RNA granules

Stress granules and processing bodies are dynamically linked sites of mRNP remodeling

Kedersha, N., Stoecklin, G., Ayodele, M. O., Yacono, P. W., Lykke‐Andersen, J., Fritzler, M. J., Scheuner, D. L., Kaufman, R. J., Golan, D. E., & Anderson, P. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502088 · Cited by 1,494 · see citing works

Inhibition of Translational Initiation by Let-7 MicroRNA in Human Cells

Pillai, R. S., Bhattacharyya, S. N., Artus-Revel, C. G., Zoller, T., Cougot, N., Basyuk, E. I., Bertrand, É., & Filipowicz, W. (2005) · Science · doi:10.1126/science.1115079 · Cited by 1,431 · see citing works

Decapping and Decay of Messenger RNA Occur in Cytoplasmic Processing Bodies

Sheth, U., & Parker, R. (2003) · Science · doi:10.1126/science.1082320 · Cited by 1,372 · see citing works

RNA-Binding Proteins Tia-1 and Tiar Link the Phosphorylation of Eif-2α to the Assembly of Mammalian Stress Granules

Kedersha, N., Gupta, M., Li, W., Miller, I. J., & Anderson, P. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.7.1431 · Cited by 1,260 · see citing works

MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies

Liu, J., Valencia-Sanchez, M. A., Hannon, G. J., & Parker, R. (2005) · Nature Cell Biology · doi:10.1038/ncb1274 · Cited by 1,234 · see citing works

From Birth to Death: The Complex Lives of Eukaryotic mRNAs

Moore, M. J. (2005) · Science · doi:10.1126/science.1111443 · Cited by 1,003 · see citing works

Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1

Farny, N. G., Kedersha, N., Ayodele, M. O., Shen, L., Stoecklin, G., Dember, L. M., & Anderson, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0715 · Cited by 1,000 · see citing works

Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors

Moeller, B. J., Cao, Y., Li, C. Y., & Dewhirst, M. W. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00115-1 · Cited by 996 · see citing works

Dynamic Shuttling of Tia-1 Accompanies the Recruitment of mRNA to Mammalian Stress Granules

Kedersha, N., Cho, M., Li, W., Yacono, P. W., Chen, S., Farny, N. G., Golan, D. E., & Anderson, P. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1257 · Cited by 815 · see citing works

Role of Stress Granules and RNA-Binding Proteins in Neurodegeneration: A Mini-Review

Vanderweyde, T. E., Youmans, K., Liu‐Yesucevitz, L., & Wolozin, B. L. (2013) · Gerontology · doi:10.1159/000354170 · Cited by 806 · see citing works

Movement of Eukaryotic mRNAs Between Polysomes and Cytoplasmic Processing Bodies

Brengues, M., Teixeira, D., & Parker, R. (2005) · Science · doi:10.1126/science.1115791 · Cited by 796 · see citing works

Stress granules: sites of mRNA triage that regulate mRNA stability and translatability

Kedersha, N., & Anderson, P. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300963 · Cited by 735 · see citing works

Processing bodies require RNA for assembly and contain nontranslating mRNAs

Teixeira, D., Sheth, U., Valencia-Sanchez, M. A., Brengues, M., & Parker, R. (2005) · RNA · doi:10.1261/rna.7258505 · Cited by 728 · see citing works

Spatial regulation of β-actin translation by Src-dependent phosphorylation of ZBP1

Hüttelmaier, S., Zenklusen, D., Lederer, M., Dictenberg, J., Lorenz, M., Meng, X.-H., Bassell, G., Condeelis, J., & Singer, R. (2005) · Nature · doi:10.1038/nature04115 · Cited by 681 · see citing works

A role for the P-body component GW182 in microRNA function

Liu, J., Rivas, F. V., Wohlschlegel, J. A., Yates, J. R., Parker, R., & Hannon, G. J. (2005) · Nature Cell Biology · doi:10.1038/ncb1333 · Cited by 680 · see citing works

Cytoplasmic foci are sites of mRNA decay in human cells

Cougot, N., Babajko, S., & Séraphin, B. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309008 · Cited by 647 · see citing works

Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies

Sen, G. L., & Blau, H. M. (2005) · Nature Cell Biology · doi:10.1038/ncb1265 · Cited by 645 · see citing works

General Translational Repression by Activators of mRNA Decapping

Coller, J. M., & Parker, R. (2005) · Cell · doi:10.1016/j.cell.2005.07.012 · Cited by 629 · see citing works

