RNA‐binding proteins and post‐transcriptional gene regulation
Open accessAbstract
RNAs in cells are associated with RNA‐binding proteins (RBPs) to form ribonucleoprotein (RNP) complexes. The RBPs influence the structure and interactions of the RNAs and play critical roles in their biogenesis, stability, function, transport and cellular localization. Eukaryotic cells encode a large number of RBPs (thousands in vertebrates), each of which has unique RNA‐binding activity and protein–protein interaction characteristics. The remarkable diversity of RBPs, which appears to have increased during evolution in parallel to the increase in the number of introns, allows eukaryotic cells to utilize them in an enormous array of combinations giving rise to a unique RNP for each RNA. In this short review, we focus on the RBPs that interact with pre‐mRNAs and mRNAs and discuss their roles in the regulation of post‐transcriptional gene expression.
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
Cites
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?
RNA-binding proteins control many steps of co- and post-transcriptional gene expression, such as splicing, polyadenylation, capping, modification, export, localization, translation, and turnover.
“RNA-binding proteins (RBPs) regulate numerous aspects of co- and post-transcriptional gene expression, including RNA splicing, polyadenylation, capping, modification, export, localization, translation and turnover1,2.”
From A compendium of RNA-binding motifs for decoding gene regulation (2013) · cites this paper as [1]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Tuerk, C., & Gold, L. (1990) · Science · doi:10.1126/science.2200121 · Cited by 10,421 · see citing works
Conserved Structures and Diversity of Functions of RNA-Binding Proteins
Burd, C. G., & Dreyfuss, G. (1994) · Science · doi:10.1126/science.8036511 · Cited by 1,878 · see citing works
Self-citationGenome-Wide Survey of Human Alternative Pre-mRNA Splicing with Exon Junction Microarrays
Johnson, J. M., Castle, J. C., Garrett-Engele, P. W., Kan, Z., Loerch, P., Armour, C. D., Santos, R., Schadt, E. E., Stoughton, R. B., & Shoemaker, D. D. (2003) · Science · doi:10.1126/science.1090100 · Cited by 1,418 · see citing works
RNA-binding proteins: modular design for efficient function
Lunde, B. M., Moore, C. L., & Varani, G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2178 · Cited by 1,322 · see citing works
Maris, C., Dominguez, C., & Allain, F. H. ‐. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04653.x · Cited by 1,135 · see citing works
Demonstration That CFTR Is a Chloride Channel by Alteration of Its Anion Selectivity
Anderson, M. P., Gregory, R. J., Thompson, S., Souza, D. W., Paul, S., Mulligan, R. C., Smith, A. E., & Welsh, M. J. (1991) · Science · doi:10.1126/science.1712984 · Cited by 1,134 · see citing works
Brennan, C. M., & Steitz*, J. A. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000854 · Cited by 1,095 · see citing works
Regulation of cap-dependent translation by eIF4E inhibitory proteins
Richter, J. D., & Sonenberg, N. (2005) · Nature · doi:10.1038/nature03205 · Cited by 972 · see citing works
The spliceosome deposits multiple proteins 20–24 nucleotides upstream of mRNA exon–exon junctions
Hir, H. L., Izaurralde, E., Maquat, L. E., & Moore, M. J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.24.6860 · Cited by 970 · see citing works
Recruitment of human muscleblind proteins to (CUG)n expansions associated with myotonic dystrophy
Miller, J. W., Urbinati, C. R., Teng‐umnuay, P., Stenberg, M. G., Byrne, B. J., Thornton, C. A., & Swanson, M. S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4439 · Cited by 937 · see citing works
Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy
Brais, B., Bouchard, J.-P., Xie, Y., Rochefort, D. L., Chrétien, N., Tomé, F. M. S., Lafrentére, R. G., Rommens, J. M., Uyama, E., Nohira, O., et al. (1998) · Nature Genetics · doi:10.1038/ng0298-164 · Cited by 804 · see citing works
Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs
Matera, A. G., Terns, R. M., & Terns, M. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2124 · Cited by 752 · see citing works
RNA stabilization by the AU‐rich element binding protein, HuR, an ELAV protein
