Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human Nuclear RNA Exosome-MTR4 Complex
Open accessAbstract
The ribonucleolytic RNA exosome interacts with RNA helicases to degrade RNA. To understand how the 3' to 5' Mtr4 helicase engages RNA and the nuclear exosome, we reconstituted 14-subunit Mtr4-containing RNA exosomes from Saccharomyces cerevisiae, Schizosaccharomyces pombe, and human and show that they unwind structured substrates to promote degradation. We loaded a human exosome with an optimized DNA-RNA chimera that stalls MTR4 during unwinding and determined its structure to an overall resolution of 3.45 Å by cryoelectron microscopy (cryo-EM). The structure reveals an RNA-engaged helicase atop the non-catalytic core, with RNA captured within the central channel and DIS3 exoribonuclease active site. MPP6 tethers MTR4 to the exosome through contacts to the RecA domains of MTR4. EXOSC10 remains bound to the core, but its catalytic module and cofactor C1D are displaced by RNA-engaged MTR4. Competition for the exosome core may ensure that RNA is committed to degradation by DIS3 when engaged by MTR4.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
EXOSC3 p.G191 is located at a key structural position at the end of the S1-domain just prior to a linker region in front of the KH-type RNA-binding domain.
“EXOSC3 p.G191 is located at a key structural position at the end of the S1-domain just prior to a linker region in front of the KH-type RNA-binding domain52.”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [52]
The Results section, “The MTR4 helicase is tethered to the exosome via EXOSC2 and MPP6” (page unavailable), identifies EXOSC3 Gly191 near the MPP6 Arg74 anchor, supporting its structural relevance. It does not locate Gly191 at the end of the S1 domain or place it before a linker and KH-type RNA-binding domain. (LLM, conf=0.86)
Experimental — accuracy not yet measuredPreviously reported structural analysis of the RNA exosome containing MTR4 and MPP6 revealed the close association of MPP6 with EXOSC3 in the cryo-EM human complex.
“Previously reported structural analysis of the RNA exosome containing both the RNA helicase MTR4 and the RNA binding protein MPP6 revealed the close association of MPP6 with EXOSC3 in the cryo-EM human complex (Fig. 6B&C, 52).”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [52]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638 · see citing works
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
<i>MolProbity</i> : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115 · see citing works
Jalview Version 2—a multiple sequence alignment editor and analysis workbench
Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M. E., & Barton, G. J. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp033 · Cited by 10,011 · see citing works
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works
MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works
Automated electron microscope tomography using robust prediction of specimen movements.
Mastronarde, D. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,446 · see citing works
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446 · see citing works
The ENCODE Project Consortium (2007) · Nature · doi:10.1038/nature05874 · Cited by 5,223 · see citing works
Quantifying the local resolution of cryo-EM density maps
Kucukelbir, A., Sigworth, F. J., & Tagare, H. D. (2013) · Nature Methods · doi:10.1038/nmeth.2727 · Cited by 1,847 · see citing works
Automated molecular microscopy: The new Leginon system
Suloway, C. J. M., Pulokas, J., Fellmann, D., Cheng, A., Guerra, F., Quispe, J. D., Stagg, S. M., Potter, C. S., & Carragher, B. O. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.03.010 · Cited by 1,681 · see citing works
Wyers, F., Rougemaille, M., Badis, G., Rousselle, J.-C., Dufour, M., Boulay, J., Regnault, B., Devaux, F., Namane, A., Séraphin, B., et al. (2005) · Cell · doi:10.1016/j.cell.2005.04.030 · Cited by 843 · see citing works
Grant, T. S., & Grigorieff, N. (2015) · eLife · doi:10.7554/elife.06980 · Cited by 840 · see citing works
Functions of the exosome in rRNA, snoRNA and snRNA synthesis
Allmang, C., Kufel, J., Chanfreau, G., Mitchell, P., Petfalski, E., & Tollervey, D. W. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5399 · Cited by 618 · see citing works
Reconstitution, Activities, and Structure of the Eukaryotic RNA Exosome
Liu, Q., Greimann, J. C., & Lima, C. D. (2006) · Cell · doi:10.1016/j.cell.2006.10.037 · Cited by 544 · see citing works
Self-citationTafforeau, L., Zorbas, C., Langhendries, J.-L., Mullineux, S.-T., Stamatopoulou, V., Mullier, R., Wacheul, L., & Lafontaine, D. L. J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.011 · Cited by 492 · see citing works
Nuclear surveillance and degradation of hypomodified initiator tRNA Met in S. cerevisiaePreprint
Kadaba, S., Krueger, A., Trice, T., Krecic, A. M., Hinnebusch, A. G., & Anderson, J. T. (2004) · Genes & Development · doi:10.1101/gad.1183804 · Cited by 487 · see citing works
