Cited by 710RNA Research and SplicingRNA Interference and Gene DeliveryRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.

P-Body Formation Is a Consequence, Not the Cause, of RNA-Mediated Gene Silencing

Open access

Eulalio, Ana, Behm-Ansmant, Isabelle, Schweizer, Daniel, Izaurralde, Elisa·2007·Molecular and Cellular Biology

DOI 10.1128/mcb.00128-07PMC PMC1900022

Open this paper in CoChat — free account

Abstract

P bodies are cytoplasmic domains that contain proteins involved in diverse posttranscriptional processes, such as mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing. The localization of these proteins and their targets in P bodies raises the question of whether their spatial concentration in discrete cytoplasmic domains is required for posttranscriptional gene regulation. We show that processes such as mRNA decay, NMD, and RNA-mediated gene silencing are functional in cells lacking detectable microscopic P bodies. Although P bodies are not required for silencing, blocking small interfering RNA or microRNA silencing pathways at any step prevents P-body formation, indicating that P bodies arise as a consequence of silencing. Consistently, we show that releasing mRNAs from polysomes is insufficient to trigger P-body assembly: polysome-free mRNAs must enter silencing and/or decapping pathways to nucleate P bodies. Thus, even though P-body components play crucial roles in mRNA silencing and decay, aggregation into P bodies is not required for function but is instead a consequence of their activity.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1128/mcb.00128-07

Cites

62 of 62 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Mechanisms of gene silencing by double-stranded RNA
Meister, G., & Tuschl, T. (2004) · Nature · doi:10.1038/nature02873 · Cited by 2,598
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
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 1,489
Relief of microRNA-Mediated Translational Repression in Human Cells Subjected to Stress
Bhattacharyya, S. N., Habermacher, R., Martiné, U., Closs, E. I., & Filipowicz, W. (2006) · Cell · doi:10.1016/j.cell.2006.04.031 · Cited by 1,384
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
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
mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexesPreprint
Behm‐Ansmant, I., Rehwinkel, J., Doerks, T., Stark, A., Bork, P., & Izaurralde, E. (2006) · Genes & Development · doi:10.1101/gad.1424106 · Cited by 1,113
RNA granules
Anderson, P., & Kedersha, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512082 · Cited by 984
P bodies: at the crossroads of post-transcriptional pathways
Eulálio, A., Behm‐Ansmant, I., & Izaurralde, E. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2080 · Cited by 970
Distinct roles for Argonaute proteins in small RNA-directed RNA cleavage pathwaysPreprint
岡村, 勝., Ishizuka, A., Siomi, H., & Siomi, M. C. (2004) · Genes & Development · doi:10.1101/gad.1210204 · Cited by 866

