzie, A., III, Steever, A. B.,Wach, A., Philippsen, P. & Pringle, J. R. (1998) Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe, Yeast, 14:943-951.
Barford, D., Jia, Z. & Tonks, N. K. (1995) Protein tyrosine phosphatases take off. Nat. Struct. Biol., 12, 1043-1053.
Ben-Levy, R., Paterson, HF., Marshall, CJ. & Yarden, Y. (1994) A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP kinase pathway. EMBO J., 13, 3302-3311.
Bloethner, S., Chen, B., Hemminki, K., Müller-Berghaus, J., Ugurel, S., Schadendorf, D. & Kumar, R. (2005) Effect of common B-RAF and N-RAS mutations on global gene expression in melanoma cell lines. Carcinogenesis, 26, 1224-1232.
Brambilla, M., Martani, F. & Branduardi, P. (2017) The recruitment of the Saccharomyces cerevisiae poly(A)-binding protein into stress granules: new insights into the contribution of the different protein domains, FEMS Yeast Res., 1;17.
Callender, J. A. & Newton, A. C. (2017) Conventional protein kinase C in the brain: 40 years later, Neuronal Signal., 1:NS20160005.
Camps, M., Nichols, A., Gillieron, C., Antonsson, B., Muda, M., Chabert, C., Boschert, U. & Arkinstall, S. (1998) Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science, 280,1262-1265.
Caunt, C. & Keyse, S. (2013) Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling. FEBS J., 280, 489-504.
Cazaubon, S., Bornancin, F. & Parker, P. J. (1994) Threonine-497 is a critical site for permissive activation of protein kinase Ca, Biochem. J., 301:443-448.
Chan, D., Liu, V., Tsao, G., Yao, K., Furukawa, T., Chan, K. & Ngan, H. (2008) Loss of MKP3 mediated by oxidative stress enhances tumorigenicity and chemoresistance of ovarian cancer cells. Carcinogenesis, 29, 1742–1750
Chen, H., Chuang, H. & Tan, T. (2019) Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability. J. Mol. Sci., 20, 2668.
Doi, A., Kita, A., Kanda, Y., Uno, T., Asami, K., Satoh, R., Nakano, K. & Sugiura, R. (2015) Geranylgeranyltransferase Cwg2-Rho4/Rho5 module is implicated in the Pmk1 MAP Kinase-mediated cell wall integrity pathway in fission yeast, Genes Cells, 20:310- 323.
Degl’Innocenti, D., Romeo, P., Tarantino, E., Sensi, M., Cassinelli, G., Catalano, V., Lanzi, C., Perrone, F., Pilotti, S., Seregni, E., Pierotti, M., Greco, A. & Borrello, M. (2013)
DUSP6/MKP3 is overexpressed in papillary and poorly differentiated thyroid carcinoma and contributes to neoplastic properties of thyroid cancer cells. Endocrine-Related Cancer, 20, 23–37.
Dhillon S., (2016) Dabrafenib plus Trametinib: a Review in Advanced Melanoma with a BRAF (V600) Mutation. Target Oncol., 3, 417-428.
Díaz-García, C., Agudo-López, A., Pérez, C., Prieto-García, E., Iglesias, L., Ponce, S., Garzotto, A., Rodríguez-Peralto, J., Cortés-Funes, H., López-Martín, J. & Agulló-Ortuño, M. (2015) Prognostic value of dual-specificity phosphatase 6 expression in non-small cell lung cancer. Tumor Biol., 36, 1199–1206.
Dutil, E. M., Toker, A. & Newton, A. C. (1998) Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1), Curr. Biol., 8:1366-1375.
Eblaghie, MC., Lunn, JS., Dickinson, RJ., Munsterberg, AE., Sanz-Ezquerro, JJ. &
Farrell, ER. et al. (2003) Negative feedback regulation of FGF signaling levels by Pyst1/MKP3 in chick embryos. Curr. Biol., 13, 1009–1018.
Ekerot, M., Stavridis, M., Delavaine, L., Mitchell, M., Staples, C., Owens, D., Keenan, I., Dickinson, R., Storey, K. & Keyse, S. (2008) Negative-feedback regulation of FGF signalling by DUSP6/MKP-3 is driven by ERK1/2 and mediated by Ets factor binding to a conserved site within the DUSP6/MKP-3 gene promoter. Biochem. J., 412, 287-298.
Fuchs, B. B. & Mylonakis, E. (2009) Our Paths Might Cross: the Role of the Fungal Cell Wall Integrity Pathway in Stress Response and Cross Talk with Other Stress Response Pathways, Eukaryot Cell, 8:1616–1625.