Evidence That Ternary Complex (eIF2-GTP-tRNA i Met )–Deficient Preinitiation Complexes Are Core Constituents of Mammalian Stress Granules

Kedersha, N., Chen, S., Farny, N. G., Li, W., Miller, I. J., Stahl, J., & Anderson, P. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-05-0221 · Cited by 624 · see citing works

Neuronal RNA Granules

Krichevsky, A. M., & Kosik, K. S. (2001) · Neuron · doi:10.1016/s0896-6273(01)00508-6 · Cited by 536 · see citing works

A schizophrenia-associated mutation of DISC1 perturbs cerebral cortex development

Kamiya, A., Kubo, K., Tomoda, T., Takaki, M., Youn, R., Ozeki, Y., Sawamura, N., Park, U., Kudo, C., Okawa, M., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1328 · Cited by 531 · see citing works

MK2‐induced tristetraprolin:14‐3‐3 complexes prevent stress granule association and ARE‐mRNA decay

Stoecklin, G., Stubbs, T., Kedersha, N., Wax, S. D., Rigby, W. F. C., Blackwell, T. K., & Anderson, P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600163 · Cited by 518 · see citing works

Disruption of GW bodies impairs mammalian RNA interference

Jakymiw, A., Lian, S., Eystathioy, T., Li, S., Satoh, M., Hamel, J. C., Fritzler, M. J., & Chan, E. K. L. (2005) · Nature Cell Biology · doi:10.1038/ncb1334 · Cited by 496 · see citing works

Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures

van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E., & Séraphin, B. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf678 · Cited by 495 · see citing works

A crucial role for GW182 and the DCP1:DCP2 decapping complex in miRNA-mediated gene silencing

Rehwinkel, J., Behm‐Ansmant, I., Gatfield, D., & Izaurralde, E. (2005) · RNA · doi:10.1261/rna.2191905 · Cited by 493 · see citing works

Multiple Processing Body Factors and the ARE Binding Protein TTP Activate mRNA Decapping

Fenger-Grøn, M., Fillman, C. L., Norrild, B., & Lykke‐Andersen, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.031 · Cited by 459 · see citing works

Heme-regulated Inhibitor Kinase-mediated Phosphorylation of Eukaryotic Translation Initiation Factor 2 Inhibits Translation, Induces Stress Granule Formation, and Mediates Survival upon Arsenite Exposure

McEwen, E. L., Kedersha, N., Song, B., Scheuner, D. L., Gilks, N., Han, A., Chen, J.-J., Anderson, P., & Kaufman, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412882200 · Cited by 448 · see citing works

The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrn1 in distinct cytoplasmic foci

Ingelfinger, D., Arndt‐Jovin, D. J., Lührmann, R., & Achsel, T. (2002) · RNA · doi:10.1017/s1355838202021726 · Cited by 404 · see citing works

Stressful initiations

Anderson, P., & Kedersha, N. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.16.3227 · Cited by 376 · see citing works

A Phosphorylated Cytoplasmic Autoantigen, GW182, Associates with a Unique Population of Human mRNAs within Novel Cytoplasmic Speckles

Eystathioy, T., Chan, E. K. L., Tenenbaum, S. A., Keene, J. D., Griffith, K. J., & Fritzler, M. J. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-11-0544 · Cited by 363 · see citing works

Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs.

Nover, L., Scharf, K., & Neumann, D. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.3.1298 · Cited by 356 · see citing works

A Mouse Cytoplasmic Exoribonuclease (mXRN1p) with Preference for G4 Tetraplex Substrates

Bashkirov, V. I., Scherthan, H., Solinger, J. A., Buerstedde, J.-M., & Heyer, W. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.4.761 · Cited by 348 · see citing works

HuR binding to cytoplasmic mRNA is perturbed by heat shock

Gallouzi, I., Brennan, C. M., Stenberg, M. G., Swanson, M. S., Eversole, A., Maizels, N., & STEITZ, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3073 · Cited by 326 · see citing works

Translational Regulation and RNA Localization in Drosophila Oocytes and Embryos

Johnstone, O., & Lasko, P. F. (2001) · Annual Review of Genetics · doi:10.1146/annurev.genet.35.102401.090756 · Cited by 322 · see citing works

SMG7 Acts as a Molecular Link between mRNA Surveillance and mRNA Decay

Unterholzner, L., & Izaurralde, E. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.013 · Cited by 309 · see citing works

The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules

Wilczynska, A., Aigueperse, C., Kress, M., Dautry, F., & Barbieri-Weill, D. (2005) · Journal of Cell Science · doi:10.1242/jcs.01692 · Cited by 302 · see citing works

Mammalian stress granules represent sites of accumulation of stalled translation initiation complexes

Kimball, S. R., Horetsky, R. L., Ron, D., Jefferson, L. S., & Harding, H. P. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00314.2002 · Cited by 291 · see citing works

The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies: FIGURE 1.

