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

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

TurboID-based proximity labeling identifies novel germline proteins that maintain E granule integrity and small RNA homeostasis in C. elegans

Li, K., Feng, X., Wang, K., Huang, X., Liu, L., Yan, C., Huang, X., Zhu, C., Wen, Q., Guang, S., et al. (2025) · Science China Life Sciences · doi:10.1007/s11427-025-3025-6 · Cited by 7

Ribonucleoprotein Granules: Between Stress and Transposable Elements

Moon, S., & Namkoong, S. (2023) · Biomolecules · doi:10.3390/biom13071027 · Cited by 8

Relating the Biogenesis and Function of P Bodies in Drosophila to Human Disease

Wilby, E. L., & Weil, T. (2023) · Genes · doi:10.3390/genes14091675 · Cited by 6

MicroRNAs targeted mTOR as therapeutic agents to improve radiotherapy outcome

Taeb, S., Rostamzadeh, D., Amini, S. M., Rahmati, M., Eftekhari, M., Safari, A., & Najafi, M. (2024) · Cancer Cell International · doi:10.1186/s12935-024-03420-3 · Cited by 7

Functional Roles of microRNAs in Cancer: microRNomes and oncomiRs Connection

López‐Camarillo, C., Marchat, L. A., Aréchaga-Ocampo, E., Azuara-Liceaga, E. I., Pérez‐Plasencia, C., Fuentes‐Mera, L., Miguel, A., & Flores‐Pérez, A. (2013) · InTech eBooks · doi:10.5772/53981 · Cited by 7

The Inhibitory Effect of Apolipoprotein B mRNA-Editing Enzyme Catalytic Polypeptide-Like 3G (APOBEC3G) and Its Family Members on the Activity of Cellular MicroRNAs

Zhang, H. (2009) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-03103-8_5 · Cited by 7

Characterization and expression of DDX6 during gametogenesis in the Chinese mitten crab Eriocheir sinensis

Li, Q., Wang, Y. L., Xie, J., Sun, W.-J., Zhu, M. L., He, L., & Wang, Q. (2015) · Genetics and Molecular Research · doi:10.4238/2015.april.30.15 · Cited by 7

mRNPs: From informosomes to stress granules

Voronina, A. S., & Пшенникова, Е. С. (2010) · Molecular Biology · doi:10.1134/s0026893310040035 · Cited by 7

Micro RNAs in Cancer

Munker, R., & Călin, G. A. (2011) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0023161 · Cited by 7

HP-Bodies – Ancestral Condensates that Regulate RNA Turnover and Protein Translation in BacteriaPreprint

Guan, J., Hurto, R. L., Rai, A., Azaldegui, C. A., Ortiz‐Rodríguez, L. A., Biteen, J. S., Freddolino, L., & Jakob, U. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.06.636932 · Cited by 7

DDX6 undergoes phase separation to modulate metabolic plasticity and chemoresistance

Bi, H., Li, W., Ren, L., Zhang, H., Dong, L., Chan, A. W. H., Wang, X., Yang, L., Zhang, X., Xue, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66966-4 · Cited by 6

EDC-3 and EDC-4 regulate embryonic mRNA clearance and biomolecular condensate specialization

Vidya, E., Jami‐Alahmadi, Y., Mayank, A. K., Rizwan, J., Xu, J. M. S., Cheng, T., Leventis, R., Sonenberg, N., Wohlschlegel, J. A., Vera, M., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114781 · Cited by 6

Investigating the role of RNA-binding protein Ssd1 in aneuploidy tolerance through network analysis

Dutcher, H. A., & Gasch, A. P. (2024) · RNA · doi:10.1261/rna.080199.124 · Cited by 8

Expression of genome defence protein members in proliferating and quiescent rat male germ cells and the Nuage dynamics

Rocha-da-Silva, L., Armelin‐Correa, L., Cantão, I. H., Flister, V. J. F., Nunes, M., & Stumpp, T. (2019) · PLoS ONE · doi:10.1371/journal.pone.0217941 · Cited by 6

Translation Arrest: A Key Player in Plant Antiviral Response

Vermeulen, A., Takken, F. L. W., & Sánchez-Camargo, V. A. (2023) · Genes · doi:10.3390/genes14061293 · Cited by 9

TNF-α stimulation inhibits siRNA-mediated RNA interference through a mechanism involving poly-(A) tail stabilization