Flagged first, then by citations

Show all 62 references

Research works printed but not linked: 1

Chu C. Y., 2006, PLoS Biol., 4, 1122

Sorted by citations

Items 201–300 of 710

RNA decay modulates gene expression and controls its fidelity
Ghosh, S., & Jacobson, A. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.25 · Cited by 70
Differential utilization of decapping enzymes in mammalian mRNA decay pathways
Li, Y., Song, M.-G., & Kiledjian, M. (2011) · RNA · doi:10.1261/rna.2439811 · Cited by 70
RNA Binding Protein Nanos2 Organizes Post-transcriptional Buffering System to Retain Primitive State of Mouse Spermatogonial Stem Cells
Zhou, Z., Shirakawa, T., Ohbo, K., Sada, A., Wu, Q., Hasegawa, K., Saba, R., & Saga, Y. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.05.014 · Cited by 69
The P Body Protein Dcp1a Is Hyper-phosphorylated during Mitosis
Aizer, A., Kafri, P., Kalo, A., & Shav‐Tal, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0049783 · Cited by 69
Molecular mechanisms of peripheral nerve regeneration: emerging roles of microRNAs
Wu, D., & Murashov, A. K. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00055 · Cited by 72
Bicc1 links the regulation of cAMP signaling in polycystic kidneys to microRNA-induced gene silencing
Piazzon, N., Maisonneuve, C., Guilleret, I., Rotman, S., & Constam, D. B. (2012) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjs027 · Cited by 71
Localization of Double-stranded Small Interfering RNA to Cytoplasmic Processing Bodies Is Ago2 Dependent and Results in Up-Regulation of GW182 and Argonaute-2
Jagannath, A., & Wood, M. J. A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-08-0796 · Cited by 68
LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing
James, V. H., Zhang, Y., Foxler, D. E., de Moor, C. H., Kong, Y. W., Webb, T. M., Self, T. J., Feng, Y., Lagos, D., Chu, C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914987107 · Cited by 67
Differential Localization of the Two T. brucei Poly(A) Binding Proteins to the Nucleus and RNP Granules Suggests Binding to Distinct mRNA Pools
Krämer, S., Bannerman-Chukualim, B., Ellis, L., Boulden, E. A., Kelly, S. L., Field, M. C., & Carrington, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054004 · Cited by 65
Argonaute Utilization for miRNA Silencing Is Determined by Phosphorylation-Dependent Recruitment of LIM-Domain-Containing Proteins
Bridge, K. S., Shah, K., Li, Y., Foxler, D. E., Wong, S. C. K., Miller, D. C., Davidson, K. M., Foster, J. G., Rose, R., Hodgkinson, M. R., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.027 · Cited by 66
The UPF1 interactome reveals interaction networks between RNA degradation and translation repression factors in Arabidopsis
Chicois, C., Scheer, H., Garcia, S., Zuber, H., Mutterer, J., Chicher, J., Hammann, P., Gagliardi, D., & Garcia, D. (2018) · The Plant Journal · doi:10.1111/tpj.14022 · Cited by 53
PABP is not essential for microRNA‐mediated translational repression and deadenylation in vitro
Fukaya, T., & Tomari, Y. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.426 · Cited by 64
A rapid inducible RNA decay system reveals fast mRNA decay in P-bodies
Blake, L. A., Watkins, L., Liu, Y., Inoue, T., & Wu, B. (2024) · Nature Communications · doi:10.1038/s41467-024-46943-z · Cited by 67
Translational control in early development: CPEB, P-bodies and germinal granules
Standart, N., & Minshall, N. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360671 · Cited by 64
Identification of GW182 and its novel isoform TNGW1 as translational repressors in Ago2-mediated silencing
Li, S., Lian, S. L., Moser, J. J., Fritzler, M. L., Fritzler, M. J., Satoh, M., & Chan, E. K. L. (2008) · Journal of Cell Science · doi:10.1242/jcs.036905 · Cited by 64
Smaug1 mRNA-silencing foci respond to NMDA and modulate synapse formation
Báez, M. V., Luchelli, L., Maschi, D., Habif, M., Pascual, M. L., Thomas, M. G., & Boccaccio, G. L. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201108159 · Cited by 67
Transcriptional riboswitches integrate timescales for bacterial gene expression control
Scull, C. E., Dandpat, S. S., Romero, R. A., & Walter, N. G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.607158 · Cited by 58
“Non-coding RNAs (ncRNAs) are vital for countless cellular mechanisms, such as ribozyme mediated catalysis of RNA processing reactions, RNA mediated gene silencing, and stabilization of phase separated particles, to name a few (Eddy, 2001; Walter and Engelke, 2002; Eulalio et al., 2007; Serganov and Patel, 2007; Carthe…”
Background
DDX6 and its orthologs as modulators of cellular and viral RNA expression
