Registro:

Referencias:

• Martin, K.C., Ephrussi, A., mRNA localization: Gene expression in the spatial dimension (2009) Cell, 136, pp. 719-730
• Coller, J., Parker, R., General translational repression by activators of mRNA decapping (2005) Cell, 122, pp. 875-886
• Holmes, L.E., Campbell, S.G., De Long, S.K., Sachs, A.B., Ashe, M.P., Loss of translational control in yeast compromised for the major mRNA decay pathway (2004) Mol Cell Biol, 24, pp. 2998-3010
• Anderson, P., Kedersha, N., RNA granules (2006) J Cell Biol, 172, pp. 803-808
• Franks, T.M., Lykke-Andersen, J., The control of mRNA decapping and P-body formation (2008) Mol Cell, 32, pp. 605-615
• Parker, R., Sheth, U., P bodies and the control of mRNA translation and degradation (2007) Mol Cell, 25, pp. 635-646
• 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
• Seydoux, G., Braun, R.E., Pathway to totipotency: Lessons from germ cells (2006) Cell, 127, pp. 891-904
• Kiebler, M.A., Bassell, G.J., Neuronal RNA granules: Movers and makers (2006) Neuron, 51, pp. 685-690
• Johnston, J.A., Ward, C.L., Kopito, R.R., Aggresomes: A cellular response to misfolded proteins (1998) J Cell Biol, 143, pp. 1883-1898
• Garcia-Mata, R., Bebok, Z., Sorscher, E.J., Sztul, E.S., Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera (1999) J Cell Biol, 146, pp. 1239-1254
• Holt, C.E., Bullock, S.L., Subcellular mRNA localization in animal cells and why it matters (2009) Science, 326, pp. 1212-1216
• Yildiz, A., Selvin, P.R., Kinesin: Walking, crawling or sliding along? (2005) Trends Cell Biol, 15, pp. 112-120
• Yildiz, A., Tomishige, M., Vale, R.D., Selvin, P.R., Kinesin walks handover-hand (2004) Science, 303, pp. 676-678
• Kural, C., Kim, H., Syed, S., Goshima, G., Gelfand, V.I., Selvin, P.R., Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement? (2005) Science, 308, pp. 1469-1472
• Shubeita, G.T., Tran, S.L., Xu, J., Consequences of motor copy number on the intracellular transport of kinesin-1-driven lipid droplets (2008) Cell, 135, pp. 1098-1107
• Delanoue, R., Davis, I., Dynein anchors its mRNA cargo after apical transport in the Drosophila blastoderm embryo (2005) Cell, 122, pp. 97-106
• Delanoue, R., Herpers, B., Soetaert, J., Davis, I., Rabouille, C., Drosophila Squid/hnRNP helps Dynein switch from a gurken mRNA transport motor to an ultrastructural static anchor in sponge bodies (2007) Dev Cell, 13, pp. 523-538
• McDougall, N., Clark, A., McDougall, E., Davis, I., Drosophila gurken (TGFalpha) mRNA localizes as particles that move within the oocyte in two dynein-dependent steps (2003) Dev Cell, 4, pp. 307-319
• Duncan, J.E., Warrior, R., The cytoplasmic dynein and kinesin motors have interdependent roles in patterning the Drosophila oocyte (2002) Curr Biol, 12, pp. 1982-1991
• Januschke, J., Gervais, L., Dass, S., Polar transport in the Drosophila oocyte requires Dynein and Kinesin I cooperation (2002) Curr Biol, 12, pp. 1971-1981
• Zimyanin, V.L., Belaya, K., Pecreaux, J., In vivo imaging of oskar mRNA transport reveals the mechanism of posterior localization (2008) Cell, 134, pp. 843-853
• Bullock, S.L., Nicol, A., Gross, S.P., Zicha, D., Guidance of bidirectional motor complexes by mRNA cargoes through control of dynein number and activity (2006) Curr Biol, 16, pp. 1447-1452
• Kanai, Y., Dohmae, N., Hirokawa, N., Kinesin transports RNA: Isolation and characterization of an RNA-transporting granule (2004) Neuron, 43, pp. 513-525
• Kiebler, M.A., Hemraj, I., Verkade, P., The mammalian staufen protein localizes to the somatodendritic domain of cultured hippocampal neurons: Implications for its involvement in mRNA transport (1999) J Neurosci, 19, pp. 288-297
