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Referencias:

• Thomas, M.G., Loschi, M., Desbats, M.A., Boccaccio, G.L., RNA granules: the good, the bad and the ugly (2011) Cell Signal, 23, pp. 324-334
• Brengues, M., Teixeira, D., Parker, R., Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies (2005) Science, 310, pp. 486-489
• Buchan, J.R., Yoon, J.H., Parker, R., Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae (2011) J Cell Sci, 124, pp. 228-239
• Buchan, J.R., Nissan, T., Parker, R., Analyzing P-bodies and stress granules in Saccharomyces cerevisiae (2010) Methods Enzymol, 470, pp. 619-640
• Aizer, A., Brody, Y., Ler, L.W., Sonenberg, N., Singer, R.H., The dynamics of mammalian P body transport, assembly, and disassembly in vivo (2008) Mol Biol Cell, 19, pp. 4154-4166
• Kedersha, N., Tisdale, S., Hickman, T., Anderson, P., Real-time and quantitative imaging of mammalian stress granules and processing bodies (2008) Methods Enzymol, 448, pp. 521-552
• Takahara, T., Maeda, T., Transient Sequestration of TORC1 into Stress Granules during Heat Stress (2012) Mol Cell, 47, pp. 242-252
• Aragon, T., van Anken, E., Pincus, D., Serafimova, I.M., Korennykh, A.V., Messenger RNA targeting to endoplasmic reticulum stress signalling sites (2009) Nature, 457, pp. 736-740
• Gaillard, H., Aguilera, A., A novel class of mRNA-containing cytoplasmic granules are produced in response to UV-irradiation (2008) Mol Biol Cell, 19, pp. 4980-4992
• Andersen, P.L., Xu, F., Ziola, B., McGregor, W.G., Xiao, W., Sequential assembly of translesion DNA polymerases at UV-induced DNA damage sites (2011) Mol Biol Cell, 22, pp. 2373-2383
• Leonhardt, H., Rahn, H.P., Weinzierl, P., Sporbert, A., Cremer, T., Dynamics of DNA replication factories in living cells (2000) J Cell Biol, 149, pp. 271-280
• Solomon, D.A., Cardoso, M.C., Knudsen, E.S., Dynamic targeting of the replication machinery to sites of DNA damage (2004) J Cell Biol, 166, pp. 455-463
• Soria, G., Speroni, J., Podhajcer, O.L., Prives, C., Gottifredi, V., p21 differentially regulates DNA replication and DNA-repair-associated processes after UV irradiation (2008) J Cell Sci, 121, pp. 3271-3282
• Baez, M.V., Luchelli, L., Maschi, D., Habif, M., Pascual, M., Smaug1 mRNA-silencing foci respond to NMDA and modulate synapse formation (2011) J Cell Biol, 195, pp. 1141-1157
• Pascual, M., Luchelli, L., Habif, M., Boccaccio, G.L., Synaptic activity regulated mRNA-silencing foci for the fine tuning of local protein synthesis at the synapse (2012) Communicative & Integrative Biology, 5, p. 4
• Campbell, S.G., Ashe, M.P., Localization of the translational guanine nucleotide exchange factor eIF2B: a common theme for GEFs? (2006) Cell Cycle, 5, pp. 678-680
• Campbell, S.G., Hoyle, N.P., Ashe, M.P., Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body: implications for translation control (2005) J Cell Biol, 170, pp. 925-934
• Taylor, E.J., Campbell, S.G., Griffiths, C.D., Reid, P.J., Slaven, J.W., Fusel alcohols regulate translation initiation by inhibiting eIF2B to reduce ternary complex in a mechanism that may involve altering the integrity and dynamics of the eIF2B body (2010) Mol Biol Cell, 21, pp. 2202-2216
• An, S., Kumar, R., Sheets, E.D., Benkovic, S.J., Reversible compartmentalization of de novo purine biosynthetic complexes in living cells (2008) Science, 320, pp. 103-106