Ostareck, D. H., Vries, I. S. N., & Ostareck‐Lederer, A. (2014) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1237 · Cited by 64
Ways and means of eukaryotic mRNA decay
Balagopal, V., Fluch, L., & Nissan, T. A. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.01.001 · Cited by 65
Distinct functions of maternal and somatic Pat1 protein paralogs
Marnef, A., Maldonado, M., Bugaut, A., Balasubramanian, S., Kress, M., Barbieri-Weill, D., & Standart, N. (2010) · RNA · doi:10.1261/rna.2295410 · Cited by 66
Reactivation of nonsense-mediated mRNA decay protects against C9orf72 dipeptide-repeat neurotoxicity
Xu, W., Bao, P., Jiang, X., Wang, H., Qin, M., Wang, R. L., Wang, T., Yang, Y. A., Lorenzini, I., Liao, L., et al. (2019) · Brain · doi:10.1093/brain/awz070 · Cited by 61
A Molecular Link between miRISCs and Deadenylases Provides New Insight into the Mechanism of Gene Silencing by MicroRNAs
Braun, J. E., Huntzinger, E., & Izaurralde, E. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012328 · Cited by 61
The RRM domain in GW182 proteins contributes to miRNA-mediated gene silencing
Eulálio, A., Tritschler, F., Büttner, R., Weichenrieder, O., Izaurralde, E., & Truffault, V. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp173 · Cited by 59
Bacterial RNA Degradosomes: Molecular Machines under Tight Control
Tejada-Arranz, A., de Crécy‐Lagard, V., & Reuse, H. D. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.10.002 · Cited by 60
Circulating microRNAs as Potential Biomarkers in Pancreatic Cancer—Advances and Challenges
Seyhan, A. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713340 · Cited by 63
The RNA helicase DHH1 is central to the correct expression of many developmentally regulated mRNAs in trypanosomes
Krämer, S., Queiroz, R., Ellis, L., Hoheisel, J. D., CLAYTON, C. E., & Carrington, M. (2010) · Journal of Cell Science · doi:10.1242/jcs.058511 · Cited by 59
Historical Survey on Chromatoid Body Research
Yokota, S. (2008) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.08010 · Cited by 61
Defects in the Secretory Pathway and High Ca2+Induce Multiple P-bodies
Kilchert, C., Weidner, J., Prescianotto‐Baschong, C., & Spang, A. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-02-0099 · Cited by 59
Attacked from All Sides: RNA Decay in Antiviral Defense
Molleston, J. M., & Cherry, S. R. (2017) · Viruses · doi:10.3390/v9010002 · Cited by 57
Concepts and functions of small RNA pathways in C. elegans
Ketting, R. F., & Cochella, L. (2020) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2020.08.002 · Cited by 56
Hepatitis B Virus-Specific miRNAs and Argonaute2 Play a Role in the Viral Life Cycle
Hayes, C. N., Akamatsu, S., Tsuge, M., Miki, D., Akiyama, R., Abe, H., Ochi, H., Hiraga, N., Imamura, M., Takahashi, S., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047490 · Cited by 58
Dynamic organization and plasticity of sponge bodies
Snee, M. J., & Macdonald, P. M. (2009) · Developmental Dynamics · doi:10.1002/dvdy.21914 · Cited by 58
Dissecting miRNA facilitated physiology and function in human breast cancer for therapeutic intervention
Sengupta, D., Deb, M., Kar, S., Pradhan, N., Parbin, S., Kirtana, R., Singh, S. P., Suma, S. G., Niharika, N., Roy, A., et al. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.05.017 · Cited by 57
Andes Virus Regulation of Cellular MicroRNAs Contributes to Hantavirus-Induced Endothelial Cell Permeability
Pepini, T., Gorbunova, E. E., Gavrilovskaya, I. N., Mackow, J., & Mackow, E. R. (2010) · Journal of Virology · doi:10.1128/jvi.01658-10 · Cited by 57
Nup358 binds to AGO proteins through its SUMO‐interacting motifs and promotes the association of target mRNA with miRISC
Sahoo, M. R., Gaikwad, S., Khuperkar, D., Ashok, M., Helen, M., Yadav, S. K., Singh, A. P., Magre, I., Deshmukh, P., Dhanvijay, S., et al. (2016) · EMBO Reports · doi:10.15252/embr.201642386 · Cited by 57
Drosophila Genome-Wide RNAi Screen Identifies Multiple Regulators of HIF–Dependent Transcription in Hypoxia
Dekanty, A., Romero, N. M., Bertolin, A. P., Thomas, M. G., Leishman, C. C., Perez-Perri, J. I., Boccaccio, G. L., & Wappner, P. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000994 · Cited by 56
Genome-wide computational identification of WG/GW Argonaute-binding proteins in Arabidopsis
Karlowski, W. M., Zieleziński, A., Carrère, J., Pontier, D., Lagrange, T., & Cooke, R. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq162 · Cited by 57
Are the Ro RNP‐associated Y RNAs concealing microRNAs? Y RNA‐derived miRNAs may be involved in autoimmunity
Verhagen, A. P. M., & Pruijn, G. J. M. (2011) · BioEssays · doi:10.1002/bies.201100048 · Cited by 57
Protein Kinases Are Associated with Multiple, Distinct Cytoplasmic Granules in Quiescent Yeast Cells
