Towards a molecular understanding of microRNA-mediated gene silencing

Most mammalian mRNAs are conserved targets of microRNAs

Friedman, R. C., Farh, K. K.-H., Burge, C. B., & Bartel, D. P. (2009) · Genome Research · doi:10.1101/gr.082701.108 · Cited by 8,462 · see citing works

Regulation of microRNA biogenesis

Ha, M., & Kim, V. N. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3838 · Cited by 5,462 · see citing works

Mammalian microRNAs predominantly act to decrease target mRNA levels

Guo, H., Ingolia, N. T., Weissman, J. S., & Bartel, D. P. (2010) · Nature · doi:10.1038/nature09267 · Cited by 3,886 · see citing works

The impact of microRNAs on protein output

Baek, D., Villén, J., Shin, C., Camargo, F. D., Gygi, S. P., & Bartel, D. P. (2008) · Nature · doi:10.1038/nature07242 · Cited by 3,592 · see citing works

Widespread changes in protein synthesis induced by microRNAs

Selbach, M., Schwanhäusser, B., Thierfelder, N., Fang, Z., Khanin, R., & Rajewsky, N. (2008) · Nature · doi:10.1038/nature07228 · Cited by 3,429 · see citing works

The mechanism of eukaryotic translation initiation and principles of its regulation

Jackson, R. J., Hellen, C. U. T., & Pestova, T. V. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2838 · Cited by 2,759 · see citing works

Gene silencing by microRNAs: contributions of translational repression and mRNA decay

Huntzinger, E., & Izaurralde, E. (2011) · Nature Reviews Genetics · doi:10.1038/nrg2936 · Cited by 2,339 · see citing works

A brain-specific microRNA regulates dendritic spine development

Schratt, G. M., Tuebing, F., Nigh, E. A., Kane, C. G., Sabatini, M. E., Kiebler, M., & Greenberg, M. E. (2006) · Nature · doi:10.1038/nature04367 · Cited by 1,786 · see citing works

Zebrafish MiR-430 Promotes Deadenylation and Clearance of Maternal mRNAs

Giraldez, A. J., Mishima, Y., Rihel, J., Grocock, R. J., Van Dongen, S., Inoue, K., Enright, A. J., & Schier, A. F. (2006) · Science · doi:10.1126/science.1122689 · Cited by 1,436 · 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

Regulation by let-7 and lin-4 miRNAs Results in Target mRNA Degradation

Bagga, S., Bracht, J. R., Hunter, S. E., Massirer, K. B., Holtz, J., Eachus, R., & Pasquinelli, A. E. (2005) · Cell · doi:10.1016/j.cell.2005.07.031 · Cited by 1,347 · see citing works

A Proteome-Scale Map of the Human Interactome Network

Rolland, T., Taşan, M., Charloteaux, B., Pevzner, S. J., Zhong, Q., Sahni, N., Yi, S. S., Lemmens, I. H., Fontanillo, C., Mosca, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.10.050 · Cited by 1,342 · see citing works

Diversifying microRNA sequence and function

Ameres, S. L., & Zamore, P. D. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3611 · Cited by 1,175 · see citing works

MicroRNAs direct rapid deadenylation of mRNA

Wu, L., Fan, J., & Belasco, J. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510928103 · Cited by 1,135 · see citing works

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 1,030 · see citing works

The mechanics of miRNA-mediated gene silencing: a look under the hood of miRISC

Fabian, M. R., & Sonenberg, N. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2296 · Cited by 1,021 · see citing works

miRNA-Mediated Gene Silencing by Translational Repression Followed by mRNA Deadenylation and Decay

Djuranović, S., Nahvi, A., & Green, R. (2012) · Science · doi:10.1126/science.1215691 · Cited by 866 · see citing works

Short RNAs Repress Translation after Initiation in Mammalian Cells

Petersen, C. P., Bordeleau, M.-È., Pelletier, J., & Sharp, P. A. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.031 · Cited by 755 · 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

Ribosome Profiling Shows That miR-430 Reduces Translation Before Causing mRNA Decay in Zebrafish

Bazzini, A. A., Lee, M. T., & Giraldez, A. J. (2012) · Science · doi:10.1126/science.1215704 · Cited by 709 · see citing works

The Crystal Structure of Human Argonaute2

Schirle, N. T., & MacRae, I. J. (2012) · Science · doi:10.1126/science.1221551 · Cited by 697 · 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

Poly(A)-tail profiling reveals an embryonic switch in translational control

Subtelny, A. O., Eichhorn, S. W., Chen, G. R., Sive, H., & Bartel, D. P. (2014) · Nature · doi:10.1038/nature13007 · Cited by 664 · see citing works

MicroRNAs control translation initiation by inhibiting eukaryotic initiation factor 4E/cap and poly(A) tail function

Humphreys, D. T., Westman, B. J., Martin, D. I. K., & Preiß, T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506482102 · Cited by 655 · see citing works

MicroRNA Inhibition of Translation Initiation in Vitro by Targeting the Cap-Binding Complex eIF4F

Mathonnet, G., Fabian, M., Svitkin, Y., Parsyan, A., Huck, L., Murata, T., Biffo, S., Merrick, W., Darżynkiewicz, E., Pillai, R., et al. (2007) · Science · doi:10.1126/science.1146067 · Cited by 636 · see citing works

The Structure of Human Argonaute-2 in Complex with miR-20a

Elkayam, E., Kuhn, C., Tocilj, A., Haase, A. D. D., Greene, E. M., Hannon, G. J., & Joshua‐Tor, L. (2012) · Cell · doi:10.1016/j.cell.2012.05.017 · Cited by 615 · see citing works

Structural basis for microRNA targeting

Schirle, N. T., Sheu‐Gruttadauria, J., & MacRae, I. J. (2014) · Science · doi:10.1126/science.1258040 · Cited by 563 · see citing works

Identification of Novel Argonaute-Associated Proteins

Meister, G., Landthaler, M., Peters, L., Chen, P., Urlaub, H., Lührmann, R., & Tuschl, T. (2005) · Current Biology · doi:10.1016/j.cub.2005.10.048 · Cited by 554 · see citing works

Translation Repression in Human Cells by MicroRNA-Induced Gene Silencing Requires RCK/p54

Chu, C., & Rana, T. M. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040210 · Cited by 521 · 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

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

mRNA Destabilization Is the Dominant Effect of Mammalian MicroRNAs by the Time Substantial Repression Ensues

Eichhorn, S. W., Guo, H., McGeary, S. E., Rodríguez‐Mias, R. A., Shin, C., Baek, D., Hsu, S., Ghoshal, K., Villén, J., & Bartel, D. P. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.028 · Cited by 491 · see citing works

Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover

Yamashita, A., Chang, T.-C., Yamashita, Y., Zhu, W., Zhong, Z., Chen, C. A., & Shyu, A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1016 · Cited by 472 · see citing works