Furukawa, T. (2009) Molecular pathology of pancreatic cancer: implications for molecular targeting therapy. Clin. Gastroenterol Hepatol., 7, S35–S39.
Furukawa, T., Sunamura, M., Motoi, F., Matsuno, S. & Horii A. (2003) Potential tumor suppressive pathway involving DUSP6/MKP-3 in pancreatic cancer. Am. J. Pathol., 162, 1807–1815.
Gould, C. M. & Newton, A. C. (2008) The Life and Death of Protein Kinase C, Curr. Drug Targets., 9:614–625.
Grallert, B., Kearsey, S. E., Lenhard, M., Carlson, C. R., Nurse, P., Boye, E. & Labib, K. (2000) A fission yeast general translation factor reveals links between protein synthesis and cell cycle controls, J. Cell Sci., 113:1447-1458.
Guil, S., Long,J. C. & Cáceres,J. F. (2006) hnRNP A1 relocalization to the stress granules reflects a role in the stress response, Mol. Cell Biol., 26:5744-5758.
Gutiérrez-Venegas, G., Arreguín-Cano, J. A., Arroyo-Cruz, R., Villeda-Navarro, M. & Méndez-Mejía, J. A. (2009) Activation of ERK1/2 by protein kinase C-alpha in response to hydrogen peroxide-induced cell death in human gingival fibroblasts, Toxicol. In Vitro., 24:319-326. Higa, M., Kita, A., Hagihara, K., Kitai, Y., Doi, A., Nagasoko, R., Satoh, R. & Sugiura, R. (2015) Spatial control of calcineurin in response to heat shock in fission yeast, Genes Cells, 20:95-107.
Hilliker, A., Gao, Z., Jankowsky, E. Parker, R. (2011) The DEAD-Box Protein Ded1 Modulates Translation by the Formation and Resolution of an eIF4F-mRNA Complex, Mol. Cell, 43:962–972. Isakov, N. (2018) Protein kinase C (PKC) isoforms in cancer, tumor promotion and tumor suppression, Semin. Cancer Biol., 48:36-52.
Hellyer, NJ., Kim, MS. & Koland, JG. (2001) Heregulin-dependent activation of phosphoinositide 3-kinase and Akt via the ErbB2/ErbB3 co-receptor. J. Biol. Chem., 276, 42153-42161.
Hoyer, K. K., Herling, M., Bagrintseva, K., Dawson, D. W., French, S. W., Renard, M., Weinger, J. G., Jones, D. & Teitell, M. A. (2005) T cell leukemia-1 modulates TCR signal strength and IFN-gamma levels through phosphatidylinositol 3-kinase and protein kinase C pathway activation, J. Immunol., 175:864-73.
Kanda, Y., Satoh, R., Matsumoto, S., Ikeda, C., Inutsuka, N., Hagihara, K., Matzno, S., Tsujimoto, S., Kita, A. & Sugiura, R. (2016) Skb5, an SH3 adaptor protein, regulates Pmk1 MAPK signaling by controlling the intracellular localization of the MAPKKK Mkh1, J. Cell Sci., 129:3189-3202.
Karnoub, A. E, & Weinberg, R. A. (2008) Ras oncogenes: split personalities. Nat Rev Mol Cell Biol 9, 517-531.
Kedersha, N., Cho, M. R., Li, W., Yacono, P. W., Chen, S., Gilks, N., Golan, D. E. & Anderson, P. (2000) Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules, J. Cell Biol., 151:1257–1268.
Kedersha, N. & Anderson, P. (2007) Mammalian stress granules and processing bodies, Methods Enzymol., 431:61-81.
Kita, A., Sugiura, R., S hoji, H., He, Y., Deng, L., Lu, Y., Sio, S. O., Takegawa, K., Sakaue, M. & Shuntoh, H. et al., (2004) Loss of Apm1, the μ1 subunit of the clathrin-associated adaptor-protein-1 complex, causes distinct phenotypes and synthetic lethality with calcineurin deletion in fission yeast, Mol. Biol. Cell, 15:2920-2931.
Kobayashi, T., Winslow, S., Sunesson, L., Hellman, U. & Larsson, C. (2012) PKCα Binds G3BP2 and Regulates Stress Granule Formation Following Cellular Stress, PLoS ONE, 7:e35820.
Kushnirov, V. V. (2000) Rapid and reliable protein extraction from yeast, Yeast, 16:857- 60.
Li, C., Scott, DA., Hatch, E., Tian, X. & Mansour, SL. (2007) Dusp6 (Mkp3) is a negative feedback regulator of FGF-stimulated ERK signaling during mouse development. Development, 134, 167–176.