• Tang, S.J., Meulemans, D., Vazquez, L., Colaco, N., Schuman, E., A role for a rat homolog of staufen in the transport of RNA to neuronal dendrites (2001) Neuron, 32, pp. 463-475
• Dictenberg, J.B., Swanger, S.A., Antar, L.N., Singer, R.H., Bassell, G.J., A direct role for FMRP in activity-dependent dendritic mRNA transport links filopodial-spine morphogenesis to fragile X syndrome (2008) Dev Cell, 14, pp. 926-939
• Davidovic, L., Jaglin, X.H., Lepagnol-Bestel, A.M., The fragile X mental retardation protein is a molecular adaptor between the neurospecific KIF3C kinesin and dendritic RNA granules (2007) Hum Mol Genet, 16 (24), pp. 3047-3058
• Sossin, W.S., des Groseillers, L., Intracellular trafficking of RNA in neurons (2006) Traffic, 7, pp. 1581-1589
• Abrahamyan, L.G., Chatel-Chaix, L., Ajamian, L., Novel Staufen1 ribonucleoproteins prevent formation of stress granules but favour encapsidation of HIV-1 genomic RNA (2010) J Cell Sci, 123 (PART 3), pp. 369-383
• 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 (PART 2), pp. 228-239
• Ling, S.C., Fahrner, P.S., Greenough, W.T., Gelfand, V.I., Transport of Drosophila fragile X mental retardation protein-containing ribonucleoprotein granules by kinesin-1 and cytoplasmic dynein (2004) Proc Natl Acad Sci USA, 101, pp. 17428-17433
• 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 (PART 21), pp. 3973-3982
• Nadezhdina, E.S., Lomakin, A.J., Shpilman, A.A., Chudinova, E.M., Ivanov, P.A., Microtubules govern stress granule mobility and dynamics (2010) Biochim Biophys Acta, 1803, pp. 361-371
• Noble, S.L., Allen, B.L., Goh, L.K., Nordick, K., Evans, T.C., Maternal mRNAs are regulated by diverse P body-related mRNP granules during early Caenorhabditis elegans development (2008) J Cell Biol, 182, pp. 559-572
• Schneider, I., Cell lines derived from late embryonic stages of Drosophila melanogaster (1972) J Embryol Exp Morphol, 27, pp. 353-365
• Yanagawa, S., Lee, J.S., Ishimoto, A., Identification and characterization of a novel line of Drosophila Schneider S2 cells that respond to wingless signaling (1998) J Biol Chem, 273, pp. 32353-32359
• Rogers, S.L., Rogers, G.C., Culture of Drosophila S2 cells and their use for RNAi-mediated loss-of-function studies and immunofluorescence microscopy (2008) Nat Protoc, 3, pp. 606-611
• Ally, S., Larson, A.G., Barlan, K., Rice, S.E., Gelfand, V.I., Oppositepolarity motors activate one another to trigger cargo transport in live cells (2009) J Cell Biol, 187, pp. 1071-1082
• Bensenor, L.B., Barlan, K., Rice, S.E., Fehon, R.G., Gelfand, V.I., Microtubule-mediated transport of the tumor-suppressor protein Merlin and its mutants (2010) Proc Natl Acad Sci USA, 107, pp. 7311-7316
• Jolly, A.L., Kim, H., Srinivasan, D., Lakonishok, M., Larson, A.G., Gelfand, V.I., Kinesin-1 heavy chain mediates microtubule sliding to drive changes in cell shape (2010) Proc Natl Acad Sci USA, 107, pp. 12151-12156
• Kim, H., Ling, S.C., Rogers, G.C., Microtubule binding by dynactin is required for microtubule organization but not cargo transport (2007) J Cell Biol, 176, pp. 641-651
• Kuznetsov, S.A., Gelfand, V.I., Bovine brain kinesin is a microtubuleactivated ATPase (1986) Proc Nat Acad Sci USA, 83, pp. 8530-8534
• Rogers, S.L., Rogers, G.C., Sharp, D.J., Vale, R.D., Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle (2002) J Cell Biol, 158, pp. 873-884