TAIL-seq: Genome-wide Determination of Poly(A) Tail Length and 3′ End Modifications

Chang, H., Lim, J., Ha, M., & Kim, V. N. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.007 · Cited by 454 · see citing works

Deadenylation is a widespread effect of miRNA regulation

Eulálio, A., Huntzinger, E., Nishihara, T., Rehwinkel, J., Fauser, M., & Izaurralde, E. (2008) · RNA · doi:10.1261/rna.1399509 · Cited by 429 · see citing works

Concordant Regulation of Translation and mRNA Abundance for Hundreds of Targets of a Human microRNA

Hendrickson, D. G., Hogan, D. J., McCullough, H. L., Myers, J. W., Herschlag, D., Ferrell, J. E., & Brown, P. O. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000238 · Cited by 418 · see citing works

GW182 interaction with Argonaute is essential for miRNA-mediated translational repression and mRNA decay

Eulálio, A., Huntzinger, E., & Izaurralde, E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1405 · Cited by 414 · see citing works

Mammalian miRNA RISC Recruits CAF1 and PABP to Affect PABP-Dependent Deadenylation

Fabian, M. R., Mathonnet, G., Sundermeier, T. R., Mathys, H., Zipprich, J. T., Svitkin, Y. V., Rivas, F. V., Jínek, M., Wohlschlegel, J. A., Doudna, J. A., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.004 · Cited by 388 · see citing works

GW182 Proteins Directly Recruit Cytoplasmic Deadenylase Complexes to miRNA Targets

Braun, J. E., Huntzinger, E., Fauser, M., & Izaurralde, E. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.007 · Cited by 371 · see citing works

Reversible Inhibition of PSD-95 mRNA Translation by miR-125a, FMRP Phosphorylation, and mGluR Signaling

Muddashetty, R. S., Nalavadi, V. C., Gross, C., Yao, X., Xing, L., Laur, O., Warren, S. T., & Bassell, G. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.006 · Cited by 364 · see citing works

miRNA repression involves GW182-mediated recruitment of CCR4–NOT through conserved W-containing motifs

Chekulaeva, M., Mathys, H., Zipprich, J. T., Attig, J., Čolić, M., Parker, R., & Filipowicz, W. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2166 · Cited by 353 · see citing works

Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation

Thermann, R., & Hentze, M. (2007) · Nature · doi:10.1038/nature05878 · Cited by 345 · see citing works

Co-translational mRNA decay in Saccharomyces cerevisiae

Hu, W., Sweet, T. J., Chamnongpol, S., Baker, K. E., & Coller, J. M. (2009) · Nature · doi:10.1038/nature08265 · Cited by 334 · see citing works

miRNA-mediated deadenylation is orchestrated by GW182 through two conserved motifs that interact with CCR4–NOT

Fabian, M. R., Cieplak-Rotowska, M. K., Frank, F., Morita, M., Green, J., Srikumar, T., Nagar, B., Yamamoto, T. S., Raught, B., Duchaîne, T. F., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2149 · Cited by 329 · see citing works

Translational Repression and eIF4A2 Activity Are Critical for MicroRNA-Mediated Gene Regulation

Meijer, H. A., Kong, Y. W., Lu, W. T., Wilczynska, A., Spriggs, R. V., Robinson, S. W., Godfrey, J. D., Willis, A. E., & Bushell, M. (2013) · Science · doi:10.1126/science.1231197 · Cited by 326 · see citing works

Reiterated WG/GW motifs form functionally and evolutionarily conserved ARGONAUTE-binding platforms in RNAi-related componentsPreprint

El‐Shami, M., Pontier, D., Lahmy, S., Braun, L., Picart, C., Véga, D., Hakimi, M., Jacobsen, S. E., Cooke, R., & Lagrange, T. (2007) · Genes & Development · doi:10.1101/gad.451207 · Cited by 321 · see citing works

Structural and Biochemical Insights to the Role of the CCR4-NOT Complex and DDX6 ATPase in MicroRNA Repression

Mathys, H., Basquin, J., Ozgur, S., Czarnocki‐Cieciura, M., Bonneau, F., Aartse, A., Dziembowski, A., Nowotny, M., Conti, E., & Filipowicz, W. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.036 · Cited by 308 · see citing works

Let-7 microRNA-mediated mRNA deadenylation and translational repression in a mammalian cell-free systemPreprint

Wakiyama, M., Takimoto, K., Ohara, O., & Yokoyama, S. (2007) · Genes & Development · doi:10.1101/gad.1566707 · Cited by 304 · see citing works

Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencingPreprint

Eulálio, A., Rehwinkel, J., Stricker, M., Huntzinger, E., Yang, S.-F., Doerks, T., Dorner, S., Peer Bork, B., Boutros, M., & Izaurralde, E. (2007) · Genes & Development · doi:10.1101/gad.443107 · Cited by 297 · see citing works

A DDX6-CNOT1 Complex and W-Binding Pockets in CNOT9 Reveal Direct Links between miRNA Target Recognition and Silencing

Chen, Y., Boland, A., Kuzuoğlu‐Öztürk, D., Bawankar, P., Loh, B., Chang, C.-T., Weichenrieder, O., & Izaurralde, E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.034 · Cited by 284 · see citing works

From guide to target: molecular insights into eukaryotic RNA-interference machinery

Ipsaro, J. J., & Joshua-Tor, L. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2931 · Cited by 281 · see citing works

Differential Regulation of Germline mRNAs in Soma and Germ Cells by Zebrafish miR-430

Mishima, Y., Giraldez, A. J., Takeda, Y., Fujiwara, T., Sakamoto, H., Schier, A. F., & Inoue, K. (2006) · Current Biology · doi:10.1016/j.cub.2006.08.086 · Cited by 276 · see citing works

RNA decay machines: Deadenylation by the Ccr4–Not and Pan2–Pan3 complexes

Wahle, E., & Winkler, G. S. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.01.003 · Cited by 247 · see citing works

A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain

Till, S., Lejeune, E., Thermann, R., Bortfeld‐Miller, M., Hothorn, M., Enderle, D., Heinrich, C., Hentze, M. W., & Ladurner, A. G. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1302 · Cited by 242 · see citing works

Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein–protein interactions

Schütz, P., Bumann, M., Oberholzer, A., Bieniossek, C., Trachsel, H., Altmann, M., & Baumann, U. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0800418105 · Cited by 239 · see citing works

Systematic Identification of C. elegans miRISC Proteins, miRNAs, and mRNA Targets by Their Interactions with GW182 Proteins AIN-1 and AIN-2

Zhang, L., Lei, D., Cheung, T. H., Dong, M., Chen, J., Sewell, A. K., Liu, X., Yates, J. R., & Han, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.014 · Cited by 238 · see citing works

Gene regulation. Structural basis for microRNA targeting.