Shah, K. H., Nostramo, R., Zhang, B., Varia, S. N., Klett, B. M., & Herman, P. K. (2014) · Genetics · doi:10.1534/genetics.114.172031 · Cited by 53
The C‐terminal α–α superhelix of Pat is required for mRNA decapping in metazoa
Braun, J. E., Tritschler, F., Haas, G., Igreja, C., Truffault, V., Weichenrieder, O., & Izaurralde, E. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.124 · Cited by 54
miRNA targeting and alternative splicing in the stress response – events hosted by membrane-less compartments
Kucherenko, M. M., & Shcherbata, H. R. (2018) · Journal of Cell Science · doi:10.1242/jcs.202002 · Cited by 55
Adaptable P body physical states differentially regulate bicoid mRNA storage during early Drosophila development
Sankaranarayanan, M., Emenecker, R. J., Wilby, E. L., Jahnel, M., Trussina, I. R. E. A., Wayland, M. T., Alberti, S., Holehouse, A. S., & Weil, T. T. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.09.021 · Cited by 55
Post-transcriptional regulation during stress
Hernández-Elvira, M., & Sunnerhagen, P. (2022) · FEMS Yeast Research · doi:10.1093/femsyr/foac025 · Cited by 58
miR-192 Induces G2/M Growth Arrest in Aristolochic Acid Nephropathy
Jenkins, R. L., Davies, L. C., Taylor, P. R., Akiyama, H., Cumbes, B., Beltrami, C., Carrington, C., Phillips, A. O., Bowen, T., & Fraser, D. J. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.12.028 · Cited by 53
Structural and functional insights into eukaryotic mRNA decapping
Ling, S. H. M., Qamra, R., & Song, H. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.44 · Cited by 52
Functionally distinct roles for eEF2K in the control of ribosome availability and p-body abundance
Smith, P. R., Loerch, S., Kunder, N., Stanowick, A. D., Lou, T., & Campbell, Z. T. (2021) · Nature Communications · doi:10.1038/s41467-021-27160-4 · Cited by 57
Pat1 proteins: a life in translation, translation repression and mRNA decay
Marnef, A., & Standart, N. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381602 · Cited by 55
Dcp1-Bodies in Mouse Oocytes
Swetloff, A., Conne, B., Huarte, J., Pitetti, J.-L., Nef, S., & Vassalli, J. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-02-0123 · Cited by 56
MicroRNAs and Mesenchymal Stem Cells
Collino, F., Bruno, S., Deregibus, M. C., Tetta, C., & Camussi, G. (2011) · Vitamins and hormones · doi:10.1016/b978-0-12-386015-6.00033-0 · Cited by 52
iTRAQ-based quantitative proteomics reveals a ferroptosis-like programmed cell death in plants infected by a highly virulent tobacco mosaic virus mutant 24A+UPD
Macharia, M. W., Das, P. P., Naqvi, N. I., & Wong, S. (2020) · Phytopathology Research · doi:10.1186/s42483-019-0043-5 · Cited by 51
Quantitative reconstitution of yeast RNA processing bodies
Currie, S. L., Xing, W., Muhlrad, D., Decker, C. J., Parker, R., & Rosen, M. K. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214064120 · Cited by 51
MicroRNA: Mechanism of gene regulation and application to livestock1
McDaneld, T. G. (2008) · Journal of Animal Science · doi:10.2527/jas.2008-1303 · Cited by 50
Ethanol facilitates hepatitis C virus replication via up-regulation of GW182 and heat shock protein 90 in human hepatoma cells
Bukong, T. N., Hou, W., Kodys, K., & Szabó, G. (2012) · Hepatology · doi:10.1002/hep.26010 · Cited by 51
Plant RNA Regulatory Network and RNA Granules in Virus Infection
Mäkinen, K. M., Lõhmus, A., & Pollari, M. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.02093 · Cited by 49
Regulation and different functions of the animal microRNA‐induced silencing complex
Frédérick, P., & Simard, M. J. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1701 · Cited by 51
Coordinated Changes in mRNA Turnover, Translation, and RNA Processing Bodies in Bronchial Epithelial Cells following Inflammatory Stimulation
Zhai, Y., Zhong, Z., Chen, C. A., Xia, Z., Ling, S., Blackburn, M. R., & Shyu, A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01237-08 · Cited by 53
Virus-induced translational arrest through 4EBP1/2-dependent decay of 5′-TOP mRNAs restricts viral infection
Hopkins, K. C., Tartell, M. A., Herrmann, C., Hackett, B. A., Taschuk, F., Panda, D., Menghani, S. V., Sabin, L. R., & Cherry, S. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1418805112 · Cited by 50
Genome-Wide Analysis of GLD-1–Mediated mRNA Regulation Suggests a Role in mRNA Storage
Scheckel, C., Gaidatzis, D., Wright, J. E., & Ciosk, R. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002742 · Cited by 50
Pat1 contributes to the RNA binding activity of the Lsm1-7–Pat1 complex
Chowdhury, A. K., Kalurupalle, S., & Tharun, S. (2014) · RNA · doi:10.1261/rna.045252.114 · Cited by 50