Mols, J., BERG, A., Otsuka, M., ZHENG, M., CHEN, J., & Han, J. (2008) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.03.007 · Cited by 6

siRNAs: The Hidden Face of the Small RNA World

Seitz, H. (2010) · Current Biology · doi:10.1016/j.cub.2009.12.027 · Cited by 6

MicroRNAs for the pediatric otolaryngologist

Strub, G. M., & Perkins, J. A. (2018) · International Journal of Pediatric Otorhinolaryngology · doi:10.1016/j.ijporl.2018.06.043 · Cited by 6

Role of DCP1-DCP2 complex regulated by viral and host microRNAs in DNA virus infection

Sun, Y., & Zhang, X. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.05.058 · Cited by 6

Drosophila Me31B is a Dual eIF4E-Interacting Protein

Layana, C., Vilardo, E. S., Corujo, G., Hernández, G., & Rivera-Pomar, R. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.167949 · Cited by 7

MICRORNAS IN THE DROSOPHILA EGG AND EARLY EMBRYO

Votruba, S. M. (2009) · TSpace (University of Toronto) · Cited by 6

Intracellular Compartmentalization: A Key Determinant of MicroRNA Functions

Nalavade, R., & Singh, M. (2023) · MicroRNA · doi:10.2174/2211536612666230330184006 · Cited by 6

Temperature-Dependent Coarse-Grained Model for Simulations of Intrinsically Disordered Protein LCST and UCST Liquid–Liquid Phase Separations

Jiang, Y., & Ha‐Duong, T. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c00212 · Cited by 6

High-throughput Methods for Dissection of Trypanosome Gene Regulatory Networks

Erben, E. (2017) · Current Genomics · doi:10.2174/1389202918666170815125336 · Cited by 4

Untangling P-Bodies: Dissecting the Complex Web of Interactions that Enable Tiered Control of Gene Expression

Kershaw, C. J., & Ashe, M. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.032 · Cited by 5

Can Dietary Actives Affect miRNAs and Alter the Course or Prevent Colorectal Cancer?

Prendecka, M., Pigoń-Zając, D., Sondej, D., Grzywna, K., Kamińska, K., Szuta, M., & Malecka-Massalska, T. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210142 · Cited by 6

Involvement of RNA granule proteins in meiotic silencing by unpaired DNA

Xiao, H., Vierling, M. M., Kennedy, R. F., Boone, E. C., Decker, L. M., Sy, V. T., Haynes, J. B., Williams, M. A., & Shiu, P. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkab179 · Cited by 5

Overview on miRNA classification, biogenesis, and functions

O’Brien, J. A., Nguyen, V. H. L., & Peng, C. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822287-4.00027-x · Cited by 6

Looking for the functions of RNA granules in ALK-transformed cells

Fawal, M.-A., Espinos, E., Jean‐Jean, O., & Morello, D. (2011) · BioArchitecture · doi:10.4161/bioa.1.2.16269 · Cited by 5

Exploring the Role of the Processing Body in Plant Abiotic Stress Response

Huang, Z., Xu, Z. F., Liu, X., Chen, G., Hu, C., Chen, M., & Liu, Y. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46090585 · Cited by 4

Stress, membraneless organelles, and liquid–liquid phase separation

Riggs, C. L., & Ivanov, P. V. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00026-9 · Cited by 4

Continuous Density Gradients to Study Argonaute and GW182 Complexes Associated with the Endocytic Pathway

Gibbings, D. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-046-1_5 · Cited by 4

The Challenges and Current Advances in Delivering RNAi as Therapeutics

Kwok, A. (2013) · RNA technologies · doi:10.1007/978-3-642-36853-0_8 · Cited by 4

RNA Processing During Early Embryogenesis: Managing Storage, Utilisation and Destruction

Macaulay, A. D., Scantland, S., & Robert, C. (2011) · InTech eBooks · doi:10.5772/20375 · Cited by 4

Ribonucleoprotein Foci in Eukaryotes: How to Translate the Silence

Layana, C., Corujo, G., & Rivera-Pomar, R. V. (2016) · Springer eBooks · doi:10.1007/978-3-319-39468-8_19 · Cited by 3

Heat Shock-Induced Transcriptional and Translational Arrest in Mammalian Cells

Goenka, A., Parihar, R., & Ganesh, S. (2018) · Heat shock proteins · doi:10.1007/978-3-319-90725-3_12 · Cited by 4

Short interfering RNA induced generation and translation of stable 5′ mRNA cleavage intermediates

Singhania, R., Pavey, S. J., Payne, E., Gu, W., Clancy, J., Jubair, L., Preiß, T., Saunders, N. A., & McMillan, N. A. J. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.06.005 · Cited by 4

mRNA Degradation and Decay

Fromont‐Racine, M., & Saveanu, C. (2014) · Springer eBooks · doi:10.1007/978-3-319-05687-6_7 · Cited by 4