Schirle, N. T., Sheu‐Gruttadauria, J., & MacRae, I. J. (2014) · Science · doi:10.2210/pdb4w5n/pdb · Cited by 227 · see citing works

Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells

Zheng, D., Ezzeddine, N., Chen, C. A., Zhu, W., He, X., & Shyu, A. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801196 · Cited by 227 · see citing works

The role of disordered protein regions in the assembly of decapping complexes and RNP granulesPreprint

Jonas, S., & Izaurralde, E. (2013) · Genes & Development · doi:10.1101/gad.227843.113 · Cited by 207 · see citing works

The GW182 protein family in animal cells: New insights into domains required for miRNA-mediated gene silencing

Eulálio, A., Tritschler, F., & Izaurralde, E. (2009) · RNA · doi:10.1261/rna.1703809 · Cited by 207 · see citing works

Kinetic analysis reveals successive steps leading to miRNA‐mediated silencing in mammalian cells

Béthune, J., Artus-Revel, C. G., & Filipowicz, W. (2012) · EMBO Reports · doi:10.1038/embor.2012.82 · Cited by 201 · see citing works

Ago–TNRC6 triggers microRNA-mediated decay by promoting two deadenylation steps

Chen, C. A., Zheng, D., Xia, Z., & Shyu, A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1709 · Cited by 194 · see citing works

Drosophila Argonaute1 and Argonaute2 Employ Distinct Mechanisms for Translational Repression

Iwasaki, S., Kawamata, T., & Tomari, Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.010 · Cited by 193 · see citing works

The Silencing Domain of GW182 Interacts with PABPC1 To Promote Translational Repression and Degradation of MicroRNA Targets and Is Required for Target Release

Zekri, L., Huntzinger, E., Heimstädt, S., & Izaurralde, E. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01081-09 · Cited by 186 · see citing works

A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5′ exonucleolytic degradation

Braun, J. E., Truffault, V., Boland, A., Huntzinger, E., Chang, C.-T., Haas, G., Weichenrieder, O., Coles, M. P., & Izaurralde, E. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2413 · Cited by 180 · see citing works

Architecture of the Nuclease Module of the Yeast Ccr4-Not Complex: the Not1-Caf1-Ccr4 Interaction

Basquin, J., Roudko, V., Rode, M., Minard‐Basquin, C., Séraphin, B., & Conti, E. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.014 · Cited by 162 · see citing works

Akt-Mediated Phosphorylation of Argonaute 2 Downregulates Cleavage and Upregulates Translational Repression of MicroRNA Targets

Horman, S. R., Janas, M. M., Litterst, C. M., Wang, B., MacRae, I. J., Sever, M. J., Morrissey, D. V., Graves, P. R., Luo, B., Umesalma, S., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.015 · Cited by 162 · see citing works

Structural Basis of Dcp2 Recognition and Activation by Dcp1

She, M., Decker, C. J., Svergun, D. I., Round, A. R., Chen, N., Muhlrad, D., Parker, R., & Song, H. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.01.002 · Cited by 153 · see citing works

The C-terminal domains of human TNRC6A, TNRC6B, and TNRC6C silence bound transcripts independently of Argonaute proteins

Lazzaretti, D., Tournier, I., & Izaurralde, E. (2009) · RNA · doi:10.1261/rna.1606309 · Cited by 153 · see citing works

The C-terminal half of human Ago2 binds to multiple GW-rich regions of GW182 and requires GW182 to mediate silencing

Lian, S. L., Li, S., Abadal, G. X., Pauley, B. A., Fritzler, M. J., & Chan, E. K. L. (2009) · RNA · doi:10.1261/rna.1229409 · Cited by 150 · see citing works

CCR4-NOT Deadenylates mRNA Associated with RNA-Induced Silencing Complexes in Human Cells

Piao, X., Zhang, X., Wu, L., & Belasco, J. G. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01481-09 · Cited by 144 · see citing works

The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4–NOT deadenylase complex

Petit, A., Wohlbold, L., Bawankar, P., Huntzinger, E., Schmidt, S., Izaurralde, E., & Weichenrieder, O. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks883 · Cited by 138 · see citing works

MicroRNAs Trigger Dissociation of eIF4AI and eIF4AII from Target mRNAs in Humans

Fukao, A., Mishima, Y., Takizawa, N., Oka, S., Imataka, H., Pelletier, J., Sonenberg, N., Thoma, C., & Fujiwara, T. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.005 · Cited by 137 · see citing works

Importance of the C-terminal domain of the human GW182 protein TNRC6C for translational repression

Zipprich, J. T., Bhattacharyya, S., Mathys, H., & Filipowicz, W. (2009) · RNA · doi:10.1261/rna.1448009 · Cited by 135 · see citing works

The structural basis of Edc3‐ and Scd6‐mediated activation of the Dcp1:Dcp2 mRNA decapping complex

Fromm, S. A., Truffault, V., Kamenz, J. L., Braun, J. E., Hoffmann, N. A., Izaurralde, E., & Sprangers, R. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.408 · Cited by 133 · see citing works

Human DDX6 effects miRNA-mediated gene silencing via direct binding to CNOT1

Rouya, C., Siddiqui, N., Morita, M., Duchaine, T., Fabian, M., & Sonenberg, N. (2014) · RNA: A publication of the RNA Society · doi:10.1261/rna.045302.114 · Cited by 133 · see citing works

Repression of C. elegans microRNA targets at the initiation level of translation requires GW182 proteins

Ding, X. C., & Großhans, H. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.275 · Cited by 131 · see citing works

Mammalian GW182 contains multiple Argonaute-binding sites and functions in microRNA-mediated translational repression

Takimoto, K., Wakiyama, M., & Yokoyama, S. (2009) · RNA · doi:10.1261/rna.1363109 · Cited by 130 · see citing works

A C-terminal silencing domain in GW182 is essential for miRNA function

Eulálio, A., Helms, S., Fritzsch, C., Fauser, M., & Izaurralde, E. (2009) · RNA · doi:10.1261/rna.1605509 · Cited by 130 · see citing works

Structural Basis for the Mutually Exclusive Anchoring of P Body Components EDC3 and Tral to the DEAD Box Protein DDX6/Me31B

Tritschler, F., Braun, J. E., Eulálio, A., Truffault, V., Izaurralde, E., & Weichenrieder, O. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.014 · Cited by 129 · see citing works

Translational Repression by Deadenylases

Cooke, A. M., Prigge, A. D., & Wickens, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.150763 · Cited by 125 · see citing works

GW182 proteins cause PABP dissociation from silenced miRNA targets in the absence of deadenylation

Zekri, L., Kuzuoğlu‐Öztürk, D., & Izaurralde, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.44 · Cited by 125 · see citing works

The Role of GW182 Proteins in miRNA-Mediated Gene Silencing

Braun, J. E., Huntzinger, E., & Izaurralde, E. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5107-5_9 · Cited by 124 · see citing works