Li, Z., Wang, N., Fang, J., Huang, J., Tian, F., Li, C. & Xie, F. (2012) Role of PKC-ERK signaling in tamoxifen-induced apoptosis and tamoxifen resistance in human breast cancer cells, Oncol. Rep., 27:1879-86.
Lucci, M., Orlandi, R., Triulzi, T., Tagliabue, E., Balsari, A. & Villa-Moruzzi, E. (2010) Expression profile of tyrosine phosphatases in HER2 breast cancer cells and tumors. Cellular Onco., 32, 361-372.
Lucke-Wold, B. P., Turner, R. C., Logsdon, A. F., Simpkins, J. W., Alkon, D. L., Smith, K. E., Chen, Y. W., Tan, Z., Huber, J. D. & Rosen, C. L. (2015) Common mechanisms of Alzheimer's disease and ischemic stroke: the role of protein kinase C in the progression of age-related neurodegeneration, J. Alzheimers Dis., 43:711-724.
Ma, Y., Kuno, T., Kita, A., Asayama, Y. & Sugiura, R. (2006) Rho2 is a target of the farnesyltransferase Cpp1 and acts upstream of Pmk1 mitogen-activated protein kinase signaling in fission yeast, Mol. Biol. Cell, 17:5028-5037.
Madrid, M., Jiménez, R., Sánchez-Mir, L., Soto, T., Franco, A., Vicente-Soler, J., Gacto,
M., Pérez, P. & Cansado, J. (2015) Multiple layers of regulation influence cell integrity control by the PKC ortholog Pck2 in fission yeast, J. Cell Sci., 128:266-280
Madrid, M., Vázquez-Marín, B., Soto, T., Franco, A., Gómez-Gil, E., Vicente-Soler, J., Gacto, M., Pérez, P. & Cansado, J. (2017) Differential functional regulation of protein kinase C (PKC) orthologs in fission yeast., J. Biol. Chem., 292:11374-11387.
Mandl, M., Slack, D. & Keyse, S. (2005) Specific inactivation and nuclear anchoring of extracellular signal-regulated kinase 2 by the inducible dual-specificity protein phosphatase DUSP5. Mol. Cell Biol., 25, 1830–1845.
Marchetti, S., Gimond, C., Chambard, J., Touboul, T., Roux, D., Pouysségur, J. & Pagés, J. (2005) Extracellular Signal-Regulated Kinases Phosphorylate Mitogen-Activated Protein Kinase Phosphatase 3/DUSP6 at Serines 159 and 197, Two Sites Critical for Its Proteasomal Degradation. Mol. Cell Biol., 25, 854-864.
Masuko, T., Sugahara, K., Kozono, M., Otsuki, S., Akiyama, T., Yamamoto, T., Toyoshima, K. & Hashimoto, Y. (1989) A murine monoclonal antibody that recognizes an extracellular domain of the human c-erbB-2 protooncogene pro- duct. Jpn. J. Cancer Res., 80, 10–14.
Maundrell, K., (1990) nmt1 of fission yeast. A highly transcribed gene completely repressed by thiamine, J. Biol. Chem., 265:10857-10864.
Mazroui, R., Huot, M. E., Tremblay, S., Filion, C., Labelle, Y. & Khandjian, E. W. (2002) Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression, Hum. Mol. Gen., 15:3007–3017.
McCubrey, J. A. et al. (2007) Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance, Biochim. Biophys. Acta., 8, 1263–1284.
Micol, V., Sanchez-Pinera, P., Villalain, J., De, A. G. & Gomez-Fernandez, J., C. (1999) Correlation between protein kinase C alpha activity andmembrane phase behavior, Biophys. J., 76, 916–927.
Mollet, S., Cougot, N., Wilczynska, A., Dautry, F., Kress, M., Bertrand, E. & Weil, D. (2008) Translationally repressed mRNA transiently cycles through stress granules during stress, Mol. Biol. Cell, 19:4469–4479.
Mukai, H. (2003) The Structure and Function of PKN, a Protein Kinase Having a Catalytic Domain Homologous to That of PKC, J. Biochem., 133:17-27.
Newton, A. C. & Jhonson, J. E. (1993) Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules, Biochim. Biophys. Acta., 1376:155-172.
Newton, A. C. (2009) Lipid activation of protein kinases, J. Lipid Res., 50:266–271.
Newton, A. C. (2010) Protein kinase C: poised to signal, Am. J. Physiol. Endocrinol. Metab., 298:E395–E402.