Eystathioy, T., Jakymiw, A., Chan, E. K. L., Séraphin, B., Cougot, N., & Fritzler, M. J. (2003) · RNA · doi:10.1261/rna.5810203 · Cited by 267 · see citing works

A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decay

Ferraiuolo, M. A., Basak, S., Dostie, J., Murray, E. L., Schoenberg, D. R., & Sonenberg, N. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504039 · Cited by 255 · see citing works

SMG7 Is a 14-3-3-like Adaptor in the Nonsense-Mediated mRNA Decay Pathway

Fukuhara, N., Ebert, J., Unterholzner, L., Lindner, D., Izaurralde, E., & Conti, E. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.010 · Cited by 242 · see citing works

ARE‐mRNA degradation requires the 5′–3′ decay pathway

Stoecklin, G., Mayo, T., & Anderson, P. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400572 · Cited by 237 · see citing works

A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1 is required for embryonic cytokinesis in Caenorhabditis elegans

Audhya, A., Barron, F. E., McLeod, I. X., Maddox, A. S., Yates, J. R., Desai, A. B., & Oegema, K. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200506124 · Cited by 232 · see citing works

Sequestration of TRAF2 into Stress Granules Interrupts Tumor Necrosis Factor Signaling under Stress Conditions

Kim, W. J., Back, S. H., Kim, V., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2450-2462.2005 · Cited by 214 · see citing works

RasGAP-Associated Endoribonuclease G3BP: Selective RNA Degradation and Phosphorylation-Dependent Localization

Tourrière, H., Gallouzi, I., Chébli, K., Capony, J. P., Mouaikel, J., van der Geer, P., & Tazi, J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.22.7747-7760.2001 · Cited by 207 · see citing works

Analysis of RNA associated with P granules in germ cells of C. elegans adults

Schisa, J. A., Pitt, J. N., & Priess, J. R. (2001) · Development · doi:10.1242/dev.128.8.1287 · Cited by 203 · see citing works

Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body

YU, J. H., Yang, W.-H., Gulick, T., Bloch, K. D., & Bloch, D. B. (2005) · RNA · doi:10.1261/rna.2142405 · Cited by 199 · see citing works

A conserved RNA-protein complex component involved in physiological germline apoptosis regulation inC. elegans

Boag, P. R., Nakamura, A., & Blackwell, T. K. (2005) · Development · doi:10.1242/dev.02060 · Cited by 163 · see citing works

Staufen Recruitment into Stress Granules Does Not Affect Early mRNA Transport in Oligodendrocytes

Thomas, M. G., Tosar, L. M., Loschi, M., Pasquini, J. M., Correale, J. D., Kindler, S., & Boccaccio, G. L. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0516 · Cited by 159 · see citing works

The insulin‐like growth factor mRNA binding‐protein IMP‐1 and the Ras‐regulatory protein G3BP associate with tau mRNA and HuD protein in differentiated P19 neuronal cells

Atlas, R., Behar, L., Elliott, E., & Ginzburg, I. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02371.x · Cited by 152 · see citing works

Survival motor neuron protein facilitates assembly of stress granules

Hua, Y., & Zhou, J. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.010 · Cited by 148 · see citing works

An isoform of eIF4E is a component of germ granules and is required for spermatogenesis inC. elegans

Amiri, A., Keiper, B. D., Kawasaki, I., et al. (2001) · Development · doi:10.1242/dev.128.20.3899 · Cited by 117 · see citing works

Progression of hair cell ejection and molecular markers of apoptosis in the avian cochlea following gentamicin treatment

Mangiardi, D. A., McLaughlin‐Williamson, K., May, K. E., et al. (2004) · The Journal of Comparative Neurology · doi:10.1002/cne.20129 · Cited by 110 · see citing works

BDNF induces translocation of initiation factor 4E to mRNA granules: Evidence for a role of synaptic microfilaments and integrins

Smart, F. M., Edelman, G., & Vanderklish, P. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.2436349100 · Cited by 105 · see citing works

