Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., Walter, P. (2015). Molecular Biology of the Cell, Six Edition. Garland Science.
Anderson, P. and Kedersha, N. (2002). Stressful initiations. J. Cell Sci. 115, 3227-3234. Anderson, P. and Kedersha, N. (2006). RNA granules. J. Cell Biol. 172, 803-808.
Anderson, P. and Kedersha, N. (2008). Stress granules: the tao of RNA triage. Trends Biochem. Sci. 33, 141-150.
Anderson, P. and Kedersha, N. (2009). RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat. Rev. Mol. Cell Biol. 10, 430-436.
Arai, S., Lee, S.C., Zhai, D., Suzuki, M., Chang, Y.T. (2014). A molecular fluorescent probe for targeted visualization of temperature at the endoplasmic reticulum. Sci. Rep. 4, 6701.
Arai, S., Suzuki, M., Park, S .J., Yoo, J.S., Wang, L., Kang, N.Y., Ha, H.H., Chang, Y.T. (2015). Mitochondria-targeted fluorescent thermometer monitors intracellular temperature gradient. Chem. Commun. 51, 8044-8047.
Backlund, M., Paukku, K., Kontula, K.K., Lehtonen, J.Y.A. (2016). Endoplasmic reticulum stress increases AT1R mRNA expression via TIA-1-dependent mechanism Nucleic Acids Res. 44, 3095-3104.
Badrinath, A.S. and White, J.G. (2003). Contrasting patterns of mitochondrial redistribution in the early lineages of Caenorhabditis elegans and Acrobeloides sp. PS1146. Dev. Biol. 258, 70-75.
Bahat, A., Caplan, S. R., Eisenbach, M. (2012). Thermotaxis of human sperm cells in extraordinarily shallow temperature gradients over a wide range. PLoS One. 7, e41915.
Barna, J., Csermely, P., Vellai, T. (2018). Roles of heat shock factor 1 beyond the heat shock response. Cell Mol. Life Sci. 75, 2897-2916.
Becker, W. (2016). Advanced time-correlated single photon counting applications.
Berlanga, J., Herrero, S., De Haro, C. (1999). Characterization of the hemin-sensitive eukaryotic initiation factor 2a kinase from mouse nonerythroid cells. J. Biol. Chem. 273, 32340–32346.
Bossinger, O. and Schierenberg, E. (1992). Transfer and tissue-specific accumulation of cytoplasmic components in embryos of Caenorhabditis elegans and Rhabditis dolichura: In vivo analysis with a low-cost signal enhancement device. Development 114, 317-330.
Brangwynne, C.P., Eckmann, C.R., Courson, D.S., Rybarska, A., Hoege, C., Gharakhani, J., Jülicher, F., Hyman, A.A. (2009). Germline P granules are liquid droplets that localize by controlled dissolution/condensation. Science 324, 1729-1732.
Brangwynne, C.P., Mitchison, T.J., and Hyman, A.A. (2011). Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes. Proc. Natl. Acad. Sci. USA 108, 4334-4339.
Brangwynne, C.P. (2013). Phase transitions and size scaling of membrane-less organelles J. Cell Biol. 203, 875-881.
Buchan, J.R., and Parker, R. (2009). Eukaryotic stress granules: the ins and outs of translation. Mol. Cell 68, 932-941.
Byerly, L., Cassada, R.C., Russell, R.L. (1976). The life cycle of the nematode Caenorhabditis elegans. I. Wild-type growth and reproduction. Dev. Biol. 51, 23-33.
Cherkasov, V., Hofmann, S., Druffel-Augustin, S., Mogk, A., Tyedmers, J., Stoecklin, G., Bukau, B. (2013). Coordination of translational control and protein homeostasis during severe heat stress. Curr. Biol. 23, 2452-2462.
Courchaine, E.M., Lu, A., Neugebauer, K.M. (2016). Droplet organelles? EMBO J. 35, 1603-1612.
Decker, C.J., Teixeira, D., Parker, R. (2007). Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae J. Cell Biol. 179, 437-449.
De Graeve, F. and Besse, F. (2018). Neuronal RNP granules: from physiological to pathological assemblies. Biol Chem. 399, 623-635.
Ding, Y., Ye, X., Zhang, G. (2005). Microcalorimetric Investigation on Aggregation and Dissolution of Poly(N-isopropylacrylamide) Chains in Water. Macromolecules 38, 904- 908.
