The DOI matches its Crossref record; 119 of the 120 references it cites were found in a registry or an index.
Structural and molecular mechanisms for the control of eukaryotic 5′–3′ mRNA decay
Abstract
5'-3' RNA decay pathways are critical for quality control and regulation of gene expression. Structural and biochemical studies have provided insights into the key nucleases that carry out deadenylation, decapping, and exonucleolysis during 5'-3' decay, but detailed understanding of how these activities are coordinated is only beginning to emerge. Here we review recent mechanistic insights into the control of 5'-3' RNA decay, including coupling between translation and decay, coordination between the complexes and activities that process 5' and 3' RNA termini, conformational control of enzymatic activity, liquid phase separation, and RNA modifications.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“A sufficiently long tail (100–150 bp) is necessary to interact with poly(A) binding proteins that form complexes necessary for initiating translation11,12 and protecting the cap from degradation by decapping enzymes13.”
From mRNA vaccines for infectious diseases: principles, delivery and clinical translation (2021) · cites this paper as [13]
Citations
Cites
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,058
N6-methyladenosine-dependent regulation of messenger RNA stability
Wang, X., Lu, Z., Gomez, A., Hon, G. C., Yue, Y., Han, D., Fu, Y., Parisien, M., Dai, Q., Jia, G., et al. (2014) · Nature · doi:10.1038/nature12730 · Cited by 4,558
Dynamic RNA Modifications in Gene Expression Regulation
Roundtree, I. A., Evans, M., Pan, T., & He, C. (2017) · Cell · doi:10.1016/j.cell.2017.05.045 · Cited by 3,512
Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation
Huang, H., Weng, H., Sun, W., Qin, X., Shi, H., Wu, H., Zhao, B. S., Mesquita, A., Liu, C., Yuan, C. L., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0045-z · Cited by 2,997
Protein Phase Separation: A New Phase in Cell Biology
Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 2,001
Gene expression regulation mediated through reversible m6A RNA methylation
Fu, Y., Dominissini, D., Rechavi, G., & He, C. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3724 · Cited by 1,961
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
Towards a molecular understanding of microRNA-mediated gene silencing
Jonas, S., & Izaurralde, E. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3965 · Cited by 1,872
Du, H., Zhao, Y., He, J., Zhang, Y., Xi, H., Liu, M., Ma, J., & Wu, L. (2016) · Nature Communications · doi:10.1038/ncomms12626 · Cited by 1,500
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
Rethinking m6A Readers, Writers, and Erasers
Meyer, K. D., & Jaffrey, S. R. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100616-060758 · Cited by 1,165
Codon Optimality Is a Major Determinant of mRNA Stability
Presnyak, V., Alhusaini, N., Chen, Y.-H., Martin, S., Morris, N., Kline, N., Olson, S., Weinberg, D., Baker, K. E., Graveley, B. R., et al. (2015) · Cell · doi:10.1016/j.cell.2015.02.029 · Cited by 1,078
Self-citationReversible methylation of m6Am in the 5′ cap controls mRNA stability
Mauer, J., Luo, X., Blanjoie, A., Jiao, X., Grozhik, A. V., Patil, D. P., Linder, B., Pickering, B. F., Vasseur, J., Chen, Q., et al. (2016) · Nature · doi:10.1038/nature21022 · Cited by 1,072
From Birth to Death: The Complex Lives of Eukaryotic mRNAs
Moore, M. J. (2005) · Science · doi:10.1126/science.1111443 · Cited by 1,035
AU-rich elements and associated factors: are there unifying principles?