MicroRNAs Block Assembly of eIF4F Translation Initiation Complex in Drosophila

Fukaya, T., Iwakawa, H., & Tomari, Y. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.004 · Cited by 120 · see citing works

Regulation of Poly(A)-binding Protein through PABP-interacting ProteinsPreprint

Derry, M. C., Yanagiya, A., Martineau, Y., & Sonenberg, N. (2006) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2006.71.061 · Cited by 120 · see citing works

The interactions of GW182 proteins with PABP and deadenylases are required for both translational repression and degradation of miRNA targets

Huntzinger, E., Kuzuoğlu‐Öztürk, D., Braun, J. E., Eulálio, A., Wohlbold, L., & Izaurralde, E. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1078 · Cited by 119 · see citing works

MicroRNAs Mediate Gene Silencing via Multiple Different Pathways in Drosophila

Fukaya, T., & Tomari, Y. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.024 · Cited by 116 · see citing works

Characterization of the miRNA-RISC loading complex and miRNA-RISC formed in the Drosophila miRNA pathway

Miyoshi, K., Okada, T. N., Siomi, H., & Siomi, M. C. (2009) · RNA · doi:10.1261/rna.1541209 · Cited by 115 · see citing works

Two PABPC1‐binding sites in GW182 proteins promote miRNA‐mediated gene silencing

Huntzinger, E., Braun, J. E., Heimstädt, S., Zekri, L., & Izaurralde, E. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.274 · Cited by 112 · see citing works

NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain

Bawankar, P., Loh, B., Wohlbold, L., Schmidt, S., & Izaurralde, E. (2013) · RNA Biology · doi:10.4161/rna.23018 · Cited by 109 · see citing works

Structural features of Argonaute–GW182 protein interactions

Pfaff, J., Hennig, J., Herzog, F., Aebersold, R. H., Sattler, M., Niessing, D., & Meister, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308510110 · Cited by 109 · see citing works

microRNA-Mediated Messenger RNA Deadenylation Contributes to Translational Repression in Mammalian Cells

Beilharz, T. H., Humphreys, D. T., Clancy, J. L., Thermann, R., Martin, D. I. K., Hentze, M. W., & Preiß, T. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006783 · Cited by 108 · see citing works

PABP and the poly(A) tail augment microRNA repression by facilitated miRISC binding

Moretti, F., Kaiser, C., Zdanowicz-Specht, A., & Hentze, M. W. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2309 · Cited by 107 · see citing works

Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation

Jínek, M., Fabian, M. R., Coyle, S. M., Sonenberg, N., & Doudna, J. A. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1768 · Cited by 106 · see citing works

Structure of the PAN3 Pseudokinase Reveals the Basis for Interactions with the PAN2 Deadenylase and the GW182 Proteins

Christie, M., Boland, A., Huntzinger, E., Weichenrieder, O., & Izaurralde, E. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.011 · Cited by 106 · see citing works

Structural Basis of Binding of P-body-associated Proteins GW182 and Ataxin-2 by the Mlle Domain of Poly(A)-binding Protein

Kozlov, G., Safaee, N., Rosenauer, A., & Gehring, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.089540 · Cited by 105 · see citing works

Pervasive and Cooperative Deadenylation of 3′UTRs by Embryonic MicroRNA Families

Wu, E., Thivierge, C., Flamand, M. N., Mathonnet, G., Vashisht, A. A., Wohlschlegel, J. A., Fabian, M. R., Sonenberg, N., & Duchaîne, T. F. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.003 · Cited by 99 · see citing works

Translational inhibition by deadenylation-independent mechanisms is central to microRNA-mediated silencing in zebrafish

Mishima, Y., Fukao, A., Kishimoto, T., Sakamoto, H., Fujiwara, T., & Inoue, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113350109 · Cited by 96 · see citing works

Poly(A) Nuclease Interacts with the C-terminal Domain of Polyadenylate-binding Protein Domain from Poly(A)-binding Protein

Siddiqui, N., Mangus, D. A., Chang, T.-C., Palermino, J.-M., Shyu, A. B., & Gehring, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701256200 · Cited by 96 · see citing works

Human 4E-T represses translation of bound mRNAs and enhances microRNA-mediated silencing

Kamenska, A., Lu, W.-T., Kubacka, D., Broomhead, H. E., Minshall, N., Bushell, M., & Standart, N. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1265 · Cited by 85 · see citing works

Drosophila miR2 Primarily Targets the m7GpppN Cap Structure for Translational Repression

Zdanowicz, A., Thermann, R., Kowalska, J., Jemielity, J., Duncan, K. E., Preiß, T., Darżynkiewicz, E., & Hentze, M. W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.009 · Cited by 79 · see citing works

miRNA repression of translation in vitro takes place during 43S ribosomal scanning

Ricci, E. P., Limousin, T., Soto‐Rifo, R., Rubilar, P. S., Décimo, D., & Ohlmann, T. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1076 · Cited by 72 · see citing works

Multiple independent domains of dGW182 function in miRNA-mediated repression in Drosophila

Chekulaeva, M., Filipowicz, W., & Parker, R. (2009) · RNA · doi:10.1261/rna.1364909 · Cited by 71 · see citing works

The DHH1/RCKp54 family of helicases: An ancient family of proteins that promote translational silencing

Presnyak, V., & Coller, J. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.03.006 · Cited by 70 · see citing works

Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation

Wolf, J., Valkov, E., Allen, M. D., Meineke, B., Gordiyenko, Y., McLaughlin, S. H., Olsen, T. M., Robinson, C. V., Bycroft, M., Stewart, M., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488373 · Cited by 70 · see citing works

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 · see citing works

Mammalian hyperplastic discs Homolog EDD Regulates miRNA-Mediated Gene Silencing

Su, H., Meng, S., Lu, Y., Trombly, M. I., Chen, J., Lin, C., Turk, A. A., & Wang, X. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.013 · Cited by 61 · see citing works

Poly(A)-binding protein modulates mRNA susceptibility to cap-dependent miRNA-mediated repression

Walters, R. W., Bradrick, S. S., & Gromeier, M. (2009) · RNA · doi:10.1261/rna.1795410 · Cited by 61 · see citing works

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 · see citing works

The structure of the Pan2–Pan3 core complex reveals cross-talk between deadenylase and pseudokinase

Schäfer, I. B., Rode, M., Bonneau, F., Schüssler, S., & Conti, E. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2834 · Cited by 55 · see citing works

The Caenorhabditis elegans GW182 protein AIN-1 interacts with PAB-1 and subunits of the PAN2-PAN3 and CCR4-NOT deadenylase complexes

Kuzuoğlu‐Öztürk, D., Huntzinger, E., Schmidt, S., & Izaurralde, E. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks218 · Cited by 55 · see citing works