Nilsson, D., Sunnerhagen, P. (2011) Cellular stress induces cytoplasmic RNA granules in fission yeast, RNA, 17:120–133. Panas, M. D., Ivanov, P. & Anderson, P. (2016) Mechanistic insights into mammalian stress granule dynamics, J. Cell Biol., 215:313–323.
Pintus, G., Tadolini, B., Posadino, A. M., Sanna, B., Debidda, M., Carru, C., Deiana, L. & Ventura, C. (2003) PKC/Raf/MEK/ERK signaling pathway modulates nativeLDLinduced E2F-1 gene expression and endothelial cell proliferation, Cardiovascular Research, 59:934–944. Sabatinos, S. A. & Forsburg, S. L. (2010) Molecular genetics of Schizosaccharomyces pombe. Methods Enzymol., 470:759-795.
Sanchez-Mir, L., Soto, T., Franco, A., Madrid, M., Viana, R. A., Vicente, L., Gacto, M., Perez, P. & Cansado, J. (2014) Rho1 GTPase and PKC Ortholog Pck1 Are Upstream Activators of the Cell Integrity MAPK Pathway in Fission Yeast, PLoS ONE, 9:e88020.
Satoh, R., Hara, N., Kawasaki, A., Takasaki, T. & Sugiura, R. (2018) Distinct modes of stress granule assembly mediated by the KH- type RNA- binding protein Rnc1, Genes Cells, 11, 778-785.
Satoh, R., Morita, T., Takada, H., Kita, A., Ishiwata, S., Doi, A., Hagihara, K., Taga, A., Matsumura, Y., Tohda, H. & Sugiura, R. (2009) Role of the RNA-binding protein Nrd1 and Pmk1 mitogen-activated protein kinase in the regulation of myosin mRNA stability in fission yeast, Mol, Biol, Cell, 9, 2473-2485.
Satoh, R., Tanaka, A., Kita, A., Morita, T., Matsumura, Y., Umeda, N., Takada, M., Hayashi, S., Tani, T. & Shinmyozu, K. et al. (2012) Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast, PLoS ONE, 7:e29683.
Sayers, L. G., Katayama, S., Nakano, K., Mellor, H., Mabuchi, I., Toda, T. & Parker, P. J. (2000) Rho-dependence of Schizosaccharomyces pombe Pck2, Genes Cells, 5:17-27.
Seki, T., Matsubayashi, H., Amano, T., Shirai, Y., Saito, N. & Sakai, N. (2005) Phosphorylation of PKC activation loop plays an important role in receptor-mediated translocation of PKC, 2005, Genes Cells, 10:225-39.
Seth, D. & Rudolph, J. (2006) Redox Regulation of MAP Kinase Phosphatase 3, Biochemistry, 45, 8476-8487.
Shao, B. & Bayraktutan, U. (2013) Hyperglycaemia promotes cerebral barrier dysfunction through activation of protein kinase C-β, Diabetes. Obes. Metab., 15:993-
999.
Sio, S. O., Suehiro, T., Sugiura, R., Takeuchi, M., Mukai, H. & Kuno, T. (2005) The role of the regulatory subunit of fission yeast calcineurin for in vivo activity and its relevanc to FK506 sensitivity, J. Biol. Chem., 280:12231-12238.
Somasekharan, S. P., El-Naggar, A., Leprivier, G., Cheng, H., Hajee, S., Grunewald, T. G. P., Zhang, F., Ng T., Delattre, O., Evdokimova, V., Wang, Y., Gleave, M. & Sorensen, P. H. (2015) YB-1 regulates stress granule formation and tumor progression by translationally activating G3BP1, J. Cell Biol., 208:913-929.
Sugiura, R., Kita, A., Shimizu, Y., Shuntoh, H., Sio, S. O., & Kuno, T. (2003) Feedback regulation of MAPK signalling by an RNA-binding protein. Nature, 424, 961-965.
Sugiura, R., Toda, T., Dhut, S., Shuntoh, H. & Kuno, T. (1999) The MAPK kinase Pek1 acts as a phosphorylation-dependent molecular switch, Nature, 399:479-483.
Sugiura, R., Toda, T., Shuntoh, H., Yanagida, M. & Kuno, T. (1998) pmp1+, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast, EMBO J., 17:140-148.
Sukumaran, S. K. & Prasadarao, N. V. (2002) Regulation of Protein Kinase C in Escherichia coli K1 Invasion of Human Brain Microvascular Endothelial Cells, J. Bio. Chem., 277:12253–12262.