Elbaum-Garfinkle, S. and Brangwynne, C.P. (2015). Liquids, Fibers, and Gels: The Many Phases of Neurodegeneration. Dev. Cell 35, 531-532.
Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C.C., Eckmann, C.R., Myong, S., Brangwynne, C.P. (2015). The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. Proc. Natl. Acad. Sci. USA 112, 7189-7194.
Elvira, G., Wasiak, S., Blandford, V., Tong, X.K., Serrano, A., Fan, X., del Rayo Sánchez-Carbente, M., Servant, F., Bell, A.W., Boismenu, D., Lacaille, J.C., McPherson, P.S., DesGroseillers, L., Sossin, W.S. (2006). Characterization of an RNA granule from developing brain. Mol. Cell. Proteomics 5, 635-651.
Evans, D.R., Singer, R.A., Johnston, G.C., Wheals, A.E. (1994). Cell-cycle mutations among the collection of Saccharomyces cerevisiae DNA mutants. FEMS Microbiol. Lett. 116, 147-153.
Farny, N.G., Kedersha, N.L., Silver, P.A. (2009). Metazoan stress granule assembly is mediated by P-eIF2alpha-dependent and -independent mechanisms. RNA 15,1814-1821.
Fujimura, K., Katahira, J., Kano, F., Yoneda, Y., Murata, M. (2009). Microscopic dissection of the process of stress granule assembly. Biochem. Biophys. Acta. 1793, 1728-1737.
Gallo, C.M., Munro, E., Rasoloson, D., Merritt, C., Seydoux, G. (2008). Processing bodies and germ granules are distinct RNA granules that interact in C. elegans embryos Dev. Biol. 323, 76-87.
Gallo, C.M., Wang, J.T., Motegi, F., Seydoux, G. (2010). Cytoplasmic partitioning of P granule components is not required to specify the germline in C. elegans. Science 330, 1685-1689.
Gota, C., Okabe, K., Funatsu, T., Harada, Y., Uchiyama, S. (2009). Hydrophilic fluorescent nanogel thermometer for intracellular thermometry. J. Am. Chem. Soc. 131, 2766-2767.
Gota, C., Uchiyama, S., Yoshihara, T., Tobita, S., Ohwada, T. (2008). Temperature- dependent fluorescence lifetime of a fluorescent polymeric thermometer, poly(N- isopropylacrylamide), labeled by polarity and hydrogen bonding sensitive 4-sulfamoyl- 7-aminobenzofurazan. J. Phys. Chem. B. 112, 2829-2836.
Gilks, N., Kedersha, N., Ayodele, M., Shen, L., Stoecklin, G., Dember, L.M., Anderson, P. (2004). Stress granule assembly is mediated by prion-like aggregation of TIA-1 Mol. Biol. Cell 15, 5383-5398.
Gray, N.K., Wickens, M. (1998). Control of translation initiation in animals. Annu. Rev. Cell Dev. Biol. 14, 399-458.
Grousl, T., Ivanov, P., Frydlova, I., Vasicova, P., Janda, F., Vojtova, J., Malinska, K., Malcova, I., Novakova, L., Janoskova, D., Valasek, L., Hasek, J. (2009). Robust heat shock induces eIF2alpha-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae. J. Cell Sci. 122, 2078-2088.
Han, T.W., Kato, M., Xie, S., Wu, L.C., Mirzaei, H., Pei, J., Chen, M., Xie, Y., Allen, J., Xiao, G., McKnight, S.L. (2012). Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Cell 149, 768-779.
Hanazawa M., Yonetani M., Sugimoto A. (2011). PGL proteins self associate and bind RNPs to mediate germ granule assembly in C. elegans. J. Cell Biol. 192, 929-937.
Heytler, P.G. and Prichard, W.W. (1962). A new class of uncoupling agents–carbonyl cyanide phenylhydrazones. Biochem. Biophys. Res. Commun. 7, 272-275.
Hoege, C. and Hyman, A.A. (2013). Principles of PAR polarity in Caenorhabditis elegans embryos. Nat. Rev. Mol. Cell Biol. 14, 315-322.
Hyman, A.A., Weber, C.A., Jülicher, F. (2014). Liquid-liquid phase separation in biology Annu. Rev. Cell Dev. Biol. 30, 39-58.