• Kloc, M., Dougherty, M.T., Bilinski, S., Three-dimensional ultrastructural analysis of RNA distribution within germinal granules of Xenopus (2002) Dev Biol, 241, pp. 79-93
• Micklem, D.R., Adams, J., Grunert, S., St. Johnston, D., Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation (2000) Embo J, 19, pp. 1366-1377
• Yoon, J.H., Choi, E.J., Parker, R., Dcp2 phosphorylation by Ste20 modulates stress granule assembly and mRNA decay in Saccharomyces cerevisiae (2010) J Cell Biol, 189, pp. 813-827
• Nimchinsky, E.A., Oberlander, A.M., Svoboda, K., Abnormal development of dendritic spines in FMR1 knock-out mice (2001) J Neurosci, 21, pp. 5139-5146
• Didiot, M.C., Subramanian, M., Flatter, E., Mandel, J.L., Moine, H., Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly (2009) Mol Biol Cell, 20, pp. 428-437
• 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 (PART 4), pp. 563-573
• Vessey, J.P., Macchi, P., Stein, J.M., A loss of function allele for murine Staufen1 leads to impairment of dendritic Staufen1-RNP delivery and dendritic spine morphogenesis (2008) Proc Natl Acad Sci USA, 105, pp. 16374-16379
• Zalfa, F., Achsel, T., Bagni, C., mRNPs, polysomes or granules: FMRP in neuronal protein synthesis (2006) Curr Opin Neurobiol, 16, pp. 265-269
• Anderson, P., Kedersha, N., Stress granules: The Tao of RNA triage (2008) Trends Biochem Sci, 33, pp. 141-150
• Blumenthal, J., Behar, L., Elliott, E., Ginzburg, I., Dcp1a phosphorylation along neuronal development and stress (2009) FEBS Lett, 583, pp. 197-201
• Kwon, S., Zhang, Y., Matthias, P., The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response (2007) Genes Dev, 21, pp. 3381-3394
• 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
• Hu, P., Shimoji, S., Hart, G.W., Site-specific interplay between OGlcNAcylation and phosphorylation in cellular regulation (2010) FEBS Lett, 584, pp. 2526-2538
• Morfini, G.A., You, Y.M., Pollema, S.L., Pathogenic huntingtin inhibits fast axonal transport by activating JNK3 and phosphorylating kinesin (2009) Nat Neurosci, 12, pp. 864-871
• Tsai, N.P., Wei, L.N., RhoA/ROCK1 signaling regulates stress granule formation and apoptosis (2010) Cell Signal, 22, pp. 668-675
• Morfini, G.A., Burns, M., Binder, L.I., Axonal transport defects in neurodegenerative diseases (2009) J Neurosci, 29, pp. 12776-12786
• Mazroui, R., di Marco, S., Kaufman, R.J., Gallouzi, I.E., Inhibition of the ubiquitin-proteasome system induces stress granule formation (2007) Mol Biol Cell, 18, pp. 2603-2618
• Soncini, C., Berdo, I., Draetta, G., Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease (2001) Oncogene, 20, pp. 3869-3879
• Kraft, C., Deplazes, A., Sohrmann, M., Peter, M., Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease (2008) Nat Cell Biol, 10, pp. 602-610
• Scadden, A.D., Inosine-containing dsRNA binds a stress-granule-like complex and downregulates gene expression in trans (2007) Mol Cell, 28, pp. 491-500
• Bass, B.L., RNA editing by adenosine deaminases that act on RNA (2002) Annu Rev Biochem, 71, pp. 817-846
• Blow, M., Futreal, P.A., Wooster, R., Stratton, M.R., A survey of RNA editing in human brain (2004) Genome Res, 14, pp. 2379-2387
• Levanon, E.Y., Eisenberg, E., Yelin, R., Systematic identification of abundant A-to-I editing sites in the human transcriptome (2004) Nat Biotechnol, 22, pp. 1001-1005
• Morse, D.P., Aruscavage, P.J., Bass, B.L., RNA hairpins in noncoding regions of human brain and Caenorhabditis elegans mRNA are edited by adenosine deaminases that act on RNA (2002) Proc Natl Acad Sci USA, 99, pp. 7906-7911
