The regulation of mRNA stability in mammalian cells: 2.0

Wu, Xiangyue; Brewer, Gary

doi:10.1016/j.gene.2012.03.021

Cited by 239RNA Research and SplicingRNA regulation and diseaseRNA and protein synthesis mechanisms

The regulation of mRNA stability in mammalian cells: 2.0

Open access

Wu, Xiangyue, Brewer, Gary·2012·Gene

DOI 10.1016/j.gene.2012.03.021PMC PMC3340483

Open this paper in CoChat — free account

Abstract

Messenger RNA decay is an essential step in gene expression to set mRNA abundance in the cytoplasm. The binding of proteins and/or noncoding RNAs to specific recognition sequences or secondary structures within mRNAs dictates mRNA decay rates by recruiting specific enzyme complexes that perform the destruction processes. Often, the cell coordinates the degradation or stabilization of functional subsets of mRNAs encoding proteins collectively required for a biological process. As well, extrinsic or intrinsic stimuli activate signal transduction pathways that modify the mRNA decay machinery with consequent effects on decay rates and mRNA abundance. This review is an update to our 2001 Gene review on mRNA stability in mammalian cells, and we survey the enormous progress made over the past decade.

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

Crossref · 10.1016/j.gene.2012.03.021

Cites

166 of 166 references verified0 citation errors · 0 not checkable

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?