The RNA helicase DDX6 regulates cell-fate specification in neural stem cells via miRNAs

Nicklas, S., Okawa, S., Hillje, A., González-Cano, L., del Sol, A., & Schwamborn, J. C. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv138 · Cited by 54 · see citing works

Functionally Diverse MicroRNA Effector Complexes Are Regulated by Extracellular Signaling

Wu, P., Isaji, M., & Carthew, R. W. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.023 · Cited by 52 · see citing works

An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay

Jonas, S., Christie, M., Peter, D., Bhandari, D., Loh, B., Huntzinger, E., Weichenrieder, O., & Izaurralde, E. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2837 · Cited by 51 · see citing works

MicroRNA Maturation and Human Disease

Hesse, M., & Arenz, C. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-703-7_2 · Cited by 40 · see citing works

eIF4GI Facilitates the MicroRNA-Mediated Gene Silencing

Ryu, I., Park, J. H., An, S., Kwon, O. S., & Jang, S. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055725 · Cited by 19 · see citing works

Overview of MicroRNA Biogenesis, Mechanisms of Actions, and Circulation

O'Brien, J., Hayder, H., Zayed, Y., & Peng, C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00402 · Cited by 5,287 · see citing works

Metazoan MicroRNAs

Bartel, D. P. (2018) · Cell · doi:10.1016/j.cell.2018.03.006 · Cited by 3,751 · see citing works

MicroRNA

Lu, T. X., & Rothenberg, M. E. (2018) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2017.08.034 · Cited by 2,425 · see citing works

Regulation of microRNA function in animals

Gebert, L. F. R., & MacRae, I. J. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0045-7 · Cited by 2,031 · see citing works

Non-coding RNA networks in cancer

Anastasiadou, E., Jacob, L. S., & Slack, F. J. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.99 · Cited by 1,901 · see citing works

The biochemical basis of microRNA targeting efficacy

(2019) · doi:10.1126/science.aav1741 · Cited by 1,570 · see citing works

Metabolism pathways of arachidonic acids: mechanisms and potential therapeutic targets

Wang, B., Wu, L., Chen, J., Dong, L., Chen, C., Zheng, W., Hu, J., Fleming, I., & Wang, D. W. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00443-w · Cited by 1,467 · see citing works

miRNAs as Biomarkers in Disease: Latest Findings Regarding Their Role in Diagnosis and Prognosis

Condrat, C. E., Thompson, D. C., Barbu, M. G., Bugnar, O. L., Boboc, A. E., Crețoiu, D., Suciu, N., Creţoiu, S. M., & Voinea, S. C. (2020) · Cells · doi:10.3390/cells9020276 · Cited by 1,357 · see citing works

Regulation of microRNA biogenesis and its crosstalk with other cellular pathways

Treiber, T., Treiber, N., & Meister, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0059-1 · Cited by 1,257 · see citing works

MicroRNA in Control of Gene Expression: An Overview of Nuclear Functions

Catalanotto, C., Cogoni, C., & Zardo, G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17101712 · Cited by 1,191 · see citing works

Reversible methylation of m6Am in the 5′ cap controls mRNA stability

Mauer, J., Luo, X., Blanjoie, A., Jiao, X., Grozhik, A. V., Patil, D. P., Linder, B., Pickering, B. F., Vasseur, J., Chen, Q., et al. (2016) · Nature · doi:10.1038/nature21022 · Cited by 1,072 · see citing works

Non-coding RNAs as drug targets

Matsui, M., & Corey, D. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.117 · Cited by 1,036 · see citing works

Non-coding RNAs: Classification, Biology and Functioning

Hombach, S., & Kretz, M. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-42059-2_1 · Cited by 959 · see citing works

Kidney fibrosis: from mechanisms to therapeutic medicines

Huang, R., Fu, P., & Ma, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01379-7 · Cited by 823 · see citing works

High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies

Youn, J., Dunham, W. H., Hong, S. J., Knight, J. D. R., Bashkurov, M., Chen, G. I., Bagci, H., Rathod, B., MacLeod, G. D. A. H., Eng, S. W. M., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2017.12.020 · Cited by 743 · see citing works

The Functions of MicroRNAs: mRNA Decay and Translational Repression

Iwakawa, H., & Tomari, Y. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.011 · Cited by 732 · see citing works

Rational Design of Immunomodulatory Hydrogels for Chronic Wound Healing

Kharaziha, M., Baidya, A., & Annabi, N. (2021) · Advanced Materials · doi:10.1002/adma.202100176 · Cited by 732 · see citing works

A network-biology perspective of microRNA function and dysfunction in cancer

Bracken, C. P., Scott, H. S., & Goodall, G. J. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.134 · Cited by 668 · see citing works

miRNA-based biomarkers, therapies, and resistance in Cancer

He, B., Zhao, Z., Cai, Q., Zhang, Y., Zhang, P., Shi, S., Xie, H., Peng, X., Yin, W., Tao, Y., et al. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.47203 · Cited by 632 · see citing works

A Network of Noncoding Regulatory RNAs Acts in the Mammalian Brain

Kleaveland, B., Shi, C. Y., Stefano, J., & Bartel, D. P. (2018) · Cell · doi:10.1016/j.cell.2018.05.022 · Cited by 594 · see citing works

Molecular mechanisms of transgenerational epigenetic inheritance

Fitz-James, M. H., & Cavalli, G. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-021-00438-5 · Cited by 589 · see citing works

mirDIP 4.1—integrative database of human microRNA target predictions

Tokár, T., Pastrello, C., Rossos, A. E. M., Abovsky, M., Hauschild, A.-C., Tsay, M. J., Lu, R., & Jurišica, I. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1144 · Cited by 568 · see citing works

Roles of mRNA poly(A) tails in regulation of eukaryotic gene expression

Passmore, L. A., & Coller, J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00417-y · Cited by 558 · see citing works

An integrated expression atlas of miRNAs and their promoters in human and mouse

The FANTOM Consortium, de Rie, D., Abugessaisa, I., Alam, T., Arner, E., Arner, P., Ashoor, H., Åström, G., Babina, M., Bertin, N., et al. (2017) · Nature Biotechnology · doi:10.1038/nbt.3947 · Cited by 561 · see citing works

A Uniform System for the Annotation of Vertebrate microRNA Genes and the Evolution of the Human microRNAome

Fromm, B., Billipp, T., Peck, L. E., Johansen, M., Tarver, J. E., King, B. L., Newcomb, J. M., Sempere, L. F., Flatmark, K., Hovig, E. J., et al. (2015) · Annual Review of Genetics · doi:10.1146/annurev-genet-120213-092023 · Cited by 525 · see citing works

Signaling pathways in rheumatoid arthritis: implications for targeted therapy

Ding, Q., Hu, W., Wang, R., Yang, Q., Zhu, M., Li, M., Cai, J., Rose, P., Mao, J., & Zhu, Y. Z. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01331-9 · Cited by 520 · see citing works