Coordinate transcriptional and post-transcriptional repression of pro-differentiation genes maintains intestinal stem cell identityPreprint

Buddika, K., Huang, Y., Ariyapala, I. S., Butrum-Griffith, A. N., Norrell, S. A., O’Connor, A. M., Patel, V. K., Rector, S. A., Slovan, M., Sokolowski, M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.27.175398 · Cited by 4

TIRR regulates mRNA export and association with P-bodies in response to DNA damage

Glossop, M. S., Chelysheva, I., Ketley, R. F., Alagia, A., & Gullerová, M. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae688 · Cited by 3

Plant P-bodies in post-transcriptional control: Composition, dynamics, and context-dependent roles

Matinahmadi, A., Zayani, Z., Majewska, K., & Smoliński, D. (2026) · Plant Communications · doi:10.1016/j.xplc.2026.101787 · Cited by 4

Active regulation mechanisms of LLPS and MLOs biogenesis

Fernández-Álvarez, A. J., Thomas, M. G., Giudice, J., & Boccaccio, G. L. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00005-1 · Cited by 3

Translation initiation factor e IF 1 A rescues hygromycin B sensitivity caused by deleting the carboxy‐terminal tail in the GPN ‐loop GTP ase Npa3

Félix‐Pérez, T., Mora‐García, M., Rebolloso‐Gómez, Y., DelaGarza‐Varela, A., Castro‐Velázquez, G., Peña‐Gómez, S. G., Riego‐Ruiz, L. R., Sánchez‐Olea, R., & Calera, M. R. (2024) · FEBS Journal · doi:10.1111/febs.17106 · Cited by 3

Insights into the target-directed miRNA degradation mechanism in Drosophila ovarian cell culture

Akulenko, N. V., Mikhaleva, E. A., Марфина, С. В., Кутелев, И. А., Kornyakov, D., Bobrov, V., Artamonov, A., Arapidi, G. P., Shender, V. О., & Ryazansky, S. S. (2025) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2025.195092 · Cited by 3

Reflections on Ten Years of History of, and Future Prospects for, GW182 and GW/P Body Research

Chan, E. K. L., Yao, B., & Fritzler, M. J. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5107-5_15 · Cited by 3

Toward elucidating the functions of miRNAs in drought stress tolerance

Shi, B., & Hussain, S. S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817112-7.00012-2 · Cited by 3

RNAI AND THE INSECT IMMUNE SYSTEM

Reynolds, S. E., & Eleftherianos, I. (2008) · Elsevier eBooks · doi:10.1016/b978-012373976-6.50014-8 · Cited by 3

Expression of miRNA-Targeted and Not-Targeted Reporter Genes Shows Mutual Influence and Intercellular Specificity

Hudy, D., & Rzeszowska‐Wolny, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315059 · Cited by 3

The EDC4-XRN1 axis controls P-body dynamics to link mRNA decapping with decayPreprint

Brothers, W. R., Ali, F. N., Kajjo, S., & Fabian, M. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.06.531261 · Cited by 3

Oncogenic KRAS promotes pancreatic ductal adenocarcinoma (PDAC) through post-transcriptionally regulated KRAS-induced granules (KGs)Preprint

Bortoletto, A. S., Yang, Z., Cardenas, M. G., Wang, M.-T., McCormick, F. P., & Parchem, R. J. (2023) · Research Square · doi:10.21203/rs.3.rs-3064215/v1 · Cited by 3

tRNA synthetase activity is required for stress granule and P-body assemblyPreprint

Baymiller, M., Helton, N. S., Dodd, B. J. T., & Moon, S. L. (2026) · Genes & Development · doi:10.1101/gad.353535.125 · Cited by 5

Ddx61-enriched condensates refine heart regeneration programs

Pronobis, M. I., DeLuca, S., Lee, S., Garcia, L., Ou, J., Bursac, N., & Poss, K. D. (2025) · Nature Communications · doi:10.1038/s41467-025-64026-5 · Cited by 2

P-bodies act as dynamic control hubs for RNA processing and storage

Feng, M. W., Mossanen-Parsi, A., Stonys, V., Hubbard, S. J., Ashe, M., & Grant, C. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111273 · Cited by 3

Role of Assemblysomes in Cellular Stress Responses

Gombás, B. G., Németh‐Szatmári, O., Nagy‐Mikó, B., & Villányi, Z. (2025) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.70009 · Cited by 5