Out of the roughly 20 currently known AUBPs, the majority are expressed in neurons and promote mRNA decay, including AUF1, TTP, and KSRP.
“Out of the roughly 20 currently known AUBPs, the majority are expressed in neurons and promote mRNA decay including, for example, AUF1, TTP, and KSRP (Table 1; Wu and Brewer 2012).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Wu and Brewer 2012
Section 4.1 says there are about 20 known AUBPs, that most recruit mRNA-degradation machinery, and that AUF1, TTP, and KSRP promote degradation. It does not establish that a majority of AUBPs are expressed in neurons. (LLM, conf=0.90)
Experimental — accuracy not yet measured
Destabilizing RBPs may promote deadenylation by blocking poly(A) binding protein (PABP) binding and/or recruiting decapping, deadenylation, and exosome components.
“Once bound to a target mRNA, destabilizing RBPs may promote deadenylation through a variety of manners such as blocking poly(A) binding protein (PABP) binding and/or recruitment of decapping, deadenylation, and exosome components (Wu and Brewer 2012).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Wu and Brewer 2012
Section 4.1 says AUF1 may prevent PABP from binding poly(A), allowing deadenylases access, and that KSRP, TTP, and BRF1 interact with deadenylation, decapping, and exosome factors. It describes those recruited factors as promoting mRNA degradation overall, however, and places exosome-mediated degradation after deadenylation; it does not say that recruiting decapping or exosome components promotes deadenylation itself. (LLM, conf=0.83)
Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Untitled work
Bartel (2004) · doi:10.1016/s0092-8674(04)00045-5 · Cited by 34,714 · see citing works
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
Untitled work
(2008) · doi:10.1038/nrg2290 · Cited by 5,199 · see citing works
Evolution and Functions of Long Noncoding RNAs
Ponting, C. P., Oliver, P. L., & Reik, W. (2009) · Cell · doi:10.1016/j.cell.2009.02.006 · Cited by 4,917 · see citing works
A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
Shaw, G. D., & Kamen, R. (1986) · Cell · doi:10.1016/0092-8674(86)90341-7 · Cited by 3,946 · 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
MicroRNA Targeting Specificity in Mammals: Determinants beyond Seed Pairing
Grimson, A., Farh, K. K.-H., Johnston, W. K., Garrett-Engele, P., Lim, L. P., & Bartel, D. P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.017 · Cited by 3,766 · see citing works
Regulation of mRNA Translation and Stability by microRNAs
Fabian, M. R., Sonenberg, N., & Filipowicz, W. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060308-103103 · Cited by 3,214 · see citing works
Transcriptome-wide Identification of RNA-Binding Protein and MicroRNA Target Sites by PAR-CLIP
Hafner, M., Landthaler, M., Burger, L., Khorshid, M., Hausser, J., Berninger, P., Rothballer, A., Ascano, M., Jungkamp, A.-C., Munschauer, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.03.009 · Cited by 2,873 · see citing works
Argonaute2 is the catalytic engine of mammalian RNAi
Liu, J., Carmell, M. A., Rivas, F. V., Marsden, C. G., Thomson, J. M., Song, J.-J., Hammond, S. M., Joshua-Tor, L., & Hannon, G. J. (2004) · Science · doi:10.1126/science.1102513 · Cited by 2,353 · see citing works
Gene silencing by microRNAs: contributions of translational repression and mRNA decay
Huntzinger, E., & Izaurralde, E. (2011) · Nature Reviews Genetics · doi:10.1038/nrg2936 · Cited by 2,339 · see citing works
Long noncoding RNAs: functional surprises from the RNA worldPreprint
Wilusz, J. E., Sunwoo, H., & Spector, D. L. (2009) · Genes & Development · doi:10.1101/gad.1800909 · Cited by 2,298 · see citing works
TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing
Chendrimada, T. P., Gregory, R. I., Kumaraswamy, E., Norman, J. A., Cooch, N. S., Nishikura, K., & Shiekhattar, R. (2005) · Nature · doi:10.1038/nature03868 · Cited by 2,103 · see citing works
A microRNA in a Multiple-Turnover RNAi Enzyme Complex
Hutvágner, G., & Zamore, P. D. (2002) · Science · doi:10.1126/science.1073827 · Cited by 2,081 · see citing works
MicroRNA biogenesis: coordinated cropping and dicing
Kim, V. N. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1644 · Cited by 2,019 · 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
Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs
Meister, G., Landthaler, M., Patkaniowska, A., Dorsett, Y., Teng, G., & Tuschl, T. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.07.007 · Cited by 1,718 · see citing works
MicroRNA-Directed Cleavage of <i>HOXB8</i> mRNA
Yekta, S., Shih, I.-H., & Bartel, D. P. (2004) · Science · doi:10.1126/science.1097434 · Cited by 1,702 · see citing works
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 · see citing works
P bodies and the control of mRNA translation and degradation
Parker, R., & Sheth, U. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.011 · Cited by 1,335 · see citing works
RNA regulons: coordination of post-transcriptional events
Keene, J. D. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2111 · Cited by 1,321 · see citing works
The highways and byways of mRNA decay
Garneau, N. L., Wilusz, J., & Wilusz, C. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2104 · Cited by 1,294 · see citing works
The Nonsense-Mediated Decay RNA Surveillance Pathway
Chang, Y.-F., Imam, J. S., & Wilkinson, M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.050106.093909 · Cited by 1,283 · 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
The Many Pathways of RNA Degradation
Houseley, J. M., & Tollervey, D. W. (2009) · Cell · doi:10.1016/j.cell.2009.01.019 · Cited by 1,220 · see citing works
MicroRNAs direct rapid deadenylation of mRNA
Wu, L., Fan, J., & Belasco, J. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510928103 · Cited by 1,135 · see citing works
AU-rich elements and associated factors: are there unifying principles?
Barreau, C. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki1012 · Cited by 1,033 · see citing works
mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexesPreprint
Behm‐Ansmant, I., Rehwinkel, J., Doerks, T., Stark, A., Bork, P., & Izaurralde, E. (2006) · Genes & Development · doi:10.1101/gad.1424106 · Cited by 1,030 · see citing works
RNA granules
Anderson, P., & Kedersha, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512082 · Cited by 984 · see citing works
MicroRNAs and small interfering RNAs can inhibit mRNA expression by similar mechanisms
Zeng, Y., Yi, R., & Cullen, B. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630797100 · Cited by 923 · see citing works
Nonsense surveillance regulates expression of diverse classes of mammalian transcripts and mutes genomic noise
Mendell, J. T., Sharifi, N., Meyers, J. L., Martínez-Murillo, F., & Dietz, H. C. (2004) · Nature Genetics · doi:10.1038/ng1429 · Cited by 880 · see citing works
AU Binding Proteins Recruit the Exosome to Degrade ARE-Containing mRNAs
Chen, C.-Y., Gherzi, R., Ong, S.-E., Chan, E. L., Raijmakers, R., Pruijn, G. J. M., Stoecklin, G., Moroni, C., Mann, M., & Karin, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00578-5 · Cited by 865 · see citing works
Involvement of MicroRNA in AU-Rich Element-Mediated mRNA Instability
Jing, Q., Huang, S., Guth, S., Zarubin, T., Motoyama, A. B., Chen, J., Padova, F. D., Lin, S., Gram, H., & Han, J. (2005) · Cell · doi:10.1016/j.cell.2004.12.038 · Cited by 849 · see citing works
The exon–exon junction complex provides a binding platform for factors involved in mRNA export and nonsense‐mediated mRNA decay
Hir, H. L., Gatfield, D., Izaurralde, E., & Moore, M. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4987 · Cited by 842 · see citing works
Movement of Eukaryotic mRNAs Between Polysomes and Cytoplasmic Processing Bodies
Brengues, M., Teixeira, D., & Parker, R. (2005) · Science · doi:10.1126/science.1115791 · Cited by 796 · see citing works
Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation
Doma, M. K., & Parker, R. (2006) · Nature · doi:10.1038/nature04530 · Cited by 764 · see citing works
The cap-to-tail guide to mRNA turnover
Wilusz, C. J., Wormington, M., & Peltz, S. W. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35067025 · Cited by 757 · see citing works
Transcriptome-wide Analysis of Regulatory Interactions of the RNA-Binding Protein HuR
Lebedeva, S., Jens, M., Theil, K., Schwanhäusser, B., Selbach, M., Landthaler, M., & Rajewsky, N. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.008 · Cited by 716 · see citing works
Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay
Matsushita, K., Takeuchi, O., Standley, D. M., Kumagai, Y., Kawagoe, T., Miyake, T., Satoh, T., Kato, H., Tsujimura, T., Nakamura, H., et al. (2009) · Nature · doi:10.1038/nature07924 · Cited by 677 · see citing works
Cytoplasmic foci are sites of mRNA decay in human cells
Cougot, N., Babajko, S., & Séraphin, B. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309008 · Cited by 647 · see citing works
RNA-quality control by the exosome
Houseley, J. M., LaCava, J., & Tollervey, D. W. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1964 · Cited by 645 · see citing works
Binding of a novel SMG-1–Upf1–eRF1–eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decayPreprint
Kashima, I., Yamashita, A., Izumi, N., Kataoka, N., Morishita, R., Hoshino, S.-I., Ohno, M., Dreyfuss, G., & Ohno, S. (2006) · Genes & Development · doi:10.1101/gad.1389006 · Cited by 645 · see citing works