RNA Exosome-Regulated Long Non-Coding RNA Transcription Controls Super-Enhancer Activity
Pefanis, E., Wang, J., Rothschild, G., Lim, J., Kazadi, D., Sun, J., Federation, A., Chao, J., Elliott, O., Liu, Z.-P., et al. (2015) · Cell · doi:10.1016/j.cell.2015.04.034 · Cited by 464 · see citing works
The regulation and functions of the nuclear RNA exosome complex
Kilchert, C., Wittmann, S., & Vasiljeva, L. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.15 · Cited by 444 · see citing works
Interaction Profiling Identifies the Human Nuclear Exosome Targeting Complex
Lubas, M., Christensen, M. S., Kristiansen, M. S., Domanski, M., Falkenby, L. G., Lykke‐Andersen, S., Andersen, J., Dziembowski, A., & Jensen, T. H. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.028 · Cited by 422 · see citing works
A single subunit, Dis3, is essentially responsible for yeast exosome core activity
Dziembowski, A., Lorentzen, E., Conti, E., & Séraphin, B. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1184 · Cited by 421 · see citing works
Structural basis for DNA duplex separation by a superfamily-2 helicase
Büttner, K., Nehring, S., & Hopfner, K. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1246 · Cited by 338 · see citing works
Endonucleolytic RNA cleavage by a eukaryotic exosome
Lebreton, A., Tomecki, R., Dziembowski, A., & Séraphin, B. (2008) · Nature · doi:10.1038/nature07480 · Cited by 335 · see citing works
PomBase: a comprehensive online resource for fission yeast
Wood, V., Harris, M. A., McDowall, M. D., Rutherford, K., Vaughan, B. W., Staines, D. M., Aslett, M., Lock, A., Bahler, J., Kersey, P. J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr853 · Cited by 321 · see citing works
de la Cruz, J., Kressler, D., Tollervey, D. W., & Linder, P. (1998) · The EMBO Journal · doi:10.1093/emboj/17.4.1128 · Cited by 321 · see citing works
Briggs, M. W., Burkard, K. T. D., & Butler, J. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13255 · Cited by 310 · see citing works
Identification of a Nuclear Exosome Decay Pathway for Processed Transcripts
Meola, N., Domanski, M., Karadoulama, E., Chen, Y., Gentil, C., Pultz, D., Vitting-Seerup, K., Lykke-Andersen, S., Andersen, J. S., Sandelin, A., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.025 · Cited by 290 · see citing works
The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L
Tomecki, R., Kristiansen, M. S., Lykke‐Andersen, S., Chlebowski, A., Larsen, K. M., Szczęsny, R. J., Drążkowska, K., Pastuła, A., Andersen, J., Stępień, P. P., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.121 · Cited by 272 · see citing works
Wan, J., Yourshaw, M., Mamsa, H., Rudnik-Schöneborn, S., Menezes, M. P., Hong, J. E., Leong, D. W., Senderek, J., Salman, M. S., Chitayat, D., et al. (2012) · Nature Genetics · doi:10.1038/ng.2254 · Cited by 257 · see citing works
RNA decay machines: The exosome
Chlebowski, A., Lubas, M., Jensen, T. H., & Dziembowski, A. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.01.006 · Cited by 246 · see citing works
The Yeast Exosome Functions as a Macromolecular Cage to Channel RNA Substrates for Degradation
Bonneau, F., Basquin, J., Ebert, J., Lorentzen, E., & Conti, E. (2009) · Cell · doi:10.1016/j.cell.2009.08.042 · Cited by 245 · see citing works
Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex
Makino, D. L., Baumgärtner, M., & Conti, E. (2013) · Nature · doi:10.1038/nature11870 · Cited by 240 · see citing works
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 · see citing works
Self-citationSchneider, C., Leung, E., Brown, J. D., & Tollervey, D. W. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn1020 · Cited by 231 · see citing works
Unravelling the dynamics of RNA degradation by ribonuclease II and its RNA-bound complex
Frazão, C., McVey, C. E., Amblar, M., Barbas, A., Vonrhein, C., Arraiano, C. M., & Carrondo, M. A. (2006) · Nature · doi:10.1038/nature05080 · Cited by 215 · see citing works
Lubas, M., Andersen, P. R., Schein, A., Dziembowski, A., Kudla, G., & Jensen, T. H. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.026 · Cited by 201 · see citing works
Identification of novel M phase phosphoproteins by expression cloning.
Matsumoto-Taniura, N., Pirollet, F., Monroe, R. R., Gerace, L., & WESTENDORF, J. M. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.9.1455 · Cited by 188 · see citing works
Lorentzen, E., Basquin, J., Tomecki, R., Dziembowski, A., & Conti, E. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.018 · Cited by 180 · see citing works
Subunit architecture of multimeric complexes isolated directly from cells
Hernández, H., Dziembowski, A., Taverner, T., Séraphin, B., & Robinson, C. V. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400702 · Cited by 177 · see citing works
Phospho-Regulated SUMO Interaction Modules Connect the SUMO System to CK2 Signaling
Stehmeier, P., & Müller, S. P. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.013 · Cited by 174 · see citing works
Sloan, K. E., Mattijssen, S., Lebaron, S., Tollervey, D. W., Pruijn, G. J. M., & Watkins, N. J. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201207131 · Cited by 165 · see citing works