Thinking about RNA? MicroRNAs in the brain
Barbato, C., Giorgi, C., Catalanotto, C., & Cogoni, C. (2008) · Mammalian Genome · doi:10.1007/s00335-008-9129-6 · Cited by 50
Canonical and Non-Canonical Barriers Facing AntimiR Cancer Therapeutics
Cheng, C., Saltzman, W. M., & Slack, F. J. (2013) · Current Medicinal Chemistry · doi:10.2174/0929867311320290004 · Cited by 49
TORC2 mediates the heat stress response in Drosophila by promoting the formation of stress granules
Jevtov, I., Zacharogianni, M., van Oorschot, M. M., van Zadelhoff, G., Aguilera-Gomez, A., Vuillez, I., Braakman, I., Hafen, E., Stocker, H., & Rabouille, C. (2015) · Journal of Cell Science · doi:10.1242/jcs.168724 · Cited by 49
Computational Model of MicroRNA Control of HIF-VEGF Pathway: Insights into the Pathophysiology of Ischemic Vascular Disease and Cancer
Zhao, C., & Popel, A. S. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004612 · Cited by 49
The Catalytic Activity of the Ubp3 Deubiquitinating Protease Is Required for Efficient Stress Granule Assembly in Saccharomyces cerevisiae
Nostramo, R., Varia, S. N., Zhang, B., Emerson, M. M., & Herman, P. K. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00609-15 · Cited by 49
Stress granules: regulators or by‐products?
Matějů, D., & Chao, J. (2021) · The FEBS Journal · doi:10.1111/febs.15821 · Cited by 41
The Stress Granule RNA-Binding Protein TIAR-1 Protects Female Germ Cells from Heat Shock inCaenorhabditis elegans
Huelgas‐Morales, G., Silva-García, C. G., Salinas, L. S., Greenstein, D., & Navarro, R. E. (2016) · G3 Genes Genomes Genetics · doi:10.1534/g3.115.026815 · Cited by 47
New epigenetic players in stroke pathogenesis: From non-coding RNAs to exosomal non-coding RNAs
Mahjoubin‐Tehran, M., Rezaei, S., Jesmani, A., Birang, N., Morshedi, K., Khanbabaei, H., Khan, H. Z., Piranviseh, A., Nejati, M., Aschner, M., et al. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111753 · Cited by 48
T-cell intracellular antigens in health and disease
Sánchez-Jiménez, C., & Izquierdo, J. M. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1053668 · Cited by 46
Posttranscriptional Modulation of Cytokine Production in T Cells for the Regulation of Excessive Inflammation by TFL
Minagawa, K., Wakahashi, K., Kawano, H., Nishikawa, S., Fukui, C., Kawano, Y., Asada, N., Sato, M. M., Sada, A., Katayama, Y., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1301619 · Cited by 45
K63-Ubiquitylation and TRAF6 Pathways Regulate Mammalian P-Body Formation and mRNA Decapping
Tenekeci, U., Poppe, M., Beuerlein, K., Buro, C., Müller, H., Weiser, H., Kettner-Buhrow, D., Porada, K., Newel, D., Xu, M., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.017 · Cited by 45
Maintenance of Proteostasis by P Body-Mediated Regulation of eIF4E Availability during Aging in Caenorhabditis elegans
Rieckher, M., Markaki, M., Princz, A., Schumacher, B., & Tavernarakis, N. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.09.009 · Cited by 46
The P-body component DECAPPING5 and the floral repressor SISTER OF FCA regulate FLOWERING LOCUS C transcription in Arabidopsis
Wang, W., Wang, C., Wang, Y., Ma, J., Wang, T., Tao, Z., Liu, P., Li, S., Hu, Y., Gu, A., et al. (2023) · The Plant Cell · doi:10.1093/plcell/koad151 · Cited by 47
The EDC4‐XRN1 interaction controls P‐body dynamics to link mRNA decapping with decay
Brothers, W. R., Ali, F. N., Kajjo, S., & Fabian, M. R. (2023) · The EMBO Journal · doi:10.15252/embj.2023113933 · Cited by 48
Small Interfering RNA-mediated Silencing Induces Target-dependent Assembly of GW/P Bodies
Lian, S., Fritzler, M. J., Katz, J., Hamazaki, T., Terada, N., Satoh, M., & Chan, E. K. L. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0070 · Cited by 45
Cytoplasmic mRNA turnover and ageing
Borbolis, F., & Syntichaki, P. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.09.006 · Cited by 39
P-body proteins regulate transcriptional rewiring to promote DNA replication stress resistance
Loll‐Krippleber, R., & Brown, G. W. (2017) · Nature Communications · doi:10.1038/s41467-017-00632-2 · Cited by 45
Dissecting the transcriptome in cardiovascular disease
Robinson, E. L., Baker, A. H., Brittan, M., McCracken, I. R., Condorelli, G., Emanueli, C., Srivastava, P. K., Gaetano, C., Thum, T., Vanhaverbeke, M., et al. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab117 · Cited by 43
Quantifying Argonaute Proteins In and Out of GW/P-Bodies: Implications in microRNA Activities
Leung, A. K. L., & Sharp, P. A. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5107-5_10 · Cited by 46
RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor
Marnef, A., Barbieri-Weill, D., & Standart, N. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-05-0415 · Cited by 42