Diverse RNA-Binding Proteins Interact with Functionally Related Sets of RNAs, Suggesting an Extensive Regulatory System
Hogan, D. J., Riordan, D. P., Gerber, A. P., Herschlag, D., & Brown, P. O. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060255 · Cited by 609 · see citing works
Nonsense-mediated mRNA decay (NMD) mechanisms
Brogna, S., & Wen, J. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1550 · Cited by 593 · see citing works
Exosome-Mediated Recognition and Degradation of mRNAs Lacking a Termination Codon
van Hoof, A., Frischmeyer, P. A., Dietz, H. C., & Parker, R. (2002) · Science · doi:10.1126/science.1067272 · Cited by 592 · see citing works
An mRNA Surveillance Mechanism That Eliminates Transcripts Lacking Termination Codons
Frischmeyer, P. A., van Hoof, A., O’Donnell, K. A., Guerrerio, A. L., Parker, R., & Dietz, H. C. (2002) · Science · doi:10.1126/science.1067338 · Cited by 590 · see citing works
Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA functionPreprint
Isken, O., & Maquat, L. E. (2007) · Genes & Development · doi:10.1101/gad.1566807 · Cited by 584 · see citing works
Identification of Novel Argonaute-Associated Proteins
Meister, G., Landthaler, M., Peters, L., Chen, P., Urlaub, H., Lührmann, R., & Tuschl, T. (2005) · Current Biology · doi:10.1016/j.cub.2005.10.048 · Cited by 554 · see citing works
A faux 3′-UTR promotes aberrant termination and triggers nonsense- mediated mRNA decay
Amrani, N., Ganesan, R., Kervestin, S., Mangus, D. A., Ghosh, S., & Jacobson, A. (2004) · Nature · doi:10.1038/nature03060 · Cited by 533 · see citing works
MK2‐induced tristetraprolin:14‐3‐3 complexes prevent stress granule association and ARE‐mRNA decay
Stoecklin, G., Stubbs, T., Kedersha, N., Wax, S. D., Rigby, W. F. C., Blackwell, T. K., & Anderson, P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600163 · Cited by 518 · see citing works
Identification of a target RNA motif for RNA-binding protein HuR
de Silanes, I. L., Zhan, M., Lal, A., Yang, X., & Gorospe, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306453101 · Cited by 502 · see citing works
Alternative miRNA Biogenesis Pathways and the Interpretation of Core miRNA Pathway Mutants
Yang, J.-S., & Lai, E. C. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.024 · Cited by 498 · 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
Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1Preprint
Lykke‐Andersen, J., & Wagner, E. (2005) · Genes & Development · doi:10.1101/gad.1282305 · Cited by 482 · see citing works
Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover
Yamashita, A., Chang, T.-C., Yamashita, Y., Zhu, W., Zhong, Z., Chen, C. A., & Shyu, A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1016 · Cited by 472 · see citing works
The regulatory activity of microRNA* species has substantial influence on microRNA and 3′ UTR evolution
Okamura, K., Phillips, M. D., Tyler, D. M., Duan, H., Chou, Y.-T., & Lai, E. C. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1409 · Cited by 461 · 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
Eukaryotic mRNPs May Represent Posttranscriptional Operons
Keene, J. D., & Tenenbaum, S. A. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00559-2 · Cited by 460 · see citing works
Multiple Processing Body Factors and the ARE Binding Protein TTP Activate mRNA Decapping
Fenger-Grøn, M., Fillman, C. L., Norrild, B., & Lykke‐Andersen, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.031 · Cited by 459 · see citing works
A KH Domain RNA Binding Protein, KSRP, Promotes ARE-Directed mRNA Turnover by Recruiting the Degradation Machinery
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
SMG6 promotes endonucleolytic cleavage of nonsense mRNA in human cells
Eberle, A. B., Lykke‐Andersen, S., Mühlemann, O., & Jensen, T. H. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1530 · Cited by 430 · see citing works
GW182 interaction with Argonaute is essential for miRNA-mediated translational repression and mRNA decay
Eulálio, A., Huntzinger, E., & Izaurralde, E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1405 · Cited by 414 · see citing works
Let Me Count the Ways: Mechanisms of Gene Regulation by miRNAs and siRNAs
Wu, L., & Belasco, J. G. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.010 · Cited by 409 · 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
Identifying mRNA subsets in messenger ribonucleoprotein complexes by using cDNA arrays
Tenenbaum, S. A., Carson, C. C., Lager, P. J., & Keene, J. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.26.14085 · Cited by 397 · see citing works
Nonsense-Mediated mRNA Decay in Mammalian Cells Involves Decapping, Deadenylating, and Exonucleolytic Activities
Lejeune, F., Li, X., & Maquat, L. E. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00349-6 · Cited by 389 · see citing works
Mammalian miRNA RISC Recruits CAF1 and PABP to Affect PABP-Dependent Deadenylation
Fabian, M. R., Mathonnet, G., Sundermeier, T. R., Mathys, H., Zipprich, J. T., Svitkin, Y. V., Rivas, F. V., Jínek, M., Wohlschlegel, J. A., Doudna, J. A., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.004 · Cited by 388 · see citing works
Multifunctional deadenylase complexes diversify mRNA control
Goldstrohm, A. C., & Wickens, M. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2370 · Cited by 377 · see citing works
Isolation and characterization of a novel ribonucleoprotein particle: large structures contain a single species of small RNA.
Kedersha, N., & Rome, L. H. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.3.699 · Cited by 373 · see citing works
GW182 Proteins Directly Recruit Cytoplasmic Deadenylase Complexes to miRNA Targets
Braun, J. E., Huntzinger, E., Fauser, M., & Izaurralde, E. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.007 · Cited by 371 · see citing works
The mammalian exosome mediates the efficient degradation of mRNAs that contain AU‐rich elements
Mukherjee, D., Gao, M., O'Connor, J. P., Raijmakers, R., Pruijn, G. J. M., Lutz, C. S., & Wilusz, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.1.165 · Cited by 365 · see citing works
NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity
Chamieh, H., Ballut, L., Bonneau, F., & Hir, H. L. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1330 · Cited by 357 · 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
miRNA repression involves GW182-mediated recruitment of CCR4–NOT through conserved W-containing motifs
Chekulaeva, M., Mathys, H., Zipprich, J. T., Attig, J., Čolić, M., Parker, R., & Filipowicz, W. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2166 · Cited by 353 · see citing works
RNA Quality Control in Eukaryotes
Doma, M. K., & Parker, R. (2007) · Cell · doi:10.1016/j.cell.2007.10.041 · Cited by 345 · see citing works
Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5′ to 3′ and 3′ to 5′Preprint
Mullen, T. E., & Marzluff, W. F. (2008) · Genes & Development · doi:10.1101/gad.1622708 · Cited by 339 · see citing works
Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways
Ivanov, P. V., Gehring, N. H., Kunz, J. B., Hentze, M. W., & Kulozik, A. E. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.17 · Cited by 331 · see citing works
miRNA-mediated deadenylation is orchestrated by GW182 through two conserved motifs that interact with CCR4–NOT
Fabian, M. R., Cieplak-Rotowska, M. K., Frank, F., Morita, M., Green, J., Srikumar, T., Nagar, B., Yamamoto, T. S., Raught, B., Duchaîne, T. F., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2149 · Cited by 329 · see citing works
Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells
Höck, J., Weinmann, L., Ender, C., Rüdel, S., Kremmer, E., Raabe, M., Urlaub, H., & Meister, G. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401088 · Cited by 310 · see citing works
Upf1 Phosphorylation Triggers Translational Repression during Nonsense-Mediated mRNA Decay
Isken, O., Kim, Y. K., Hosoda, N., Mayeur, G. L., Hershey, J. W. B., & Maquat, L. E. (2008) · Cell · doi:10.1016/j.cell.2008.02.030 · Cited by 307 · see citing works
The expanding world of small RNAs
Großhans, H., & Filipowicz, W. (2008) · Nature · doi:10.1038/451414a · Cited by 305 · see citing works
Early nonsense: mRNA decay solves a translational problem
Amrani, N., Sachs, M. S., & Jacobson, A. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1942 · Cited by 287 · see citing works
The ever-increasing complexities of the exon junction complex
Tange, T. Ø., Nott, A., & Moore, M. J. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.03.012 · Cited by 274 · see citing works
The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
Liu, H., Rodgers, N. D., Jiao, X., & Kiledjian, M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf448 · Cited by 267 · see citing works
MicroRNAs Silence Gene Expression by Repressing Protein Expression and/or by Promoting mRNA DecayPreprint
BEHM-ANSMANT, I., REHWINKEL, J., & Izaurralde, E. (2006) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2006.71.013 · Cited by 261 · see citing works
Posttranslational Regulation of Tristetraprolin Subcellular Localization and Protein Stability by p38 Mitogen-Activated Protein Kinase and Extracellular Signal-Regulated Kinase Pathways
Brook, M., Tchen, C. R., Santalucı́a, T., McIlrath, J. M., Arthur, J. S. C., Saklatvala, J., & Clark, A. R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2408-2418.2006 · Cited by 250 · see citing works
p38 Mitogen-Activated Protein Kinase- and HuR-Dependent Stabilization of p21 Cip1 mRNA Mediates the G 1 /S Checkpoint