Structure of an Rrp6–RNA exosome complex bound to poly(A) RNA
Wasmuth, E. V., Januszyk, K., & Lima, C. D. (2014) · Nature · doi:10.1038/nature13406 · Cited by 151 · see citing works
Self-citationHuman Telomerase RNA Processing and Quality Control
Tseng, C.-K., Wang, H.-F., Burns, A. M., Schroeder, M. R., Gaspari, M., & Baumann, P. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.075 · Cited by 148 · see citing works
Weir, J. R., Bonneau, F., Hentschel, J., & Conti, E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004953107 · Cited by 147 · see citing works
Threading the barrel of the RNA exosome
Schneider, C., & Tollervey, D. W. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.06.013 · Cited by 144 · see citing works
The RNA exosome and RNA exosome-linked disease
Morton, D. J., Kuiper, E. G., Jones, S. K., Leung, S. W., Corbett, A. H., & Fasken, M. B. (2017) · RNA · doi:10.1261/rna.064626.117 · Cited by 144 · see citing works
Ogami, K., Richard, P., Chen, Y., Hoque, M., Li, W., Moresco, J. J., Yates, J. R., Tian, B., & Manley, J. L. (2017) · Genes & Development · doi:10.1101/gad.302604.117 · Cited by 143 · see citing works
RNA degradation paths in a 12-subunit nuclear exosome complex
Makino, D. L., Schuch, B., Stegmann, E., Baumgärtner, M., Minard‐Basquin, C., & Conti, E. (2015) · Nature · doi:10.1038/nature14865 · Cited by 142 · see citing works
Mechanism of Dis3l2 substrate recognition in the Lin28–let-7 pathway
Faehnle, C. R., Walleshauser, J., & Joshua‐Tor, L. (2014) · Nature · doi:10.1038/nature13553 · Cited by 135 · see citing works
Schilders, G., van Dijk, E., & Pruijn, G. J. M. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm082 · Cited by 132 · see citing works
Structure of the nuclear exosome captured on a maturing preribosome
Schuller, J. M., Falk, S., Fromm, L., Hurt, E., & Conti, E. (2018) · Science · doi:10.1126/science.aar5428 · Cited by 124 · see citing works
The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing
Jackson, R. N., Klauer, A. A., Hintze, B. J., Robinson, H., van Hoof, A., & Johnson, S. J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.107 · Cited by 121 · see citing works
Activities of human RRP6 and structure of the human RRP6 catalytic domain
Januszyk, K., Liu, Q., & Lima, C. D. (2011) · RNA · doi:10.1261/rna.2763111 · Cited by 120 · see citing works
Self-citationWasmuth, E. V., & Lima, C. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.012 · Cited by 114 · see citing works
Self-citationThe exosome‐binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase
Schuch, B., Feigenbutz, M., Makino, D. L., Falk, S., Minard‐Basquin, C., Mitchell, P., & Conti, E. (2014) · The EMBO Journal · doi:10.15252/embj.201488757 · Cited by 110 · see citing works
Wang, H., Wang, J., Ding, F., Callahan, K. P., Bratkowski, M. A., Butler, J. S., Nogales, E., & Ke, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705526104 · Cited by 99 · see citing works
Wang, X., Jia, H., Jankowsky, E., & Anderson, J. T. (2007) · RNA · doi:10.1261/rna.808608 · Cited by 94 · see citing works
Zinder, J. C., Wasmuth, E. V., & Lima, C. D. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.038 · Cited by 87 · see citing works
Self-citationStead, J. A., Costello, J. L., Livingstone, M. J., & Mitchell, P. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm614 · Cited by 82 · see citing works
RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex
Jia, H., Wang, X., Anderson, J. T., & Jankowsky, E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201085109 · Cited by 78 · see citing works
Reconstitution of the complete pathway of ITS2 processing at the pre-ribosome
Fromm, L., Falk, S., Flemming, D., Schuller, J. M., Thoms, M., Conti, E., & Hurt, E. (2017) · Nature Communications · doi:10.1038/s41467-017-01786-9 · Cited by 77 · see citing works
Halbach, F., Rode, M., & Conti, E. (2011) · RNA · doi:10.1261/rna.029553.111 · Cited by 75 · see citing works
Nuclear Proximity of Mtr4 to RNA Exosome Restricts DNA Mutational Asymmetry
Lim, J., Giri, P. K., Kazadi, D., Laffleur, B., Zhang, W., Grinstein, V., Pefanis, E., Brown, L. M., Ladewig, E., Martin, O. A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.03.043 · Cited by 74 · see citing works
The molecular spectrum and clinical impact of DIS 3 mutations in multiple myeloma
Weißbach, S., Langer, C., Puppe, B., Nedeva, T., Bach, E., Kull, M., Bargou, R. C., Einsele, H., Rosenwald, A., Knop, S. T., et al. (2014) · British Journal of Haematology · doi:10.1111/bjh.13256 · Cited by 67 · see citing works
Visualization of distinct substrate-recruitment pathways in the yeast exosome by EM
Liu, J., Bratkowski, M. A., Liu, X., Niu, C.-Y., Ke, A., & Wang, H. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2736 · Cited by 62 · see citing works
Puno, M. R., & Lima, C. D. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803530115 · Cited by 62 · see citing works
Self-citationThe exosome complex establishes a barricade to erythroid maturation