• Brouha, B., Schustak, J., Badge, R.M., Hot L1s account for the bulk of retrotransposition in the human population (2003) Proc Natl Acad Sci USA, 100, pp. 5280-5285
• Jin, P., Zarnescu, D.C., Ceman, S., Biochemical and genetic interaction between the fragile X mental retardation protein and the microRNA pathway (2004) Nat Neurosci, 7, pp. 113-117
• Souquere, S., Mollet, S., Kress, M., Dautry, F., Pierron, G., Weil, D., Unravelling the ultrastructure of stress granules and associated Pbodies in human cells (2009) J Cell Sci, 15-122 (PART 20), pp. 3619-3626
• Moser, J.J., Eystathioy, T., Chan, E.K., Fritzler, M.J., Markers of mRNA stabilization and degradation, and RNAi within astrocytoma GW bodies (2007) J Neurosci Res, 85, pp. 3619-3631
• Goodier, J.L., Zhang, L., Vetter, M.R., Kazazian Jr., H.H., LINE-1 ORF1 protein localizes in stress granules with other RNA-binding proteins, including components of RNA interference RNA-induced silencing complex (2007) Mol Cell Biol, 27, pp. 6469-6483
• Gibbings, D., Voinnet, O., Control of RNA silencing and localization by endolysosomes (2010) Trends Cell Biol, 20, pp. 491-501
• Pepper, A.S., Beerman, R.W., Bhogal, B., Jongens, T.A., Argonaute2 suppresses Drosophila fragile X expression preventing neurogenesis and oogenesis defects (2009) PLoS One, 4, pp. e7618
• Wang, H.W., Noland, C., Siridechadilok, B., Structural insights into RNA processing by the human RISC-loading complex (2009) Nat Struct Mol Biol, 16, pp. 1148-1153
• Kedersha, N., Chen, S., Gilks, N., Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules (2002) Mol Biol Cell, 13, pp. 195-210
• Kedersha, N., Stoecklin, G., Ayodele, M., Stress granules and processing bodies are dynamically linked sites of mRNP remodeling (2005) J Cell Biol, 169, pp. 871-884
• Young, J.C., Barral, J.M., Ulrich Hartl, F., More than folding: Localized functions of cytosolic chaperones (2003) Trends Biochem Sci, 28, pp. 541-547
• Tourriere, H., Chebli, K., Zekri, L., The RasGAP-associated endoribonuclease G3BP assembles stress granules (2003) J Cell Biol, 160, pp. 823-831
• Schubert, U., Anton, L.C., Gibbs, J., Norbury, C.C., Yewdell, J.W., Bennink, J.R., Rapid degradation of a large fraction of newly synthesized proteins by proteasomes (2000) Nature, 404, pp. 770-774
• Ellgaard, L., Helenius, A., ER quality control: Towards an understanding at the molecular level (2001) Curr Opin Cell Biol, 13, pp. 431-437
• Imai, J., Yashiroda, H., Maruya, M., Yahara, I., Tanaka, K., Proteasomes and molecular chaperones: Cellular machinery responsible for folding and destruction of unfolded proteins (2003) Cell Cycle, 2, pp. 585-590
• Rock, K.L., Gramm, C., Rothstein, L., Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules (1994) Cell, 78, pp. 761-771
• Wojcik, C., de Martino, G.N., Intracellular localization of proteasomes (2003) Int J Biochem Cell Biol, 35, pp. 579-589
• Wojcik, C., Schroeter, D., Stoehr, M., Wilk, S., Paweletz, N., An inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces arrest in G2-phase and metaphase in HeLa cells (1996) Eur J Cell Biol, 70, pp. 172-178
• Johnston, J.A., Dalton, M.J., Gurney, M.E., Kopito, R.R., Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis (2000) Proc Natl Acad Sci USA, 97, pp. 12571-12576
• Kristiansen, M., Messenger, M.J., Klohn, P.C., Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis (2005) J Biol Chem, 280, pp. 38851-38861
• McNaught, K.S., Mytilineou, C., Jnobaptiste, R., Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures (2002) J Neurochem, 81, pp. 301-306