Lafarga, V., Cuadrado, A., de Silanes, I. L., Bengoechea, R., Fernández-Capetillo, Ó., & Nebreda, Á. R. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00210-09 · Cited by 242 · see citing works
Recycling of eukaryotic posttermination ribosomal complexes.
Pisarev, A., Hellen, C., & Pestova, T. (2007) · Cell · doi:10.1016/j.cell.2007.08.041 · Cited by 241 · see citing works
TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elementsPreprint
Franks, T. M., & Lykke‐Andersen, J. (2007) · Genes & Development · doi:10.1101/gad.1494707 · Cited by 240 · see citing works
Systematic Identification of C. elegans miRISC Proteins, miRNAs, and mRNA Targets by Their Interactions with GW182 Proteins AIN-1 and AIN-2
Zhang, L., Lei, D., Cheung, T. H., Dong, M., Chen, J., Sewell, A. K., Liu, X., Yates, J. R., & Han, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.014 · Cited by 238 · see citing works
p38-Dependent Phosphorylation of the mRNA Decay-Promoting Factor KSRP Controls the Stability of Select Myogenic Transcripts
Briata, P., Forcales, S. V., Ponassi, M., Corte, G., Chen, C., Karin, M., Puri, P., & Gherzi, R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.021 · Cited by 236 · 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
The Pioneer Round of Translation: Features and Functions
Maquat, L. E., Tarn, W., & Isken, O. (2010) · Cell · doi:10.1016/j.cell.2010.07.022 · Cited by 231 · see citing works
Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells
Zheng, D., Ezzeddine, N., Chen, C. A., Zhu, W., He, X., & Shyu, A. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801196 · Cited by 227 · see citing works
Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core
Tange, T. Ø., Shibuya, T., Jurica, M. S., & Moore, M. J. (2005) · RNA · doi:10.1261/rna.2155905 · Cited by 212 · see citing works
Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1
Kaygun, H., & Marzluff, W. F. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb972 · Cited by 208 · see citing works
Involvement of KSRP in the post-transcriptional regulation of human iNOS expression-complex interplay of KSRP with TTP and HuR
Linker, K., Pautz, A., Fechir, M., Hubrich, T., Greeve, J. C., & Kleinert, H. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki797 · Cited by 200 · see citing works
Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proinflammatory cytokine mRNAsPreprint
Lu, J., Sadri, N., & Schneider, R. J. (2006) · Genes & Development · doi:10.1101/gad.1467606 · Cited by 199 · see citing works
The role of AUF1 in regulated mRNA decay
Gratacós, F. M., & Brewer, G. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.26 · Cited by 199 · see citing works
Self-citation
Analysis of Turnover and Translation Regulatory RNA-Binding Protein Expression through Binding to Cognate mRNAs
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
Ago–TNRC6 triggers microRNA-mediated decay by promoting two deadenylation steps
Chen, C. A., Zheng, D., Xia, Z., & Shyu, A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1709 · Cited by 194 · see citing works
Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover studied by RNA interference
Raineri, I. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh282 · Cited by 194 · see citing works
CRD-BP Protects the Coding Region of βTrCP1 mRNA from miR-183-Mediated Degradation
Elcheva, I. A., Goswami, S., Noubissi, F. K., & Spiegelman, V. S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.007 · Cited by 192 · see citing works
The Silencing Domain of GW182 Interacts with PABPC1 To Promote Translational Repression and Degradation of MicroRNA Targets and Is Required for Target Release
Zekri, L., Huntzinger, E., Heimstädt, S., & Izaurralde, E. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01081-09 · Cited by 186 · see citing works
Tristetraprolin (TTP)-14-3-3 Complex Formation Protects TTP from Dephosphorylation by Protein Phosphatase 2a and Stabilizes Tumor Necrosis Factor-α mRNA
Sun, L., Stoecklin, G., Way, S. V., Hinkovska‐Galcheva, V., Guo, R., Anderson, P., & Shanley, T. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607347200 · Cited by 184 · see citing works
Deciphering the role of RNA-binding proteins in the post-transcriptional control of gene expression
Kishore, S., Luber, S., & Zavolan, M. (2010) · Briefings in Functional Genomics · doi:10.1093/bfgp/elq028 · Cited by 178 · see citing works
The non-coding RNA of the multidrug resistance-linked vault particle encodes multiple regulatory small RNAs
Persson, H., Kvist, A., Vallon‐Christersson, J., Medstrand, P., Borg, Å., & Rovira, C. (2009) · Nature Cell Biology · doi:10.1038/ncb1972 · Cited by 173 · see citing works
Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylasesPreprint
Funakoshi, Y., Doi, Y., Hosoda, N., Uchida, N., Osawa, M., Shimada, I., Tsujimoto, M., Suzuki, T., Katada, T., & Hoshino, S.-I. (2007) · Genes & Development · doi:10.1101/gad.1597707 · Cited by 171 · see citing works
Proximity of the poly(A)-binding protein to a premature termination codon inhibits mammalian nonsense-mediated mRNA decay
Silva, A. L., Ribeiro, P. C., Inácio, Â., Liebhaber, S. A., & Romão, L. (2008) · RNA · doi:10.1261/rna.815108 · Cited by 162 · see citing works
Characterization of human Smg5/7a: A protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1
Chiu, S.-Y., Serin, G., Ohara, O., & Maquat, L. E. (2003) · RNA · doi:10.1261/rna.2137903 · Cited by 161 · see citing works
Ubiquitin‐mediated proteolysis of HuR by heat shock
Abdelmohsen, K., Srikantan, S., Yang, X., Lal, A., Kim, H. H., Kuwano, Y., Galbán, S., Becker, K. G., Kamara, D. F., de Cabo, R., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.67 · Cited by 158 · see citing works
Nonsense-mediated mRNA decay (NMD) in animal embryogenesis: to die or not to die, that is the question
Hwang, J., & Maquat, L. E. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.03.008 · Cited by 149 · see citing works
CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells
Hosoda, N., Kim, Y. K., Lejeune, F., & Maquat, L. E. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb995 · Cited by 149 · see citing works
CCR4-NOT Deadenylates mRNA Associated with RNA-Induced Silencing Complexes in Human Cells
Piao, X., Zhang, X., Wu, L., & Belasco, J. G. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01481-09 · Cited by 144 · see citing works
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
The peptidyl-prolyl isomerase Pin1 regulates the stability of granulocyte-macrophage colony-stimulating factor mRNA in activated eosinophils
Shen, Z.-J., Esnault, S. J., & Malter, J. S. (2005) · Nature Immunology · doi:10.1038/ni1266 · Cited by 127 · see citing works
Analysis of CUGBP1 Targets Identifies GU-Repeat Sequences That Mediate Rapid mRNA Decay
Rattenbacher, B., Beisang, D. J., Wiesner, D. L., Jeschke, J. C., von Hohenberg, M., Louis, I. V.-S., & Bohjanen, P. R. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00624-10 · Cited by 123 · see citing works
Tethering KSRP, a Decay-Promoting AU-Rich Element-Binding Protein, to mRNAs Elicits mRNA Decay
Chou, C., Mulky, A., Maitra, S., Lin, W., Gherzi, R., Kappes, J. C., & Chen, C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3695-3706.2006 · Cited by 116 · see citing works
Phosphorylation of p40AUF1 Regulates Binding to A + U-rich mRNA-destabilizing Elements and Protein-induced Changes in Ribonucleoprotein Structure
Wilson, G. M., Lu, J., Sutphen, K., Suarez, Y., Sinha, S., Brewer, B. Y., Villanueva-Feliciano, E. C., Ysla, R. M., Charles, S., & Brewer, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305775200 · Cited by 114 · see citing works
Self-citation
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
Nuclear Import and Export Functions in the Different Isoforms of the AUF1/Heterogeneous Nuclear Ribonucleoprotein Protein Family
Sarkar, B., Lu, J., & Schneider, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301176200 · Cited by 111 · see citing works
Signatures of RNA binding proteins globally coupled to effective microRNA target sitesPreprint
Skanderup, A. J., Wen, J., Marks, D. S., & Krogh, A. (2010) · Genome Research · doi:10.1101/gr.103259.109 · Cited by 110 · see citing works
Tristetraprolin Regulates the Expression of the Human Inducible Nitric-Oxide Synthase Gene
Fechir, M., Linker, K., Pautz, A., Hubrich, T., Förstermann, U., Rodríguez‐Pascual, F., & Kleinert, H. (2005) · Molecular Pharmacology · doi:10.1124/mol.104.008763 · Cited by 102 · see citing works
Structural and Functional Insights into Dom34, a Key Component of No-Go mRNA Decay
Lee, H. H., Kim, Y.-S., Kim, K. H., Heo, I., Kim, S. K., Kim, O., Kim, H. K., Yoon, J., Kim, H. S., Kim, D., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.019 · Cited by 102 · see citing works
Remodeling of the pioneer translation initiation complex involves translation and the karyopherin importin βPreprint
Sato, H., & Maquat, L. E. (2009) · Genes & Development · doi:10.1101/gad.1817109 · Cited by 98 · see citing works
eIF4G is required for the pioneer round of translation in mammalian cells
Lejeune, F., Ranganathan, A. C., & Maquat, L. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb824 · Cited by 94 · see citing works
Yeast histone genes show dosage compensation
Osley, M. A., & Hereford, L. M. (1981) · Cell · doi:10.1016/0092-8674(81)90327-5 · Cited by 92 · see citing works
Structure of Yeast Dom34
Graille, M., Chaillet, M., & TILBEURGH, H. V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708224200 · Cited by 92 · see citing works
The AU-rich element mRNA decay-promoting activity of BRF1 is regulated by mitogen-activated protein kinase-activated protein kinase 2