Jain, S., Wheeler, J.R., Walters, R.W., Agrawal, A., Barsic, A., Parker, R. (2016). ATPase-modulated stress granules contain a diverse proteome and substructure. Cell 164, 487-498.
Kahvejian, A., Svitkin, Y.V., Sukareieh, R., M'Boutchou, M.N., Sonenberg, N. (2005). Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev. 19, 104-113.
Kamei, Y., Suzuki, M., Watanabe, K., Fujimori, K., Kawasaki, T., Deguchi, T., Yoneda, Y., Todo, T., Takagi, S., Funatsu, T., Yuba, S. (2009). Infrared laser-mediated gene induction in targeted single cells in vivo. Nat. Methods 6, 79-81.
Kato, M., Han, T.W., Xie, S., Shi, K., Du, X., Wu, L.C., Mirzaei, H., Goldsmith, E.J., Longgood, J., Pei, J., Grishin, N.V., Frantz, D.E., Schneider, J.W., Chen, S., Li, L., Sawaya, M.R., Eisenberg, D., Tycko, R., McKnight, S.L. (2012). Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell 149, 753-767.
Kedersha, N.L., Gupta, M., Li, W., Miller, I., Anderson, P. (1999). RNA- binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2a to the as- sembly of mammalian stress granules. J. Cell Biol. 147, 1431-1441.
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., and Anderson, P. (2002). Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem. Soc. Trans. 30, 963-969.
Kedersha, N., Chen, S., Gilks, N., Li, W., Miller, I.J., Stahl, J., Anderson, P. (2002). Evidence that ternary complex (eIF2-GTP-tRNA iMet)-deficient preini-tiation complexes are core constituents of mammalian stress granules. Mol. Biol. Cell 13, 195- 210.
Kedersha, N., Stoecklin, G., Ayodele, M., Yacono, P., Lykke-Andersen, J., Fritzler, M.J., Scheuner, D., Kaufman, R.J., Golan, D.E., Anderson, P. (2005). Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J. Cell Biol. 169, 871-884.
Kedersha, N. and Anderson, P. (2007). Mammalian stress granules and processing bodies. Methods Enzymol. 431, 61-81.
Kedersha, N., Ivanov, P., and Anderson, P. (2013). Stress granules and cell signaling: more than just a passing phase? Trends Biochem. Sci. 38, 494-506.
Kedersha, N., Panas, M.D., Achorn, C.A., Lyons, S., Tisdale, S., Hickman, T., Thomas, M., Lieberman, J., McInerney, G.M., Ivanov, P., Anderson, P. (2016). G3BP-Caprin1- USP10 complexes mediate stress granule condensation and associate with 40S subunits. J. Cell Biol. 212, 845-860.
Khong, A., Matheny, T., Jain, S., Mitchell, S.F., Wheeler, J.R., Parker, R. (2017). The Stress Granule Transcriptome Reveals Principles of mRNA Accumulation in Stress Granules. Mol. Cell 68, 808-820.
Kimble, J., Hodgkin, J., Smith, T., Smith, J. (1982). Suppression of an amber mutation by microinjection of suppressor tRNA in C. elegans. Nature 299, 456-458.
Kiyonaka S., Kajimoto T., Sakaguchi R., Shinmi D., Omatsu-Kanbe M., Matsuura H., Imamura H., Yoshizaki T., Hamachi I., Morii T., Mori Y. (2013) Genetically encoded fluorescent thermosensors visualize subcellular thermoregulation in living cells. Nat. Methods 10, 1232-1238.
Kroschwald, S., Maharana, S., Mateju, D., Malinovska, L., Nüske, E., Poser, I., Richter, D., Alberti, S. (2015). Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules. eLife. 4, e06807.
Li, Y.R., King, O.D., Shorter, J., Gitler, A.D. (2013). Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201, 361-372.
Lin, Y., Protter, D.S.W., Rosen, M.K., Parker, R. (2015). Formation and maturation of phases-separated liquid droplets by RNA-binding proteins. Mol. Cell 60, 208-219.
Mateju, D., Franzmann, T.M., Patel, A., Kopach, A., Boczek, E.E., Maharana, S., Lee, H.O., Carra, S., Hyman, A.A., Alberti, S. (2017). An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function. EMBO J. 36, 1669-1687.
