Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth(437 views) Lignitto L, Arcella A, Sepe M, Rinaldi L, Delle Donne R, Gallo A, Stefan E, Bachmann VA, Oliva MA, Tiziana Storlazzi C, L'Abbate A, Brunetti A, Gargiulo S, Gramanzini M, Insabato L, Garbi C, Gottesman ME, Feliciello A
Keywords: Binding Protein, Hippo Protein, Mps One Binder 1, Tumor Suppressor Protein, Ubiquitin Protein Ligase, Ubiquitin Protein Ligase Praja2, Unclassified Drug, Aggression, Bioaccumulation, Brain, Cell Organelle, Enzyme Activity, Growth, Signaling, Animal Experiment, Animal Model, Animal Tissue, Article, Cancer Growth, Cancer Model, Cell Proliferation, Controlled Study, Down Regulation, Embryo, Glioblastoma, Human, Human Cell, Human Tissue, In Vivo Study, Mouse, Nonhuman, Protein Degradation, Protein Protein Interaction, Signal Transduction, Ubiquitination, Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Brain Neoplasms, Cell Line, Hek293 Cells, Nude, Biological, Molecular Sequence Data, Protein Binding, Protein-Serine-Threonine Kinases, Proteolysis, Ubiquitin-Protein Ligases,
Affiliations: *** IBB - CNR ***
Dipartimento di Medicina Molecolare and Biotecnologie Mediche, University Federico II, IEOS-CNR, 80131 Naples, Italy
I.R.C.C.S Neuromed Località Camerelle, Pozzilli, Italy
Institute of Biochemistry and Center for Molecular Biosciences Innsbruck (CMBI), Innrain 80/82, A-6020 Innsbruck, Austria
Dipartimento di Biologia, University of Bari, 70126 Bari, Italy
Dipartimento di Scienze Biomediche Avanzate, Istituto di Biostrutture e Bioimmagini Consiglio Nazionale Delle Ricerche (IBB CNR), University Federico II, 80131 Naples, Italy
Institute of Cancer Research, Columbia University Medical Center, New York, NY 10032, United States
I. R. C. C. S Neuromed Localit Camerelle, Pozzilli, Italy
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Yu, F. X., Regulation of the Hippo-YAP pathway by G-protein-coupled receptor signaling (2012) Cell, 150, pp. 780-791
Xiao, G. H., The NF2 tumour suppressor gene product, merlin, inhibits cell proliferation and cell cycle progression by repressing cyclin D1 expression (2005) Mol. Cell Biol, 25, pp. 2384-2394
Bading, J. R., Shields, A. F., Imaging of cell proliferation: Status and prospects (2008) Journal of Nuclear Medicine, 49 (SUPPL. 6), pp. 64S-80S. , http: //jnm. snmjournals. org/cgi/reprint/49/Suppl_2/64S, DOI 10. 2967/jnumed. 107. 046391
Goldenberg, S. J., Marblestone, J. G., Mattern, M. R., Nicholson, B., Strategies for the identification of ubiquitin ligase inhibitors (2010) Biochem. Soc. Trans, 38, pp. 132-136
Marine, J. C., Lozano, G., Mdm2-mediated ubiquitylation: P53 and beyond (2010) Cell Death Differ, 17, pp. 93-102
Cheok, C. F., Verma, C. S., Baselga, J., Lane, D. P., Translating p53 into the clinic. Nature reviews (2011) Clin. Oncol, 8, p. 568
Ho, K. C., Itch E3-ubiquitin ligase regulates large tumour suppressor 1 stability (2011) Proc. Natl Acad. Sci. USA, 108, pp. 4870-4875. , [corrected]
Proteolysis of MOB1 by the ubiquitin ligase praja2 attenuates Hippo signalling and supports glioblastoma growth
Vitiello M, Finamore E, Falanga A, Raieta K, Cantisani M, Galdiero F, Pedone C, Galdiero M, Galdiero S * Fusion in Coq(479 views) Lecture Notes In Computer Science (ISSN: 0302-9743, 0302-974335404636319783540463634, 0302-974335402975459783540297543), 2001; 2178LNCS: 583-596. Impact Factor:0.415 ViewExport to BibTeXExport to EndNote