• Olanow, C.W., Perl, D.P., de Martino, G.N., McNaught, K.S., Lewy-body formation is an aggresome-related process: A hypothesis (2004) Lancet Neurol, 3, pp. 496-503
• Beaudoin, S., Goggin, K., Bissonnette, C., Grenier, C., Roucou, X., Aggresomes do not represent a general cellular response to protein misfolding in mammalian cells (2008) BMC Cell Biol, 9, p. 59
• Kakizuka, A., Protein precipitation: A common etiology in neurodegenerative disorders? (1998) Trends Genet, 14, pp. 396-402
• Ross, C.A., Poirier, M.A., Protein aggregation and neurodegenerative disease (2004) Nat Med, 10 (SUPPL), pp. S10-7
• Soto, C., Unfolding the role of protein misfolding in neurodegenerative diseases (2003) Nat Rev Neurosci, 4, pp. 49-60
• Thomas, M.G., Martinez Tosar, L.J., Loschi, M., Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes (2005) Mol Biol Cell, 16, pp. 405-420
• Fujimura, K., Katahira, J., Kano, F., Yoneda, Y., Murata, M., Microscopic dissection of the process of stress granule assembly (2009) Biochim Biophys Acta, 1793, pp. 1728-1737
• Ivanov, P.A., Chudinova, E.M., Nadezhdina, E.S., Disruption of microtubules inhibits cytoplasmic ribonucleoprotein stress granule formation (2003) Exp Cell Res, 290, pp. 227-233
• Kolobova, E., Efimov, A., Kaverina, I., Microtubule-dependent association of AKAP350A and CCAR1 with RNA stress granules (2009) Exp Cell Res, 315, pp. 542-555
• Kedersha, N., Cho, M.R., Li, W., Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules (2000) J Cell Biol, 151, pp. 1257-1268
• Tsai, N.P., Tsui, Y.C., Wei, L.N., Dynein motor contributes to stress granule dynamics in primary neurons (2009) Neuroscience, 159, pp. 647-656
• Hasek, J., Kovarik, P., Valasek, L., Rpg1p, the subunit of the Saccharomyces cerevisiae eIF3 core complex, is a microtubuleinteracting protein (2000) Cell Motil Cytoskeleton, 45, pp. 235-246
• de Boer, S.R., You, Y., Szodorai, A., Conventional kinesin holoenzymes are composed of heavy and light chain homodimers (2008) Biochemistry, 47, pp. 4535-4543
• Vale, R.D., The molecular motor toolbox for intracellular transport (2003) Cell, 112, pp. 467-480
• Morfini, G., Pigino, G., Opalach, K., 1-Methyl-4-phenylpyridinium affects fast axonal transport by activation of caspase and protein kinase C (2007) Proc Natl Acad Sci USA, 104, pp. 2442-2447
• Prusiner, S.B., Hsiao, K.K., Human prion diseases (1994) Ann Neurol, 35, pp. 385-395
• Perutz, M.F., Amyloid fibrils. Mutations make enzyme polymerize (1997) Nature, 385, pp. 773-775
• Burakov, A., Kovalenko, O., Semenova, I., Zhapparova, O., Nadezhdina, E., Rodionov, V., Cytoplasmic dynein is involved in the retention of microtubules at the centrosome in interphase cells (2008) Traffic, 9, pp. 472-480
• Deacon, S.W., Serpinskaya, A.S., Vaughan, P.S., Dynactin is required for bidirectional organelle transport (2003) J Cell Biol, 160, pp. 297-301
• Johnston, J.A., Illing, M.E., Kopito, R.R., Cytoplasmic dynein/dynactin mediates the assembly of aggresomes (2002) Cell Motil Cytoskeleton, 53, pp. 26-38
• Munch, C., Sedlmeier, R., Meyer, T., Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS (2004) Neurology, 63, pp. 724-726
• Munch, C., Rosenbohm, A., Sperfeld, A.D., Heterozygous R1101K mutation of the DCTN1 gene in a family with ALS and FTD (2005) Ann Neurol, 58, pp. 777-780
• Hafezparast, M., Klocke, R., Ruhrberg, C., Mutations in dynein link motor neuron degeneration to defects in retrograde transport (2003) Science, 300, pp. 808-812
• la Monte, B.H., Wallace, K.E., Holloway, B.A., Disruption of dynein/dynactin inhibits axonal transport in motor neurons causing late-onset progressive degeneration (2002) Neuron, 34, pp. 715-727
• Iwata, A., Riley, B.E., Johnston, J.A., Kopito, R.R., HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin (2005) J Biol Chem, 280, pp. 40282-40292
• Wang, L., Nguyen, T.V., McLaughlin, R.W., Sikkink, L.A., Ramirez-Alvarado, M., Weinshilboum, R.M., Human thiopurine Smethyltransferase pharmacogenetics: Variant allozyme misfolding and aggresome formation (2005) Proc Natl Acad Sci USA, 102, pp. 9394-9399
• Kawaguchi, Y., Kovacs, J.J., McLaurin, A., Vance, J.M., Ito, A., Yao, T.P., The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress (2003) Cell, 115, pp. 727-738
• Hideshima, T., Bradner, J.E., Chauhan, D., Anderson, K.C., Intracellular protein degradation and its therapeutic implications (2005) Clin Cancer Res, 11 (24 PART 1), pp. 8530-8533
• Dompierre, J.P., Godin, J.D., Charrin, B.C., Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation (2007) J Neurosci, 27, pp. 3571-3583
• Reed, N.A., Cai, D., Blasius, T.L., Microtubule acetylation promotes kinesin-1 binding and transport (2006) Curr Biol, 16, pp. 2166-2172
• Williams, A.J., Paulson, H.L., Polyglutamine neurodegeneration: Protein misfolding revisited (2008) Trends Neurosci, 31, pp. 521-528
• Lee, H.J., Lee, S.J., Characterization of cytoplasmic alpha-synuclein aggregates. Fibril formation is tightly linked to the inclusionforming process in cells (2002) J Biol Chem, 277, pp. 48976-48983
• Shin, Y., Klucken, J., Patterson, C., Hyman, B.T., McLean, P.J., The cochaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways (2005) J Biol Chem, 280, pp. 23727-23734
• Ardley, H.C., Scott, G.B., Rose, S.A., Tan, N.G., Robinson, P.A., UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease (2004) J Neurochem, 90, pp. 379-391
• Neumann, M., Sampathu, D.M., Kwong, L.K., Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis (2006) Science, 314, pp. 130-133
• Perry, G., Friedman, R., Kang, D.H., Manetto, V., Autilio-Gambetti, L., Gambetti, P., Antibodies to the neuronal cytoskeleton are elicited by Alzheimer paired helical filament fractions (1987) Brain Res., 420, pp. 233-242
• Rujano, M.A., Bosveld, F., Salomons, F.A., Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes (2006) PLoS Biol, 4, pp. e417
• Arai, T., Hasegawa, M., Akiyama, H., TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis (2006) Biochem Biophys Res Commun, 351, pp. 602-611
• Buratti, E., Baralle, F.E., The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation (2010) RNA Biol, 7, pp. 420-429
• Hasegawa, M., Arai, T., Nonaka, T., Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis (2008) Ann Neurol, 64, pp. 60-70
• Zhang, Y.J., Xu, Y.F., Dickey, C.A., Progranulin mediates caspasedependent cleavage of TAR DNA binding protein-43 (2007) J Neurosci, 27, pp. 10530-10534
• Zhang, Y.J., Xu, Y.F., Cook, C., Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity (2009) Proc Natl Acad Sci USA, 106, pp. 7607-7612
• Colombrita, C., Zennaro, E., Fallini, C., TDP-43 is recruited to stress granules in conditions of oxidative insult (2009) J Neurochem, 111, pp. 1051-1061
• Nishimoto, Y., Ito, D., Yagi, T., Nihei, Y., Tsunoda, Y., Suzuki, N., Characterization of alternative isoforms and inclusion body of the TAR DNA-binding protein-43 (2010) J Biol Chem, 285, pp. 608-619
• Volkening, K., Leystra-Lantz, C., Yang, W., Jaffee, H., Strong, M.J., Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS) (2009) Brain Res, 1305, pp. 168-182
• Liu-Yesucevitz, L., Bilgutay, A., Zhang, Y.J., Tar DNA binding protein-43 (TDP-43) associates with stress granules: Analysis of cultured cells and pathological brain tissue (2010) PLoS One, 5, pp. e13250
• Hubbert, C., Guardiola, A., Shao, R., HDAC6 is a microtubuleassociated deacetylase (2002) Nature, 417, pp. 455-458
• Matsuyama, A., Shimazu, T., Sumida, Y., In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation (2002) Embo J, 21, pp. 6820-6831
• Iliev, A.I., Djannatian, J.R., Opazo, F., Rapid microtubule bundling and stabilization by the Streptococcus pneumoniae neurotoxin pneumolysin in a cholesterol-dependent, non-lytic and Srckinase dependent manner inhibits intracellular trafficking (2009) Mol Microbiol, 71, pp. 461-477
• Tonami, K., Kurihara, Y., Aburatani, H., Uchijima, Y., Asano, T., Kurihara, H., Calpain 6 is involved in microtubule stabilization and cytoskeletal organization (2007) Mol Cell Biol, 27, pp. 2548-2561
• Gao, Y.S., Hubbert, C.C., Yao, T.P., The microtubule-associated histone deacetylase 6 (HDAC6) regulates epidermal growth factor receptor (EGFR) endocytic trafficking and degradation J Biol Chem, 285, pp. 11219-11226
• Pugacheva, E.N., Jablonski, S.A., Hartman, T.R., Henske, E.P., Golemis, E.A., HEF1-dependent Aurora A activation induces disassembly of the primary cilium (2007) Cell, 129, pp. 1351-1363
• Naranatt, P.P., Krishnan, H.H., Smith, M.S., Chandran, B., Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus (2005) J Virol, 79, pp. 1191-1206
• Warren, J.C., Rutkowski, A., Cassimeris, L., Infection with replicationdeficient adenovirus induces changes in the dynamic instability of host cell microtubules (2006) Mol Biol Cell, 17, pp. 3557-3568
• Gitcho, M.A., Baloh, R.H., Chakraverty, S., TDP-43 A315T mutation in familial motor neuron disease (2008) Ann Neurol, 63, pp. 535-538
• van Deerlin, V.M., Leverenz, J.B., Bekris, L.M., TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: A genetic and histopathological analysis (2008) Lancet Neurol, 7, pp. 409-416
• Sreedharan, J., Blair, I.P., Tripathi, V.B., TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis (2008) Science, 319, pp. 1668-1672
• Rutherford, N.J., Zhang, Y.J., Baker, M., Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis (2008) PLoS Genet, 4, pp. e1000193
• Kabashi, E., Daoud, H., Riviere, J.B., No TARDBP mutations in a French Canadian population of patients with Parkinson disease (2009) Arch Neurol, 66, pp. 281-282
• Yokoseki, A., Shiga, A., Tan, C.F., TDP-43 mutation in familial amyotrophic lateral sclerosis (2008) Ann Neurol, 63, pp. 538-542
• Arai, T., Ikeda, K., Akiyama, H., Identification of aminoterminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration (2004) Ann Neurol, 55, pp. 72-79
• di Figlia, M., Sapp, E., Chase, K.O., Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain (1997) Science, 277, pp. 1990-1993
• Mende-Mueller, L.M., Toneff, T., Hwang, S.R., Chesselet, M.F., Hook, V.Y., Tissue-specific proteolysis of Huntingtin (htt) in human brain: Evidence of enhanced levels of N-and C-terminal htt fragments in Huntington's disease striatum (2001) J Neurosci, 21, pp. 1830-1837
• Selkoe, D.J., Yamazaki, T., Citron, M., The role of APP processing and trafficking pathways in the formation of amyloid betaprotein (1996) Ann N Y Acad Sci, 777, pp. 57-64
• Sisodia, S.S., Price, D.L., Role of the beta-amyloid protein in Alzheimer's disease (1995) Faseb J, 9, pp. 366-370
• Dekanty, A., Romero, N.M., Bertolin, A.P., Drosophila genomewide RNAi screen identifies multiple regulators of HIF-dependent transcription in hypoxia (2010) PLoS Genet, 6, pp. e1000994

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------