Barreau, C. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki1012 · Cited by 907
Nonsense-mediated mRNA decay: an intricate machinery that shapes transcriptomes
Lykke‐Andersen, S., & Jensen, T. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4063 · Cited by 843
P-Body Purification Reveals the Condensation of Repressed mRNA Regulons
Hubstenberger, A., Courel, M., Bénard, M., Souquère, S., Ernoult‐Lange, M., Chouaib, R., Zhou, Y., Morlot, J.-B., Munier, A., Fradet, M., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.003 · Cited by 808
The enzymes and control of eukaryotic mRNA turnover
Parker, R., & Song, H. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb724 · Cited by 730
P-body formation is a consequence, not the cause, of RNA-mediated gene silencing
Eulalio, A., Behm-Ansmant, I., Schweizer, D., & Izaurralde, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00128-07 · Cited by 710
P-bodies: Composition, properties and functions
Luo, Y., Na, Z., & Slavoff, S. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01162 · Cited by 538
Coller, J., & Parker, R. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074032 · Cited by 500
Self-citationTAIL-seq: Genome-wide Determination of Poly(A) Tail Length and 3′ End Modifications
Chang, H., Lim, J., Ha, M., & Kim, V. N. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.007 · Cited by 454
Slobodin, B., Han, R., Calderone, V., Vrielink, J. A. F. O., Loayza-Puch, F., Elkon, R., & Agami, R. (2017) · Cell · doi:10.1016/j.cell.2017.03.031 · Cited by 434
XRN 5′→3′ exoribonucleases: Structure, mechanisms and functions
Nagarajan, V. K., Jones, C. I., Newbury, S. F., & Green, P. J. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.03.005 · Cited by 395
RNA Degradation in Saccharomyces cerevisae
Parker, R. (2012) · Genetics · doi:10.1534/genetics.111.137265 · Cited by 377
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
The Ccr4‐Not complex is a key regulator of eukaryotic gene expression
Collart, M. A. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1332 · Cited by 362
Co-translational mRNA decay in Saccharomyces cerevisiae
Hu, W., Sweet, T. J., Chamnongpol, S., Baker, K. E., & Coller, J. M. (2009) · Nature · doi:10.1038/nature08265 · Cited by 334
Self-citationAn improved MS2 system for accurate reporting of the mRNA life cycle
Tutucci, E., Vera, M., Biswas, J., Garcia, J. F., Parker, R., & Singer, R. H. (2017) · Nature Methods · doi:10.1038/nmeth.4502 · Cited by 332
Fabian, M. R., Cieplak, M. K., Frank, F., Morita, M., Green, J., Srikumar, T., Nagar, B., Yamamoto, T., Raught, B., Duchaine, T. F., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2149 · Cited by 329
Widespread Co-translational RNA Decay Reveals Ribosome Dynamics
Pelechano, V., Wu, W., & Steinmetz, L. M. (2015) · Cell · doi:10.1016/j.cell.2015.05.008 · Cited by 319
Bazzini, A., Viso, F. D., Moreno-Mateos, M. A., Johnstone, T. G., Vejnar, C. E., Qin, Y., Yao, J., Khokha, M. K., & Giráldez, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694699 · Cited by 309
Chen, Y., Boland, A., Kuzuoğlu‐Öztürk, D., Bawankar, P., Loh, B., Chang, C.-T., Weichenrieder, O., & Izaurralde, E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.034 · Cited by 306
Target-specific requirements for enhancers of decapping in miRNA-mediated gene silencingPreprint
Eulálio, A., Rehwinkel, J., Stricker, M., Huntzinger, E., Yang, S.-F., Doerks, T., Dorner, S., Peer Bork, B., Boutros, M., & Izaurralde, E. (2007) · Genes & Development · doi:10.1101/gad.443107 · Cited by 297
The DEAD-Box Protein Dhh1p Couples mRNA Decay and Translation by Monitoring Codon Optimality
Radhakrishnan, A., Chen, Y.-H., Martin, S., Alhusaini, N., Green, R., & Coller, J. (2016) · Cell · doi:10.1016/j.cell.2016.08.053 · Cited by 297
Self-citationShort poly(A) tails are a conserved feature of highly expressed genes
Lima, S. A., Chipman, L. B., Nicholson, A. L., Chen, Y.-H., Yee, B. A., Yeo, G. W.-M., Coller, J., & Pasquinelli, A. E. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3499 · Cited by 292
Self-citationCodon Usage and 3′ UTR Length Determine Maternal mRNA Stability in Zebrafish
Mishima, Y., & Tomari, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.027 · Cited by 288
Structural basis for the recruitment of the human CCR4–NOT deadenylase complex by tristetraprolin