The DEAD Box Helicase RDE-12 Promotes Amplification of RNAi in Cytoplasmic Foci in C. elegans
Yang, H., Vallandingham, J., Shiu, P. K., Li, H., Hunter, C. P., & Mak, H. Y. (2014) · Current Biology · doi:10.1016/j.cub.2014.01.008 · Cited by 42
MicroRNA-mediated target mRNA cleavage and 3′-uridylation in human cells
Xu, K., Lin, J., Zandi, R., Roth, J. A., & Ji, L. (2016) · Scientific Reports · doi:10.1038/srep30242 · Cited by 45
RNA Degradation in Neurodegenerative Disease
Weskamp, K., & Barmada, S. J. (2018) · Advances in neurobiology · doi:10.1007/978-3-319-89689-2_5 · Cited by 41
RNA helicase DDX6 and scaffold protein GW182 in P-bodies promote biogenesis of stress granules.
Majerciak, V., Zhou, T., Kruhlak, M., & Zheng, Z.-M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad585 · Cited by 34
The Me31B DEAD-Box Helicase Localizes to Postsynaptic Foci and Regulates Expression of a CaMKII Reporter mRNA in Dendrites of Drosophila Olfactory Projection Neurons
Hillebrand, J., Pan, K., Kokaram, A. C., Barbee, S. A., Parker, R., & Ramaswami, M. (2010) · Frontiers in Neural Circuits · doi:10.3389/fncir.2010.00121 · Cited by 41
Global Phosphoproteomics Identifies a Major Role for AKT and 14-3-3 in Regulating EDC3
Larance, M., Rowland, A. F., Hoehn, K. L., Humphreys, D. T., Preiß, T., Guilhaus, M., & James, D. E. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900435-mcp200 · Cited by 41
GW-Bodies and P-Bodies Constitute Two Separate Pools of Sequestered Non-Translating RNAs
Patel, P. H., Barbee, S. A., & Blankenship, J. T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0150291 · Cited by 41
Regulation of nonsense-mediated mRNA decay in neural development and disease
Lee, J. S., Yang, S., Sun, Y., & Guo, J. U. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab022 · Cited by 37
Stress granule and P-body clearance: Seeking coherence in acts of disappearance
Buchan, J. R. (2024) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2024.01.002 · Cited by 40
RNA: The Unsuspected Conductor in the Orchestra of Macromolecular Crowding
Zacco, E., Broglia, L., Kurihara, M., Monti, M. M., Gustincich, S., Pastore, A., Plath, K., Nagakawa, S., Cerase, A., de Groot, N. S., et al. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00575 · Cited by 41
mi RNA s and HIV : unforeseen determinants of host‐pathogen interaction
Swaminathan, S., Murray, D. D., & Kelleher, A. D. (2013) · Immunological Reviews · doi:10.1111/imr.12077 · Cited by 40
EDC3 phosphorylation regulates growth and invasion through controlling P-body formation and dynamics
Bearss, J. J., Padi, S. K. R., Singh, N., Cardó‐Vila, M., Song, J. H., Mouneimne, G., Fernandes, N., Li, Y., Harter, M. R., Gard, J. M. C., et al. (2021) · EMBO Reports · doi:10.15252/embr.202050835 · Cited by 39
Intracellular trafficking and dynamics of P bodies
Aizer, A., & Shav‐Tal, Y. (2008) · Prion · doi:10.4161/pri.2.4.7773 · Cited by 40
Translation regulation in response to stress
Williams, T. D., & Rousseau, A. (2024) · FEBS Journal · doi:10.1111/febs.17076 · Cited by 45
The RNA-binding Proteins FMR1, Rasputin and Caprin Act Together with the UBA Protein Lingerer to Restrict Tissue Growth in Drosophila melanogaster
Baumgartner, R., Stocker, H., & Hafen, E. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003598 · Cited by 39
Formation of GW/P bodies as marker for microRNA‐mediated regulation of innate immune signaling in THP‐1 cells
Pauley, K. M., Satoh, M., Pauley, B. A., Dominguez‐Gutierrez, P. R., Wallet, S. M., Holliday, L. S., Cha, S., Reeves, W. H., & Chan, E. K. L. (2009) · Immunology and Cell Biology · doi:10.1038/icb.2009.84 · Cited by 39
The role of microRNAs in HIV-1 pathogenesis and therapy
Swaminathan, S., Murray, D. D., & Kelleher, A. D. (2012) · AIDS · doi:10.1097/qad.0b013e328352adca · Cited by 39
The microRNA-argonaute complex: A platform for mRNA modulation
Hammell, C. M. (2008) · RNA Biology · doi:10.4161/rna.5.3.6570 · Cited by 38
The 5′–3′ exoribonuclease Pacman is required for normal male fertility and is dynamically localized in cytoplasmic particles in Drosophila testis cells
Zabolotskaya, M. V., Grima, D. P., Lin, M., Chou, T.-B., & Newbury, S. F. (2008) · Biochemical Journal · doi:10.1042/bj20071720 · Cited by 40
Biogenesis and function of endogenous and exogenous siRNAs
Snead, N. M., & Rossi, J. J. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.14 · Cited by 40
Phosphorylation of a Human Microprotein Promotes Dissociation of Biomolecular Condensates
Na, Z., Luo, Y., Cui, D. S., Khitun, A., Smelyansky, S. R., Loria, J. P., & Slavoff, S. A. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05386 · Cited by 36