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
BRF1 Protein Turnover and mRNA Decay Activity Are Regulated by Protein Kinase B at the Same Phosphorylation Sites
Benjamin, D., Schmidlin, M., Lu, M., Gross, B., & Moroni, C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01099-06 · Cited by 91 · see citing works
The Polypyrimidine Tract-binding Protein (PTB) Is Involved in the Post-transcriptional Regulation of Human Inducible Nitric Oxide Synthase Expression
Pautz, A., Linker, K., Hubrich, T., Korhonen, R., Altenhöfer, S., & Kleinert, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603915200 · Cited by 87 · see citing works
Global analysis of the mammalian RNA degradome reveals widespread miRNA-dependent and miRNA-independent endonucleolytic cleavage
Bracken, C. P., Szubert, J. M., Mercer, T. R., Dinger, M. E., Thomson, D. W., Mattick, J. S., Michael, M., & Goodall, G. J. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr110 · Cited by 87 · 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
CRD-BP shields c-myc and MDR-1 RNA from endonucleolytic attack by a mammalian endoribonuclease
Sparanese, D. S., & Lee, C. H. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkl1148 · Cited by 84 · see citing works
The Expanding Universe of Noncoding RNAsPreprint
Hannon, G. J., Rivas, F. V., Murchison, E. P., & STEITZ, J. A. (2006) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2006.71.064 · Cited by 78 · see citing works
Chaperone Hsp27, a Novel Subunit of AUF1 Protein Complexes, Functions in AU-Rich Element-Mediated mRNA Decay
Sinsimer, K. S., Gratacós, F. M., Knapinska, A. M., Lu, J., Krause, C. D., Wierzbowski, A. V., Maher, L. R., Scrudato, S., Rivera, Y. M., Gupta, S., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00431-08 · Cited by 76 · see citing works
Self-citation
Assembly of AUF1 with eIF4G–poly(A) binding protein complex suggests a translation function in AU-rich mRNA decay
Lu, J., Bergman, N., Sadri, N., & Schneider, R. J. (2006) · RNA · doi:10.1261/rna.2308106 · Cited by 75 · see citing works
Endogenous ribosomal frameshift signals operate as mRNA destabilizing elements through at least two molecular pathways in yeast
Belew, A. T., Advani, V. M., & Dinman, J. D. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1220 · Cited by 74 · see citing works
Polyamines Regulate the Stability of JunD mRNA by Modulating the Competitive Binding of Its 3′ Untranslated Region to HuR and AUF1
Zou, T., Rao, J. N., Liu, L., Xiao, L., Yu, T., Jiang, P., Gorospe, M., & Wang, J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00807-10 · Cited by 74 · see citing works
Alternatively Expressed Domains of AU-rich Element RNA-binding Protein 1 (AUF1) Regulate RNA-binding Affinity, RNA-induced Protein Oligomerization, and the Local Conformation of Bound RNA Ligands
Zucconi, B. E., Ballin, J. D., Brewer, B. Y., Ross, C. R., Huang, J. S., Toth, E. A., & Wilson, G. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.180182 · Cited by 72 · see citing works
Molecular Requirements for RNA-induced Silencing Complex Assembly in the Drosophila RNA Interference Pathway
Pham, J. W., & Sontheimer, E. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509202200 · Cited by 71 · see citing works
Identification of a signature motif in target mRNAs of RNA-binding protein AUF1
Mazan-Mamczarz, K., Kuwano, Y., Zhan, M., White, E. J., Martindale, J. L., Lal, A., & Gorospe, M. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn929 · Cited by 71 · see citing works
Chaperone Hsp27 Modulates AUF1 Proteolysis and AU-Rich Element-Mediated mRNA Degradation
Knapinska, A. M., Gratacós, F. M., Krause, C. D., Hernandez, K. O., Jensen, A. G., Bradley, J. J., Wu, X., Pestka, S., & Brewer, G. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00907-10 · Cited by 63 · see citing works
Self-citation
Circadian Amplitude of Cryptochrome 1 Is Modulated by mRNA Stability Regulation via Cytoplasmic hnRNP D Oscillation
Woo, K., Ha, D.-C., Lee, K., Kim, D., Kim, T., & Kim, K. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01154-09 · Cited by 60 · see citing works
Expression of Noncoding Vault RNA in Human Malignant Cells and Its Importance in Mitoxantrone Resistance
Gopinath, S. C. B., Wadhwa, R., & Kumar, P. K. R. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-10-0242 · Cited by 60 · see citing works
Characterization of 3′hExo, a 3′ Exonuclease Specifically Interacting with the 3′ End of Histone mRNA
Yang, X.-C., Purdy, M. M., Marzluff, W. F., & Domiński, Z. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602947200 · Cited by 58 · see citing works
Human INT6/eIF3e is required for nonsense‐mediated mRNA decay
Morris, C., Wittmann, J., Jäck, H., & Jalinot, P. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400955 · Cited by 58 · see citing works
Characterization of the Interaction between Neuronal RNA-binding Protein HuD and AU-rich RNA
Park-Lee, S., Kim, S., & Laird‐Offringa, I. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307105200 · Cited by 51 · see citing works
A "liaison dangereuse" between AUF1/hnRNPD and the oncogenic tyrosine kinase NPM-ALK
Fawal, M.-A., Armstrong, F., Ollier, S., Dupont, H., Touriol, C., Monsarrat, B., Delsol, G., Payrastre, B., & Morello, D. (2006) · Blood · doi:10.1182/blood-2006-04-014902 · Cited by 49 · see citing works
Perturbation of thymocyte development in nonsense-mediated decay (NMD)-deficient mice
Frischmeyer‐Guerrerio, P. A., Montgomery, R. A., Warren, D. S., Cooke, S. K., Lutz, J., Sonnenday, C. J., Guerrerio, A. L., & Dietz, H. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019352108 · Cited by 49 · see citing works
Two separate regions essential for nuclear import of the hnRNP D nucleocytoplasmic shuttling sequence
Suzuki, M., Iijima, M., Nishimura, A., Tomozoe, Y., Kamei, D., & Yamada, M. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04820.x · Cited by 47 · see citing works
14‐3‐3σ is a p37 AUF1‐binding protein that facilitates AUF1 transport and AU‐rich mRNA decay
He, C., & Schneider, R. J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601264 · Cited by 46 · see citing works
Skiing Toward Nonstop mRNA Decay
Maquat, L. E. (2002) · Science · doi:10.1126/science.1071285 · Cited by 45 · see citing works
MicroRNA Modulation of RNA-Binding Protein Regulatory Elements
George, A. D., & Tenenbaum, S. A. (2006) · RNA Biology · doi:10.4161/rna.3.2.3250 · Cited by 43 · see citing works
Polysome-Bound Endonuclease PMR1 Is Targeted to Stress Granules via Stress-Specific Binding to TIA-1
Yang, F., Peng, Y., Murray, E. L., Otsuka, Y., Kedersha, N., & Schoenberg, D. R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00090-06 · Cited by 40 · see citing works
AUF1 Cell Cycle Variations Define Genomic DNA Methylation by Regulation of DNMT1 mRNA Stability
Torrisani, J., Unterberger, A., Tendulkar, S. R., Shikimi, K., & Moshe Szyf, A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01236-06 · Cited by 39 · see citing works
Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome
Anderson, J. R., Mukherjee, D., Muthukumaraswamy, K., Moraes, K. C. M., Wilusz, C. J., & Wilusz, J. (2006) · RNA · doi:10.1261/rna.144606 · Cited by 38 · see citing works
A cell type–restricted mRNA surveillance pathway triggered by ribosome extension into the 3′ untranslated region
Kong, J., & Liebhaber, S. A. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1256 · Cited by 37 · see citing works
Similar Regulation of Human Inducible Nitric-oxide Synthase Expression by Different Isoforms of the RNA-binding Protein AUF1
Pautz, A., Linker, K., Altenhöfer, S., Heil, S., Schmidt, N., Art, J., Knauer, S. K., Stauber, R. H., Sadri, N., Pont, A. R., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m809314200 · Cited by 36 · see citing works
Human UPF1 Participates in Small RNA-Induced mRNA Downregulation
Jin, H., Suh, M. R., Han, J., Yeom, K., Lee, Y., Heo, I., Ha, M., Hyun, S., & Kim, V. N. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00653-09 · Cited by 35 · see citing works
Functional dissection of hnRNP D suggests that nuclear import is required before hnRNP D can modulate mRNA turnover in the cytoplasm
Chen, C. A., Xu, N., Zhu, W., & Shyu, A. (2004) · RNA · doi:10.1261/rna.5269304 · Cited by 34 · see citing works
Endonuclease-mediated mRNA Decay Requires Tyrosine Phosphorylation of Polysomal Ribonuclease 1 (PMR1) for the Targeting and Degradation of Polyribosome-bound Substrate mRNA
Yang, F., Peng, Y., & Schoenberg, D. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409776200 · Cited by 28 · see citing works
Genome-wide regulatory analysis using en masse nuclear run-ons emRUNs and ribonomic profiling with autoimmune sera
Tenenbaum, S. A., Carson, C. C., Atasoy, U., & Keene, J. D. (2003) · Gene · doi:10.1016/s0378-1119(03)00661-9 · Cited by 27 · see citing works
“Alu”strious long ncRNAs and their roles in shortening mRNA half-lives
Gong, C., & Maquat, L. E. (2011) · Cell Cycle · doi:10.4161/cc.10.12.15589 · Cited by 26 · see citing works
The ARE-associated factor AUF1 binds poly(A) in vitro in competition with PABP
Sagliocco, F. A., Laloo, B., Cosson, B., Laborde, L., Castroviejo, M., Rosenbaum, J., Ripoche, J., & Grosset, C. F. (2006) · Biochemical Journal · doi:10.1042/bj20060328 · Cited by 21 · see citing works
Nonsense Codons Trigger an RNA Partitioning Shift
Bhalla, A. D., Gudikote, J. P., Wang, J., Chan, W.-K., Chang, Y.-F., Olivas, O. R., & Wilkinson, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805193200 · Cited by 19 · see citing works