McIver, S. C., Kang, Y.-A., DeVilbiss, A., O’Driscoll, C. A., Ouellette, J. N., Pope, N. J., Campreciós, G., Chang, C.-J., Yang, D. T., Bouhassira, E. E., et al. (2014) · Blood · doi:10.1182/blood-2014-04-571083 · Cited by 61 · see citing works
Wasmuth, E. V., Zinder, J. C., Zattas, D., Das, M., & Lima, C. D. (2017) · eLife · doi:10.7554/elife.29062 · Cited by 60 · see citing works
Self-citationAttacked from All Sides: RNA Decay in Antiviral Defense
Molleston, J. M., & Cherry, S. R. (2017) · Viruses · doi:10.3390/v9010002 · Cited by 55 · see citing works
Mpp6 Incorporation in the Nuclear Exosome Contributes to RNA Channeling through the Mtr4 Helicase
Falk, S., Bonneau, F., Ebert, J., Kögel, A., & Conti, E. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.033 · Cited by 52 · see citing works
CryoEM structure of yeast cytoplasmic exosome complex
Liu, J., Niu, C.-Y., Wu, Y., Tan, D., Wang, Y., Ye, M., Liu, Y., Zhao, W., Zhou, K., Liu, Q., et al. (2016) · Cell Research · doi:10.1038/cr.2016.56 · Cited by 51 · see citing works
Transcriptome-wide analysis of alternative routes for RNA substrates into the exosome complex
Delan‐Forino, C., Schneider, C., & Tollervey, D. W. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006699 · Cited by 50 · see citing works
Novel EXOSC3 mutation causes complicated hereditary spastic paraplegia
Halevy, A., Lerer, I., Cohen, R., Kornreich, L., Shuper, A., Gamliel, M., Zimerman, B.-E., Korabi, I., Meiner, V., Straussberg, R., et al. (2014) · Journal of Neurology · doi:10.1007/s00415-014-7457-x · Cited by 46 · see citing works
The RNA Exosome Channeling and Direct Access Conformations Have Distinct In Vivo Functions
Han, J., & van Hoof, A. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.059 · Cited by 37 · see citing works
Cooling-induced SUMOylation of EXOSC10 down-regulates ribosome biogenesis
Knight, J. R. P., Bastide, A., Peretti, D., Roobol, A., Roobol, J., Mallucci, G. R., Smales, C. M., & Willis, A. E. (2016) · RNA · doi:10.1261/rna.054411.115 · Cited by 33 · see citing works
Chapter 10 Reconstitution of RNA Exosomes from Human and Saccharomyces cerevisiae
Greimann, J. C., & Lima, C. D. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)02610-4 · Cited by 26 · see citing works
Self-citationLorentzen, E., & Conti, E. (2012) · Archaea · doi:10.1155/2012/721869 · Cited by 25 · see citing works
Flagged first, then by citations
1 of the 81 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Regulation of long non-coding RNAs and genome dynamics by the RNA surveillance machinery
Nair, L., Chung, H., & Basu, U. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0209-0 · Cited by 203 · see citing works
Cellular RNA surveillance in health and disease
Wolin, S. L., & Maquat, L. E. (2019) · Science · doi:10.1126/science.aax2957 · Cited by 157 · see citing works
Cellular functions of eukaryotic RNA helicases and their links to human diseases
Bohnsack, K. E., Yi, S., Venus, S., Jankowsky, E., & Bohnsack, M. T. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00628-5 · Cited by 131 · see citing works
Binding specificities of human RNA-binding proteins toward structured and linear RNA sequencesPreprint
Jolma, A., Zhang, J., Mondragón, E., Morgunova, E. Y., Kivioja, T., Laverty, K. U., Yin, Y., Zhu, F., Bourenkov, G. P., Morris, Q., et al. (2020) · Genome Research · doi:10.1101/gr.258848.119 · Cited by 121 · see citing works
EXOSC10 is required for RPA assembly and controlled DNA end resection at DNA double-strand breaks
Domingo‐Prim, J., Endara-Coll, M., Bonath, F., Jimeno, S., Prados‐Carvajal, R., Friedländer, M. R., Huertas, P., & Visa, N. (2019) · Nature Communications · doi:10.1038/s41467-019-10153-9 · Cited by 104 · see citing works
Wu, D., Deng, S., Li, L., Liu, T., Zhang, T., Li, J., Yu, Y., & Xu, Y. X. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04004-z · Cited by 104 · see citing works
Davidson, L., Francis, L. I., Cordiner, R. A., Eaton, J. D., Estell, C., Macías, S., Cáceres, J. F., & West, S. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.012 · Cited by 101 · see citing works
Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism
Warkocki, Z., Liudkovska, V., Gewartowska, O., Mroczek, S., & Dziembowski, A. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2018.0162 · Cited by 76 · see citing works
Systematic Discovery of Endogenous Human Ribonucleoprotein Complexes
Mallam, A. L., Sae-Lee, W., Schaub, J. M., Tu, F., Battenhouse, A. M., Jang, Y. J., Kim, J., Wallingford, J. B., Finkelstein, I. J., Marcotte, E. M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.060 · Cited by 74 · see citing works
Post-transcriptional regulation in spermatogenesis: all RNA pathways lead to healthy sperm
Morgan, M., Kumar, L., Li, Y., & Baptissart, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04012-4 · Cited by 67 · see citing works
The RNA Exosome and Human Disease
Fasken, M. B., Morton, D. J., Kuiper, E. G., Jones, S. K., Leung, S. W., & Corbett, A. H. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9822-7_1 · Cited by 58 · see citing works