Regulation of cytoplasmic stress granules by apoptosis-inducing factor

Candé, C., Vahsen, N., Métivier, D., Tourrière, H., Chébli, K., Garrido, C., Tazi, J., & Kroemer, G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01356 · Cited by 98 · see citing works

Studies on germ cells. I. The history of the germ cells in insects with special reference to the Keimbahn‐determinants. II. The origin and significance of the Keimbahn‐determinants in animals

Hegner, R. W. (1914) · Journal of Morphology · doi:10.1002/jmor.1050250302 · Cited by 90 · see citing works

Transcriptional silencing and translational control: key features of early germline development

Leatherman, J. L., & Jongens, T. A. (2003) · BioEssays · doi:10.1002/bies.10247 · Cited by 90 · see citing works

DcpS can act in the 5′–3′ mRNA decay pathway in addition to the 3′–5′ pathway

van Dijk, E., Hir, H. L., & Séraphin, B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1635192100 · Cited by 90 · see citing works

Caenorhabditis elegansDecapping Proteins: Localization and Functional Analysis of Dcp1, Dcp2, and DcpS during Embryogenesis

Lall, S., Piano, F., & Davis, R. E. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0622 · Cited by 66 · see citing works

Prolonged translation arrest in reperfused hippocampal cornu Ammonis 1 is mediated by stress granules

Kayali, F. M., Montie, H. L., Rafols, J. A., et al. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.05.047 · Cited by 65 · see citing works

Sum1, a Component of the Fission Yeast eIF3 Translation Initiation Complex, Is Rapidly Relocalized During Environmental Stress and Interacts with Components of the 26S Proteasome

Dunand-Sauthier, I., Walker, C. A., Wilkinson, C. R. M., et al. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-06-0301 · Cited by 62 · see citing works

Apoptosis: eating sensibly

Gregory, C. D., & Brown, S. B. (2005) · Nature Cell Biology · doi:10.1038/ncb1205-1161 · Cited by 40 · see citing works

Requirement for P granules and meiosis for accumulation of the germline RNA helicase CGH-1

Navarro, R. E., & Blackwell, T. K. (2005) · genesis · doi:10.1002/gene.20136 · Cited by 33 · see citing works

The Message and the Messenger: Delivering RNA in Neurons

Kosik, K. S., & Krichevsky, A. M. (2002) · Science s STKE · doi:10.1126/stke.2002.126.pe16 · Cited by 33 · see citing works

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012 · see citing works

SUnSET, a nonradioactive method to monitor protein synthesis

Schmidt, E. K., Clavarino, G., Ceppi, M., & Pierre, P. (2009) · Nature Methods · doi:10.1038/nmeth.1314 · Cited by 1,706 · see citing works

Hallmarks of neurodegenerative diseases

Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789 · see citing works

P bodies and the control of mRNA translation and degradation

Parker, R., & Sheth, U. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.011 · Cited by 1,335 · see citing works

Tuning gene expression to changing environments: from rapid responses to evolutionary adaptation

López-Maury, L., Marguerat, S., & Bähler, J. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2398 · Cited by 1,061 · see citing works

P-body formation is a consequence, not the cause, of RNA-mediated gene silencing

Eulalio, A., Behm-Ansmant, I., Schweizer, D., & Izaurralde, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00128-07 · Cited by 710 · see citing works

Signalling to translation: How signal transduction pathways control the protein synthetic machinery

Proud, C. G. (2007) · Biochemical Journal · doi:10.1042/bj20070024 · Cited by 520 · see citing works

Restricting retrotransposons: a review

Goodier, J. L. (2016) · Mobile DNA · doi:10.1186/s13100-016-0070-z · Cited by 436 · see citing works

The Pathophysiology of Fragile X (and What It Teaches Us about Synapses)

Bhakar, A. L., Dölen, G., & Bear, M. F. (2012) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-060909-153138 · Cited by 370 · see citing works

Fragile X syndrome: causes, diagnosis, mechanisms, and therapeutics

Bagni, C., Tassone, F., Neri, G., & Hagerman, R. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63141 · Cited by 321 · see citing works

Single-molecule analysis of gene expression using two-color RNA labeling in live yeast

Hocine, S., Raymond, P., Zenklusen, D., Chao, J. A., & Singer, R. H. (2013) · Nature Methods · doi:10.1038/nmeth.2305 · Cited by 297 · see citing works