Life of RISC: Formation, action, and degradation of RNA-induced silencing complex

Iwakawa, H.-O., & Tomari, Y. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.11.026 · Cited by 488 · see citing works

The N 6 -Methyladenosine mRNA Methylase METTL3 Controls Cardiac Homeostasis and Hypertrophy

Dorn, L. E., Lasman, L., Chen, J., Xu, X., Hund, T. J., Medvedovic, M., Hanna, J. H., van Berlo, J. H., & Accornero, F. (2019) · Circulation · doi:10.1161/circulationaha.118.036146 · Cited by 468 · see citing works

MicroRNAs in Cardiovascular Disease

Barwari, T., Joshi, A., & Mayr, M. (2016) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2016.09.945 · Cited by 447 · see citing works

Non-coding RNAs in hepatocellular carcinoma: molecular functions and pathological implications

Wong, C., Tsang, F. H., & Ng, I. O. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2017.169 · Cited by 426 · see citing works

tRNA fragments (tRFs) guide Ago to regulate gene expression post-transcriptionally in a Dicer-independent manner

Kuscu, C., Kumar, P., Kiran, M., Su, Z., Malik, A. A., & Dutta, A. (2018) · RNA · doi:10.1261/rna.066126.118 · Cited by 412 · see citing works

Epigenetic regulation in the tumor microenvironment: molecular mechanisms and therapeutic targets

Yang, J., Xu, J., Wang, W. T., Zhang, B., Yu, X., & Shi, S. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01480-x · Cited by 404 · see citing works

MicroRNAs: From Mechanism to Organism

Dexheimer, P. J., & Cochella, L. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00409 · Cited by 393 · see citing works

New frontiers in translational control of the cancer genome

Truitt, M. L., & Ruggero, D. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.27 · Cited by 378 · see citing works

Cardiac progenitor cell-derived exosomes prevent cardiomyocytes apoptosis through exosomal miR-21 by targeting PDCD4

Xiao, J., Pan, Y., Li, X. H., Yang, X. Y., Feng, Y. L., Tan, H. H., Jiang, L., Feng, J., & Yu, X. Y. (2016) · Cell Death & Disease · doi:10.1038/cddis.2016.181 · Cited by 373 · see citing works

Epigenetics in hepatocellular carcinoma

Nagaraju, G. P., Dariya, B., Kasa, P., Peela, S., & El‐Rayes, B. F. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.07.017 · Cited by 346 · see citing works

Evolution and Biological Roles of Alternative 3′UTRs

Mayr, C. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.012 · Cited by 329 · see citing works

The pro-metastasis effect of circANKS1B in breast cancer

Zeng, K., He, B., Yang, B. B., Xu, T., Chen, X., Xu, M., Liu, X., Sun, H., Pan, Y., & Wang, S. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0914-x · Cited by 319 · see citing works

The emerging role of epigenetics in human autoimmune disorders

Mazzone, R., Zwergel, C., Artico, M., Taurone, S., Ralli, M., Greco, A., & Mai, A. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0632-2 · Cited by 318 · see citing works

Translational Control in CancerPreprint

Robichaud, N., Sonenberg, N., Ruggero, D., & Schneider, R. J. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032896 · Cited by 309 · see citing works

Erratum: New frontiers in translational control of the cancer genome

Truitt, M., & Ruggero, D. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.30 · Cited by 306 · see citing works

A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis

Treiber, T., Treiber, N., Plessmann, U., Harlander, S., Daiß, J. L., Eichner, N., Lehmann, G. J., Schall, K., Urlaub, H., & Meister, G. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.03.014 · Cited by 296 · see citing works

Codon Usage and 3′ UTR Length Determine Maternal mRNA Stability in Zebrafish

Mishima, Y., & Tomari, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.027 · Cited by 295 · see citing works

circHIPK3 regulates cell proliferation and migration by sponging miR-124 and regulating AQP3 expression in hepatocellular carcinoma

Chen, G., Shi, Y., Liu, M., & Sun, J. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0204-3 · Cited by 291 · see citing works

The multiple functions of RNA helicases as drivers and regulators of gene expression

Bourgeois, C. F., Mortreux, F., & Auboeuf, D. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.50 · Cited by 284 · see citing works

microRNAs Biogenesis, Functions and Role in Tumor Angiogenesis

Annese, T., Tamma, R., Giorgis, M. D., & Ribatti, D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.581007 · Cited by 294 · see citing works

Short poly(A) tails are a conserved feature of highly expressed genes

Lima, S. A., Chipman, L. B., Nicholson, A. L., Chen, Y.-H., Yee, B. A., Yeo, G. W.-M., Coller, J., & Pasquinelli, A. E. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3499 · Cited by 282 · see citing works

Anti-miRNA oligonucleotides: A comprehensive guide for design

Lima, J., Cerqueira, L., Figueiredo, C., Oliveíra, C., & Azevedo, N. F. (2018) · RNA Biology · doi:10.1080/15476286.2018.1445959 · Cited by 278 · see citing works

Intracellular and extracellular microRNA: An update on localization and biological role

Makarova, J. A., Shkurnikov, M. Y., Wicklein, D., Lange, T., Samatov, T. R., Turchinovich, A. A., & Tonevitsky, A. (2016) · Progress in Histochemistry and Cytochemistry · doi:10.1016/j.proghi.2016.06.001 · Cited by 260 · see citing works

Phase Transitions in the Assembly and Function of Human miRISC

Sheu‐Gruttadauria, J., & MacRae, I. J. (2018) · Cell · doi:10.1016/j.cell.2018.02.051 · Cited by 258 · see citing works

An Argonaute phosphorylation cycle promotes microRNA-mediated silencing

Golden, R. J., Chen, B., Li, T., Braun, J., Manjunath, H., Chen, X., Wu, J., Schmid, V., Chang, T.-C., Kopp, F. B., et al. (2017) · Nature · doi:10.1038/nature21025 · Cited by 259 · see citing works

The clinical potential of circulating microRNAs in obesity

Ji, C., & Guo, X. (2019) · Nature Reviews Endocrinology · doi:10.1038/s41574-019-0260-0 · Cited by 260 · see citing works

The Role of Exosomes and Exosomal MicroRNA in Cardiovascular Disease

Zheng, D., Huo, M., Li, B., Wang, W., Piao, H., Wang, Y., Zhu, Z., Li, D., Wang, T., & Liu, K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.616161 · Cited by 251 · see citing works

miRPathDB 2.0: a novel release of the miRNA Pathway Dictionary Database

Kehl, T., Kern, F., Backes, C., Fehlmann, T., Stöckel, D., Meese, E. U., Lenhof, H., & Keller, A. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1022 · Cited by 244 · see citing works