Nair, L., Zhang, W., Laffleur, B., Jha, M. K., Lim, J., Lee, H. J., Wu, L., Alvarez, N. S., Liu, Z., Munteanu, E. L., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.037 · Cited by 59 · see citing works
Extraction of mRNA from Stalled Ribosomes by the Ski Complex
Zinoviev, A., Ayupov, R. K., Abaeva, I. S., Hellen, C. U. T., & Pestova, T. V. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.011 · Cited by 60 · see citing works
Distinct and evolutionary conserved structural features of the human nuclear exosome complex
Gerlach, P., Schuller, J. M., Bonneau, F., Basquin, J., Reichelt, P., Falk, S., & Conti, E. (2018) · eLife · doi:10.7554/elife.38686 · Cited by 59 · see citing works
Structural basis for RNA surveillance by the human nuclear exosome targeting (NEXT) complex
Puno, M. R., & Lima, C. D. (2022) · Cell · doi:10.1016/j.cell.2022.04.016 · Cited by 57 · see citing works
Self-citationLingaraju, M., Johnsen, D., Schlundt, A., Langer, L. M., Basquin, J., Sattler, M., Heick Jensen, T., Falk, S., & Conti, E. (2019) · Nature Communications · doi:10.1038/s41467-019-11339-x · Cited by 55 · see citing works
Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases
Liudkovska, V., & Dziembowski, A. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1622 · Cited by 51 · see citing works
Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.011 · Cited by 55 · see citing works
Different mechanisms for translocation by monomeric and hexameric helicases
Gao, Y., & Yang, W. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.003 · Cited by 52 · see citing works
The RNA exosome nuclease complex regulates human embryonic stem cell differentiation
Belair, C., Sim, S., Kim, K., Tanaka, Y., Park, I., and, & Wolin, S. L. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201811148 · Cited by 51 · see citing works
Kögel, A., Keidel, A., Bonneau, F., Schäfer, I. B., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.01.009 · Cited by 51 · see citing works
Structure of the Maturing 90S Pre-ribosome in Association with the RNA Exosome
Lau, B. H. S., Cheng, J., Flemming, D., Venuta, G. L., Berninghausen, O., Beckmann, R., & Hurt, E. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.009 · Cited by 48 · see citing works
NRDE2 negatively regulates exosome functions by inhibiting MTR4 recruitment and exosome interactionPreprint
Wang, J., Chen, J., Wu, G., Zhang, H., Du, X., Chen, S., Zhang, L., Wang, K., Fan, J., Gao, S., et al. (2019) · Genes & Development · doi:10.1101/gad.322602.118 · Cited by 47 · see citing works
Rapid factor depletion highlights intricacies of nucleoplasmic RNA degradation
Gockert, M., Schmid, M., Jakobsen, L., Jens, M., Andersen, J., & Jensen, T. H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac001 · Cited by 45 · see citing works
RNA helicases are hubs that orchestrate exosome-dependent 3′–5′ decay
Weick, E., & Lima, C. D. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.09.010 · Cited by 42 · see citing works
Self-citationFilling Adeno-Associated Virus Capsids: Estimating Success by Cryo-Electron Microscopy
Subramanian, S., Maurer, A. C., Bator, C. M., Makhov, A. M., Conway, J. F., Turner, K. B., Marden, J. H., Vandenberghe, L. H., & Hafenstein, S. L. (2019) · Human Gene Therapy · doi:10.1089/hum.2019.041 · Cited by 40 · see citing works
Regulation of RNA helicase activity: principles and examples
Donsbach, P., & Klostermeier, D. (2021) · Biological Chemistry · doi:10.1515/hsz-2020-0362 · Cited by 36 · see citing works
Exosome-Derived LncRNAs in Lung Cancer
Fan, T. T., Sun, N., & He, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01728 · Cited by 37 · see citing works
Substrate specificity of the TRAMP nuclear surveillance complexes
Delan-Forino, C., Spanos, C., Rappsilber, J., & Tollervey, D. (2020) · Nature Communications · doi:10.1038/s41467-020-16965-4 · Cited by 36 · see citing works
Nuclear RNA homeostasis promotes systems-level coordination of cell fate and senescence
Han, X., Xing, L., Hong, Y., Zhang, X., Hao, B., Lu, J. Y., Huang, M., Wang, Z., Ma, S., Zhan, G., et al. (2024) · Cell stem cell · doi:10.1016/j.stem.2024.03.015 · Cited by 36 · see citing works
Beyond gene expression: how MYC relieves transcription stress
Papadopoulos, D., Uhl, L., Ha, S. A., & Eilers, M. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.06.008 · Cited by 34 · see citing works
Post-transcriptional control of cellular differentiation by the RNA exosome complex
de Andrade, I. F., Mehta, C., & Bresnick, E. H. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa883 · Cited by 30 · see citing works
Catalytic activities, molecular connections, and biological functions of plant RNA exosome complexes
Lange, H., & Gagliardi, D. (2021) · The Plant Cell · doi:10.1093/plcell/koab310 · Cited by 32 · see citing works
The zinc-finger protein Red1 orchestrates MTREC submodules and binds the Mtl1 helicase arch domain
Dobrev, N., Ahmed, Y. L., Sivadas, A., Soni, K., Fischer, T., & Sinning, I. (2021) · Nature Communications · doi:10.1038/s41467-021-23565-3 · Cited by 30 · see citing works
Biology of RNA Surveillance in Development and Disease