Mechanisms of dendritic mRNA transport and its role in synaptic tagging

Doyle, M., & Kiebler, M. A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.278 · Cited by 288 · see citing works

p16INK4a Translation Suppressed by miR-24

Lal, A., Kim, H. H., Abdelmohsen, K., Kuwano, Y., Pullmann, R., Srikantan, S., Subrahmanyam, R., Martindale, J. L., Yang, X., Ahmed, F., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001864 · Cited by 268 · see citing works

The regulation of mRNA stability in mammalian cells: 2.0

Wu, X., & Brewer, G. (2012) · Gene · doi:10.1016/j.gene.2012.03.021 · Cited by 239 · see citing works

Systematic analysis of ribophagy in human cells reveals bystander flux during selective autophagy

An, H., & Harper, J. W. (2018) · Nature Cell Biology · doi:10.1038/s41556-017-0007-x · Cited by 181 · see citing works

Role of Alix in miRNA packaging during extracellular vesicle biogenesis

IAVELLO, A., FRECH, V. S. L., GAI, C., DEREGIBUS, M. C., QUESENBERRY, P. J., & CAMUSSI, G. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2488 · Cited by 175 · see citing works

Ribonomic Analysis of Human Pum1 Reveals <i>cis-trans</i> Conservation across Species despite Evolution of Diverse mRNA Target Sets

Morris, A. R., Mukherjee, N., & Keene, J. D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00155-08 · Cited by 155 · see citing works

Retinoic acid regulates RARα-mediated control of translation in dendritic RNA granules during homeostatic synaptic plasticity

Maghsoodi, B., Poon, M. M., Nam, C. I., Aoto, J., Ting, P., & Chen, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804801105 · Cited by 138 · see citing works

Integrating the DNA damage and protein stress responses during cancer development and treatment

Gorgoulis, V. G., Pefani, D., Pateras, I. S., & Trougakos, I. P. (2018) · The Journal of Pathology · doi:10.1002/path.5097 · Cited by 108 · see citing works

The Nuclear Transcription Factor RARα Associates with Neuronal RNA Granules and Suppresses Translation

Chen, N., Onisko, B., & Napoli, J. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802314200 · Cited by 89 · see citing works

RNA-binding proteins with basic-acidic dipeptide (BAD) domains self-assemble and aggregate in Alzheimer's disease

Bishof, I., Dammer, E. B., Duong, D. M., Kundinger, S. R., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001747 · Cited by 80 · see citing works

Cell stress is related to re-localization of Argonaute 2 and to decreased RNA interference in human cells

Detzer, A., Engel, C., Wünsche, W., & Sczakiel, G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1216 · Cited by 74 · see citing works

Cellular oxygen sensing, signalling and how to survive translational arrest in hypoxia

Fähling, M. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2008.01894.x · Cited by 57 · see citing works

Surviving hypoxia by modulation of mRNA translation rate

Fähling, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00875.x · Cited by 54 · see citing works

Molecular and Cellular Aspects of Mental Retardation in the Fragile X Syndrome: From Gene Mutation/s to Spine Dysmorphogenesis

De Rubeis, S., Fernández, E., Buzzi, A., Di Marino, D., & Bagni, C. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-7091-0932-8_23 · Cited by 48 · see citing works

Intracellular localization and interaction of mRNA binding proteins as detected by FRET

David Gerecht, P. S., Taylor, M. A., & Port, J. D. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-69 · Cited by 22 · see citing works

A exonuclease XRNA e o metabolismo de mRNA em Trypanosoma cruzi

da Costa, J. F. (2015)

Granules Harboring Translationally Active mRNAs Provide a Platform for P-Body Formation following Stress

Lui, J., Castelli, L. M., Pizzinga, M., Simpson, C. E., Hoyle, N. P., Bailey, K. L., Campbell, S. G., & Ashe, M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.040 · Cited by 71 · see citing works

Analyzing P-Bodies and Stress Granules in Saccharomyces cerevisiae

Buchan, J. R., Nissan, T. A., & Parker, R. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)70025-2 · Cited by 71 · see citing works

Translationally Repressed mRNA Transiently Cycles through Stress Granules during Stress

Mollet, S., Cougot, N., Wilczynska, A., Dautry, F., Kress, M., Bertrand, É., & Barbieri-Weill, D. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0499 · Cited by 241 · see citing works

P bodies promote stress granule assembly in Saccharomyces cerevisiae

Buchan, J. R., Muhlrad, D., & Parker, R. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200807043 · Cited by 517 · see citing works