Multifaceted Role of Neuropilins in the Immune System: Potential Targets for Immunotherapy

Roy, S., Bag, A. K., Singh, R. K., Talmadge, J. E., Batra, S. K., & Datta, K. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01228 · Cited by 237 · see citing works

miRNA Targets: From Prediction Tools to Experimental Validation

Riolo, G., Cantara, S., Marzocchi, C., & Ricci, C. (2020) · Methods and Protocols · doi:10.3390/mps4010001 · Cited by 242 · see citing works

Circulating myocardial microRNAs from infarcted hearts are carried in exosomes and mobilise bone marrow progenitor cells

Cheng, M., Yang, J., Zhao, X., Zhang, E., Zeng, Q., Yu, Y., Liu, Y., Wu, B., Yi, G., Mao, X., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08895-7 · Cited by 240 · see citing works

The ZSWIM8 ubiquitin ligase mediates target-directed microRNA degradation

Shi, C. Y., Kingston, E. R., Kleaveland, B., Lin, D. H., Stubna, M. W., & Bartel, D. P. (2020) · Science · doi:10.1126/science.abc9359 · Cited by 239 · see citing works

Locked nucleic acid: modality, diversity, and drug discovery

Hagedorn, P., Persson, R., Funder, E. D., Albæk, N., Diemer, S. L., Hansen, D. J., Møller, M. R., Papargyri, N., Christiansen, H., Hansen, B. R., et al. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.09.018 · Cited by 237 · see citing works

Cardiac myocyte miR-29 promotes pathological remodeling of the heart by activating Wnt signaling

Sassi, Y., Avramopoulos, P., Ramanujam, D. P., Grüter, L., Werfel, S., Giosele, S., Brunner, A., Esfandyari, D., Papadopoulou, A. S., Strooper, B. D., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01737-4 · Cited by 240 · see citing works

microRNA strand selection: Unwinding the rules

Medley, J. C., Panzade, G., & Zinovyeva, A. Y. (2021) · WIREs RNA · doi:10.1002/wrna.1627 · Cited by 225 · see citing works

The Gene Ontology knowledgebase in 2026

G, S. A. J. P. S. J. M. D. M. P. N. A. B. C. C. E. F., Aleksander, S. A., Balhoff, J., Carbon, S., Cherry, J., Ebert, D., Feuermann, M., Gaudet, P., Harris, N., Hill, D. P., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1292 · Cited by 261 · see citing works

New Directions in Therapeutic Angiogenesis and Arteriogenesis in Peripheral Arterial Disease

Annex, B. H., & Cooke, J. P. (2021) · Circulation Research · doi:10.1161/circresaha.121.318266 · Cited by 203 · see citing works

The Dynamics of Cytoplasmic mRNA Metabolism

Eisen, T. J., Eichhorn, S. W., Subtelny, A. O., Lin, K. S., McGeary, S. E., Gupta, S., & Bartel, D. P. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.005 · Cited by 177 · see citing works

siRNA Specificity: RNAi Mechanisms and Strategies to Reduce Off-Target Effects

Neumeier, J., & Meister, G. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2020.526455 · Cited by 200 · see citing works

The microbiome regulates amygdala-dependent fear recall

Hoban, A. E., Stilling, R. M., Moloney, G., Shanahan, F., Dinan, T. G., Clarke, G., & Cryan, J. F. (2018) · Molecular Psychiatry · doi:10.1038/mp.2017.100 · Cited by 197 · see citing works

Split-BioID a conditional proteomics approach to monitor the composition of spatiotemporally defined protein complexes

Schopp, I. M., Ramirez, C. C. A., Debeljak, J., Kreibich, E., Skribbe, M., Wild, K., & Béthune, J. (2017) · Nature Communications · doi:10.1038/ncomms15690 · Cited by 189 · see citing works

Epigenetic effects of metformin: from molecular mechanisms to clinical implications

Bridgeman, S. C., Ellison, G. C., Melton, P. E., Newsholme, P., & Mamotte, C. D. S. (2018) · Diabetes, Obesity and Metabolism · doi:10.1111/dom.13262 · Cited by 190 · see citing works

MicroRNA Biomarkers and Platelet Reactivity

Sunderland, N. P., Skroblin, P., Barwari, T., Huntley, R. P., Lu, R., Joshi, A., Lovering, R. C., & Mayr, M. (2017) · Circulation Research · doi:10.1161/circresaha.116.309303 · Cited by 193 · see citing works

The p38 pathway, a major pleiotropic cascade that transduces stress and metastatic signals in endothelial cells

Corre, I., Paris, F., & Huot, J. (2017) · Oncotarget · doi:10.18632/oncotarget.18264 · Cited by 195 · see citing works

Extracellular superoxide dismutase and its role in cancer

Griess, B., Tom, E. C., Domann, F. E., & Teoh-Fitzgerald, M. L. T. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.013 · Cited by 195 · see citing works

Transfection of microRNA Mimics Should Be Used with Caution

Jin, H. Y., González-Martín, A., Miletic, A. V., Lai, M., Knight, S., Sabouri-Ghomi, M., Head, S. R., Macauley, M. S., Rickert, R. C., & Xiao, C. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00340 · Cited by 194 · see citing works

Classical and noncanonical functions of miRNAs in cancers

Dragomir, M. P., Knutsen, E., & Călin, G. A. (2021) · Trends in Genetics · doi:10.1016/j.tig.2021.10.002 · Cited by 194 · see citing works

Anatomy of RISC : how do small RNAs and chaperones activate Argonaute proteins?

Nakanishi, K. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1356 · Cited by 195 · see citing works

RNA-based recognition and targeting: sowing the seeds of specificity

Gorski, S. A., Vogel, J., & Doudna, J. A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.174 · Cited by 191 · see citing works

Silencio/CG9754 connects the Piwi-piRNA complex to the cellular heterochromatin machinery

Sienski, G., Batki, J., Senti, K.-A., Dönertas, D., Tirian, L., Meixner, K., & Brennecke, J. (2015) · Genes & Development · doi:10.1101/gad.271908.115 · Cited by 185 · see citing works

Browsing the oldest antioxidant enzyme: catalase and its multiple regulation in cancer

Galasso, M., Gambino, S., Romanelli, M. G., Donadelli, M., & Scupoli, M. T. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.06.010 · Cited by 184 · see citing works

Degradation dynamics of microRNAs revealed by a novel pulse-chase approachPreprint

Marzi, M. J., Ghini, F., Cerruti, B., de Pretis, S., Bonetti, P., Giacomelli, C., Gorski, M. M., Kress, T. R., Pelizzola, M., Müller, H., et al. (2016) · Genome Research · doi:10.1101/gr.198788.115 · Cited by 184 · see citing works

Noncoding RNAs regulate alternative splicing in Cancer

Liu, Y., Liu, X., Lin, C., Jia, X., Zhu, H., Song, J. H., & Zhang, Y. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01798-2 · Cited by 183 · see citing works