Laffleur, B., & Basu, U. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.01.004 · Cited by 29 · see citing works
Yeast Ssd1 is a non-enzymatic member of the RNase II family with an alternative RNA recognition site
Bayne, R. A. L., Jayachandran, U., Kasprowicz, A., Bresson, S. M., Tollervey, D. W., Wallace, E. W. J., & Cook, A. G. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab615 · Cited by 27 · see citing works
Tasak, M., & Phizicky, E. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010215 · Cited by 26 · see citing works
Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex
Foucher, A.-E., Touat-Todeschini, L., Juarez-Martinez, A. B., Rakitch, A., Laroussi, H., Karczewski, C., Acajjaoui, S., Soler-López, M., Cusack, S., Mackereth, C. D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32542-3 · Cited by 26 · see citing works
Structural basis of mRNA decay by the human exosome–ribosome supercomplex
Kögel, A., Keidel, A., Loukeri, M.-J., Kuhn, C. C., Langer, L. M., Schäfer, I. B., & Conti, E. (2024) · Nature · doi:10.1038/s41586-024-08015-6 · Cited by 25 · see citing works
Caught in the act—Visualizing ribonucleases during eukaryotic ribosome assembly
Schneider, C., & Bohnsack, K. E. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1766 · Cited by 24 · see citing works
Structural overview of macromolecular machines involved in ribosome biogenesis
Frazier, M. N., Pillon, M. C., Kocaman, S., Gordon, J., & Stanley, R. E. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.09.003 · Cited by 24 · see citing works
Tomecki, R., Drazkowska, K., Kobylecki, K., & Tudek, A. (2023) · WIREs RNA · doi:10.1002/wrna.1795 · Cited by 18 · see citing works
Nuclear RNA Exosome and Pervasive Transcription: Dual Sculptors of Genome Function
Ogami, K., & Suzuki, H. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413401 · Cited by 23 · see citing works
Control of RNA degradation in cell fate decision
Deng, M., Wang, X., Xiong, Z. Q., & Tang, P. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1164546 · Cited by 23 · see citing works
Mtr4 RNA helicase structures and interactions
Olsen, K. J., & Johnson, S. J. (2021) · Biological Chemistry · doi:10.1515/hsz-2020-0329 · Cited by 22 · see citing works
To Process or to Decay: A Mechanistic View of the Nuclear RNA ExosomePreprint
Lingaraju, M., Schuller, J. M., Falk, S., Gerlach, P., Bonneau, F., Basquin, J., Benda, C., & Conti, E. (2019) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2019.84.040295 · Cited by 22 · see citing works
Qin, C., Li, T., Chen, L., Zhao, B., Li, Z., Zhao, Y., & Wang, W. (2024) · Cancer Cell International · doi:10.1186/s12935-024-03456-5 · Cited by 21 · see citing works
Stuparević, I., Novačić, A., Rahmouni, A. R., Fernandez, A., Lamb, N. J. C., & Primig, M. (2021) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12693 · Cited by 20 · see citing works
RNA-Degrading Exosome Complexes: Molecular Mechanisms and Structural Insights
Keidel, A., Long, C. L., Iwasa, J., & Conti, E. (2025) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111822-115115 · Cited by 18 · see citing works
Zebrafish Ski7 tunes RNA levels during the oocyte-to-embryo transition
Cabrera-Quio, L. E., Schleiffer, A., Mechtler, K., & Pauli, A. (2021) · PLOS Genetics · doi:10.1371/journal.pgen.1009390 · Cited by 18 · see citing works
de Amorim, J. L., Leung, S. W., Haji‐Seyed‐Javadi, R., Hou, Y., Yu, D. S., Ghalei, H., Khoshnevis, S., Yao, B., & Corbett, A. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105646 · Cited by 18 · see citing works
Fasken, M. B., Leung, S. W., Cureton, L. A., Al-Awadi, M., Al‐Kindy, A., van Hoof, A., Khoshnevis, S., Ghalei, H., Al-Maawali, A. A., & Corbett, A. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107571 · Cited by 17 · see citing works
RNA surveillance by the RNA helicase MTR4 determines volume of mouse oocytes
Wu, Y., Deng, Z., Rong, Y., Bu, G., Wu, Y.-K., Wu, X., Cheng, H., & Fan, H. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.009 · Cited by 16 · see citing works
Keidel, A., Kögel, A., Reichelt, P., Kowalinski, E., Schäfer, I. B., & Conti, E. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.09.037 · Cited by 15 · see citing works
Das, M., Zattas, D., Zinder, J. C., Wasmuth, E. V., Henri, J., & Lima, C. D. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024846118 · Cited by 14 · see citing works
Self-citationRNA splicing: a dual-edged sword for hepatocellular carcinoma
Kashyap, A., Tripathi, G., Tripathi, A., Rao, R., Kashyap, M., Bhat, A., Kumar, D., Rajhans, A., Kumar, P., Chandrashekar, D. S., et al. (2022) · Medical Oncology · doi:10.1007/s12032-022-01726-8 · Cited by 14 · see citing works
A shape-shifting nuclease unravels structured RNA
Meze, K., Axhemi, A. A., Thomas, D. R., Doymaz, A., & Joshua‐Tor, L. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00923-x · Cited by 13 · see citing works
Damseh, N. S., Obeidat, A. N., Ahammed, K. S., Ashhab, M., Awwad, M. A., & van Hoof, A. (2023) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.63198 · Cited by 13 · see citing works
Effects of senataxin and RNA exosome on B-cell chromosomal integrity