McCormick, C. and Khaperskyy, D.A. (2017). Translation inhibition and stress granules in the antiviral immune response. Nat. Rev. Immunol. 17, 647-660.
McEwen, E., Kedersha, N., Song, B., Scheuner, D., Gilks, N., Han, A., Chen, J.J., Anderson, P., Kaufman, R.J. (2005). Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J Biol. Chem. 280, 16925-16933.
Mello, C.C. and Fire, A. (1995). DNA transformation. H.F. Epstein, D.C. Shakes (Eds.), Caenorhabditis elegans: Modern Biological Analysis of an Organism, Academic Press, Inc, San Diego, CA. 451-482.
Mello, C.C., Kramer, J.M., Stinchcomb, D., Ambros, V. (1991). Efficient gene transfer in C. elegans: extrachromosomal maintenance and integration of transforming sequences EMBO J. 10, 3959-3970.
Molliex, A., Temirov, J., Lee, J., Coughlin, M., Kanagaraj, A.P., Kim, H.J., Mittag, T., Taylor, J.P. (2015). Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Cell 163, 123-133.
Montell, C. and Caterina, M.J. (2007). Thermoregulation: channels that are cool to the core. Curr. Biol. 17, 885-887.
Morimoto, R.I. (1993). Cells in stress: transcriptional activation of heat shock genes. Science 259, 1409-1410.
Morimoto, R.I. (1998). Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12, 3788-3796.
Murakami, T., Qamar, S., Lin, J.Q., Schierle, G.S., Rees, E., Miyashita, A., Costa, A.R., Dodd, R.B., Chan, F.T., Michel, C.H., et al. (2015). ALS/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function. Neuron 88, 678-690
Nakamura, T. and Matsuoka, I. (1978). Calorimetric studies of heat of respiration of mitochondria. J. Biochem. 84, 39-46.
Nakano, M., Arai, Y., Kotera, I., Okabe, K., Kamei, Y., Nagai, T. (2017). Genetically encoded ratiometric fluorescent thermometer with wide range and rapid response. PLoS One 12, e0172344.
Naranmandura, H., Xu, S., Sawata, T., Hao, W.H., Liu, H., Bu, N., Ogra, Y., Lou, Y.J., Suzuki, N. (2011). Mitochondria are the main target organelle for trivalent monomethylarsonous acid (MMA(III))-induced cytotoxicity. Chem. Res. Toxicol. 24, 1094-1103.
Niewidok, B., Igaev, M., Pereira da Graca, A., Strassner, A., Lenzen, C., Richter, C.P., Piehler, J., Kurre, R., Brandt, R. (2018). Single-molecule imaging reveals dynamic biphasic partition of RNA-binding proteins in stress granules. J. Cell Biol. 217, 1303- 1318.
Nott, T.J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T.D., Bazett-Jones, D.P., Pawson, T., Forman-Kay, J.D., Baldwin, A.J. (2015). Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. Mol. Cell 57, 936-947.
Okabe, K., Harada, Y., Zhang, J., Tadakuma, H., Tani, T., Funatsu, T. (2011). Real time monitoring of endogenous cytoplasmic mRNA using linear antisense 2'-O-methyl RNA probes in living cells. Nucleic Acids Res. 39, e20.
Okabe, K., Inada, N., Gota, C., Harada, Y., Funatsu, T., Uchiyama, S. (2012). Intracellular temperature mapping with a fluorescent polymeric thermometer and fluorescence lifetime imaging microscopy. Nat. Commun. 3:705.
Okabe, K., Sakaguchi, R., Shi, B., Kiyonaka, S. (2018). Intracellular thermometry with fluorescent sensors for thermal biology. Pflugers Arch. 470, 717-731.
Panas, M.D., Ivanov, P., and Anderson, P. (2016). Mechanistic insights into mammalian stress granule dynamics. J. Cell Biol. 215, 313-323.
Patel, A., Lee, H.O., Jawerth, L., Maharana, S., Jahnel, M., Hein, M.Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T.M., Pozniakovski, A., Poser, I., Maghelli, N., Royer, L.A., Weigert, M., Myers, E.W., Grill, E.W., Grill, S., Drechsel, D., Hyman, A.A., Alberti, S. (2015). A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation. Cell 162, 1066-1077.