Fabian, M. R., Frank, F., Rouya, C., Siddiqui, N., Lai, W. S., Karetnikov, A., Blackshear, P. J., Nagar, B., & Sonenberg, N. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2572 · Cited by 273
Phase Transitions in the Assembly and Function of Human miRISC
Sheu‐Gruttadauria, J., & MacRae, I. J. (2018) · Cell · doi:10.1016/j.cell.2018.02.051 · Cited by 261
Global Analysis of Eukaryotic mRNA Degradation Reveals Xrn1-Dependent Buffering of Transcript Levels
Sun, M., Schwalb, B., Pirkl, N., Maier, K. C., Schenk, A., Failmezger, H., Tresch, A., & Cramer, P. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.010 · Cited by 260
Webster, M. W., Chen, Y.-H., Stowell, J. A. W., Alhusaini, N., Sweet, T. J., Graveley, B. R., Coller, J., & Passmore, L. A. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.033 · Cited by 258
Self-citationKretschmer, J., Rao, H., Hackert, P., Sloan, K. E., Höbartner, C., & Bohnsack, M. T. (2018) · RNA · doi:10.1261/rna.064238.117 · Cited by 252
Molecular basis for the recognition of methylated adenines in RNA by the eukaryotic YTH domain
Luo, S., & Tong, L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412742111 · Cited by 246
Decapping Activators in Saccharomyces cerevisiae Act by Multiple Mechanisms
Nissan, T. A., Rajyaguru, P. I., She, M., Song, H., & Parker, R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.025 · Cited by 245
PABP Cooperates with the CCR4-NOT Complex to Promote mRNA Deadenylation and Block Precocious Decay
Yi, H., Park, J., Ha, M., Lim, J., Chang, H., & Kim, V. N. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.009 · Cited by 242
A Transcriptome-wide Atlas of RNP Composition Reveals Diverse Classes of mRNAs and lncRNAs
Tuck, A., & Tollervey, D. W. (2013) · Cell · doi:10.1016/j.cell.2013.07.047 · Cited by 240
Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactorsPreprint
Zinder, J. C., & Lima, C. D. (2017) · Genes & Development · doi:10.1101/gad.294769.116 · Cited by 234
The Dynamics of mRNA Turnover Revealed by Single-Molecule Imaging in Single Cells
Horvathova, I., Voigt, F., Kotrys, A. V., Zhan, Y., Artus-Revel, C. G., Eglinger, J., Stadler, M. B., Giorgetti, L., & Chao, J. A. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.030 · Cited by 225
Decapping is preceded by 3′ uridylation in a novel pathway of bulk mRNA turnover
Rissland, O. S., & Norbury, C. J. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1601 · Cited by 224
Chan, L. Y., Mugler, C. F., Heinrich, S., Vallotton, P., & Weis, K. (2018) · eLife · doi:10.7554/elife.32536 · Cited by 214
Loh, B., Jonas, S., & Izaurralde, E. (2013) · Genes & Development · doi:10.1101/gad.226951.113 · Cited by 212
Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast
Sachs, A. B., & Deardorff, J. A. (1992) · Cell · doi:10.1016/0092-8674(92)90246-9 · Cited by 209
The role of disordered protein regions in the assembly of decapping complexes and RNP granulesPreprint
Jonas, S., & Izaurralde, E. (2013) · Genes & Development · doi:10.1101/gad.227843.113 · Cited by 207
Brannan, K. W., Kim, H., Erickson, B., Glover-Cutter, K. M., Kim, S., Fong, N., Kiemele, L., Hansen, K. C., Davis, R. E., Lykke‐Andersen, J., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.03.006 · Cited by 205
Nonsense‐mediated mRNA decay: novel mechanistic insights and biological impact
Karousis, E. D., Nasif, S., & Mühlemann, O. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1357 · Cited by 201
Caponigro, G., Muhlrad, D., & Parker, R. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5141 · Cited by 189
Targeted mRNA Degradation by Deadenylation-Independent Decapping
Badis, G., Saveanu, C., Fromont‐Racine, M., & Jacquier, A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.028 · Cited by 165
Structural Basis of Dcp2 Recognition and Activation by Dcp1
She, M., Decker, C. J., Svergun, D. I., Round, A. R., Chen, N., Muhlrad, D., Parker, R., & Song, H. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.01.002 · Cited by 163
Cho, H., Kim, K. M., & Kim, Y. K. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.11.022 · Cited by 161
Chowdhury, A. K., Mukhopadhyay, J., & Tharun, S. (2007) · RNA · doi:10.1261/rna.502507 · Cited by 161
Mechanistic Insights into MicroRNA-Mediated Gene SilencingPreprint
Duchaîne, T. F., & Fabian, M. R. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032771 · Cited by 156