Kazadi, D., Lim, J., Rothschild, G., Grinstein, V., Laffleur, B., Bécherel, O. J., Lavin, M. F., & Basu, U. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e03442 · Cited by 13 · see citing works
Dual modes of ZFC3H1 confer selectivity in nuclear RNA sorting
Fan, J., Wang, Y., Wen, M., Deng, T., Wu, K., Yan, K., Jia, P., Zhu, Y. N., Liu, Q., Zou, H., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.09.032 · Cited by 12 · see citing works
Exosomal Long Noncoding RNAs in NSCLC: Dysfunctions and Clinical Potential
Lin, H., Li, J., Wang, M., Zhang, X., & Zhu, T. (2023) · Journal of Cancer · doi:10.7150/jca.84506 · Cited by 12 · see citing works
Zhang, N., Olsen, K. J., Ball, D., Johnson, S. J., & D’Arcy, S. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac170 · Cited by 12 · see citing works
An RNA Metabolism and Surveillance Quartet in the Major Histocompatibility Complex
Zhou, D., Lai, M., Luo, A., & Yu, C. Y. (2019) · Cells · doi:10.3390/cells8091008 · Cited by 12 · see citing works
RNA-regulatory exosome complex confers cellular survival to promote erythropoiesis
Mehta, C., de Andrade, I. F., Matson, D. R., Dewey, C. N., & Bresnick, E. H. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab367 · Cited by 12 · see citing works
Xiong, C., Sun, Z., Yu, J., & Lin, Y. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.797968 · Cited by 11 · see citing works
RetractedKilchert, C., Kecman, T., Priest, E. L., Hester, S., Aydin, E., Kuś, K., Roßbach, O., Castelló, A., Mohammed, S., & Vasiljeva, L. (2020) · Genome Research · doi:10.1101/gr.257006.119 · Cited by 10 · see citing works
The making and breaking of tRNAs by ribonucleases
Hobson, J. J., Papadopoulos, R., Hayne, C. K., & Stanley, R. E. (2024) · Trends in Genetics · doi:10.1016/j.tig.2024.03.007 · Cited by 10 · see citing works
Sterrett, M. C., Enyenihi, L., Leung, S. W., Hess, L., Strassler, S. E., Farchi, D., Lee, R. S., Withers, E. S., Kremsky, I., Baker, R. E., et al. (2021) · RNA · doi:10.1261/rna.078618.120 · Cited by 9 · see citing works
Fujiwara, N., Shigemoto, M., Hirayama, M., Fujita, K., Seno, S., Matsuda, H., Nagahama, M., & Masuda, S. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac559 · Cited by 10 · see citing works
Cesaro, G., da Soler, H. T., Guerra-Slompo, E. P., Haouz, A., Legrand, P., Zanchin, N. I. T., & Guimarães, B. G. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1199 · Cited by 10 · see citing works
Genome‐scale molecular principles of mRNA half‐life regulation in yeast
Basu, S., Mallik, S., Hait, S., & Kundu, S. (2020) · FEBS Journal · doi:10.1111/febs.15670 · Cited by 10 · see citing works
Sterrett, M. C., Cureton, L. A., Cohen, L. N., van Hoof, A., Khoshnevis, S., Fasken, M. B., Corbett, A. H., & Ghalei, H. (2025) · RNA · doi:10.1261/rna.080447.125 · Cited by 9 · see citing works
Ishida, Y.-I., Miyao, S., Saito, M., Hiraishi, N., & Nagahama, M. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.105919 · Cited by 9 · see citing works
RNA processing mechanisms contribute to genome organization and stability in B cells
Miglierina, E., Ordanoska, D., Noir, S. L., & Laffleur, B. (2024) · Oncogene · doi:10.1038/s41388-024-02952-2 · Cited by 7 · see citing works
Out or decay: fate determination of nuclear RNAs
Wang, J., & Cheng, H. (2020) · Essays in Biochemistry · doi:10.1042/ebc20200005 · Cited by 8 · see citing works
Yuan, Y., Mao, X., Abubakar, Y. S., Zheng, W., Wang, Z., Zhou, J., & Zheng, H. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.05058-22 · Cited by 8 · see citing works
Che, R., Panah, M., Mirani, B., Knowles, K., Ostapovich, A., Majumdar, D., Chen, X., DeSimone, J., White, W., Noonan, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59998-3 · Cited by 7 · see citing works
4D structural biology–quantitative dynamics in the eukaryotic RNA exosome complex
Liebau, J., Lazzaretti, D., Fürtges, T., Bichler, A., Pilsl, M., Rudack, T., & Sprangers, R. (2025) · Nature Communications · doi:10.1038/s41467-025-62982-6 · Cited by 7 · see citing works
Regulation of RNA-binding proteins by small biomolecules
Miao, W., Porter, D. F., Lopez-Pajares, V., & Khavari, P. A. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00914-4 · Cited by 7 · see citing works
Microfluidic strategies for separation and analysis of circulating exosomes
Chen, W., Gan, Z., & Qin, J. (2021) · Chinese Journal of Chromatography · doi:10.3724/sp.j.1123.2021.07005 · Cited by 7 · see citing works
Batista, M., Langendijk-Genevaux, P. S., Kwapisz, M., Canal, I., Phung, D. K., Plassart, L., Capeyrou, R., Moalic, Y., Jebbar, M., Flament, D., et al. (2024) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqae026 · Cited by 6 · see citing works
A structural biology view on the enzymes involved in eukaryotic mRNA turnover
Krempl, C., Lazzaretti, D., & Sprangers, R. (2023) · Biological Chemistry · doi:10.1515/hsz-2023-0182 · Cited by 6 · see citing works
RNA lifetime control, from stereochemistry to gene expression
Dendooven, T., Luisi, B. F., & Bandyra, K. J. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.002 · Cited by 6 · see citing works