Takada, H., Nishimura, M., Asayama, Y., Mannse, Y., Ishiwata, S., Kita, A., Doi, A., Nishida, A., Kai, N. & Moriuchi, S. et al. (2007) Atf1 is a target of the mitogen-activated protein kinase Pmk1 and regulates cell integrity in fission yeast., Mol. Biol. Cell, 18:4794-4802. Satoh, R., Hagihara, K., Matsuura, K., Manse, Y., Kita, A., Kunoh, T., Masuko, T., Moriyama, M., Moriyama, H., Tanabe, G., Muraoka, O. & Sugiura, R. (2017) Identification of ACA-28, a 1'-acetoxychavicol acetate analogue compound, as a novel modulator of ERK MAPK signaling, which preferentially kills human melanoma cells. Genes Cells, 22, 608-618.
Takahara, T. & Maeda, T. (2012) Transient sequestration of TORC1 into stress granules during heat stress, Mol. Cell, 47:242-252.
Thedieck, K., Holzwarth, B., Prentzell, M. T., Boehlke, C., Kläsener, K., Ruf, S., Sonntag, A. G., Maerz, L., Grellscheid, S. N., Kremmer, E., Nitschke, R., Kuehn, E. W., Jonker, J. W., Groen, A. K., Reth, M., Hall, M. N. & Baumeister, R. (2013) Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in cancer cells, Cell, 154:859-874.
Toda, T., Dhut, S., Superti-Furga, G., Gotoh, Y., Nishida, E., Sugiura, R. & Kuno, T. (1996) The fission yeast pmk1+ gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions, coordinately with the protein kinase C pathway, Mol. Cell. Biol., 16:6752-6764.
Toda, T., Shimanuki, M. & Yanagida, M. (1993) Two novel protein kinase C-related genes of fission yeast are essential for cell viability and implicated in cell shape control, EMBO J., 12:1987-1995.
Verbeek, D. S., Goedhart, J., Bruinsma, L., Sinke, R. J. & Reits, E. A. (2008) PKC gamma mutations in spinocerebellar ataxia type 14 affect C1 domain accessibility and kinase activity leading to aberrant MAPK signaling, J. Cell Sci., 121:2339-2349.
Walton, G. M. et al. (1987) A three-step purification procedure for protein kinase C: Characterization of the purified enzyme, Anal. Biochem., 161:425–437.
Watanabe, M., Chen, C. & Levin, D. E. (1994) Saccharomyces cerevisiae PKC1 Encodes a Protein Kinase C (PKC) Homolog with a Substrate Specificity Similar to That of Mammalian PKC, J. Biol. Chem., 269:16829-16836.
Wheeler, J. R., Jain, S., Khong, A. & Parker, R. (2017) Isolation of yeast and mammalian stress granule cores, Methods., 126:12-17.
Wheeler, J. R., Matheny, T., Jain, S., Abrisch, R. & Parker, R. (2016) Distinct stages in stress granule assembly and disassembly, eLife, 5, e18413.
Wippich, F., Bodenmiller, B., Trajkovska, M. G., Wanka, S., Aebersold, R. & Pelkmans, L. (2013) Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling, 2013, Cell, 152:791-805.
Yang, Y. S., Kato, M., Wu, X., Litsios, A., Sutter, B. M., Wang, Y., Hsu, C. H., Wood, N E., Lemoff, A., Mirzaei, H., Heinemann, M. & Tu, B. P. (2019) Yeast Ataxin-2 Forms an Intracellular Condensate Required for the Inhibition of TORC1 Signaling during Respiratory Growth, Cell, 177:697-710.
Yoon, J. H., Choi, E. J. & Parker, R. (2010) Dcp2 phosphorylation by Ste20 modulates stress granule assembly and mRNA decay in Saccharomyces cerevisiae, J. Cell Biol., 189:813-827.
Zhang, Q., Sharma, N. R., Zheng, Z. & Chen, M. (2019) Viral Regulation of RNA Granules in Infected Cells, Virol. Sin., 34:175–191.
Zhang, Z., Kobayashi, S., Borczuk, A., Leidner, R., Laframboise, T., Levine, A. & Halmos, B. (2010) Dual specificity phosphatase 6 (DUSP6) is an ETS-regulated negative feedback mediator of oncogenic ERK signaling in lung cancer cells. Carcinogenesis, 31, 577-86.
Zuchegna, C., Zazzo, E., Moncharmont, B. & Messina, S. (2020) Dual-specificity phosphatase (DUSP6) in human glioblastoma: epithelial-to-mesenchymal transition (EMT) involvement. BMC Res. Notes, 13, 374.
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