Peng, S., Chen, C. A., Xu, N., & Shyu, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3461 · Cited by 739 · see citing works
Spatial regulation of β-actin translation by Src-dependent phosphorylation of ZBP1
Hüttelmaier, S., Zenklusen, D., Lederer, M., Dictenberg, J., Lorenz, M., Meng, X.-H., Bassell, G., Condeelis, J., & Singer, R. (2005) · Nature · doi:10.1038/nature04115 · Cited by 681 · see citing works
Higuchi, M., Single, F. N., Köhler, M. G., Sommer, B., Sprengel, R., & SEEBURG, P. H. (1993) · Cell · doi:10.1016/0092-8674(93)90622-w · Cited by 662 · see citing works
Gerber, A. P., Herschlag, D., & Brown, P. O. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020079 · Cited by 651 · see citing works
The dsRNA protein kinase PKR: Virus and cell control
García, M. A., Meurs, E. F., & Esteban, M. (2007) · Biochimie · doi:10.1016/j.biochi.2007.03.001 · Cited by 644 · see citing works
CLIP: A method for identifying protein–RNA interaction sites in living cells
Ule, J., Jensen, K. B., Mele, A., & Darnell, R. B. (2005) · Methods · doi:10.1016/j.ymeth.2005.07.018 · Cited by 597 · see citing works
The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a
Guil, S., & Cáceres, J. F. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1250 · Cited by 567 · see citing works
Characterization of a β-Actin mRNA Zipcode-Binding Protein
Ross, A. F., Oleynikov, Y., Kislauskis, E., Taneja, K. L., & Singer, R. H. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.4.2158 · Cited by 563 · see citing works
TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus
Grüter, P., Tabernero, C., von Kobbe, C., Schmitt, C., Saavedra, C., Bachi, A., Wilm, M., Felber, B. K., & Izaurralde, E. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80065-9 · Cited by 560 · see citing works
Szabo, A., Dalmau, J., Manley, G., Rosenfeld, M., Wong, E., Henson, J., Posner, J. B., & Furneaux, H. M. (1991) · Cell · doi:10.1016/0092-8674(91)90184-z · Cited by 553 · see citing works
Comparative genomics and evolution of proteins involved in RNA metabolism
Anantharaman, V. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.7.1427 · Cited by 541 · see citing works
Richter, J. D. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.04.004 · Cited by 526 · see citing works
The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
Zhou, Z., Luo, M., Sträßer, K., Katahira, J., Hurt, E., & Reed, R. (2000) · Nature · doi:10.1038/35030160 · Cited by 517 · see citing works
Zhang, B., Gallegos, M. E., Puoti, A., Durkin, E., Fields, S., Kimble, J. E., & Wickens, M. (1997) · Nature · doi:10.1038/37297 · Cited by 510 · see citing works
A three-hybrid system to detect RNA-protein interactions in vivo.
SenGupta, D. J., Zhang, B., Kraemer, B. C., Pochart, P., Fields, S., & Wickens, M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8496 · Cited by 510 · see citing works
Liver Disintegration in the Mouse Embryo Caused by Deficiency in the RNA-editing Enzyme ADAR1
Hartner, J. C., Schmittwolf, C., Kispert, A., Müller, A. M., Higuchi, M., & Seeburg, P. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311347200 · Cited by 508 · see citing works
Stress-induced Apoptosis Associated with Null Mutation of ADAR1 RNA Editing Deaminase Gene
Wang, Q., Miyakoda, M., Yang, W., Khillan, J. S., Stachura, D. L., Weiss, M. J., & Nishikura, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310162200 · Cited by 501 · see citing works
Modular Recognition of RNA by a Human Pumilio-Homology Domain
Wang, X., McLachlan, J., Zamore, P. D., & Hall, T. M. T. (2002) · Cell · doi:10.1016/s0092-8674(02)00873-5 · Cited by 498 · see citing works
RNA-MEDIATED NEUROMUSCULAR DISORDERS
Ranum, L. P. W., & Cooper, T. A. (2006) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.113014 · Cited by 472 · see citing works
The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
Makeyev, A. V., & Liebhaber, S. A. (2002) · RNA · doi:10.1017/s1355838202024627 · Cited by 469 · see citing works
Davis, B. M., McCurrach, M. E., Taneja, K. L., Singer, R. H., & Housman, D. E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7388 · Cited by 468 · see citing works
Timchenko, L., Miller, J. W., Timchenko, N. A., DeVore, D. R., Datar, K. V., Lin, L., Roberts, R., Caskey, C. T., & Swanson, M. S. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.22.4407 · Cited by 465 · see citing works
Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease
Mandel, C. R., Kaneko, S., Zhang, H., Gebauer, D., Vethantham, V., Manley, J. L., & Tong, L. (2006) · Nature · doi:10.1038/nature05363 · Cited by 458 · see citing works
Hake, L. E., & Richter, J. D. (1994) · Cell · doi:10.1016/0092-8674(94)90547-9 · Cited by 454 · see citing works
Kuyumcu-Martinez, N. M., Wang, G., & Cooper, T. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.027 · Cited by 445 · see citing works
The Mex67p‐mediated nuclear mRNA export pathway is conserved from yeast to human
Katahira, J., Sträßer, K., Podtelejnikov, A. V., Mann, M., Jung, J. U., & Hurt, E. (1999) · The EMBO Journal · doi:10.1093/emboj/18.9.2593 · Cited by 441 · see citing works
Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA
Andersen, C. B. F., Ballut, L., Johansen, J., Chamieh, H., Nielsen, K. H., Oliveira, C. L. P., Pedersen, J. S., Séraphin, B., Hir, H. L., & Andersen, G. R. (2006) · Science · doi:10.1126/science.1131981 · Cited by 437 · see citing works
Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells
Lejeune, F., & Maquat, L. E. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.03.002 · Cited by 430 · see citing works
The Crystal Structure of the Exon Junction Complex Reveals How It Maintains a Stable Grip on mRNA
Bono, F., Ebert, J., Lorentzen, E., & Conti, E. (2006) · Cell · doi:10.1016/j.cell.2006.08.006 · Cited by 423 · see citing works
Reversible cross-linking combined with immunoprecipitation to study RNA–protein interactions in vivo
Niranjanakumari, S. (2002) · Methods · doi:10.1016/s1046-2023(02)00021-x · Cited by 410 · see citing works
Nott, A., Hir, H. L., & Moore, M. J. (2004) · Genes & Development · doi:10.1101/gad.1163204 · Cited by 408 · see citing works
Maskin Is a CPEB-Associated Factor that Transiently Interacts with eIF-4E
Stebbins-Boaz, B., Cao, Q., de Moor, C. D., Méndez, R., & Richter, J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80230-0 · Cited by 404 · see citing works
Stutz, F., Bachi, A., Doerks, T., Kos‐Braun, I. C., Séraphin, B., Wilm, M. S., Peer Bork, B., & Izaurralde, E. (2000) · RNA · doi:10.1017/s1355838200000078 · Cited by 382 · see citing works
Palladino, M. J., Keegan, L. P., O’Connell, M. A., & Reenan, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)00049-0 · Cited by 379 · see citing works
Nervous System Targets of RNA Editing Identified by Comparative Genomics
Hoopengardner, B., Bhalla, T., Staber, C., & Reenan, R. (2003) · Science · doi:10.1126/science.1086763 · Cited by 376 · see citing works
Ayala, Y. M., Pantano, S., D’Ambrogio, A., Buratti, E., Brindisi, A., Marchetti, C., Romano, M., & Baralle, F. E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.038 · Cited by 375 · see citing works
Jurica, M. S., Licklider, L. J., Gygi, S. P., Grigorieff, N., & Moore, M. J. (2002) · RNA · doi:10.1017/s1355838202021088 · Cited by 370 · see citing works
Mili, S., & STEITZ, J. A. (2004) · RNA · doi:10.1261/rna.7151404 · Cited by 369 · see citing works
Quality control of mRNA 3′-end processing is linked to the nuclear exosome
Hilleren, P. J., McCarthy, T., Rosbash, M., Parker, R., & Jensen, T. H. (2001) · Nature · doi:10.1038/35097110 · Cited by 364 · see citing works
An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay
Palacios, I. M., Gatfield, D., Johnston, D. S., & Izaurralde, E. (2004) · Nature · doi:10.1038/nature02351 · Cited by 362 · see citing works
Bobola, N., Jansen, R., Shin, T. H., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81048-x · Cited by 359 · see citing works
The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity
Ballut, L., Marchadier, B., Baguet, A., Tomasetto, C., Séraphin, B., & Hir, H. L. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb990 · Cited by 357 · see citing works
Symplekin and xGLD-2 Are Required for CPEB-Mediated Cytoplasmic Polyadenylation
Barnard, D. C., Ryan, K., Manley, J. L., & Richter, J. D. (2004) · Cell · doi:10.1016/j.cell.2004.10.029 · Cited by 334 · see citing works
Kataoka, N., Yong, J., Kim, V. N., Velázquez, F., Perkinson, R. A., Wang, F., & Dreyfuss, G. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00065-4 · Cited by 331 · see citing works
Self-citationHuR binding to cytoplasmic mRNA is perturbed by heat shock
Gallouzi, I., Brennan, C. M., Stenberg, M. G., Swanson, M. S., Eversole, A., Maizels, N., & STEITZ, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3073 · Cited by 326 · see citing works
Dreyfuss, G., Adam, S. A., & Choi, Y. D. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.3.415 · Cited by 326 · see citing works
Self-citationBuckanovich, R. J., Posner, J. B., & Darnell, R. B. (1993) · Neuron · doi:10.1016/0896-6273(93)90077-5 · Cited by 318 · see citing works
Opposing polymerase-deadenylase activities regulate cytoplasmic polyadenylation.
Kim, J. H., & Richter, J. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.08.016 · Cited by 305 · see citing works
Kim, V. N., Kataoka, N., & Dreyfuss, G. (2001) · Science · doi:10.1126/science.1062829 · Cited by 299 · see citing works
Self-citationWhy is Hu where? Shuttling of early-response-gene messenger RNA subsets
Keene, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.5 · Cited by 294 · see citing works
3′-End processing of pre-mRNA in eukaryotes
Wahle, E., & Rüegsegger, U. (1999) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1999.tb00400.x · Cited by 294 · see citing works
eIF4A3 is a novel component of the exon junction complex
CHAN, C. C., Dostie, J., Diem, M. D., Feng, W., Mann, M., Rappsilber, J., & Dreyfuss, G. (2004) · RNA · doi:10.1261/rna.5230104 · Cited by 292 · see citing works
Self-citationY14 and hUpf3b Form an NMD-Activating Complex
Gehring, N. H., Neu‐Yilik, G., Schell, T., Hentze, M. W., & Kulozik, A. E. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00142-4 · Cited by 291 · see citing works
Identification of alternative splicing regulators by RNA interference in Drosophila
Park, J. W., Parisky, K. M., Celotto, A. M., Reenan, R. A., & Graveley, B. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407004101 · Cited by 290 · see citing works
Arginine methylation facilitates the nuclear export of hnRNP proteinsPreprint
Shen, E. C., Henry, M. F., Weiss, V. H., Valentini, S. R., Silver, P. A., & Lee, M. S. (1998) · Genes & Development · doi:10.1101/gad.12.5.679 · Cited by 289 · see citing works
Editor meets silencer: crosstalk between RNA editing and RNA interference
Nishikura, K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2061 · Cited by 281 · see citing works
Shibuya, T., Tange, T. Ø., Sonenberg, N., & Moore, M. J. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb750 · Cited by 274 · see citing works
Nuclear mRNA Export Requires Complex Formation between Mex67p and Mtr2p at the Nuclear Pores
Santos-Rosa, H., Moreno, H., Simos, G., Segref, A., Fahrenkrog, B., Panté, N., & Hurt, E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6826 · Cited by 264 · see citing works
Miyamura, Y., Suzuki, T., Kono, M., Inagaki, K., Ito, S., Suzuki, N., & Tomita, Y. (2003) · The American Journal of Human Genetics · doi:10.1086/378209 · Cited by 259 · see citing works
REF proteins mediate the export of spliced and unspliced mRNAs from the nucleus
Rodrigues, J. P., Rode, M., Gatfield, D., Blencowe, B. J., Carmo‐Fonseca, M., & Izaurralde, E. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1030 · Cited by 250 · see citing works
Structure of Pumilio Reveals Similarity between RNA and Peptide Binding Motifs
Edwards, T. A., Pyle, S. E., Wharton, R. P., & Aggarwal, A. K. (2001) · Cell · doi:10.1016/s0092-8674(01)00318-x · Cited by 250 · see citing works
Crystal Structure of a Pumilio Homology Domain
Wang, X., Zamore, P. D., & Hall, T. M. T. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00229-5 · Cited by 248 · see citing works
Kataoka, N., Diem, M. D., Kim, V. N., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6424 · Cited by 242 · see citing works
Engineering RNA sequence specificity of Pumilio repeats
Cheong, C.-G., & Hall, T. M. T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606294103 · Cited by 232 · see citing works
Keene, J. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111145598 · Cited by 230 · see citing works
Real-Time Visualization of ZBP1 Association with β-Actin mRNA during Transcription and Localization
Oleynikov, Y., & Singer, R. H. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00044-7 · Cited by 229 · see citing works
Cao, Q., & Richter, J. D. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf353 · Cited by 219 · see citing works
PKR—A protein kinase regulated by double-stranded RNA
Clemens, M. J. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(96)00169-0 · Cited by 216 · see citing works
Translation Is Required to Remove Y14 from mRNAs in the Cytoplasm
Dostie, J., & Dreyfuss, G. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00902-8 · Cited by 215 · see citing works
Self-citationShe2p, a novel RNA‐binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p
Böhl, F., Kruse, C., Frank, A., Ferring, D., & Jansen, R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.20.5514 · Cited by 209 · see citing works
Leffers, H. C. B., Dejgaard, K., & Celis, J. E. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0447h.x · Cited by 205 · see citing works
Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies.
Dreyfuss, G., Choi, Y. D., & Adam, S. A. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.6.1104 · Cited by 204 · see citing works
Self-citationThe protein Mago provides a link between splicing and mRNA localization
Hir, H. L., Gatfield, D., Kos‐Braun, I. C., et al. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve245 · Cited by 204 · see citing works
An interaction between U2AF 65 and CF Im links the splicing and 3′ end processing machineries
Millevoi, S., Loulergue, C., Dettwiler, S., Karaa, Z. S., Keller, W., Antoniou, M. N., & Vagner, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601331 · Cited by 203 · see citing works
Kyburz, A., Friedlein, A., Langen, H., & Keller, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.037 · Cited by 198 · see citing works
Ferraiuolo, M. A., Lee, C., Ler, L. W., Hsu, J. L., Costa‐Mattioli, M., Luo, M., Reed, R., & Sonenberg, N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400933101 · Cited by 186 · see citing works
Evidence that polyadenylation factor CPSF-73 is the mRNA 3′ processing endonuclease
Ryan, K., Calvo, O., & Manley, J. L. (2004) · RNA · doi:10.1261/rna.5214404 · Cited by 183 · see citing works
The Y14 protein communicates to the cytoplasm the position of exon–exon junctions
Kim, V. N., Yong, J., Kataoka, N., Abel, L., Diem, M. D., & Dreyfuss, G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.2062 · Cited by 181 · see citing works
Self-citationmRNA polyadenylation and its coupling to other RNA processing reactions and to transcription
Minvielle-Sébastia, L., & Keller, W. D. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80049-0 · Cited by 178 · see citing works
A novel mode of RBD-protein recognition in the Y14–Mago complex
Fribourg, S., Gatfield, D., Izaurralde, E., & Conti, E. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb926 · Cited by 170 · see citing works
Specificity of RNA Binding by CPEB: Requirement for RNA Recognition Motifs and a Novel Zinc Finger
Hake, L. E., Méndez, R., & Richter, J. D. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.685 · Cited by 170 · see citing works
Bienroth, S., Wahle, E., Suter‐Crazzolara, C., & Keller, W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55058-4 · Cited by 168 · see citing works
ADAR Gene Family and A-to-I RNA Editing: Diverse Roles in Posttranscriptional Gene Regulation
Valente, L., & Nishikura, K. (2005) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(04)79006-6 · Cited by 168 · see citing works
Protein families and RNA recognition
Chen, Y., & Varani, G. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04650.x · Cited by 163 · see citing works
hnRNP A1 associates with telomere ends and stimulates telomerase activity
Zhang, Q., Manche, L., Xu, R.-M., & Krainer, A. R. (2006) · RNA · doi:10.1261/rna.58806 · Cited by 162 · see citing works
A structured retroviral RNA element that mediates nucleocytoplasmic export of intron-containing RNA
Ernst, R. K., Bray, M., Rekosh, D., & Hammarskjöld, M.-L. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.1.135 · Cited by 159 · see citing works
Smith, J. J., Rücknagel, K. P., Schierhorn, A., Tang, J., Németh, A., Linder, M., Herschman, H. R., & Wahle, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13229 · Cited by 146 · see citing works
The Drosophila melanogaster Genome
Lasko, P. F. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.2.f51 · Cited by 141 · see citing works
Structure of the Y14-Magoh Core of the Exon Junction Complex
Lau, C.-K., Diem, M. D., Dreyfuss, G., et al. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00328-2 · Cited by 139 · see citing works
Self-citationYu, M. C., Bachand, F., McBride, A. E., Komili, S., Casolari, J. M., & Silver, P. A. (2004) · Genes & Development · doi:10.1101/gad.1223204 · Cited by 133 · see citing works
Reichert, V. L., Hir, H. L., Jurica, M. S., & Moore, M. J. (2002) · Genes & Development · doi:10.1101/gad.1030602 · Cited by 131 · see citing works
Sarkissian, M., Méndez, R., & Richter, J. D. (2004) · Genes & Development · doi:10.1101/gad.1136004 · Cited by 130 · see citing works
Cross‐linking of mRNA to Proteins by Irradiation of Intact Cells with Ultraviolet Light
Wagenmakers, A. J. M., Reinders, R. J., & VENROOIJ, W. J. V. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb07207.x · Cited by 128 · see citing works
RNA localization in yeast: moving towards a mechanism
Gonsalvez, G. B., Urbinati, C. R., & Long, R. M. (2005) · Biology of the Cell · doi:10.1042/bc20040066 · Cited by 125 · see citing works
ATP-Dependent Recruitment of Export Factor Aly/REF onto Intronless mRNAs by RNA Helicase UAP56
Taniguchi, I., & Ohno, M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01341-07 · Cited by 121 · see citing works
Diem, M. D., Chan, C. C., Younis, I., et al. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1321 · Cited by 116 · see citing works
Degot, S., Hir, H. L., Alpy, F., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402754200 · Cited by 114 · see citing works
SUMO Modification of Heterogeneous Nuclear Ribonucleoproteins
Vassileva, M. T., & Matunis, M. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.9.3623-3632.2004 · Cited by 114 · see citing works
SEUNINGEN, I. V., Ostrowski, J., Bustelo, X. R., Sleath, P. R., & Bomsztyk, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26976 · Cited by 111 · see citing works
Dreyfuss, G., Adam, S. A., & Choi, Y. D. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.3.415-423.1984 · Cited by 110 · see citing works
Self-citationA single spacer nucleotide determines the specificities of two mRNA regulatory proteins
Opperman, L., Hook, B. A., DeFino, M. C., et al. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1010 · Cited by 104 · see citing works
Vertebrate GLD2 poly(A) polymerases in the germline and the brain
Rouhana, L., Wang, L., Buter, N., KWAK, J. E., Schiltz, C. A., González, T., Kelley, A. E., Landry, C. F., & Wickens, M. (2005) · RNA · doi:10.1261/rna.2630205 · Cited by 104 · see citing works
Rigo, F., & Martinson, H. G. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01410-07 · Cited by 100 · see citing works
Schullery, D. S., Ostrowski, J., Denisenko, O. N., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.15101 · Cited by 96 · see citing works
Dejgaard, K., Leffers, H. C. B., Rasmussen, H. H., et al. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1116 · Cited by 93 · see citing works
Characterization of Heterogeneous Nuclear RNA-Protein Complexes In Vivo with Monoclonal Antibodies
Dreyfuss, G., Choi, Y. D., & Adam, S. A. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.6.1104-1114.1984 · Cited by 88 · see citing works
Self-citationCrystal structure of theDrosophilaMago nashi–Y14 complexPreprint
Shi, H., & Xu, R.-M. (2003) · Genes & Development · doi:10.1101/gad.260403 · Cited by 84 · see citing works
Delineation of a Novel Pathway That Regulates CD154 (CD40 Ligand) Expression
Hamilton, B. J., Genin, A., Cron, R. Q., & Rigby, W. F. C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.23.2.510-525.2003 · Cited by 82 · see citing works
Mayrand, S. H., Setyono, B., Greenberg, J. R., & Pederson, T. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.90.2.380 · Cited by 75 · see citing works
Lee, M. H. (2006) · WormBook · doi:10.1895/wormbook.1.79.1 · Cited by 75 · see citing works
Nuclear ribonucleoprotein particles probed in living cells.
Mayrand, S. H., & Pederson, T. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.4.2208 · Cited by 74 · see citing works
Mootz, D. E., Ho, D. M., & Hunter, C. P. (2004) · Development · doi:10.1242/dev.01196 · Cited by 72 · see citing works
Decrease in hnRNP A/B expression during erythropoiesis mediates a pre‐mRNA splicing switch
Hou, V., Lersch, R., Gee, S. L., Ponthier, J. L., Lo, A., Wu, M., Turck, C. W., Koury, M. J., Krainer, A. R., Mayeda, A., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf625 · Cited by 69 · see citing works
[28] Ultraviolet-induced cross-linking of rna to proteins in vivo
Piñol-Roma, S., Adam, S. A., Choi, Y. D., et al. (1989) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(89)80114-4 · Cited by 66 · see citing works
Ostrowski, J., Sims, J. E., Sibley, C. H., et al. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98959-3 · Cited by 64 · see citing works
Regulation of the Nuclear Poly(A)-binding Protein by Arginine Methylation in Fission Yeast
Perreault, A., Lemieux, C., & Bachand, F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610512200 · Cited by 62 · see citing works
How Arginine-Rich Domains Coordinate mRNA Maturation Events
Godin, K. S., & Varani, G. (2007) · RNA Biology · doi:10.4161/rna.4.2.4869 · Cited by 61 · see citing works
Specificity in the interaction of hnRNA and mRNA with proteins as revealed by in vivo cross linking
van Eekelen, C. A., Riemen, T., & VENROOIJ, W. J. V. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)81125-8 · Cited by 57 · see citing works
Translational control of maternal RNAs
Evans, T. (2005) · WormBook · doi:10.1895/wormbook.1.34.1 · Cited by 57 · see citing works
NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C
Inoue, M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.8.1743 · Cited by 32 · see citing works
A three-hybrid screen identifies mRNAs controlled by a regulatory protein
Seay, D. J., Hook, B. A., Evans, K., & Wickens, M. (2006) · RNA · doi:10.1261/rna.145306 · Cited by 31 · see citing works
Autoregulation of GLD-2 cytoplasmic poly(A) polymerase
Rouhana, L., & Wickens, M. (2006) · RNA · doi:10.1261/rna.333507 · Cited by 29 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132 · see citing works
A compendium of RNA-binding motifs for decoding gene regulation
Ray, D., Kazan, H., Cook, K. B., Weirauch, M. T., Najafabadi, H. S., Li, X., Gueroussov, S., Albu, M., Zheng, H., Yang, A., et al. (2013) · Nature · doi:10.1038/nature12311 · Cited by 1,480 · see citing works
A large-scale binding and functional map of human RNA-binding proteins
Van Nostrand, E. L., Freese, P., Pratt, G. A., Wang, X., Wei, X., Xiao, R., Blue, S. M., Chen, J.-Y., Cody, N. A. L., Dominguez, D., et al. (2020) · Nature · doi:10.1038/s41586-020-2077-3 · Cited by 1,317 · see citing works
Genetic compensation: A phenomenon in search of mechanisms
El-Brolosy, M. A., & Stainier, D. Y. R. (2017) · PLOS Genetics · doi:10.1371/journal.pgen.1006780 · Cited by 829 · see citing works
Deep learning in bioinformatics: Introduction, application, and perspective in the big data era
Li, Y., Huang, C., Ding, L., Li, Z., Pan, Y., & Gao, X. (2019) · Methods · doi:10.1016/j.ymeth.2019.04.008 · Cited by 401 · 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
Targeting an RNA-Binding Protein Network in Acute Myeloid Leukemia
Wang, E., Lu, S. X., Pastore, A., Chen, X., Imig, J., Chun-Wei Lee, S., Hockemeyer, K., Ghebrechristos, Y. E., Yoshimi, A., Inoue, D., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.010 · Cited by 338 · see citing works
An overview of molecular basis of iron metabolism regulation and the associated pathologies
Silva, B., & Faustino, P. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.03.011 · Cited by 300 · see citing works
An artificial PPR scaffold for programmable RNA recognition
Coquille, S., Filipovska, A., Chia, T., Rajappa, L., Lingford, J. P., Razif, M. F. M., Thore, S., & Rackham, O. (2014) · Nature Communications · doi:10.1038/ncomms6729 · Cited by 120 · see citing works
Wei, Y.-N., Hu, H.-Y., Xie, G.-C., Fu, N., Ning, Z.-B., Zeng, R., & Khaitovich, P. (2015) · Genome Biology · doi:10.1186/s13059-015-0608-2 · Cited by 117 · see citing works
An overview of rational design of mRNA-based therapeutics and vaccines
To, K. K. W., & Cho, W. C. S. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1935859 · Cited by 110 · see citing works
Identification of Conserved Proteomic Networks in Neurodegenerative Dementia
Swarup, V., Chang, T. S., Duong, D. M., Dammer, E. B., Dai, J., Lah, J. J., Johnson, E. C. B., Seyfried, N. T., Levey, A. I., & Geschwind, D. H. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107807 · Cited by 78 · see citing works
Identification of conserved proteomic networks in neurodegenerative dementia
Swarup, V., Chang, T. S., Duong, D. M., Dammer, E. B., Lah, J. J., Johnson, E. E. C. B., Seyfried, N. T., Levey, A. I., & Geschwind, D. H. (2019) · doi:10.1101/825802 · Cited by 78 · see citing works
Khymenets, O., Fitó, M., Covas, M.-I., Farré, M., Pujadas, M.-A., Muñoz, D., Konstantinidou, V., & Torre, R. D. L. (2009) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2008.0079 · Cited by 68 · see citing works
Stress Granules Contain Rbfox2 with Cell Cycle-related mRNAs
Park, C., Choi, S., Kim, Y.-E., Lee, S., Park, S.-H., Adelstein, R. S., Kawamoto, S., & Kim, K. K. (2017) · Scientific Reports · doi:10.1038/s41598-017-11651-w · Cited by 49 · see citing works
Nithin, C., Ghosh, P., & Bujnicki, J. M. (2018) · Genes · doi:10.3390/genes9090432 · Cited by 48 · see citing works
RBM45 reprograms lipid metabolism promoting hepatocellular carcinoma via Rictor and ACSL1/ACSL4
Wang, C., Chen, Z., Yi, Y., Ding, Y., Xu, F., Kang, H., Lin, K., Shu, X., Zhong, Z., Zhang, Z., et al. (2024) · Oncogene · doi:10.1038/s41388-023-02902-4 · Cited by 42 · see citing works
Aberrant sodium channel activity in the complex seizure disorder of <i>Celf4</i> mutant mice
Sun, W., Wagnon, J. L., Mahaffey, C. L., Briese, M., Ule, J., & Frankel, W. N. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2012.240168 · Cited by 36 · see citing works
- Authors
- Glisovic, T., Bachorik, J. L., Yong, J., & Dreyfuss, G.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Dreyfuss, Gideon
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2008-03-13
- Volume
- 582
- Issue
- 14
- Pages
- 1977-1986
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- PMC
- PMC2858862
- OpenAlex
- W1984574291
- Cited by
- 1,398
- References
- 134
- Citations by year
- 2026: 53 · 2025: 80 · 2024: 100 · 2023: 93 · 2022: 79 · 2021: 94 · 2020: 116 · 2019: 102 · 2018: 101 · 2017: 95 · 2016: 84 · 2015: 73 · 2014: 86 · 2013: 64 · 2012: 57
- FWCI
- 3.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- RNA-binding proteins, post-transcriptional regulation, ribonucleoprotein complexes, pre-mRNA, mRNA, RNA stability, RNA transport, RNA localization, introns
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Ribonucleoproteins
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