Hojka-Osińska, A., Chlebowski, A., Grochowska, J., Owczarek, E. P., Affek, K., Kłosowska-Kosicka, K., Szczęsny, R. J., & Dziembowski, A. (2021) · iScience · doi:10.1016/j.isci.2021.103036 · Cited by 6 · see citing works
MYC: The Guardian of Its Own Chaos
Gaballa, A., Krenz, B., & Uhl, L. (2025) · BioEssays · doi:10.1002/bies.70010 · Cited by 5 · see citing works
Sterrett, M. C., Farchi, D., Strassler, S. E., Boise, L. H., Fasken, M. B., & Corbett, A. H. (2023) · G3: Genes, Genomes, Genetics · doi:10.1093/g3journal/jkad049 · Cited by 5 · see citing works
Li, J., Hou, Y., Gu, X., Yue, L., Guo, L., Li, D., & Dong, X. (2020) · RNA Biology · doi:10.1080/15476286.2020.1777379 · Cited by 5 · see citing works
Assembly of multicomponent machines in RNA metabolism: A common theme in mRNA decay pathways
de Amorim, A. M., & Chakrabarti, S. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1684 · Cited by 5 · see citing works
RNA-binding protein Mub1 and the nuclear RNA exosome act to fine-tune environmental stress response
Birot, A., Kilchert, C., Kuś, K., Priest, E., Alwash, A. A., Castelló, A., Mohammed, S., & Vasiljeva, L. (2021) · Life Science Alliance · doi:10.26508/lsa.202101111 · Cited by 5 · see citing works
MTR4 adaptor PICT1 functions in two distinct steps during pre-rRNA processing
Miyao, S., Saito, K., Oshima, R., Kawahara, K., & Nagahama, M. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.11.018 · Cited by 5 · see citing works
Binding specificities of human RNA binding proteins towards structured and linear RNA sequencesPreprint
Jolma, A., Zhang, J., Mondragón, E., Morgunova, E. Y., Kivioja, T., Laverty, K. U., Yin, Y., Zhu, F., Bourenkov, G. P., Morris, Q., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/317909 · Cited by 5 · see citing works
Runnebohm, A. M., Wijeratne, H. R. S., Barron, M. P., Smith-Kinnaman, W. R., Rooney, J. D., Peck Justice, S. A., Cureton, L. A., Holland, A., Ghalei, H., Pelletier, S., et al. (2025) · doi:10.1101/2025.05.31.657176 · Cited by 4 · see citing works
HELZ2 Regulates Apob mRNA Stability to Modulate Fatty Liver Disease and Atherosclerosis
Jiang, Y., & Zhang, Z. (2025) · Circulation · doi:10.1161/circulationaha.125.076468 · Cited by 4 · see citing works
Majerčiak, V., Alvarado-Hernandez, B., Ma, Y., Duduskar, S. N., Lobanov, A. V., Cam, M., & Zheng, Z. (2024) · mBio · doi:10.1128/mbio.03172-24 · Cited by 4 · see citing works
Conformational Switching of the Nuclear Exosome during Ribosome Biogenesis
Kummer, E., & Ban, N. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00593 · Cited by 4 · see citing works
Reconstitution of the Human Nuclear RNA Exosome
Januszyk, K., Weick, E., & Lima, C. D. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9822-7_23 · Cited by 4 · see citing works
Self-citationKilchert, C., Kecman, T., Priest, E. L., Hester, S., Kuś, K., Castelló, A., Mohammed, S., & Vasiljeva, L. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/748194 · Cited by 4 · see citing works
Ahammed, K. S., Fasken, M. B., Corbett, A. H., & van Hoof, A. (2025) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkaf036 · Cited by 3 · see citing works
The nuclear exosome co-factor MTR4 shapes the transcriptome for meiotic initiation
Zhang, L., Wang, J., Tang, Z., Lin, Z., Su, R., Hu, N., Tang, Y., Ge, G., Fan, J., Tong, M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57898-0 · Cited by 3 · see citing works
Purification and characterization of Mtr4 and TRAMP from S. cerevisiae
Yim, M., Denson, J., Gold, M. D., & Johnson, S. J. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.03.042 · Cited by 3 · see citing works
- Authors
- Weick, E.-M., Puno, M. R., Januszyk, K., Zinder, J. C., DiMattia, M. A., & Lima, C. D.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Lima, Christopher D.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2018-06
- Volume
- 173
- Issue
- 7
- Pages
- 1663-1677.e21
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC6124691
- OpenAlex
- W2808298553
- Cited by
- 153
- References
- 81
- Citations by year
- 2026: 20 · 2025: 17 · 2024: 14 · 2023: 19 · 2022: 17 · 2021: 20 · 2020: 20 · 2019: 22 · 2018: 4
- FWCI
- 5.87
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Simons Foundation (SF349247)
- NYSTAR
- NIH NIGMS (GM103310)
- Agouron Institute (F00316)
- NIH (S10 OD019994-01)
- National Institute of General Medical Sciences of the NIH (R01GM079196, R35GM118080)
- NIH-NCI-Cancer Center (P30 CA008748)
- Human Frontier Science Program
- 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
- RNA exosome, RNA degradation, MPP6, RNA unwinding, Saccharomyces cerevisiae, Schizosaccharomyces pombe
- MeSH terms
- DNA, DNA Helicases, Exoribonucleases, Humans, Image Processing, Computer-Assisted, Membrane Proteins, Protein Binding, RNA, Saccharomyces cerevisiae, Schizosaccharomyces, Substrate Specificity, Catalytic Domain, Cryoelectron Microscopy, RNA Helicases, Protein Structure, Quaternary, RNA Stability, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Exosome Multienzyme Ribonuclease Complex
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