Flagged first, then by citations

Research works printed but not linked: 2

Chang N Yi J Guo G Liu X Shang Y Tong T Cui Q Zhan M Gorospe M Wang W HuR uses AUF1 as a cofactor to promote p16INK4 mRNA decay Mol Cell Biol 30 2010 3875 86 20498276 PMC2916395
Filipowicz W Bhattacharyya SN Sonenberg N Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight? Nat Rev Genet 9 2008 102 14 18197166

Sorted by citations

Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): The next decade
Vandooren, J., den Steen, P. E. V., & Opdenakker, G. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.770819 · Cited by 767 · see citing works
Untitled work
Seidah (2014) · doi:10.1161/circresaha.114.301621 · Cited by 596 · see citing works
Sequence, Structure, and Context Preferences of Human RNA Binding Proteins
Dominguez, D., Freese, P., Alexis, M. S., Su, A., Hochman, M., Palden, T., Bazile, C., Lambert, N. J., Van Nostrand, E. L., Pratt, G. A., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.001 · Cited by 562 · see citing works
Protein Aggregation Capture on Microparticles Enables Multipurpose Proteomics Sample Preparation*
Batth, T. S., Tollenaere, M. A. X., Rüther, P. L., González-Franquesa, A., Prabhakar, B. S., Bekker‐Jensen, S., Deshmukh, A. S., & Olsen, J. V. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.001270 · Cited by 448 · see citing works
The challenge and prospect of mRNA therapeutics landscape
Weng, Y., Li, C., Yang, T., Hu, B., Zhang, M., Guo, S., Xiao, H., Liang, X.-J., & Huang, Y. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107534 · Cited by 417 · see citing works
Nanotechnologies in delivery of mRNA therapeutics using nonviral vector-based delivery systems
Guan, S., & Rosenecker, J. (2017) · Gene Therapy · doi:10.1038/gt.2017.5 · Cited by 389 · see citing works
Luteolin: A Flavonoid that Has Multiple Cardio-Protective Effects and Its Molecular Mechanisms
Luo, Y., Shang, P., & Li, D. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00692 · Cited by 278 · see citing works
Interleukin-17 enhances immunosuppression by mesenchymal stem cells
Han, X., Yang, Q., Lin, L., Xu, C., Zheng, C., Chen, X., Han, Y., Li, M., Cao, W., Cao, K., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.85 · Cited by 189 · see citing works
Self-citation
Biomaterials for mRNA delivery
Islam, M. A., Reesor, E. K. G., Xu, Y., Zope, H. R., Zetter, B. R., & Shi, J. (2015) · Biomaterials Science · doi:10.1039/c5bm00198f · Cited by 176 · see citing works
Molecular and tissue alterations of collagens in fibrosis
Ricard‐Blum, S., Baffet, G., & Théret, N. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.02.004 · Cited by 170 · see citing works
The Role of lncRNAs in Gene Expression Regulation through mRNA Stabilization
Sebastian‐delaCruz, M., González‐Moro, I., Olazagoitia‐Garmendia, A., Castellanos–Rubio, A., & Santín, I. (2021) · Non-Coding RNA · doi:10.3390/ncrna7010003 · Cited by 169 · see citing works
Specificity factors in cytoplasmic polyadenylation
Charlesworth, A. G., Meijer, H. A., & de Moor, C. H. (2013) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1171 · Cited by 160 · see citing works
LARP1 post-transcriptionally regulates mTOR and contributes to cancer progression
Mura, M., Hopkins, T. G., Michael, T., Latip, N. A., Weir, J., Aboagye, E. O., Mauri, F. A., Jameson, C., Sturge, J., Gabra, H., et al. (2014) · Oncogene · doi:10.1038/onc.2014.428 · Cited by 146 · see citing works
Protein Regulation in Signal TransductionPreprint
Lee, M. J., & Yaffe, M. B. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005918 · Cited by 148 · see citing works
Eukaryotic mRNA Decay: Methodologies, Pathways, and Links to Other Stages of Gene Expression
Pérez-Ortín, J. E., Alepuz, P. M., Chávez, S., & Choder, M. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.029 · Cited by 142 · see citing works
Nucleic acid degradation as barrier to gene delivery: a guide to understand and overcome nuclease activity
Zhang, H., Vandesompele, J., Braeckmans, K., Smedt, S. C. D., & Remaut, K. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00194f · Cited by 140 · see citing works
mRNA nanomedicine: Design and recent applications
Kubiatowicz, L. J., Mohapatra, A., Krishnan, N., Fang, R. H., & Zhang, L. (2022) · Exploration · doi:10.1002/exp.20210217 · Cited by 130 · see citing works
Post-transcriptional control of gene expression by AUF1: Mechanisms, physiological targets, and regulation
White, E. J., Brewer, G., & Wilson, G. M. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.12.002 · Cited by 128 · see citing works
Self-citation
Cytoplasmic functions of TDP-43 and FUS and their role in ALS
Birsa, N., Bentham, M. P., & Fratta, P. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.023 · Cited by 127 · see citing works
Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction
Bronicki, L. M., & Jasmin, B. J. (2013) · RNA · doi:10.1261/rna.039164.113 · Cited by 126 · see citing works
The potential of circulating cell-free RNA as a cancer biomarker: challenges and opportunities
Zaporozhchenko, I. A., Ponomaryova, A. A., RYKOVA, E. Y., & Laktionov, P. P. (2018) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2018.1425143 · Cited by 118 · see citing works
The Hippo Pathway Prevents YAP/TAZ-Driven Hypertranscription and Controls Neural Progenitor Number
Lavado, A., Park, J. Y., Paré, J., Finkelstein, D., Pan, H., Xu, B., Fan, Y., Kumar, R. P., Neale, G. A. M., Kwak, Y. D., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.09.021 · Cited by 114 · see citing works
AUF1 regulation of coding and noncoding RNA
White, E. J., Matsangos, A. E., & Wilson, G. M. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1393 · Cited by 106 · see citing works
The fate of the messenger is pre-determined: A new model for regulation of gene expression
Haimovich, G., Choder, M., Singer, R. H., & Trcek, T. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.01.004 · Cited by 103 · see citing works
Genome-wide analysis reveals a switch in the translational program upon oocyte meiotic resumption
Luong, X. G., Daldello, E. M., Rajkovic, G., Yang, C., & Conti, M. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa010 · Cited by 98 · see citing works
ScanFold: an approach for genome-wide discovery of local RNA structural elements—applications to Zika virus and HIV
Andrews, R. J., Roche, J., & Moss, W. N. (2018) · PeerJ · doi:10.7717/peerj.6136 · Cited by 94 · see citing works
Fates of Retroviral Core Components during Unrestricted and TRIM5-Restricted Infection
Kutluay, S. B., Pérez-Caballero, D., & Bieniasz, P. D. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003214 · Cited by 92 · see citing works
Nanoparticle technology for mRNA: Delivery strategy, clinical application and developmental landscape
Li, X., Qi, J., Wang, J., Hu, W., Zhou, W., Wang, Y., & Li, T. (2024) · Theranostics · doi:10.7150/thno.84291 · Cited by 96 · see citing works
Progesterone Directly and Rapidly Inhibits GnRH Neuronal Activity via Progesterone Receptor Membrane Component 1
Bashour, N. M., & Wray, S. (2012) · Endocrinology · doi:10.1210/en.2012-1122 · Cited by 88 · see citing works
A GC-rich sequence feature in the 3′ UTR directs UPF1-dependent mRNA decay in mammalian cellsPreprint
Imamachi, N., Salam, K. A., Suzuki, Y., & Akimitsu, N. (2016) · Genome Research · doi:10.1101/gr.206060.116 · Cited by 88 · see citing works
Identification of IL-34 in teleost fish: Differential expression of rainbow trout IL-34, MCSF1 and MCSF2, ligands of the MCSF receptor
Wang, T., Kono, T., Monte, M. M., Kuse, H., Costa, M. M., Korenaga, H., Maehr, T., Husain, M., Sakai, M., & Secombes, C. J. (2012) · Molecular Immunology · doi:10.1016/j.molimm.2012.09.008 · Cited by 84 · see citing works
Poly(ADP-ribose) polymerase-13 and RNA regulation in immunity and cancer
Kwan, T. T., Bock, F. J., & Chang, P. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.03.002 · Cited by 76 · see citing works
Pre-mRNA processing includes N6 methylation of adenosine residues that are retained in mRNA exons and the fallacy of “RNA epigenetics”
Darnell, R. B., Ke, S., & Darnell, J. E., Jr. (2017) · RNA · doi:10.1261/rna.065219.117 · Cited by 78 · see citing works
The coral immune response facilitates protection against microbes during tissue regeneration
van de Water, J. A. J. M., Ainsworth, T. D., Leggat, W. P., Bourne, D. G., Willis, B. L., & van Oppen, M. J. H. (2015) · Molecular Ecology · doi:10.1111/mec.13257 · Cited by 76 · see citing works
CCAR1 5′ UTR as a natural miRancer of miR-1254 overrides tamoxifen resistance
Li, G., Wu, X., Qian, W., Cai, H., Sun, X., Zhang, W., Tan, S. H., Wu, Z., Qian, P., Ding, K., et al. (2016) · Cell Research · doi:10.1038/cr.2016.32 · Cited by 76 · see citing works
Self-citation
HDAC Inhibition Induces MicroRNA-182, which Targets RAD51 and Impairs HR Repair to Sensitize Cells to Sapacitabine in Acute Myelogenous Leukemia
Lai, T.-H., Ewald, B., Zecevic, A., Liu, C., Sulda, M. L., Papaioannou, D., Garzon, R., Blachly, J. S., Plunkett, W. K., & Sampath, D. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1063 · Cited by 74 · see citing works
Functional and molecular insights into KSRP function in mRNA decay
Briata, P., Chen, C., Ramos, A., & Gherzi, R. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.11.003 · Cited by 73 · see citing works
Transcriptome analysis reveals sexual disparities in gene expression in rat brain microvessels
Chandra, P. K., Čikić, S., Baddoo, M., Rutkai, I., Guidry, J. J., Flemington, E. K., Katakam, P. V. G., & Busija, D. W. (2021) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x21999553 · Cited by 70 · see citing works
Messenger RNA (mRNA) nanoparticle tumour vaccination
Phua, K. K. L., Nair, S. K., & Leong, K. W. (2014) · Nanoscale · doi:10.1039/c4nr01346h · Cited by 70 · see citing works
Decoupling the impact of microRNAs on translational repression versus RNA degradation in embryonic stem cells
Freimer, J. W., Hu, T., & Blelloch, R. (2018) · eLife · doi:10.7554/elife.38014 · Cited by 69 · see citing works
Poly(A)-specific ribonuclease (PARN): An allosterically regulated, processive and mRNA cap-interacting deadenylase
Virtanen, A., Henriksson, N., Nilsson, P., & Nissbeck, M. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.771132 · Cited by 68 · see citing works
Injectable Biodegradable Chitosan‐Alginate 3D Porous Gel Scaffold for mRNA Vaccine Delivery
Yan, J., Chen, R., Zhang, H., & Bryers, J. D. (2018) · Macromolecular Bioscience · doi:10.1002/mabi.201800242 · Cited by 68 · see citing works
Competing Interactions of RNA-Binding Proteins, MicroRNAs, and Their Targets Control Neuronal Development and Function
Gardiner, A. S., Twiss, J. L., & Perrone‐Bizzozero, N. I. (2015) · Biomolecules · doi:10.3390/biom5042903 · Cited by 65 · see citing works
PHLPP2 Downregulation Contributes to Lung Carcinogenesis Following B[a]P/B[a]PDE Exposure
Huang, H., Pan, X., Jin, H., Li, Y., Zhang, L., Yang, C., Liu, P., Liu, Y., Chen, L., Li, J., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2829 · Cited by 65 · see citing works
Hsp70 Is a Novel Posttranscriptional Regulator of Gene Expression That Binds and Stabilizes Selected mRNAs Containing AU-Rich Elements
Kishor, A., Tandukar, B., Ly, Y. V., Toth, E. A., Suarez, Y., Brewer, G., & Wilson, G. M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.01275-12 · Cited by 65 · see citing works
Self-citation
MicroRNA Stability in FFPE Tissue Samples: Dependence on GC Content
Kakimoto, Y., Tanaka, M., Kamiguchi, H., Ochiai, E., & Osawa, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163125 · Cited by 65 · see citing works
Antiproliferative protein Tob directly regulates c-myc proto-oncogene expression through cytoplasmic polyadenylation element-binding protein CPEB
Ogami, K., Hosoda, N., Funakoshi, Y., & Hoshino, S.-I. (2012) · Oncogene · doi:10.1038/onc.2012.548 · Cited by 60 · see citing works
Integrase-RNA interactions underscore the critical role of integrase in HIV-1 virion morphogenesis
Elliott, J. L., Eschbach, J. E., Koneru, P. C., Li, W., Puray-Chavez, M., Townsend, D., Lawson, D. Q., Engelman, A. N., Kvaratskhelia, M., & Kutluay, S. B. (2020) · eLife · doi:10.7554/elife.54311 · Cited by 59 · see citing works
Long Non-Coding RNA-Ribonucleoprotein Networks in the Post-Transcriptional Control of Gene Expression
Briata, P., & Gherzi, R. (2020) · Non-Coding RNA · doi:10.3390/ncrna6030040 · Cited by 55 · see citing works
Advanced Biomaterials for Cell‐Specific Modulation and Restore of Cancer Immunotherapy
Ruan, S., Huang, Y., He, M., & Gao, H. (2022) · Advanced Science · doi:10.1002/advs.202200027 · Cited by 54 · see citing works
Histone Hypervariants H2A.Z.1 and H2A.Z.2 Play Independent and Context-Specific Roles in Neuronal Activity-Induced Transcription ofArc/Arg3.1and Other Immediate Early Genes
Dunn, C. J., Sarkar, P., Bailey, E. R., Farris, S., Zhao, M., Ward, J. M., Dudek, S. M., & Saha, R. N. (2017) · eNeuro · doi:10.1523/eneuro.0040-17.2017 · Cited by 55 · see citing works