Drosophila Clu ribonucleoprotein particle dynamics rely on the availability of functional Clu and translating ribosomes

Hwang, H. J., Sheard, K. M., & Cox, R. T. (2025) · Journal of Cell Science · doi:10.1242/jcs.263730 · Cited by 2

Clu1/Clu form mitochondria-associated granules upon metabolic transitions and regulate mitochondrial protein translation via ribosome interactions

Miller‐Fleming, L., Au, W. H., Raik, L., Rebelo‐Guiomar, P., Schmitz, J., Cho, H. Y., Czako, A., & Whitworth, A. J. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011773 · Cited by 4

Trailer Hitch tunes condensate phase behavior and mRNA partitioning to regulate P-body homeostasis during Drosophila melanogaster oogenesis

Milano, S. N., Bayer, L. V., Ko, J. J., Posner, G. S., Casella, C. E., & Bratu, D. P. (2026) · RNA · doi:10.1261/rna.081011.126 · Cited by 2

RNAi and miRNA pathways in mammals I – molecular mechanisms

Svoboda, P. (2020) · Karolinum Press eBooks · doi:10.14712/9788024643724.3 · Cited by 2

Computational Framework for Analysis of Prey–Prey Associations in Interaction Proteomics Identifies Novel Human Protein–Protein Interactions and Networks

Saha, S., Dazard, J.-E., Xu, H., & Ewing, R. M. (2012) · Journal of Proteome Research · doi:10.1021/pr300227y · Cited by 2

mRNA Turnover in Trypanosomes

CLAYTON, C. E. (2011) · Nucleic acids and molecular biology · doi:10.1007/978-3-642-28687-2_4 · Cited by 2

An RNA granule for translation quality control in Saccharomyces cerevisiae

Dhaliwal, J. S., Panozzo, C., Bénard, L., & Zerges, W. (2022) · Journal of Cell Science · doi:10.1242/jcs.260388 · Cited by 4

Reversing Age-Related DNA Damage Through Engineered DNA Repair

Steer, C. J., & Kren, B. T. (2010) · Springer eBooks · doi:10.1007/978-90-481-3999-6_21 · Cited by 2

Alteration of MicroRNA Biogenesis Pathways in Cancers

Das, S., & Ghosal, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811022-5.00003-6 · Cited by 2

MicroRNAs in Cancer: From Diagnosis to Therapeutics

Shah, K., & Rawal, R. (2020) · Springer eBooks · doi:10.1007/978-981-15-1067-0_9 · Cited by 2

Pathophysiology of miR-146a in lung cancer. Prospects of rising of efficiency of targeted therapy

Иванович, В. В., Romashova, J. E., & Shabanov, P. D. (2021) · Reviews on Clinical Pharmacology and Drug Therapy · doi:10.17816/rcf194359-381 · Cited by 4

Gawky (GW) is the Drosophila melanogaster GW182 homologue.

Li, J., Hobman, T., & Simmonds, A. (2013) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-5107-5_8 · Cited by 3

MicroRNA: from fundamental research to their application

Shirina, T. V., Bobrovskaya, M. T., & Kozlov, E. A. (2007) · Biopolymers and Cell · doi:10.7124/bc.000781 · Cited by 2

Translation-dependent and independent mRNA decay occur through mutually exclusive pathways that are defined by ribosome density during T Cell activationPreprint

Mercier, B. C., Labaronne, E., Cluet, D., Bicknell, A. A., Corbin, A., Guiguettaz, L., Aubé, F., Modolo, L., Auboeuf, D., Moore, M. J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.16.341222 · Cited by 2

Mechanism of Repression by the Sequence-Specific mRNA-Binding Protein Vts1p

Bieman, M. A. (2014) · TSpace (University of Toronto) · Cited by 1

The role of ER exit sites in maintaining P-body organization and transmitting ER stress response during Drosophila melanogaster oogenesisPreprint

Milano, S. N., Bayer, L. V., Ko, J. J., Casella, C. E., & Bratu, D. P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.03.601952 · Cited by 2

Movements of HIV-1 genomic RNA-APOBEC3F complexes and PKR reveal cytoplasmic and nuclear PKR defenses and HIV-1 evasion strategies

Marin, M., Golem, S., Kozak, S. L., & Kabat, D. (2015) · Virus Research · doi:10.1016/j.virusres.2015.11.023 · Cited by 1

A Method for Rapid Inducible RNA Decay

Blake, L. A., Watkins, L., & Wu, B. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4176-7_13 · Cited by 1

Remodeling of Germ Cell mRNPs for Translational Control

Keiper, B. D., & Huggins, H. P. (2025) · Biology · doi:10.3390/biology14101430 · Cited by 1