Identification of a Human Cytoplasmic Poly(A) Nuclease Complex Stimulated by Poly(A)-binding Protein
Uchida, N., Hoshino, S.-I., & Katada, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309125200 · Cited by 151
Spatial Organization of Single mRNPs at Different Stages of the Gene Expression Pathway
Adivarahan, S., Livingston, N. M., Nicholson, B. L., Rahman, S., Wu, B., Rissland, O. S., & Zenklusen, D. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.010 · Cited by 149
Ozgur, S., Basquin, J., Kamenska, A., Filipowicz, W., Standart, N., & Conti, E. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.033 · Cited by 139
New insights into decapping enzymes and selective mRNA decay
Grudzien‐Nogalska, E., & Kiledjian, M. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1379 · Cited by 137
3′ Terminal oligo U-tract-mediated stimulation of decapping
Song, M.-G., & Kiledjian, M. (2007) · RNA · doi:10.1261/rna.765807 · Cited by 136
2′-O-methylation in mRNA disrupts tRNA decoding during translation elongation
Choi, J., Indrisiunaite, G., DeMi̇rci̇, H., Ieong, K.-W., Wang, J., Petrov, A. N., Prabhakar, A., Rechavi, G., Dominissini, D., He, C., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0030-z · Cited by 135
The structural basis of Edc3‐ and Scd6‐mediated activation of the Dcp1:Dcp2 mRNA decapping complex
Fromm, S. A., Truffault, V., Kamenz, J. L., Braun, J. E., Hoffmann, N. A., Izaurralde, E., & Sprangers, R. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.408 · Cited by 133
Connections Underlying Translation and mRNA Stability
Radhakrishnan, A., & Green, R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.05.025 · Cited by 132
The cryo-EM structure of a ribosome–Ski2-Ski3-Ski8 helicase complex
Schmidt, C. M., Kowalinski, E., Shanmuganathan, V., Defenouillère, Q., Braunger, K., Heuer, A., Pech, M., Namane, A., Berninghausen, O., Fromont‐Racine, M., et al. (2016) · Science · doi:10.1126/science.aaf7520 · Cited by 124
Chang, C.-T., Bercovich, N., Loh, B., Jonas, S., & Izaurralde, E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku129 · Cited by 122
Structural and functional control of the eukaryotic mRNA decapping machinery
Arribas-Layton, M., Wu, D., Lykke‐Andersen, J., & Song, H. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.12.006 · Cited by 120
Yu, X., Willmann, M. R., Anderson, S. J., & Gregory, B. D. (2016) · The Plant Cell · doi:10.1105/tpc.16.00456 · Cited by 120
mRNA Decapping Is Promoted by an RNA-Binding Channel in Dcp2
Deshmukh, M. V., Jones, B. N., Quang-Dang, D.-U., Flinders, J., Floor, S. N., Kim, C. J., Jemielity, J., Kałek, M., Darżynkiewicz, E., & Gross, J. D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.11.027 · Cited by 115
Self-citationContext-dependent deposition and regulation of mRNAs in P-bodies
Wang, C., Schmich, F., Srivatsa, S., Weidner, J., Beerenwinkel, N., & Spang, A. (2018) · eLife · doi:10.7554/elife.29815 · Cited by 112
Fromm, S. A., Kamenz, J. L., Nöldeke, E. R., Neu, A., Zocher, G., & Sprangers, R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201402885 · Cited by 111
Emerging roles for RNA degradation in viral replication and antiviral defense
Abernathy, E., & Glaunsinger, B. A. (2015) · Virology · doi:10.1016/j.virol.2015.02.007 · Cited by 98
Sharif, H., Ozgur, S., Sharma, K., Minard‐Basquin, C., Urlaub, H., & Conti, E. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt600 · Cited by 98
BTG/TOB factors impact deadenylases
Mauxion, F., Chen, C. A., Séraphin, B., & Shyu, A. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.008 · Cited by 97
Codon usage bias controls mRNA and protein abundance in trypanosomatids
Jeacock, L., Faria, J. R. C., & Horn, D. (2018) · eLife · doi:10.7554/elife.32496 · Cited by 97
Poly(A)-binding proteins are required for diverse biological processes in metazoans
Smith, R. W., Blee, T. K. P., & Gray, N. K. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140111 · Cited by 95
Schütz, S., Nöldeke, E. R., & Sprangers, R. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx353 · Cited by 95
Architecture of the Lsm1-7-Pat1 Complex: A Conserved Assembly in Eukaryotic mRNA Turnover
Sharif, H., & Conti, E. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.004 · Cited by 91
Cytoplasmic deadenylation: regulation of mRNA fate