• Narayanaswamy, R., Levy, M., Tsechansky, M., Stovall, G.M., O'Connell, J.D., Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation (2009) Proc Natl Acad Sci U S A, 106, pp. 10147-10152
• An, S., Deng, Y., Tomsho, J.W., Kyoung, M., Benkovic, S.J., Microtubule-assisted mechanism for functional metabolic macromolecular complex formation (2010) Proc Natl Acad Sci U S A, 107, pp. 12872-12876
• Noree, C., Sato, B.K., Broyer, R.M., Wilhelm, J.E., Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster (2010) J Cell Biol, 190, pp. 541-551
• Walther, T.C., Brickner, J.H., Aguilar, P.S., Bernales, S., Pantoja, C., Eisosomes mark static sites of endocytosis (2006) Nature, 439, pp. 998-1003
• Mao, Y.S., Zhang, B., Spector, D.L., Biogenesis and function of nuclear bodies (2011) Trends Genet, 27, pp. 295-306
• White, J.P., Lloyd, R.E., Regulation of stress granules in virus systems (2012) Trends Microbiol
• Beckham, C.J., Parker, R., P bodies, stress granules, and viral life cycles (2008) Cell Host Microbe, 3, pp. 206-212
• Raaben, M., Groot Koerkamp, M.J., Rottier, P.J., de Haan, C.A., Mouse hepatitis coronavirus replication induces host translational shutoff and mRNA decay, with concomitant formation of stress granules and processing bodies (2007) Cell Microbiol, 9, pp. 2218-2229
• Colombrita, C., Zennaro, E., Fallini, C., Weber, M., Sommacal, A., TDP-43 is recruited to stress granules in conditions of oxidative insult (2009) J Neurochem, 111, pp. 1051-1061
• Dormann, D., Rodde, R., Edbauer, D., Bentmann, E., Fischer, I., ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import (2010) Embo J
• Hua, Y., Zhou, J., Survival motor neuron protein facilitates assembly of stress granules (2004) FEBS Lett, 572, pp. 69-74
• Mazroui, R., Huot, M.E., Tremblay, S., Filion, C., Labelle, Y., Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression (2002) Hum Mol Genet, 11, pp. 3007-3017
• Ohn, T., Kedersha, N., Hickman, T., Tisdale, S., Anderson, P., A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly (2008) Nat Cell Biol, 10, pp. 1224-1231
• Loschi, M., Leishman, C.C., Berardone, N., Boccaccio, G.L., Dynein and kinesin regulate stress-granule and P-body dynamics (2009) J Cell Sci, 122, pp. 3973-3982
• Tsai, N.P., Ho, P.C., Wei, L.N., Regulation of stress granule dynamics by Grb7 and FAK signalling pathway (2008) Embo J, 27, pp. 715-726
• Anderson, P., Kedersha, N., Visibly stressed: the role of eIF2, TIA-1, and stress granules in protein translation (2002) Cell Stress Chaperones, 7, pp. 213-221
• Moreno, J.A., Radford, H., Peretti, D., Steinert, J.R., Verity, N., Sustained translational repression by eIF2[agr]-P mediates prion neurodegeneration (2012) Nature Advance Online Publication
• Thomas, M.G., Tosar, L.J., Desbats, M.A., Leishman, C.C., Boccaccio, G.L., Mammalian Staufen 1 is recruited to stress granules and impairs their assembly (2009) J Cell Sci, 122, pp. 563-573
• Thomas, M.G., Luchelli, L., Pascual, M., Gottifredi, V., Boccaccio, G.L., A monoclonal antibody against p53 cross-reacts with processing bodies (2012) PLoS ONE, 7, pp. e36447
• Thomas, M.G., Martinez Tosar, L.J., Loschi, M., Pasquini, J.M., Correale, J., Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes (2005) Mol Biol Cell, 16, pp. 405-420
• Baez, M.V., Boccaccio, G.L., Mammalian Smaug is a translational repressor that forms cytoplasmic foci similar to stress granules (2005) J Biol Chem, 280, pp. 43131-43140

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