Epigenetic inactivation of the p53-induced long noncoding RNA TP53 target 1 in human cancer

Díaz‐Lagares, Á., Crujeiras, A. B., López-Serra, P., Soler, M., Setién, F., Goyal, A., Sandoval, J., Hashimoto, Y., Martínez‐Cardús, A., Gómez, A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608585113 · Cited by 180 · see citing works

TGF-β signaling alters H4K20me3 status via miR-29 and contributes to cellular senescence and cardiac aging

Lyu, G., Guan, Y., Zhang, C., Zong, L., Sun, L., Huang, X., Huang, L., Zhang, L., Tian, X., Zhou, Z., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04994-z · Cited by 176 · see citing works

The Role of microRNAs in Inflammation

Das, K., & Rao, L. V. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415479 · Cited by 177 · see citing works

A novel class of microRNA-recognition elements that function only within open reading frames

Zhang, K., Zhang, X., Cai, Z., Zhou, J., Cao, R., Zhao, Y., Chen, Z., Wang, D., Ruan, W., Zhao, Q. C., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0136-3 · Cited by 169 · see citing works

Mechanisms of the Epithelial–Mesenchymal Transition and Tumor Microenvironment in Helicobacter pylori-Induced Gastric Cancer

Baj, J., Korona‐Głowniak, I., Forma, A., Maani, A., Sitarz, R., Rahnama, M., Radzikowska, E., & Portincasa, P. (2020) · Cells · doi:10.3390/cells9041055 · Cited by 173 · see citing works

Biogenesis and mechanisms of microRNA‐mediated gene regulation

Rani, V., & Sengar, R. S. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28029 · Cited by 172 · see citing works

Current Advances in RNA Therapeutics for Human Diseases

Zogg, H., Singh, R., & Ro, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052736 · Cited by 173 · see citing works

The Clinical Application of MicroRNAs in Infectious Disease

Drury, R. E., O’Connor, D., & Pollard, A. J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01182 · Cited by 169 · see citing works

MicroRNA Expression Levels Are Altered in the Cerebrospinal Fluid of Patients with Young-Onset Alzheimer’s Disease

McKeever, P. M., Schneider, R., Taghdiri, F., Weichert, A., Multani, N., Brown, R. A., Boxer, A. L., Karydas, A., Miller, B. L., Robertson, J., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1032-x · Cited by 175 · see citing works

Modern plant biotechnology as a strategy in addressing climate change and attaining food security

Munaweera, T. I. K., Jayawardana, N. U., Rajaratnam, R., & Dissanayake, N. M. (2022) · Agriculture & Food Security · doi:10.1186/s40066-022-00369-2 · Cited by 182 · see citing works

circGSK3β promotes metastasis in esophageal squamous cell carcinoma by augmenting β-catenin signaling

Hu, X., Wu, D., He, X., Zhao, H., He, Z., Lin, J., Wang, K., Wang, W., Pan, Z., Lin, H., et al. (2019) · Molecular Cancer · doi:10.1186/s12943-019-1095-y · Cited by 169 · see citing works

Comprehensive Analysis of Human microRNA–mRNA Interactome

Plotnikova, O., Baranova, A., & Skoblov, M. (2019) · bioRxiv · doi:10.3389/fgene.2019.00933 · Cited by 130 · see citing works

Epigenetic Associations between lncRNA/circRNA and miRNA in Hepatocellular Carcinoma

Han, T., Hur, K., Cho, H., & Ban, H. S. (2020) · Cancers · doi:10.3390/cancers12092622 · Cited by 172 · see citing works

Signaling pathways in hepatocellular carcinoma

García‐Lezana, T., Lopez-Canovas, J. L., & Villanueva, A. (2020) · Advances in cancer research · doi:10.1016/bs.acr.2020.10.002 · Cited by 168 · see citing works

Structural Foundations of RNA Silencing by Argonaute

Sheu‐Gruttadauria, J., & MacRae, I. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.07.018 · Cited by 157 · see citing works

Extracellular miRNA: A Collision of Two Paradigms

Turchinovich, A. A., Tonevitsky, A., & Burwinkel, B. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.004 · Cited by 162 · see citing works

The roles of miRNAs as potential biomarkers in lung diseases

Alipoor, S. D., Adcock, I. M., Garssen, J., Mortaz, E., Varahram, M., Mirsaeidi, M. S., & Velayati, A. A. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.09.015 · Cited by 156 · see citing works

Evolution of RNA- and DNA-guided antivirus defense systems in prokaryotes and eukaryotes: common ancestry vs convergence

Koonin, E. V. (2017) · Biology Direct · doi:10.1186/s13062-017-0177-2 · Cited by 152 · see citing works

A microRNA signature from serum exosomes of patients with glioma as complementary diagnostic biomarker

Santangelo, A., Imbrucè, P., Gardenghi, B., Belli, L., Agushi, R., Tamanini, A., Munari, S., Bossi, A., Scambi, I., Benati, D., et al. (2017) · Journal of Neuro-Oncology · doi:10.1007/s11060-017-2639-x · Cited by 160 · see citing works

Magnaporthe oryzae Induces the Expression of a MicroRNA to Suppress the Immune Response in Rice

Zhang, X., Bao, Y., Shan, D., Wang, Z., Song, X., Wang, Z., Wang, J., He, L., Wu, L., Zhang, Z., et al. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.17.01665 · Cited by 158 · see citing works

Endogenous transcripts control miRNA levels and activity in mammalian cells by target-directed miRNA degradation

Ghini, F., Rubolino, C., Climent, M., Simeone, I., Marzi, M. J., & Nicassio, F. (2018) · Nature Communications · doi:10.1038/s41467-018-05182-9 · Cited by 154 · see citing works

This Week in Science

(2011) · Science · doi:10.1126/science.2011.331.6017.twis

Mechanistic Insights into MicroRNA-Mediated Gene SilencingPreprint

Duchaîne, T. F., & Fabian, M. R. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032771 · Cited by 146 · see citing works

miRNA-Mediated Gene Silencing by Translational Repression Followed by mRNA Deadenylation and Decay

Djuranović, S., Nahvi, A., & Green, R. (2012) · Science · doi:10.1126/science.1215691 · Cited by 866 · see citing works

Gene silencing by microRNAs: contributions of translational repression and mRNA decay

Huntzinger, E., & Izaurralde, E. (2011) · Nature Reviews Genetics · doi:10.1038/nrg2936 · Cited by 2,339 · see citing works

Kinetic analysis reveals successive steps leading to miRNA‐mediated silencing in mammalian cells

Béthune, J., Artus-Revel, C. G., & Filipowicz, W. (2012) · EMBO Reports · doi:10.1038/embor.2012.82 · Cited by 201 · see citing works