Wiederhold, K., & Passmore, L. A. (2010) · Biochemical Society Transactions · doi:10.1042/bst0381531 · Cited by 91
Almeida, C. D., Scheer, H., Zuber, H., & Gagliardi, D. (2017) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1440 · Cited by 82
Structural Basis of the PNRC2-Mediated Link between mRNA Surveillance and Decapping
Lai, T., Cho, H., Liu, Z., Bowler, M. W., Piao, S., Parker, R., Kim, Y. K., & Song, H. (2012) · Structure · doi:10.1016/j.str.2012.09.009 · Cited by 80
Reconstitution of Targeted Deadenylation by the Ccr4-Not Complex and the YTH Domain Protein Mmi1
Stowell, J. A. W., Webster, M. W., Kögel, A., Wolf, J., Shelley, K. L., & Passmore, L. A. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.10.066 · Cited by 79
mRNA deadenylation by Pan2–Pan3
Wolf, J., & Passmore, L. A. (2014) · Biochemical Society Transactions · doi:10.1042/bst20130211 · Cited by 78
Eukaryotic RNA 5′-End NAD + Capping and DeNADding
Kiledjian, M. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.005 · Cited by 78
Analysis of the association between codon optimality and mRNA stability in Schizosaccharomyces pombe
Harigaya, Y., & Parker, R. (2016) · BMC Genomics · doi:10.1186/s12864-016-3237-6 · Cited by 76
Analysis of Mutations in the Yeast mRNA Decapping Enzyme
Tharun, S., & Parker, R. (1999) · Genetics · doi:10.1093/genetics/151.4.1273 · Cited by 75
Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation
Wolf, J., Valkov, E., Allen, M. D., Meineke, B., Gordiyenko, Y., McLaughlin, S. H., Olsen, T. M., Robinson, C. V., Bycroft, M., Stewart, M., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488373 · Cited by 74
Presnyak, V., & Coller, J. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.03.006 · Cited by 70
Self-citationControl of mRNA decapping by positive and negative regulatory elements in the Dcp2 C-terminal domain
He, F., & Jacobson, A. (2015) · RNA · doi:10.1261/rna.052449.115 · Cited by 70
Distinct modes of recruitment of the CCR4–NOT complex by Drosophila and vertebrate Nanos
Raisch, T., Bhandari, D., Sabath, K., Helms, S., Valkov, E., Weichenrieder, O., & Izaurralde, E. (2016) · The EMBO Journal · doi:10.15252/embj.201593634 · Cited by 70
Charenton, C., Gaudon, C., Fourati, Z., Taverniti, V., Back, R., Kolesnikova, O., Séraphin, B., & Graille, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711680114 · Cited by 64
Caponigro, G., Muhlrad, D., & Parker, R. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.9.5141-5148.1993 · Cited by 64
Structure of the active form of Dcp1–Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator
Charenton, C., Taverniti, V., Gaudon, C., Back, R., Séraphin, B., & Graille, M. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3300 · Cited by 63
The structure of the Pan2–Pan3 core complex reveals cross-talk between deadenylase and pseudokinase
Schäfer, I. B., Rode, M., Bonneau, F., Schüssler, S., & Conti, E. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2834 · Cited by 61
Structural basis of mRNA-cap recognition by Dcp1–Dcp2
Mugridge, J. S., Ziemniak, M., Jemielity, J., & Gross, J. D. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3301 · Cited by 60
Self-citation4EHP-independent repression of endogenous mRNAs by the RNA-binding protein GIGYF2
Ramirez, C. C. A., Hubbe, P., Mandel, N., & Béthune, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky198 · Cited by 60
The architecture of the Schizosaccharomyces pombe CCR4-NOT complex
Ukleja, M., Cuéllar, J., Siwaszek, A., Kasprzak, J. M., Czarnocki‐Cieciura, M., Bujnicki, J. M., Dziembowski, A., & Valpuesta, J. (2016) · Nature Communications · doi:10.1038/ncomms10433 · Cited by 59
RNA tales – how embryos read and discard messages from mom
Despic, V., & Neugebauer, K. M. (2018) · Journal of Cell Science · doi:10.1242/jcs.201996 · Cited by 56
Structure of the Dcp2–Dcp1 mRNA-decapping complex in the activated conformation
Valkov, E., Muthukumar, S., Chang, C.-T., Jonas, S., Weichenrieder, O., & Izaurralde, E. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3232 · Cited by 55
Mugridge, J. S., Tibble, R. W., Ziemniak, M., Jemielity, J., & Gross, J. D. (2018) · Nature Communications · doi:10.1038/s41467-018-03536-x · Cited by 53
Self-citationChanges in conformational equilibria regulate the activity of the Dcp2 decapping enzyme
