From unwinding to clamping — the DEAD box RNA helicase family

Molecular mechanisms of translational control

Gebauer, F., & Hentze, M. W. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1488 · Cited by 991

The Transformation Suppressor Pdcd4 Is a Novel Eukaryotic Translation Initiation Factor 4A Binding Protein That Inhibits Translation

Yang, H.-S., Jansen, A. P., Komar, A. A., Zheng, X., Merrick, W. C., Costes, S., Lockett, S. J., Sonenberg, N., & Colburn, N. H. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.26-37.2003 · Cited by 494

PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains

Suzuki, C., Garces, R. G., Edmonds, K. A., Hiller, S., Hyberts, S. G., Marintchev, A., & Wagner, G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712235105 · Cited by 165

Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap‐complex function

von der Haar, T., & McCarthy, J. E. G. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03172.x · Cited by 137

A census of human RNA-binding proteins

Gerstberger, S., Hafner, M., & Tuschl, T. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3813 · Cited by 2,032

A brave new world of RNA-binding proteins

Hentze, M. W., Castello, A., Schwarzl, T., & Preiss, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,821

Combinatorial optimization of mRNA structure, stability, and translation for RNA-based therapeutics

Leppek, K., Byeon, G. W., Kladwang, W., Wayment-Steele, H. K., Kerr, C. H., Xu, A. F., Kim, D. S., Topkar, V. V., Choe, C., Rothschild, D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28776-w · Cited by 399

Combinatorial optimization of mRNA structure, stability, and translation for RNA-based therapeutics

Leppek, K., Byeon, G. W., Kladwang, W., Wayment-Steele, H. K., Kerr, C. H., Xu, A. F., Kim, D. S., Topkar, V. V., Choe, C., Rothschild, D., et al. (2021) · doi:10.1101/2021.03.29.437587 · Cited by 399

G4C2 Repeat RNA Initiates a POM121-Mediated Reduction in Specific Nucleoporins in C9orf72 ALS/FTD

Coyne, A. N., Zaepfel, B. L., Hayes, L., Fitchman, B., Salzberg, Y., Luo, E.-C., Bowen, K., Trost, H., Aigner, S., Rigo, F., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.027 · Cited by 156

CRISPR-Cas9 Screens Identify the RNA Helicase DDX3X as a Repressor of C9ORF72 (GGGGCC)n Repeat-Associated Non-AUG Translation

Cheng, W., Wang, S., Zhang, Z., Morgens, D. W., Hayes, L. R., Lee, S., Portz, B., Xie, Y., Nguyen, B. V., Haney, M. S., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.09.003 · Cited by 138

eIF4A2 drives repression of translation at initiation by Ccr4-Not through purine-rich motifs in the 5′UTR

Wilczynska, A., Gillen, S. L., Schmidt, T., Meijer, H. A., Jukes-Jones, R., Langlais, C., Kopra, K., Lu, W.-T., Godfrey, J. D., Hawley, B. R., et al. (2019) · Genome Biology · doi:10.1186/s13059-019-1857-2 · Cited by 62

Targeting eIF4A-Dependent Translation of KRAS Signaling Molecules

Singh, K., Lin, J., Lecomte, N., Mohan, P., Gokce, A., Sanghvi, V. R., Jiang, M., Grbovic-Huezo, O., Burčul, A., Stark, S. G., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-2929 · Cited by 39

CIKS/DDX3X Interaction Controls the Stability of the Zc3h12a mRNA Induced by IL-17

Somma, D., Mastrovito, P., Grieco, M., Lavorgna, A., Pignalosa, A., Formisano, L., Salzano, A. M., Scaloni, A., Pacifico, F., Siebenlist, U., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401589 · Cited by 36

Evolution of the Genetic Code by Incorporation of Amino Acids that Improved or Changed Protein Function

Francis, B. R. (2013) · Journal of Molecular Evolution · doi:10.1007/s00239-013-9567-y · Cited by 34

ReLo is a simple and rapid colocalization assay to identify and characterize direct protein–protein interactions

Salgania, H. K., Metz, J., & Jeske, M. (2024) · Nature Communications · doi:10.1038/s41467-024-47233-4 · Cited by 17

Extended DNA threading through a dual-engine motor module of the activating signal co-integrator 1 complex

Jia, J., Hilal, T., Bohnsack, K. E., Chernev, A., Tsao, N., Bethmann, J., Arumugam, A., Parmely, L., Holton, N., Loll, B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37528-3 · Cited by 12

Challenges in Therapeutically Targeting the RNA‐Recognition Motif

Schmeing, S., & Hart, P. '. (2024) · WIREs RNA · doi:10.1002/wrna.1877 · Cited by 11

Continuous millisecond conformational cycle of a DEAH box helicase reveals control of domain motions by atomic-scale transitions

Becker, R. A., & Hub, J. S. (2023) · Communications Biology · doi:10.1038/s42003-023-04751-z · Cited by 7

Short-range translocation by a restriction enzyme motor triggers diffusion along DNA

Göse, M., Magill, E. E., Hughes-Games, A., Shaw, S. J., Diffin, F. M., Rawson, T., Nagy, Z., Seidel, R., & Szczelkun, M. D. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01504-1 · Cited by 3

Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry

Yazaki, J., Yamanashi, T., Nemoto, S., Kobayashi, A., Han, Y.-W., Hasegawa, T., Iwase, A., Ishikawa, M., Konno, R., Imami, K., et al. (2024) · Biology Methods and Protocols · doi:10.1093/biomethods/bpae039 · Cited by 2

The SSU Processome Component Utp25p is a Pseudohelicase

Helwer, R., & Charette, J. M. (2022) · doi:10.1101/2022.07.08.499361 · Cited by 1

40S ribosomal subunits scan mRNA for the start codon by one-dimensional diffusion

Wakabayashi, H., Zhu, M., Grayhack, E. J., Mathews, D. H., & Ermolenko, D. N. (2025) · RNA · doi:10.1261/rna.080493.125