DDX6 induces immunosuppression in cancer by disrupting structural stability of endogenous double-stranded RNAs

Ng, L., Tano, V., Pitcheshwar, P., Gan, W. L., Xie, J., Zhou, J., Chong, H. C., Chin, D., Ren, X., An, Ö., et al. (2026) · Science Immunology · doi:10.1126/sciimmunol.aea6909 · Cited by 1

MicroRNAs: A Potential Resource and Tool in Enhancing Plant Tolerance to Drought

Shi, B. (2016) · Springer eBooks · doi:10.1007/978-3-319-32423-4_8 · Cited by 1

The Challenges and Current Advances in Delivering RNAi as Therapeutics

Kwok, A. (2013) · Springer eBooks · doi:10.1007/978-3-662-45775-7_8 · Cited by 1

Drosophila and human Headcase define a new family of ribonucleotide granule proteins required for stress response

Ricolo, D., Casanova, J., & Giannios, P. (2025) · Science Advances · doi:10.1126/sciadv.ads2086 · Cited by 1

Imaging the cytoplasmic lives of single mRNAs.

Misiaszek, A., & Chao, J. A. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169513 · Cited by 1

RNA duplexes in transcriptional regulation

Swaminathan, S., Hood, C. L., Suzuki, K., & Kelleher, A. D. (2010) · BioMolecular Concepts · doi:10.1515/bmc.2010.021 · Cited by 1

In search of the transcriptional blueprints of a competent oocyte

Pasquariello, R., Bocchi, V. D., Brevini, T. A. L., & Gandolfi, F. (2016) · Animal Reproduction · doi:10.21451/1984-3143-ar894 · Cited by 1

microRNAs in Brain Endothelium and Inflammation

Roig-Carles, D., Cerutti, C., Lopez‐Ramirez, M. A., Wu, D., Male, D. K., de Vries, H. E., & Romero, I. A. (2017) · Springer eBooks · doi:10.1007/978-3-319-45514-3_7 · Cited by 1

Multiphase complex droplets

Spruijt, E. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00015-4 · Cited by 1

Harnessing RNAi to Silence Viral Gene Expression

Arbuthnot, P. B. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-410518-8.00002-8 · Cited by 1

The Interplay between Eukaryotic mRNA Degradation and Translation

Hu, W. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10057-4 · Cited by 1

MicroRNA Regulation in GW/P Body Cell Biology, Lipopolysaccharide Signaling, and Rheumatoid Arthritis

Pauley, K. M. (2008) · DigitalCommons-Cedarville (Cedarville University) · Cited by 1

Characterizing functional domains of the RNA helicase RHAU involved in subcellular localization and RNA interaction

Chalupníková, K. (2008) · edoc (University of Basel) · doi:10.5451/unibas-004702513 · Cited by 1

Proteomics of the endoplasmic reticulum to determine cellular organization and protein function

Jain, M. D. (2009) · doi:10.82308/15158 · Cited by 1

Anti-viral RNAi and its suppression in plants.

Ciomperlik, J. J. (2010) · OakTrust (Texas A&M University Libraries) · Cited by 1

New features of micro-RNA regulation of mRNA translation and stability revealed by expression of targeted or not targeted reporter genesPreprint

Hudy, D., & Rzeszowska‐Wolny, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.16.484663 · Cited by 1

A single pathogen-secreted protein reprograms plants for drought resiliencePreprint

Subieta, K., Weber, L., Lübbers, J.-N., Wiesotzki, K., Pierdzig, L., Thurow, C., Schmitz, J., Lipka, U., Heimel, K., Schmitt, K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.09.632073 · Cited by 1

P-body formation is required for yeast proliferation in the phyllospherePreprint

Sekioka, F., Shiraishi, K., Akagi, M., Habata, A., Arima, Y., Sakai, Y., & Yurimoto, H. (2025) · eLife · doi:10.7554/elife.109276.1 · Cited by 1

Probing microRNA Activity in vitro and inside Cells using Single Molecule Microscopy.

Pitchiaya, S. (2012) · Deep Blue (University of Michigan)

MiRNA profiling of tumor-derived exosomes

Vitrant, D. G. (2010) · D-Scholarship@Pitt (University of Pittsburgh)

microRNA Dysregulation in Psychiatric Disorders

Xu, B., Gogos, J. A., & Karayiorgou, M. (2009) · Research and perspectives in neurosciences · doi:10.1007/978-3-642-04298-0_11

Mechanism of cap-snatching in hantaviruses

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