Protter, D.S.W. and Parker, R. (2016). Principles and Properties of Stress Granules. Trends Cell Biol. 26, 668-679.
Richter, K., Haslbeck, M., Buchner, J. (2010). The heat shock response: life on the verge of death. J. Mol. Cell 40, 253-266.
Saha, S., Weber, C.A., Nousch, M., Adame-Arana, O., Hoege, C., Hein, M.Y., Osborne- Nishimura, E., Mahamid, J., Jahnel, M., Jawerth, L., Pozniakovski, A., Eckmann, C.R., Jülicher, F., Hyman, A.A. (2016). Polar Positioning of Phase-Separated Liquid Compartments in Cells Regulated by an mRNA Competition Mechanism. Cell 166, 1572- 1584.
Sheth, U., Pitt, J., Dennis, S., Priess, J.R., (2010). Perinuclear P granules are the principal sites of mRNA export in adult C. elegans germ cells. Development 137, 1305-1314.
Smith, H.E., Fabritius, A.S., Jaramillo-Lambert, A., Golden, A. (2016). Mapping challenging mutations by whole-genome sequencing. G3 (Bethesda) 6, 1297-1304.
Somasekharan, S.P., El-Naggar, A., Leprivier, G., Cheng, H., Hajee, S., Grunewald, T.G., 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.
Souquere, S., Mollet, S., Kress, M., Dautry, F., Pierron, G. Weil, D. (2009). Unravelling the ultrastructure of stress granules and associated P-bodies in human cells. J. Cell Sci. 122, 3619-3626.
Tarun, S.Z. and Sachs, A.B. (1995). A common function for mRNA 5’ and 3’ ends in translation initiation in yeast. Genes & Dev. 9, 2997-3007.
Thomas, M.G., Martinez Tosar, L.J., Desbats, M.A., Leishman, C.C., Boccaccio, G.L. (2009). Mammalian Staufen 1 is recruited to stress granules and impairs their assembly J. Cell Sci. 155, 563-573.
Tompa, P. (2005). The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 579, 3346-3354.
Tourriere, H., Chebli, L. Zekri, K., Courselaud, B., Blanchard, J.M., Bertrand, E., Tazi, J. (2003). The RasGAP-associated endoribonuclease G3BP assembles stress granules J. Cell Biol. 160, 823-831.
Tsai, W-C., Gayatri, S., Reineke, L.C., Sbardella, G., Bedford, M.T., Lloyd, R.E. (2016). Arginine demethylation of G3BP1 promotes stress granule assembly. J. Biol. Chem. 291, 22671-22685.
Unsworth, H., Raguz, S., Edwards, H. J., Higgins, C. F. and Yague, E. (2010). mRNA escape from stress granule sequestration is dictated by localization to the endoplasmic reticulum. FASEB J. 24, 3370-3380.
Valiente-Echeverria, F., Melnychuk, L., Vyboh, K., Ajamian, L., Gallouzi, I.E., Bernard, N., Mouland, A.J. (2014). eEF2 and Ras-GAP SH3 domain-binding protein (G3BP1) modulate stress granule assembly during HIV-1 infection. Nat. Commun. 5:4819.
Van Treeck, B., Protter, D.S.W., Matheny, T., Khong, A., Link, C.D., Parker, R. (2018). RNA self-assembly contributes to stress granule formation and defining the stress granule transcriptome. Proc. Natl. Acad. Sci. USA 115, 2734-2739.
Voets, T., Talavera, K., Owsianik, G., Nilius, B. (2005). Sensing with TRP channels Nat. Biol. Chem. 1, 85-92.
Warner, D.A. and Shine, R. (2008). The adaptive significance of temperature-dependent sex determination in a reptile. Nature 451, 566-569.
Wang, J.T. and Seydoux, G. (2014). P granules. Curr. Biol. 24, 637-638.
Weber, S.C. and Brangwynne, C.P. (2012). Getting RNA and protein in phase. Cell 149, 1188-1191.
Wheeler, J.R., Matheny, T., Jain, S., Abrisch, R., Parker, R. (2016). Distinct stages in stress granule assembly and disassembly. eLife 5, 1-25.
Zhang, J., Okabe, K., Tani, T., Funatsu, T. (2011). Dynamic association-dissociation and harboring of endogenous mRNAs in stress granules. J. Cell Sci. 24, 4087- 4095.
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