Wurm, J. P., Holdermann, I., Overbeck, J. H., Mayer, P., & Sprangers, R. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704496114 · Cited by 52
An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay
Jonas, S., Christie, M., Peter, D., Bhandari, D., Loh, B., Huntzinger, E., Weichenrieder, O., & Izaurralde, E. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2837 · Cited by 51
Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition
Borja, M. S., Piotukh, K., Freund, C., & Gross, J. D. (2010) · RNA · doi:10.1261/rna.2382011 · Cited by 51
Self-citationCotranslational microRNA mediated messenger RNA destabilization
Tat, T. T., Maroney, P. A., Chamnongpol, S., Coller, J., & Nilsen, T. W. (2016) · eLife · doi:10.7554/elife.12880 · Cited by 50
Self-citationGeneral decapping activators target different subsets of inefficiently translated mRNAs
He, F., Celik, A., Wu, C., & Jacobson, A. (2018) · eLife · doi:10.7554/elife.34409 · Cited by 50
Sgromo, A., Raisch, T., Backhaus, C., Keskeny, C., Alva, V., Weichenrieder, O., & Izaurralde, E. (2017) · RNA · doi:10.1261/rna.064584.117 · Cited by 49
Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation
Wu, D., Muhlrad, D., Bowler, M. W., Jiang, S., Liu, Z., Parker, R., & Song, H. (2013) · Cell Research · doi:10.1038/cr.2013.152 · Cited by 47
Li, Y., Dai, J., Song, M.-G., Fitzgerald-Bocarsly, P. A., & Kiledjian, M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06328-11 · Cited by 42
Dissecting the functions of SMG5, SMG7, and PNRC2 in nonsense-mediated mRNA decay of human cells
Nicholson, P., Gkratsou, A., Josi, C., Colombo, M., & Mühlemann, O. (2018) · RNA · doi:10.1261/rna.063719.117 · Cited by 42
Control of mRNA decapping by autoinhibition
Paquette, D. R., Tibble, R. W., Daifuku, T., & Gross, J. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky233 · Cited by 39
Self-citationFloor, S. N., Borja, M. S., & Gross, J. D. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113620109 · Cited by 35
Self-citationHe, F., Li, C., Roy, B., & Jacobson, A. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01584-13 · Cited by 29
Mille viae in eukaryotic mRNA decapping
Valkov, E., Jonas, S., & Weichenrieder, O. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.05.009 · Cited by 26
Kolesnikova, O., Back, R., Graille, M., & Séraphin, B. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt607 · Cited by 22
Cited by
Sorted by citations
mRNA vaccines for infectious diseases: principles, delivery and clinical translation
Chaudhary, N., Weissman, D., & Whitehead, K. A. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00283-5 · Cited by 1,555
The emerging role of RNA modifications in the regulation of mRNA stability
Boo, S. H., & Kim, Y. K. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0407-z · Cited by 588
Opportunities and Challenges in the Delivery of mRNA-Based Vaccines
Wadhwa, A., Aljabbari, A., Lokras, A., Foged, C., & Thakur, A. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12020102 · Cited by 584
Regulation of gene expression in trypanosomatids: living with polycistronic transcription
CLAYTON, C. E. (2019) · Open Biology · doi:10.1098/rsob.190072 · Cited by 280
mRNA vaccines in disease prevention and treatment
Zhang, G., Tang, T., Chen, Y., Huang, X., & Liang, T. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01579-1 · Cited by 273
Metadata
- Authors
- Mugridge, J. S., Coller, J., & Gross, J. D.
- Affiliations
- University of California, San Francisco (US)
- Case Western Reserve University (US)
- Corresponding author
- Gross, John D.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2018-12
- Volume
- 25
- Issue
- 12
- Pages
- 1077-1085
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2901347859
- Cited by
- 133
- References
- 120
- Citations by year
- 2026: 9 · 2025: 12 · 2024: 27 · 2023: 9 · 2022: 23 · 2021: 22 · 2020: 25 · 2019: 6
- FWCI
- 1.30
- Type
- journal article
- Language
- en
- Update notices
- correction (2018-12-21)
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM080465)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- deadenylation, decapping, liquid phase separation, RNA modification, gene expression regulation, mRNA quality control
- MeSH terms
- Gene Expression Regulation, Models, Molecular, RNA, Messenger, RNA Stability
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