Mutations in DCPS and EDC3 in autosomal recessive intellectual disability indicate a crucial role for mRNA decapping in neurodevelopment
Ahmed, I., Buchert, R., Zhou, M., Jiao, X., Mittal, K., Sheikh, T. I., Scheller, U., Vasli, N., Rafiq, M., Brohi, M. Q., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv069 · Cited by 54 · see citing works
Azithromycin decreases NALP3 mRNA stability in monocytes to limit inflammasome-dependent inflammation
Lendermon, E. A., Coon, T. A., Bednash, J. S., Weathington, N. M., McDyer, J. F., & Mallampalli, R. K. (2017) · Respiratory Research · doi:10.1186/s12931-017-0608-8 · Cited by 53 · see citing works
TDP-43 regulatesβ-adducin(Add2) transcript stability
Costessi, L., Porro, F., Iaconcig, A., & Muro, A. F. (2014) · RNA Biology · doi:10.1080/15476286.2014.996081 · Cited by 50 · see citing works
Pat1 contributes to the RNA binding activity of the Lsm1-7–Pat1 complex
Chowdhury, A. K., Kalurupalle, S., & Tharun, S. (2014) · RNA · doi:10.1261/rna.045252.114 · Cited by 50 · see citing works
KSHV ORF57, a Protein of Many Faces
Majerčiak, V., & Zheng, Z. (2015) · Viruses · doi:10.3390/v7020604 · Cited by 49 · see citing works
RNA processing in the male germline: Mechanisms and implications for fertility
Legrand, J. M. D., & Hobbs, R. M. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.10.006 · Cited by 49 · see citing works
Transcriptional and post-transcriptional controls for tuning gene expression in plants
Zhong, V., Archibald, B. N., & Brophy, J. A. N. (2022) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2022.102315 · Cited by 48 · see citing works
Pegylated IFN-α regulates hepatic gene expression through transient Jak/STAT activation
Dill, M. T., Makowska, Z., Trincucci, G., Gruber, A. J., Vogt, J. E., Sinnreich, M. F., Calabrese, D., Krol, I., Lau, D., Terracciano, L., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci70408 · Cited by 48 · see citing works
Going beyond Integration: The Emerging Role of HIV-1 Integrase in Virion Morphogenesis
Elliott, J. L., & Kutluay, S. B. (2020) · Viruses · doi:10.3390/v12091005 · Cited by 46 · see citing works
Interplay between viruses and host mRNA degradation
Narayanan, K., & Makino, S. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.12.003 · Cited by 44 · see citing works
Enhanced production of L-sorbose from D-sorbitol by improving the mRNA abundance of sorbitol dehydrogenase in Gluconobacter oxydansWSH-003
Xu, S., Wang, X., Du, G., Zhou, J., & Chen, J. (2014) · Microbial Cell Factories · doi:10.1186/s12934-014-0146-8 · Cited by 44 · see citing works
New compound ChlA-F induces autophagy-dependent anti-cancer effect via upregulating Sestrin-2 in human bladder cancer
Hua, X., Xu, J., Deng, X., Xu, J., Li, J., Zhu, D., Zhu, J., Jin, H., Tian, Z., Huang, H., et al. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.08.013 · Cited by 44 · see citing works
Emerging roles for ribonucleoprotein modification and remodeling in controlling RNA fate
Lee, S. R., & Lykke‐Andersen, J. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.05.001 · Cited by 43 · see citing works
Hypoxic Effects on Matrix Metalloproteinases’ Expression in the Tumor Microenvironment and Therapeutic Perspectives
González-Ávila, G., Sommer, B., Flores‐Soto, E., & Aquino‐Gálvez, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242316887 · Cited by 42 · see citing works
Luteolin Inhibits Inflammatory Responses via p38/MK2/TTP-mediated mRNA Stability
Wu, W., Li, D., Zong, Y., Zhu, H., Pan, D., Xu, T., Wang, T., & Wang, T. (2013) · Molecules · doi:10.3390/molecules18078083 · Cited by 42 · see citing works
Combinatorial mRNA binding by AUF1 and Argonaute 2 controls decay of selected target mRNAs
Wu, X., Chesoni, S., Rondeau, G., Tempesta, C., Patel, R., Charles, S., Daginawala, N., Zucconi, B. E., Kishor, A., Xu, G., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gks1453 · Cited by 41 · see citing works
Self-citation
MiR 20a,-20b and -200c are involved in hydrogen sulfide stimulation of VEGF production in human placental trophoblasts
Hu, T., Wang, G., Guo, X.-J., Sun, Q., He, P., Gu, H., Huang, Y., Gao, L., & Ni, X. (2016) · Placenta · doi:10.1016/j.placenta.2016.01.019 · Cited by 42 · see citing works
Competition and collaboration between RNA ‐binding proteins and microRNAs
Ho, J. J. D., & Marsden, P. A. (2013) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1197 · Cited by 40 · see citing works
Emerging roles for microRNA in the regulation of Drosophila circadian clock
Xue, Y., & Zhang, Y. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0401-8 · Cited by 41 · see citing works
mRNA Decay Factor AUF1 Binds the Internal Ribosomal Entry Site of Enterovirus 71 and Inhibits Virus Replication
Lin, J., Li, M.-L., & Brewer, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103827 · Cited by 40 · see citing works
Self-citation
Amplified Host Defense by Toll-Like Receptor-Mediated Downregulation of the Glucocorticoid-Induced Leucine Zipper (GILZ) in Macrophages
Hoppstädter, J., Diesel, B., Linnenberger, R., Hachenthal, N., Flamini, S., Minet, M., Leidinger, P., Backes, C., Grässer, F. A., Meese, E. U., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2018.03111 · Cited by 39 · see citing works
Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions
Kishor, A., White, E. J., Matsangos, A. E., Yan, Z., Tandukar, B., & Wilson, G. M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.785394 · Cited by 38 · see citing works
Elevated seawater temperatures have a limited impact on the coral immune response following physical damage
van de Water, J. A. J. M., Leggat, W. P., Bourne, D. G., van Oppen, M. J. H., Willis, B. L., & Ainsworth, T. D. (2015) · Hydrobiologia · doi:10.1007/s10750-015-2243-z · Cited by 37 · see citing works
Long noncoding RNAs in cell differentiation and pluripotency
Chen, L., & Zhang, S. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2451-5 · Cited by 36 · see citing works
Mechanisms and Functions of the RNA Polymerase II General Transcription Machinery during the Transcription Cycle
Archuleta, S. R., Goodrich, J. A., & Kugel, J. F. (2024) · Biomolecules · doi:10.3390/biom14020176 · Cited by 35 · see citing works
A novel cantharidin analog N-Benzylcantharidinamide reduces the expression of MMP-9 and invasive potentials of Hep3B via inhibiting cytosolic translocation of HuR
Lee, J., Chung, T., Choi, H., Lee, C. H., Eun, J. S., Han, Y. T., Choi, J., Kim, S., Han, C., Jeong, H.-S., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.035 · Cited by 35 · see citing works
MicroRNAs and lncRNAs in senescence: A re‐view
Bischof, O., & Martínez‐Zamudio, R. I. (2015) · IUBMB Life · doi:10.1002/iub.1373 · Cited by 34 · see citing works
Allosteric HIV-1 Integrase Inhibitors Lead to Premature Degradation of the Viral RNA Genome and Integrase in Target Cells
Madison, M. K., Lawson, D. Q., Elliott, J. L., Ozantürk, A. N., Koneru, P. C., Townsend, D., Errando, M., Kvaratskhelia, M., & Kutluay, S. B. (2017) · Journal of Virology · doi:10.1128/jvi.00821-17 · Cited by 34 · see citing works
C-C motif chemokine ligand (CCL) production in equine peripheral blood mononuclear cells identified by newly generated monoclonal antibodies
Schnabel, C. L., Wemette, M., Babasyan, S., Freer, H., Baldwin, C. L., & Wagner, B. (2018) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2018.09.003 · Cited by 34 · see citing works
HDAC6 involves in regulating the lncRNA-microRNA-mRNA network to promote the proliferation of glioblastoma cells
Wu, A.-C., Yang, W., Chang, K., Lee, J., Liou, J., Su, R.-Y., Cheng, S. M., Hwang, D., Kikkawa, U., Hsu, T., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02257-w · Cited by 34 · see citing works
A genomic region transcribed into a long noncoding RNA interacts with the Prss42/Tessp‐2 promoter in spermatocytes during mouse spermatogenesis, and its flanking sequences can function as enhancers
Yoneda, R., Satoh, Y., Yoshida, I., Kawamura, S., Kotani, T., & Kimura, A. P. (2016) · Molecular Reproduction and Development · doi:10.1002/mrd.22650 · Cited by 34 · see citing works
Effects of growth differentiation factor-9 and FSH on in vitro development, viability and mRNA expression in bovine preantral follicles
de Vasconcelos, G. L., Saraiva, M. V. A., Costa, J. J. N., Passos, M. J., Silva, A. W. B., Rossi, R. O. D. S., Portela, A. M. L. R., Duarte, A. B. G., Magalhães-Padilha, D. M., Campello, C. C., et al. (2012) · Reproduction Fertility and Development · doi:10.1071/rd12173 · Cited by 31 · see citing works
Signaling pathways that control mRNA turnover
Thapar, R., & Denmon, A. P. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.03.026 · Cited by 31 · see citing works
Hsp27 and F-Box Protein β-TrCP Promote Degradation of mRNA Decay Factor AUF1
Li, M., Defren, J., & Brewer, G. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00931-12 · Cited by 31 · see citing works
Self-citation
mRNA-based modalities for infectious disease management
Zhang, M., Hussain, A., Yang, H., Zhang, J., Liang, X., & Huang, Y. (2022) · Nano Research · doi:10.1007/s12274-022-4627-5 · Cited by 33 · see citing works
The pregnant myometrium is epigenetically activated at contractility-driving gene loci prior to the onset of labor in mice
Shchuka, V. M., Abatti, L. E., Hou, H., Khader, N., Dorogin, A., Wilson, M. D., Shynlova, O. P., & Mitchell, J. A. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000710 · Cited by 31 · see citing works
Aberrant lncRNA Expression in Multiple Myeloma
Meng, H., Han, L., Hong, C., Ding, J., & Huang, Q. (2017) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/096504017x15123872205507 · Cited by 30 · see citing works
The CCR4-NOT Complex Mediates Deadenylation and Degradation of Stem Cell mRNAs and Promotes Planarian Stem Cell Differentiation
Solana, J., Gamberi, C., Mihaylova, Y., Grosswendt, S., Chen, C., Lasko, P. F., Rajewsky, N., & Aboobaker, A. A. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1004003 · Cited by 31 · see citing works
The Polyadenosine RNA-binding Protein, Zinc Finger Cys3His Protein 14 (ZC3H14), Regulates the Pre-mRNA Processing of a Key ATP Synthase Subunit mRNA
Wigington, C. P., Morris, K. J., Newman, L. E., & Corbett, A. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.754069 · Cited by 30 · see citing works
Role of post‐transcriptional regulation of mRNA stability in renal pathophysiology: focus on chronic kidney disease
Feigerlová, E., & Battaglia-Hsu, S.-F. (2016) · The FASEB Journal · doi:10.1096/fj.201601087rr · Cited by 29 · see citing works
Identification of a Recently Active Mammalian SINE Derived from Ribosomal RNA
Longo, M. S., Brown, J., Zhang, C., O’Neill, M. J., & O'Neill, R. J. W. (2015) · Genome Biology and Evolution · doi:10.1093/gbe/evv015 · Cited by 28 · see citing works
The search for RNA-binding proteins: a technical and interdisciplinary challenge
Smith, J. M., Sandow, J. J., & Webb, A. I. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200688 · Cited by 27 · see citing works
The inflammatory regulation of TRPA1 expression in human A549 lung epithelial cells
Luostarinen, S., Hämäläinen, M., Hatano, N., Muraki, K., & Moilanen, E. (2021) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2021.102059 · Cited by 28 · see citing works
Functional proteasome complex is required for turnover of islet amyloid polypeptide in pancreatic β-cells
Bhowmick, D. C., & Jeremic, A. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002414 · Cited by 28 · see citing works
Unique IL-13Rα2/STAT3 mediated IL-13 regulation detected in lung conventional dendritic cells, 24 h post viral vector vaccination
Roy, S. B., Liu, H.-Y., Jaeson, M. I., Deimel, L. P., & Ranasinghe, C. (2020) · Scientific Reports · doi:10.1038/s41598-020-57815-z · Cited by 28 · see citing works
miR-3619-3p promotes papillary thyroid carcinoma progression via Wnt/β-catenin pathway
Yu, S., Cao, S., Hong, S., Lin, X., Guan, H., Chen, S., Zhang, Q., Lv, W., Li, Y., & Xiao, H. (2019) · Annals of Translational Medicine · doi:10.21037/atm.2019.10.71 · Cited by 27 · see citing works
Mathematical modeling of combinatorial regulation suggests that apparent positive regulation of targets by miRNA could be an artifact resulting from competition for mRNA
Nyayanit, D. A., & Gadgil, C. J. (2015) · RNA · doi:10.1261/rna.046862.114 · Cited by 26 · see citing works
Immunological quality and performance of tumor vessel-targeting CAR-T cells prepared by mRNA-EP for clinical research
Inoo, K., Inagaki, R., Fujiwara, K., Sasawatari, S., Kamigaki, T., Nakagawa, S., & Okada, N. (2016) · Molecular Therapy — Oncolytics · doi:10.1038/mto.2016.24 · Cited by 25 · see citing works
The pathogenesis of amyotrophic lateral sclerosis: Mitochondrial dysfunction, protein misfolding and epigenetics
Chen, W., Guo, L., Li, M., Wei, C., Li, S., & Xu, R. (2022) · Brain Research · doi:10.1016/j.brainres.2022.147904 · Cited by 26 · see citing works

Authors: Wu, X., & Brewer, G.
Corresponding author: Brewer, Gary
ORCID: Wu, Xiangyue
Brewer, Gary
Venue: Gene
Publisher: Elsevier BV
Published: 2012-05
Volume: 500
Issue: 1
Pages: 10-21
ISSN: 0378-1119 (ISSN-L)
DOI: 10.1016/j.gene.2012.03.021
PMC: PMC3340483
OpenAlex: W2069208087
Cited by: 239
References: 166
Citations by year: 2026: 4 · 2025: 15 · 2024: 14 · 2023: 5 · 2022: 14 · 2021: 8 · 2020: 16 · 2019: 20 · 2018: 21 · 2017: 20 · 2016: 26 · 2015: 27 · 2014: 14 · 2013: 25 · 2012: 10
FWCI: 2.24
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Gene (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Rutgers University Community Repository (Rutgers University) (submittedVersion)
Funders: National Institutes of Health
National Cancer Institute (R01CA052443)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: mRNA stability, mRNA degradation, mRNA secondary structure, non-coding RNA, RNA-binding proteins, signal transduction, gene expression regulation, mRNA levels, mammalian cells
MeSH terms: Animals, Gene Expression Regulation, Humans, RNA-Binding Proteins, RNA Stability, MicroRNAs, Metabolic Networks and Pathways

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

The regulation of mRNA stability in mammalian cells: 2.0

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks