The role of the 3' untranslated region in post-transcriptional regulation of protein expression in mammalian cells.
Open accessAbstract
The untranslated regions (UTRs) at the 3'end of mRNA transcripts contain important sequences that influence the fate of mRNA and thus proteosynthesis. In this review, we summarize the information known to date about 3'end processing, sequence characteristics including related binding proteins and the role of 3'UTRs in several selected signaling pathways to delineate their importance in the regulatory processes in mammalian cells. In addition to reviewing recent advances in the more well known aspects, such as cleavage and polyadenylation processes that influence mRNA stability and location, we concentrate on some newly emerging concepts of the role of the 3'UTR, including alternative polyadenylation sites in relation to proliferation and differentiation and the recognition of the multi-functional properties of non-coding RNAs, including miRNAs that commonly target the 3'UTR. The emerging picture is of a highly complex set of regulatory systems that include autoregulation, cooperativity and competition to fine tune proteosynthesis in context-dependent manners.
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?
The function of the 3′ UTR is to maintain mRNA stability.
“Conversely, the function of the 3′ UTR is to maintain mRNA stability.135,136”
From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [136]
Sequences of 5′ and 3′ untranslated regions (UTRs) play a key role in the stability of mRNA molecules and in their translational efficiency.
“Sequences of 5′ and 3′ untranslated regions (UTRs) are responsible for translational efficiency and stability of mRNA.”
From Effects of Combinations of Untranslated-Region Sequences on Translation of mRNA (2023) · cites this paper as [3]
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
MicroRNAs: Target Recognition and Regulatory Functions
Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.01.002 · Cited by 20,068 · see citing works
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
miRBase: tools for microRNA genomics
Griffiths‐Jones, S., Saini, H. K., van Dongen, S., & Enright, A. J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm952 · Cited by 4,349 · 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
The Transcriptional Landscape of the Mammalian Genome
Carninci, P., Kasukawa, T., Katayama, S., Gough, J., Frith, M. C., Maeda, N., Oyama, R., Ravasi, T., Lenhard, B., Wells, C. A., et al. (2005) · Science · doi:10.1126/science.1112014 · Cited by 3,492 · see citing works
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166 · see citing works
3′ Non-coding region sequences in eukaryotic messenger RNA
Proudfoot, N. J., & Brownlee, G. G. (1976) · Nature · doi:10.1038/263211a0 · Cited by 3,021 · see citing works
p21 in cancer: Intricate networks and multiple activities
Abbas, T., & Dutta, A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2657 · Cited by 2,712 · see citing works
Characterization of Mammalian Selenoproteomes
Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigó, R., & Gladyshev, V. N. (2003) · Science · doi:10.1126/science.1083516 · Cited by 2,353 · see citing works
AU-rich elements: characterization and importance in mRNA degradation
Chen, C.-Y. A., & Shyu, A.-B. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89102-1 · Cited by 1,948 · see citing works
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736 · see citing works
Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613 · see citing works
MicroRNA-10a binds the 5’UTR of ribosomal protein mRNAs and enhances their translation
Ørom, U. A., Nielsen, F. C., & Lund, A. H. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.001 · Cited by 1,384 · see citing works
Sandberg, R., Neilson, J. R., Sarma, A., Sharp, P. A., & Burge, C. B. (2008) · Science · doi:10.1126/science.1155390 · Cited by 1,349 · see citing works
lncRNAs transactivate STAU1-mediated mRNA decay by duplexing with 3′ UTRs via Alu elements
Gong, C., & Maquat, L. E. (2011) · Nature · doi:10.1038/nature09701 · Cited by 1,261 · see citing works
Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR
Lytle, J., Yario, T. A., & STEITZ, J. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703820104 · Cited by 1,196 · see citing works
From Birth to Death: The Complex Lives of Eukaryotic mRNAs
Moore, M. J. (2005) · Science · doi:10.1126/science.1111443 · Cited by 1,003 · see citing works
A large-scale analysis of mRNA polyadenylation of human and mouse genes
Tian, B. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki158 · Cited by 944 · see citing works
Farazi, T. A., Spitzer, J., Morozov, P. S., & Tuschl, T. (2010) · The Journal of Pathology · doi:10.1002/path.2806 · Cited by 892 · see citing works
p53 represses c-Myc through induction of the tumor suppressor miR-145
Sachdeva, M., Zhu, S., Wu, F., Wu, H., Walia, V., Kumar, S. R., Elble, R. C., Watabe, K., & Mo, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808042106 · Cited by 841 · see citing works
Lai, W. S., Carballo, E., Strum, J. R., Kennington, E. A., Phillips, R. S., & Blackshear, P. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4311 · Cited by 730 · see citing works
microRNA‐122 stimulates translation of hepatitis C virus RNA
Henke, J. I., Goergen, D., Zheng, J., Song, Y., Schüttler, C. G., Fehr, C., Jünemann, C., & Niepmann, M. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.244 · Cited by 677 · see citing works
Regulation of p53 Translation and Induction after DNA Damage by Ribosomal Protein L26 and Nucleolin
Takagi, M., Absalon, M. J., McLure, K. G., & Kastan, M. B. (2005) · Cell · doi:10.1016/j.cell.2005.07.034 · Cited by 656 · see citing works
Mukherjee, N., Corcoran, D. L., Nusbaum, J. D., Reid, D. W., Georgiev, S., Hafner, M., Ascano, M., Tuschl, T., Ohler, U., & Keene, J. D. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.007 · Cited by 654 · see citing works
Ji, Z., Lee, J. Y., Pan, Z., Jiang, B., & Tian, B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900028106 · Cited by 595 · see citing works
Lal, A., Navarro, F., Maher, C. A., Maliszewski, L. E., Yan, N., O’Day, E. M., Chowdhury, D., Dykxhoorn, D. M., Tsai, P., Hofmann, O., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.020 · Cited by 573 · see citing works
Molecular Architecture of the Human Pre-mRNA 3′ Processing Complex
Shi, Y., Giammartino, D. C. D., Taylor, D. J., Sarkeshik, A., Rice, W. J., Yates, J. R., Frank, J., & Manley, J. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.028 · Cited by 560 · see citing works
The Nonamer UUAUUUAUU Is the Key AU-Rich Sequence Motif That Mediates mRNA Degradation
Zubiaga, A. M., Belasco, J. G., & Greenberg, M. E. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.4.2219 · Cited by 543 · see citing works
HuR Regulates p21 mRNA Stabilization by UV Light
Wang, W., Furneaux, H., Cheng, H., Caldwell, M. C., Hutter, D., Liu, Y., Holbrook, N. J., & Gorospe, M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.760-769.2000 · Cited by 539 · see citing works
Phosphorylation of HuR by Chk2 Regulates SIRT1 Expression
Abdelmohsen, K., Pullmann, R., Lal, A., Kim, H. H., Galbán, S., Yang, X., Blethrow, J. D., Walker, M., Shubert, J., Gillespie, D. A., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.011 · Cited by 527 · 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
Alternative poly(A) site selection in complex transcription units: means to an end?
Edwalds-Gilbert, G. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.13.2547 · Cited by 509 · see citing works
TIA‐1 is a translational silencer that selectively regulates the expression of TNF‐α
Piecyk, M., Wax, S. D., Beck, A., Kedersha, N., Gupta, M., Maritim, B., Chen, S., Gueydan, C., Kruys, V., Streuli, M., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.15.4154 · Cited by 509 · see citing works
Mammalian Staufen1 Recruits Upf1 to Specific mRNA 3′UTRs so as to Elicit mRNA Decay
Kim, Y. K., Furic, L., DesGroseillers, L., & Maquat, L. E. (2005) · Cell · doi:10.1016/j.cell.2004.11.050 · Cited by 494 · see citing works
Concurrent versus individual binding of HuR and AUF1 to common labile target mRNAs
Lal, A., Mazan‐Mamczarz, K., Kawai, T., Yang, X., Martindale, J. L., & Gorospe, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600305 · Cited by 461 · 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
Gherzi, R., Lee, K., Briata, P., Wegmüller, D., Moroni, C., Karin, M., & Chen, C. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.05.002 · Cited by 454 · see citing works
HuR regulates cyclin A and cyclin B1 mRNA stability during cell proliferation
Wang, W., Caldwell, M. C., Lin, S., Furneaux, H., & Gorospe, M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.10.2340 · Cited by 446 · see citing works
RNA-binding protein HuR enhances p53 translation in response to ultraviolet light irradiation
Mazan-Mamczarz, K., Galbán, S., de Silanes, I. L., Martindale, J. L., Atasoy, U., Keene, J. D., & Gorospe, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1432104100 · Cited by 445 · see citing works
Protein factors in pre-mRNA 3′-end processing
Mandel, C. R., Bai, Y., & Tong, L. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7474-3 · Cited by 415 · see citing works
A Pumilio-induced RNA structure switch in p27-3′ UTR controls miR-221 and miR-222 accessibility
Kedde, M., van Kouwenhove, M., Zwart, W. T., Vrielink, J. A. F. O., Elkon, R., & Agami, R. (2010) · Nature Cell Biology · doi:10.1038/ncb2105 · Cited by 406 · see citing works
Molecular mechanisms of eukaryotic pre-mRNA 3′ end processing regulation
Millevoi, S., & Vagner, S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1176 · Cited by 393 · 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
Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein
Sawicka, K., Bushell, M., Spriggs, K. A., & Willis, A. E. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360641 · Cited by 332 · see citing works
HuR 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
ARED 3.0: the large and diverse AU-rich transcriptome
Bakheet, T. M. (2005) · Nucleic Acids Research · doi:10.1093/nar/gkj052 · Cited by 318 · see citing works
Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family
Callebaut, I. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf470 · Cited by 311 · see citing works
Muckenthaler, M., Gray, N. K., & Hentze, M. W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80282-8 · Cited by 297 · see citing works
Dean, J. L. E., Wait, R., Mahtani, K. R., Sully, G., Clark, A. R., & Saklatvala, J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.3.721-730.2001 · Cited by 294 · see citing works
Loflin, P. T., Chen, C.-Y. A., & Shyu, A. B. (1999) · Genes & Development · doi:10.1101/gad.13.14.1884 · Cited by 293 · see citing works
Biased alternative polyadenylation in human tissues
Zhang, H., Lee, J. Y., & Tian, B. (2005) · Genome biology · doi:10.1186/gb-2005-6-12-r100 · Cited by 292 · see citing works
New perspectives on connecting messenger RNA 3′ end formation to transcription
Proudfoot, N. J. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.03.007 · Cited by 285 · see citing works
The Impact of miRNA Target Sites in Coding Sequences and in 3′UTRs
Fang, Z., & Rajewsky, N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018067 · Cited by 280 · see citing works
RNA-Binding Proteins HuR and PTB Promote the Translation of Hypoxia-Inducible Factor 1α
Galbán, S., Kuwano, Y., Pullmann, R., Martindale, J. L., Kim, H. H., Lal, A., Abdelmohsen, K., Yang, X., Dang, Y., Liu, J. O., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00973-07 · Cited by 279 · see citing works
Wagner, B. J., DeMaria, C. T., Sun, Y., Wilson, G. M., & Brewer, G. (1998) · Genomics · doi:10.1006/geno.1997.5142 · Cited by 274 · see citing works
Human Fip1 is a subunit of CPSF that binds to U‐rich RNA elements and stimulates poly(A) polymerase
Kaufmann, I., Martin, G., Friedlein, A., Langen, H., & Keller, W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600070 · Cited by 257 · see citing works
Murthy, K. G. K., & Manley, J. L. (1995) · Genes & Development · doi:10.1101/gad.9.21.2672 · Cited by 254 · see citing works
A stress-responsive RNA switch regulates VEGFA expression
Ray, P. S., Jia, J., Yao, P., Majumder, M., Hatzoglou, M., & Fox, P. L. (2008) · Nature · doi:10.1038/nature07598 · Cited by 250 · see citing works
A sequence downstream of AAUAAA is required for rabbit β-globin mRNA 3′-end formation
Gil, A., & Proudfoot, N. J. (1984) · Nature · doi:10.1038/312473a0 · Cited by 249 · see citing works
HU, J., Lutz, C. S., Wilusz, J., & Tian, B. (2005) · RNA · doi:10.1261/rna.2107305 · Cited by 249 · see citing works
Statistical analysis of vertebrate sequences reveals that long genes are scarce in GC-rich isochores
Duret, L., Mouchiroud, D., & Gautier, C. (1995) · Journal of Molecular Evolution · doi:10.1007/bf00163235 · Cited by 246 · see citing works
Human selenoproteins at a glance
Gromer, S., Eubel, J., Lee, B. L., & Jacob, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5143-y · Cited by 245 · see citing works
Koeller, D. M., Casey, J. L., Hentze, M. W., Gerhardt, E. M., Chan, L.-N. L., Klausner, R. D., & Harford, J. B. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3574 · Cited by 242 · see citing works
In silico detection of control signals: mRNA 3′-end-processing sequences in diverse species
Graber, J. H., Cantor, C. R., Mohr, S. C., & Smith, T. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.14055 · Cited by 242 · see citing works
Genome-wide Analysis Identifies Interleukin-10 mRNA as Target of Tristetraprolin
Stoecklin, G., Tenenbaum, S. A., Mayo, T., Chittur, S. V., George, A. D., Baroni, T. E., Blackshear, P. J., & Anderson, P. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709657200 · Cited by 239 · see citing works
Conserved GU-Rich Elements Mediate mRNA Decay by Binding to CUG-Binding Protein 1
Louis, I. V.-S., Tahoe, N. M., Fan, D., Larsson, O. S., Rattenbacher, B., SternJohn, J. R., Vasdewani, J., Karypis, G., Reilly, C., Bitterman, P. B., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.11.024 · Cited by 234 · see citing works
A Mechanism for the Regulation of Pre-mRNA 3′ Processing by Human Cleavage Factor Im
Brown, K. M., & Gilmartin, G. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00453-2 · Cited by 226 · see citing works
Venkataraman, K., Brown, K. M., & Gilmartin, G. M. (2005) · Genes & Development · doi:10.1101/gad.1298605 · Cited by 223 · see citing works
Four factors are required for 3'-end cleavage of pre-mRNAs.Preprint
Takagaki, Y., Ryner, L. C., & Manley, J. L. (1989) · Genes & Development · doi:10.1101/gad.3.11.1711 · Cited by 223 · see citing works
Ostareck‐Lederer, A., Ostareck, D. H., Cans, C., Neubauer, G., Bomsztyk, K., Superti‐Furga, G., & Hentze, M. W. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4535-4543.2002 · Cited by 222 · see citing works
Functional cloning of BRF1, a regulator of ARE‐dependent mRNA turnover
Stoecklin, G., Colombi, M., Raineri, I., Leuenberger, S., Mallaun, M., Schmidlin, M., Gross, B., Lu, M., Kitamura, T., & Moroni, C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf444 · Cited by 212 · see citing works
MKP-1 mRNA Stabilization and Translational Control by RNA-Binding Proteins HuR and NF90
Kuwano, Y., Kim, H. H., Abdelmohsen, K., Pullmann, R., Martindale, J. L., Yang, X., & Gorospe, M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00165-08 · Cited by 209 · see citing works
Brennan, S. E., Kuwano, Y., Alkharouf, N. W., Blackshear, P. J., Gorospe, M., & Wilson, G. M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4238 · Cited by 205 · see citing works
Lai, W. S., Parker, J. S., Grissom, S. F., Stumpo, D. J., & Blackshear, P. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00945-06 · Cited by 203 · see citing works
Pullmann, R., Kim, H. H., Abdelmohsen, K., Lal, A., Martindale, J. L., Yang, X., & Gorospe, M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00500-07 · Cited by 199 · see citing works
Staufen1 regulates diverse classes of mammalian transcripts
Kim, Y. K., Furic, L., Parisien, M., Major, F., DesGroseillers, L., & Maquat, L. E. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601712 · Cited by 197 · see citing works
Translational control by cytoplasmic polyadenylation in Xenopus oocytes
Radford, H. E., Meijer, H. A., & de Moor, C. H. (2008) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.02.002 · Cited by 191 · see citing works
Clement, S. L., Scheckel, C., Stoecklin, G., & Lykke‐Andersen, J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00717-10 · Cited by 190 · see citing works
Translational Control of Cytochrome c by RNA-Binding Proteins TIA-1 and HuR
Kawai, T., Lal, A., Yang, X., Galbán, S., Mazan-Mamczarz, K., & Gorospe, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.3295-3307.2006 · Cited by 187 · see citing works
Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes
Chavatte, L., Brown, B. A., & Driscoll, D. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb922 · Cited by 184 · see citing works
Nuclear Export of NF90 Is Required for Interleukin-2 mRNA Stabilization
Shim, J., Lim, H., Yates, J. R., & Karin, M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00730-x · Cited by 184 · 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
de Vries, H., Rüegsegger, U., Hübner, W., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5895 · Cited by 181 · see citing works
Barabino, S. M. L., & Keller, W. D. (1999) · Cell · doi:10.1016/s0092-8674(00)80057-4 · Cited by 179 · see citing works
Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation
Liao, B., Hu, Y., & Brewer, G. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1249 · Cited by 173 · see citing works
Loss of HuR Is Linked to Reduced Expression of Proliferative Genes during Replicative Senescence
Wang, W., Yang, X., Cristofalo, V. J., Holbrook, N. J., & Gorospe, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5889-5898.2001 · Cited by 171 · see citing works
The RNA-binding Protein HuR Regulates the Expression of Cyclooxygenase-2
Sengupta, S., Jang, B., Wu, M.-T., Paik, J., Furneaux, H., & Hla, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301813200 · Cited by 163 · see citing works
Combinatorial mRNA Regulation: Iron Regulatory Proteins and Iso-iron-responsive Elements (Iso-IREs)
Theil, E. C., & Eisenstein, R. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000019200 · Cited by 162 · see citing works
Antiapoptotic function of RNA‐binding protein HuR effected through prothymosin α
Lal, A., Kawai, T., Yang, X., Mazan-Mamczarz, K., & Gorospe, M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600661 · Cited by 161 · see citing works
Marchese, F. P., Aubareda, A., Tudor, C., Saklatvala, J., Clark, A. R., & Dean, J. L. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.136473 · Cited by 149 · see citing works
Tristetraprolin Binds to the 3′-Untranslated Region of Cyclooxygenase-2 mRNA
Sawaoka, H., Dixon, D. A., Oates, J. A., & Boutaud, O. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300016200 · Cited by 144 · see citing works
ARED Organism: expansion of ARED reveals AU-rich element cluster variations between human and mouse
Halees, A. S., El-Badrawi, R., & Khabar, K. S. A. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm959 · Cited by 142 · see citing works
Chapman, S. B., Lindzen, R. S., & Reidel, D. (2005) · Cited by 140 · see citing works
Translational regulation of human p53 gene expression.
Fu, L., Minden, M. D., & Benchimol, S. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00812.x · Cited by 138 · see citing works
Cok, S. J., Acton, S. J., & Morrison, A. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302547200 · Cited by 136 · see citing works
Lee, J. E., Lee, J. Y., Wilusz, J., Tian, B., & Wilusz, C. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011201 · Cited by 133 · see citing works
Abdelmohsen, K., Tominaga, K., Lee, E. K., Srikantan, S., Kang, M. J., Kim, M. M., Selimyan, R., Martindale, J. L., Yang, X., Carrier, F., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr488 · Cited by 133 · see citing works
Vumbaca, F., Phoenix, K. N., Rodríguez‐Pinto, D., Han, D. K. M., & Claffey, K. P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02078-06 · Cited by 129 · see citing works
Chen, J., & Kastan, M. B. (2010) · Genes & Development · doi:10.1101/gad.1968910 · Cited by 127 · see citing works
Repression of VEGFA by CA‐rich element‐binding microRNAs is modulated by hnRNP L
Jafarifar, F., Yao, P., Eswarappa, S. M., & Fox, P. L. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.38 · Cited by 120 · see citing works
Leptomycin B, an Inhibitor of the Nuclear Export Receptor CRM1, Inhibits COX-2 Expression
Jang, B., Muñoz-Nájar, U., Paik, J., Claffey, K. P., Yoshida, M., & Hla, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200620200 · Cited by 117 · see citing works
Giles, K. M., Daly, J. M., Beveridge, D. J., Thomson, A. M., Voon, D. C., Furneaux, H. M., Jazayeri, J. A., & Leedman, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208439200 · Cited by 114 · see citing works
Iron Regulation and the Cell Cycle
Sánchez, M., Galy, B., Dandekar, T., Bengert, P., Vainshtein, Y., Stolte, J., Muckenthaler, M. U., & Hentze, M. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603876200 · Cited by 112 · see citing works
HuR Uses AUF1 as a Cofactor To Promote p16<sup>INK4</sup> mRNA Decay
Chang, N., Yi, J., Guo, G., Liu, X., Shang, Y., Tong, T., Cui, Q., Zhan, M., Gorospe, M., & Wang, W. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00169-10 · Cited by 112 · see citing works
Sarkar, B., Lu, J., & Schneider, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301176200 · Cited by 111 · see citing works
Secombe, J., Pierce, S. B., & Eisenman, R. N. (2004) · Cell · doi:10.1016/s0092-8674(04)00336-8 · Cited by 110 · see citing works
Al‐Ahmadi, W., Alghamdi, M. A., Al‐Haj, L., Al‐Saif, M., & Khabar, K. S. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp223 · Cited by 110 · see citing works
RNPC1 modulates the RNA-binding activity of, and cooperates with, HuR to regulate p21 mRNA stability
Cho, J. Y., Zhang, J., & Chen, X. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1229 · Cited by 107 · see citing works
NF90 selectively represses the translation of target mRNAs bearing an AU-rich signature motif
Kuwano, Y., Pullmann, R., Marasa, B. S., Abdelmohsen, K., Lee, E. K., Yang, X., Martindale, J. L., Zhan, M., & Gorospe, M. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp861 · Cited by 105 · see citing works
Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding
Díaz‐Moreno, I., Hollingworth, D., Frenkiel, T. A., Kelly, G. P., Martin, S. R., Howell, S. A., García‐Mayoral, M. F., Gherzi, R., Briata, P., & Ramos, A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1558 · Cited by 104 · see citing works
Essafi‐Benkhadir, K., Onesto, C., Stebe, E., Moroni, C., & Pagès, G. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-06-0570 · Cited by 101 · see citing works
Increased stability of the p16 mRNA with replicative senescence
Wang, W., Martindale, J. L., Yang, X., Chrest, F. J., & Gorospe, M. (2005) · The EMBO Reports · doi:10.1038/sj.embor.7400346 · Cited by 101 · see citing works
HuR Contributes to Cyclin E1 Deregulation in MCF-7 Breast Cancer Cells
Guo, X., & Hartley, R. S. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4362 · Cited by 99 · see citing works
Al‐Souhibani, N., Al‐Ahmadi, W., Hesketh, J. E., Blackshear, P. J., & Khabar, K. S. A. (2010) · Oncogene · doi:10.1038/onc.2010.168 · Cited by 98 · see citing works
Shi, L., Zhao, G., Qiu, D., Godfrey, W. R., Vogel, H. S., Rando, T. A., Hu, H., & Kao, P. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411034200 · Cited by 98 · see citing works
Gareau, C., Fournier, M., Filion, C., Coudert, L., Martel, D. T., Labelle, Y., & Mazrouï, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020254 · Cited by 98 · see citing works
Regulation of Bcl-2 Expression by HuR in HL60 Leukemia Cells and A431 Carcinoma Cells
Ishimaru, D., Ramalingam, S., Sengupta, T. K., Bandyopadhyay, S., Dellis, S., Tholanikunnel, B. G., Fernandes, D., & Spicer, E. K. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0476 · Cited by 95 · see citing works
The p53 target Wig-1 regulates p53 mRNA stability through an AU-rich element
Vilborg, A., Glahder, J. A., Wilhelm, M., Bersani, C., Corcoran, M., Mahmoudi, S., Rosenstierne, M. W., Grandér, D., Farnebo, M., Norrild, B., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900862106 · Cited by 94 · see citing works
Erlitzki, R., Long, J. C., & Theil, E. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207918200 · Cited by 94 · see citing works
Maitra, S., Chou, C., Luber, C. A., Lee, K., Mann, M., & Chen, C. (2008) · RNA · doi:10.1261/rna.983708 · Cited by 91 · see citing works
Posttranscriptional Derepression of GADD45α by Genotoxic Stress
Lal, A., Abdelmohsen, K., Pullmann, R., Kawai, T., Galbán, S., Yang, X., Brewer, G., & Gorospe, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.016 · Cited by 89 · see citing works
Latrèche, L., Jean‐Jean, O., Driscoll, D. M., & Chavatte, L. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp635 · Cited by 88 · see citing works
Posttranscriptional regulation of gene networks by GU-rich elements and CELF proteins
Louis, I. V.-S., & Bohjanen, P. R. (2008) · RNA Biology · doi:10.4161/rna.7056 · Cited by 85 · see citing works
Distinct roles of two Yth1p domains in 3′‐end cleavage and polyadenylation of yeast pre‐mRNAs
Barabino, S. M. L., Ohnacker, M., & Keller, W. D. (2000) · The EMBO Journal · doi:10.1093/emboj/19.14.3778 · Cited by 82 · see citing works
Novel functional role of CA repeats and hnRNP L in RNA stability
Hui, J., Reither, G., & Bindereif, A. (2003) · RNA · doi:10.1261/rna.5660803 · Cited by 82 · see citing works
Sureban, S. M., Murmu, N., Rodriguez, P., May, R. J., Maheshwari, R., Dieckgraefe, B. K., Houchen, C. W., & Anant, S. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.12.031 · Cited by 75 · see citing works
Pan, Y., Chen, H., & Kilberg, M. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507802200 · Cited by 73 · see citing works
Scoumanne, A., Cho, S. J., Zhang, J., & Chen, X. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq778 · Cited by 73 · see citing works
Polymorphisms in p53 and the p53 pathway: roles in cancer susceptibility and response to treatment
Hrstka, R., Coates, P. J., & Vojtěšek, B. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00634.x · Cited by 71 · see citing works
Self-citationA novel iron responsive element in the 3′UTR of human MRCKα
Čmejla, R., Petrák, J., & Čmejlová, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.155 · Cited by 68 · see citing works
Reimann, I., Huth, A., Thiele, H., & Thiele, B. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5315 · Cited by 61 · see citing works
Yu, Q., Cok, S. J., Zeng, C., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m203526200 · Cited by 61 · see citing works
Autoregulatory Suppression of c-Myc by miR-185-3p
Liao, J., & Lu, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.262030 · Cited by 57 · see citing works
Quaking Regulates Hnrnpa1 Expression through Its 3′ UTR in Oligodendrocyte Precursor Cells
Zearfoss, N. R., Clingman, C. C., Farley, B. M., McCoig, L. M., & Ryder, S. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001269 · Cited by 57 · see citing works
Kandasamy, K., Joseph, K., Subramaniam, K., Raymond, J. R., & Tholanikunnel, B. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405937200 · Cited by 50 · see citing works
Messias, A. C., Harnisch, C., Ostareck‐Lederer, A., et al. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.025 · Cited by 46 · see citing works
Global assessment of GU-rich regulatory content and function in the human transcriptome
Halees, A. S., Hitti, E., Al‐Saif, M., Mahmoud, L., Louis, I. V.-S., Beisang, D. J., Bohjanen, P. R., & Khabar, K. S. A. (2011) · RNA Biology · doi:10.4161/rna.8.4.16283 · Cited by 44 · see citing works
Díaz‐Moreno, I., Hollingworth, D., Kelly, G. P., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq216 · Cited by 44 · see citing works
Cooperative Role of the RNA-Binding Proteins Hzf and HuR in p53 Activation
Nakamura, H., Kawagishi, H., Watanabe, A., Sugimoto, K., Maruyama, M., & Sugimoto, M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01424-10 · Cited by 43 · see citing works
Zhu, P., Jiang, W. I., Cao, L., Yu, W., Pei, Y., Yang, X., Wan, B., Liu, J. O., Yi, Q., & Yu, L. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000849 · Cited by 42 · see citing works
Ryan, K., & Bauer, D. L. V. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.03.016 · Cited by 42 · see citing works
Dual localization of the RNA binding protein CUGBP-1 to stress granule and perinucleolar compartment
Fujimura, K., Kano, F., & Murata, M. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.10.024 · Cited by 41 · see citing works
Meyer, S., Urbanke, C., & Wahle, E. (2002) · Biochemistry · doi:10.1021/bi0160866 · Cited by 37 · see citing works
hnRNP L binds to CA repeats in the 3′UTR of bcl-2 mRNA
Lee, D.-H., Lim, M.-H., Youn, D., et al. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.069 · Cited by 31 · see citing works
mRNA stability control: a clandestine force in normal and malignant hematopoiesis
Steinman, R. A. (2007) · Leukemia · doi:10.1038/sj.leu.2404656 · Cited by 30 · see citing works
Leibovich, L., Mandel‐Gutfreund, Y., & Zohar Yakhini, B. (2010) · Silence · doi:10.1186/1758-907x-1-17 · Cited by 23 · see citing works
Phosphorylation of the HuR ligand APRIL by casein kinase 2 regulates CD83 expression
Chemnitz, J., Pieper, D., Grüttner, C., & Hauber, J. (2009) · European Journal of Immunology · doi:10.1002/eji.200838619 · Cited by 22 · see citing works
In vivo post‐transcriptional regulation of CD154 in mouse CD4+ T cells
Vavassori, S., Shi, Y., Chen, C., et al. (2009) · European Journal of Immunology · doi:10.1002/eji.200839163 · Cited by 21 · see citing works
Bubenik, J. L., Ladd, A. N., Gerber, C. A., Budiman, M. E., & Donna, D. (2009) · RNA Biology · doi:10.4161/rna.6.1.7569 · Cited by 16 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Advances in COVID-19 mRNA vaccine development
Fang, E., Liu, X., Li, M., Zhang, Z., Song, L., Zhu, B., Wu, X., Liu, J., Zhao, D., & Li, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00950-y · Cited by 601 · see citing works
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 · see citing works
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 · see citing works
Kwon, H., Kim, M., Seo, Y., Moon, Y. S., Lee, H. J., Lee, K., & Lee, H. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2017.11.034 · Cited by 208 · see citing works
Biomedical applications of mRNA nanomedicine
Xiong, Q., Lee, G. Y., Ding, J., Li, W., & Shi, J. (2018) · Nano Research · doi:10.1007/s12274-018-2146-1 · Cited by 125 · see citing works
Yang, S. W., Li, L., Connelly, J. P., Porter, S. N., Kodali, K., Gan, H., Park, J. M., Tacer, K. F., Tillman, H., Peng, J., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.022 · Cited by 79 · see citing works
Effects of Combinations of Untranslated-Region Sequences on Translation of mRNA
Kirshina, A., Vasileva, O., Kunyk, D., Seregina, K., Muslimov, A., Ivanov, R., & Reshetnikov, V. (2023) · Biomolecules · doi:10.3390/biom13111677 · Cited by 26 · see citing works
- Authors
- Matoulkova, E., Michalova, E., Vojtesek, B., & Hrstka, R.
- Affiliations
- Masaryk Memorial Cancer Institute (CZ)
- Corresponding author
- Hrstka, Roman
- ORCID
- Hrstka, Roman
- Venue
- RNA Biology
- Publisher
- Informa UK Limited
- Published
- 2012-05
- Volume
- 9
- Issue
- 5
- Pages
- 563-576
- ISSN
- 1547-6286 (ISSN-L)
- 1555-8584
- OpenAlex
- W2054574453
- Cited by
- 357
- References
- 150
- Citations by year
- 2026: 13 · 2025: 14 · 2024: 14 · 2023: 25 · 2022: 31 · 2021: 38 · 2020: 47 · 2019: 43 · 2018: 45 · 2017: 21 · 2016: 19 · 2015: 16 · 2014: 20 · 2013: 11
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- RNA Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Regional Development Fund (CZ.1.05/2.1.00/03.0101)
- 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 › Cancer Research › Cancer-related molecular mechanisms research
- Keywords
- 3' untranslated region, post-transcriptional regulation, mRNA stability, mRNA localization, 3' end processing, cleavage and polyadenylation, microRNA, non-coding RNA, autoregulation, cell proliferation and differentiation, signaling pathways, mammalian cells
- MeSH terms
- Animals, Base Sequence, Humans, Promoter Regions, Genetic, RNA Processing, Post-Transcriptional, RNA, Messenger, RNA-Binding Proteins, 3' Untranslated Regions, Polyadenylation, RNA Interference, MicroRNAs
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review