Authors: Eulalio, A., Behm-Ansmant, I., Schweizer, D., & Izaurralde, E.
Affiliations: MPI for Developmental Biology, Spemannstrasse 35, D-72076 Tübingen, Germany
Max Planck Institute for Developmental Biology (DE)
Corresponding author: Izaurralde, Elisa
ORCID: Izaurralde, Elisa
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2007-06-01
Volume: 27
Issue: 11
Pages: 3970-3981
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.00128-07
PMC: PMC1900022
OpenAlex: W2101555571
Cited by: 710
References: 62
Citations by year: 2026: 18 · 2025: 20 · 2024: 25 · 2023: 26 · 2022: 34 · 2021: 33 · 2020: 30 · 2019: 26 · 2018: 31 · 2017: 29 · 2016: 30 · 2015: 32 · 2014: 40 · 2013: 45 · 2012: 58
FWCI: 22.81
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
Max Planck Institute for Plasma Physics (submittedVersion)
Funders: European Molecular Biology Organization
Max-Planck-Gesellschaft
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: P-bodies, RNA-mediated gene silencing, siRNA, microRNA, nonsense-mediated mRNA decay, mRNA degradation, post-transcriptional regulation, polysome association, mRNA decapping
MeSH terms: Animals, Drosophila melanogaster, Humans, Polyribosomes, Ribonucleoproteins, RNA, Messenger, Gene Silencing, RNA Stability, Cytoplasmic Structures, Drosophila Proteins, RNA, Small Interfering, MicroRNAs

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

P-Body Formation Is a Consequence, Not the Cause, of RNA-Mediated Gene Silencing

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks