Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome
Open accessAbstract
In mammalian cells, spurious transcription results in a vast repertoire of unproductive non-coding RNAs, whose deleterious accumulation is prevented by rapid decay. The nuclear exosome targeting (NEXT) complex plays a central role in directing non-functional transcripts to exosome-mediated degradation, but the structural and molecular mechanisms remain enigmatic. Here, we elucidated the architecture of the human NEXT complex, showing that it exists as a dimer of MTR4-ZCCHC8-RBM7 heterotrimers. Dimerization preconfigures the major MTR4-binding region of ZCCHC8 and arranges the two MTR4 helicases opposite to each other, with each protomer able to function on many types of RNAs. In the inactive state of the complex, the 3' end of an RNA substrate is enclosed in the MTR4 helicase channel by a ZCCHC8 C-terminal gatekeeping domain. The architecture of a NEXT-exosome assembly points to the molecular and regulatory mechanisms with which the NEXT complex guides RNA substrates to the exosome.
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?
Catalytic activities of the RNA exosome are mediated by associated 3'−5' exonucleases EXOSC10 and DIS3 or accessory factors such as MTR4, while core components including EXOSC3 provide structural stability and facilitate substrate recognition and/or RNA threading.
“The catalytic activities of the RNA exosome are mediated by associated 3’−5’ exonucleases EXOSC10 and DIS3 or accessory factors such as the RNA helicase MTR4, while core components including EXOSC3 provide structural stability and facilitate substrate recognition and/or RNA threading through the protein complex core39–43.”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [39]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
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.
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
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · 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
Genome engineering using the CRISPR-Cas9 system
Ran, F. A., Hsu, P. D., Wright, J., Agarwala, V., Scott, D. A., & Zhang, F. (2013) · Nature Protocols · doi:10.1038/nprot.2013.143 · Cited by 11,133 · see citing works
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · 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
UCSF ChimeraX: Meeting modern challenges in visualization and analysis
Goddard, T. D., Huang, C. C., Meng, E. C., Pettersen, E. F., Couch, G. S., Morris, J. H., & Ferrin, T. E. (2018) · Protein Science · doi:10.1002/pro.3235 · Cited by 5,267 · see citing works
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,926 · see citing works
New tools for automated high-resolution cryo-EM structure determination in RELION-3
Zivanov, J., Nakane, T., Forsberg, B., Kimanius, D., Hagen, W., Lindahl, E., & Scheres, S. (2018) · eLife · doi:10.7554/elife.42166 · Cited by 4,377 · see citing works
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · see citing works
Highly accurate protein structure prediction for the human proteome
Tunyasuvunakool, K., Adler, J., Wu, Z., Green, T., Zielinski, M., Žídek, A., Bridgland, A., Cowie, A., Meyer, C., Laydon, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03828-1 · Cited by 3,025 · see citing works
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416 · see citing works
An auxin-based degron system for the rapid depletion of proteins in nonplant cells
Nishimura, K., Fukagawa, T., Takisawa, H., Kakimoto, T., & Kanemaki, M. (2009) · Nature Methods · doi:10.1038/nmeth.1401 · Cited by 1,663 · see citing works
Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs
Bepler, T., Morin, A., Rapp, M., Brasch, J., Shapiro, L., Noble, A., & Berger, B. (2018) · Nature Methods · doi:10.1038/s41592-019-0575-8 · Cited by 1,455 · see citing works
Efficient transposition of the piggyBac (PB) transposon in mammalian cells and mice
Ding, S., Wu, X., Li, G., Han, M., Zhuang, Y., & Xu, T. (2005) · Cell · doi:10.1016/j.cell.2005.07.013 · Cited by 1,009 · see citing works
Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M., & Tollervey, D. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80432-8 · Cited by 947 · see citing works
Addressing Preferred Specimen Orientation in Single-Particle Cryo-EM through Tilting
Tan, Y.-Z., Baldwin, P. R., Davis, J., Williamson, J., Potter, C., Carragher, B., & Lyumkis, D. (2017) · Nature Methods · doi:10.1038/nmeth.4347 · Cited by 920 · see citing works
RNA Degradation by the Exosome Is Promoted by a Nuclear Polyadenylation Complex
LaCava, J., Houseley, J. M., Saveanu, C., Petfalski, E., Thompson, E., Jacquier, A., & Tollervey, D. W. (2005) · Cell · doi:10.1016/j.cell.2005.04.029 · Cited by 870 · 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
New tools for the analysis and validation of cryo-EM maps and atomic models
Afonine, P. V., Klaholz, B. P., Moriarty, N. W., Poon, B. K., Sobolev, O. V., Terwilliger, T. C., Adams, P. D., & Urzhumtsev, A. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318009324 · Cited by 719 · see citing works
A New Yeast Poly(A) Polymerase Complex Involved in RNA Quality Control
Vaňáčová, Š., Wolf, J., Martin, G., Blank, D., Dettwiler, S., Friedlein, A., Langen, H., Keith, G., & Keller, W. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030189 · Cited by 567 · 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
Software tools for automated transmission electron microscopy
Schorb, M., Haberbosch, I., Hagen, W. J. H., Schwab, Y., & Mastronarde, D. N. (2019) · Nature Methods · doi:10.1038/s41592-019-0396-9 · Cited by 508 · 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
Self-citationA 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
Self-citationIdentification 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
Self-citationImprovement of cryo-EM maps by density modification
Terwilliger, T. C., Ludtke, S. J., Read, R. J., Adams, P. D., & Afonine, P. V. (2020) · Nature Methods · doi:10.1038/s41592-020-0914-9 · Cited by 287 · 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
Self-citationRNA 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
Self-citationThe 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
Self-citationCrystal 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
Self-citationTargeting 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
Focus: The interface between data collection and data processing in cryo-EM.
Biyani, N., Righetto, R., McLeod, R., Caujolle-Bert, D., Castaño-Díez, D., Goldie, K., & Stahlberg, H. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.03.007 · Cited by 203 · 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
Self-citationThe Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins
Thoms, M., Thomson, E., Baßler, J., Gnädig, M., Griesel, S., & Hurt, E. (2015) · Cell · doi:10.1016/j.cell.2015.07.060 · Cited by 192 · see citing works
Controlling nuclear RNA levels
Schmid, M., & Jensen, T. H. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0013-2 · Cited by 155 · see citing works
Self-citationWeick, E.-M., Puno, M. R., Januszyk, K., Zinder, J. C., DiMattia, M. A., & Lima, C. D. (2018) · Cell · doi:10.1016/j.cell.2018.05.041 · Cited by 153 · see citing works
Human 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
Self-citationRNA 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
Self-citationStructure 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
Self-citationThe 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
Gable, D. L., Gaysinskaya, V. A., Atik, C. C., Talbot, C. C., Kang, B., Stanley, S. E., Pugh, E., Amat-Codina, N., Schenk, K. M., Arcasoy, M. O., et al. (2019) · Genes & Development · doi:10.1101/gad.326785.119 · Cited by 121 · see citing works
Wasmuth, E. V., & Lima, C. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.012 · Cited by 114 · see citing works
Conditional Degrons for Controlling Protein Expression at the Protein Level
Natsume, T., & Kanemaki, M. T. (2017) · Annual Review of Genetics · doi:10.1146/annurev-genet-120116-024656 · Cited by 111 · see citing works
The 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
Self-citationSouth, T., & Summers, M. F. (1993) · Protein Science · doi:10.1002/pro.5560020102 · Cited by 107 · 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
Falk, S., Weir, J. R., Hentschel, J., Reichelt, P., Bonneau, F., & Conti, E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.07.020 · Cited by 77 · see citing works
Self-citationThe Nuclear RNA Exosome and Its Cofactors
Schmid, M., & Jensen, T. H. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-31434-7_4 · Cited by 77 · see citing works
Self-citationRNA Surveillance by the Nuclear RNA Exosome: Mechanisms and Significance
Ogami, K., Chen, Y., & Manley, J. L. (2018) · Non-Coding RNA · doi:10.3390/ncrna4010008 · Cited by 75 · see citing works
Diminished nuclear RNA decay upon Salmonella infection upregulates antibacterial noncoding RNAs
Imamura, K., Takaya, A., Ishida, Y., Fukuoka, Y., Taya, T., Nakaki, R., Kakeda, M., Imamachi, N., Sato, A., Yamada, T., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201797723 · Cited by 68 · see citing works
Self-citationRBM7 subunit of the NEXT complex binds U-rich sequences and targets 3′-end extended forms of snRNAs
Hroššová, D., Šikorský, T., Potěšil, D., Bartošovič, M., Pasulka, J., Zdráhal, Z., Štefl, R., & Vaňáčová, Š. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv240 · Cited by 64 · see citing works
Rrp6, Rrp47 and Cofactors of the Nuclear Exosome
Butler, J. S., & Mitchell, P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7841-7_8 · 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
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
Winczura, K., Schmid, M., Iasillo, C., Molloy, K. R., Harder, L. M., Andersen, J., LaCava, J., & Jensen, T. H. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.037 · Cited by 60 · see citing works
Self-citationDistinct 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
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
Self-citationStructure of the RBM7–ZCCHC8 core of the NEXT complex reveals connections to splicing factors
Falk, S., Finogenova, K., Melko, M., Benda, C., Lykke‐Andersen, S., Jensen, T. H., & Conti, E. (2016) · Nature Communications · doi:10.1038/ncomms13573 · Cited by 52 · see citing works
Self-citationMpp6 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
Self-citationKögel, 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
Self-citationNRDE2 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
Garland, W., & Jensen, T. H. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1572 · Cited by 46 · see citing works
Self-citationFalk, S., Tants, J., Basquin, J., Thoms, M., Hurt, E., Sattler, M., & Conti, E. (2017) · RNA · doi:10.1261/rna.062901.117 · Cited by 42 · see citing works
Self-citationAltered RNA metabolism due to a homozygousRBM7mutation in a patient with spinal motor neuropathy
Giunta, M., Edvardson, S., Xu, Y., Schuelke, M., Gómez-Durán, A., Boczonadi, V., Elpeleg, O. N., Müller, J. S., & Horváth, R. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw149 · Cited by 42 · see citing works
Langer, L. M., Bonneau, F., Gat, Y., & Conti, E. (2021) · eLife · doi:10.7554/elife.72353 · Cited by 36 · see citing works
Self-citationTo 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
Self-citationMtr4 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
Landscape of Intertwined Associations in Multi-Domain Homo-Oligomeric Proteins
MacKinnon, S. S., & Wodak, S. J. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.11.003 · Cited by 17 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Genetics of human telomere biology disorders
Revy, P., Kannengiesser, C., & Bertuch, A. A. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00527-z · Cited by 242 · see citing works
Rouvière, J. O., Salerno-Kochan, A., Lykke‐Andersen, S., Garland, W., Dou, Y., Rathore, O. S., Molska, E. Š., Wu, G., Schmid, M., Bugai, A., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.05.028 · Cited by 57 · see citing works
Self-citationThe evolving genetic landscape of telomere biology disorder dyskeratosis congenita
Tummala, H., Walne, A. J., Badat, M., Patel, M., Walne, A. M., Alnajar, J., Chow, C. C., Albursan, I., Frost, J. M., Ballard, D., et al. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00118-x · Cited by 28 · see citing works
CRISPR-Cas13 technology portfolio and alliance with other genetic tools
Wu, S., Tian, P., & Tan, T. (2022) · Biotechnology Advances · doi:10.1016/j.biotechadv.2022.108047 · 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
Polák, P., Garland, W., Rathore, O. S., Schmid, M., Salerno-Kochan, A., Jakobsen, L., Gockert, M., Gerlach, P., Silla, T., Andersen, J., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113325 · Cited by 21 · see citing works
Self-citationThe MYCN oncoprotein is an RNA-binding accessory factor of the nuclear exosome targeting complex
Papadopoulos, D., Ha, S. A., Fleischhauer, D., Uhl, L., Russell, T. J., Mikičić, I., Schneider, K., Brem, A., Valanju, O. R., Cossa, G., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.04.007 · Cited by 21 · see citing works
The role of hepatocyte-derived extracellular vesicles in liver and extrahepatic diseases
Li, S., Fang, C. R., Zhang, Z., Xu, R., Shi, H., & Yan, Y. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117502 · Cited by 21 · see citing works
(2024) · doi:10.1016/j.celrep.2023.113639 · Cited by 20 · see citing works
Self-citationStructural basis of MALAT1 RNA maturation and mascRNA biogenesis
Skeparnias, I., Bou‐Nader, C., Anastasakis, D. G., Fan, L., Wang, Y., Hafner, M., & Zhang, J. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01340-4 · Cited by 19 · 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
Self-citationLin, F., Wang, T., Ai, J., Wang, J., Huang, C., Tian, W., Lan, T., Fu, L., & Chen, X. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102108 · Cited by 15 · see citing works
Deciphering the regulatory landscape of enhancer RNAs in health and disease
Wang, Q., ten Dijke, P., & Fan, C. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02436-z · Cited by 15 · 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
RNA 3′end tailing safeguards cells against products of pervasive transcription termination
Wu, G., Rouvière, J. O., Schmid, M., & Jensen, T. H. (2024) · Nature Communications · doi:10.1038/s41467-024-54834-6 · Cited by 7 · see citing works
Self-citationTu, S., Zou, J., Xiong, C., Dai, C., Sun, H., Luo, D., Jin, M., Chen, H., & Zhou, H. (2024) · Journal of Virology · doi:10.1128/jvi.00796-24 · Cited by 7 · see citing works
Uncovering the functions and mechanisms of regulatory elements-associated non-coding RNAs
Fosseprez, O., & Cuvier, O. (2024) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2024.195059 · Cited by 6 · see citing works
Defining the roles of the Integrator, NEXT, and nuclear exosome complexes in Drosophila oogenesis
Lee, Y., Biasini, A., Tipping, C., Hong, S. H., & Zamore, P. D. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116329 · Cited by 6 · see citing works
Bhat, S. S., Asgari, M., Mermet, S., Mishra, P., & Kindgren, P. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae503 · Cited by 6 · see citing works
A functional connection between the Microprocessor and a variant NEXT complex
Imamura, K., Garland, W., Schmid, M., Jakobsen, L., Sato, K., Rouvière, J. O., Jakobsen, K. P., Burlacu, E., Loureiro, M., Lykke‐Andersen, S., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.10.015 · Cited by 6 · see citing works
Self-citationMTR4 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
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2024) · eLife · doi:10.7554/elife.94407.2.sa0 · Cited by 5 · see citing works
Vidal, R., Leen, E. N., Herold, S., et al. (2024) · eLife · doi:10.7554/elife.94407.2.sa1 · Cited by 5 · see citing works
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2024) · eLife · doi:10.7554/elife.94407 · Cited by 4 · see citing works
C-terminal determinants for RNA binding motif 7 protein stability and RNA recognition
Sobeh, A. M., & Eichhorn, C. D. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106928 · Cited by 3 · see citing works
Samajdar, A., Amato, R., Jo, S., Cordes, E., Tai, A., Raffa, G. D., & Batista, L. F. Z. (2026) · Genes & Development · doi:10.1101/gad.353100.125 · Cited by 3 · see citing works
Kuhn, C. C., Chand, M. K., Todesca, S., Williams, K., Keidel, A., Garland, W., Jensen, T. H., & Conti, E. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag088 · Cited by 2 · see citing works
Self-citationRażew, M., & Galej, W. P. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.06.017 · Cited by 2 · see citing works
Genetic aspects of telomere biology disorders
de Tocqueville, S., Morel, H., Ba, I., Revy, P., & Kannengiesser, C. (2025) · Seminars in Hematology · doi:10.1053/j.seminhematol.2026.03.011 · Cited by 2 · see citing works
The Hidden Layer of RNA Variants
Taniue, K., & Akimitsu, N. (2023) · RNA technologies · doi:10.1007/978-3-031-36390-0_17 · Cited by 2 · see citing works
EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery
Wijeratne, H. R. S., Runnebohm, A. M., Barron, M. P., Hampton, A. J., Li, R., Peck Justice, S. A., Lenceski, S. H., Rooney, J. D., Smith-Kinnaman, W. R., Chang, G. S., et al. (2026) · doi:10.64898/2026.01.26.701775 · Cited by 1 · see citing works
Enhancer RNAs: similarities with both lncRNAs and mRNAs reveal novel functions
Vlasov, P. A., & Manley, J. L. (2026) · RNA Biology · doi:10.1080/15476286.2026.2682066 · Cited by 1 · see citing works
Direct RNA-binding by MYCN mediates feedback from RNA processing to transcription controlPreprint
Papadopoulos, D., Ha, S. A., Fleischhauer, D., Uhl, L., Schneider, K., Mikičić, I., Russell, T. J., Brem, A., Valanju, O. R., Gallant, P., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.16.553474 · Cited by 1 · see citing works
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.18.567687 · Cited by 1 · see citing works
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2024) · eLife · doi:10.7554/elife.94407.1 · Cited by 1 · see citing works
CNOT1 contributes to small nuclear non-coding RNA maturationPreprint
Sako, H., Umehara, C., Sakurai, R., & Yamamoto, T. (2025) · Research Square · doi:10.21203/rs.3.rs-6043401/v1 · Cited by 1 · see citing works
RNA decay via the nuclear exosome is essential for Piwi-mediated transposon silencingPreprint
Yu, C., Manolova, T., Tirián, L., Handler, D., Hohmann, U., Nemčko, F., de Montserrat, J. P. I., Collet, G. G., Schnabl, J., Blake, E., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.16.694471 · Cited by 2 · see citing works
Vidal, R. S., Leen, E. N., Herold, S., et al. (2024) · eLife · doi:10.7554/elife.94407.1.sa2
Vidal, R., Leen, E. N., Herold, S., et al. (2024) · eLife · doi:10.7554/elife.94407.2.sa2
Vidal, R., Leen, E. N., Herold, S., et al. (2024) · eLife · doi:10.7554/elife.94407.2.sa3
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2024) · eLife · doi:10.7554/elife.94407.2
Vidal, R. S., Leen, E. N., Herold, S., Müller, M., Fleischhauer, D., Schülein‐Völk, C., Papadopoulos, D., Röschert, I., Uhl, L., Ade, C. P., et al. (2024) · eLife · doi:10.7554/elife.94407.3
Intracellular replication dynamics of influenza A virus impose strong bottleneck effectsPreprint
Segredo-Otero, E. A., & Gresham, D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.18.665558
Pan, Y., Zuo, H., Yan, X., Li, J., Li, Y., Li, J., Wu, Y., Hong, L., Wang, M., Wu, A., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116650
CNOT1 contributes to small nuclear non-coding RNA maturation
Umehara, C., Sakurai, R., Sako, H., & Yamamoto, T. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.153185
Precision in RNA degradation: helicases, ribosome and RNA polymerase stalling, and RNA modifications
Whisenant, D., Soltys, J., Estrella, J. D., & Basu, U. (2026) · Trends in Cell Biology · doi:10.1016/j.tcb.2026.04.005
The RNA exosome: mechanisms of RNA surveillance, regulation, and disease
Upadhyai, P., Quadri, N., & Chandran, D. (2026) · RNA Biology · doi:10.1080/15476286.2026.2685379
RNA exonuclease REXO4 resolves m6A-marked R-loops and suppresses anti-tumor immunity
Zhang, J., Bao, K., Hou, Y., Zhao, N., Chen, Q., Yang, Z., Nie, R., Zhang, C., Wang, H., Zhang, H., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.06.036
Li, Y.-J., Tian, K.-Y., Li, S.-L., Wang, Y., Cao, Q., Wang, S.-H., Zhang, X.-H., Wang, X.-G., Lian, H.-G., Liu, X., et al. (2026) · Biochimica et Biophysica Acta - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168374
HUSH, NEXT PROMPT: Epigenetics and the Nuclear RNA Exosome in Human Aging and Disease
Newman, A. G., & Singh, P. B. (2026) · Cells · doi:10.3390/cells15151378
Stochastic intracellular replication dynamics shape population-level evolution in Influenza A Virus
Segredo-Otero, E. A., & Gresham, D. (2026) · Virus Evolution · doi:10.1093/ve/veag050
DNTTIP2 coordinates RNA exosome activities to ensure fidelity of human ribosome assembly
Pisano, A., Bourdeaux, J., Mazur, J., Roses, F., Roméo, Y., Petfalski, E., Arx, T. V., Portugal-Calisto, D., Oborská‐Oplová, M., Peña, C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76536-x
Mechanisms of transcription termination across the coding and noncoding loci of the genome
Song, A., Hu, M., & Chen, F. (2026) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-026-01005-8
Li, Y., Tian, K., Wang, Y., Wu, S., Qi, C., Wang, S., Zhang, X., Wang, X., Lian, H., Liu, X., et al. (2026) · iScience · doi:10.1016/j.isci.2026.117498
- Authors
- Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H., & Conti, E.
- Affiliations
- Max Planck Society (DE)
- Aarhus University (DK)
- Corresponding author
- Gerlach, Piotr
- Conti, Elena
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2022-07
- Volume
- 82
- Issue
- 13
- Pages
- 2505-2518.e7
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC9278407
- OpenAlex
- W4281874261
- Cited by
- 55
- References
- 73
- Citations by year
- 2026: 14 · 2025: 9 · 2024: 21 · 2023: 6 · 2022: 5
- FWCI
- 3.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 1035, TRR 237, GRK1721, SFB TRR237)
- Max-Planck-Gesellschaft
- Novo Nordisk
- Novo Nordisk Fonden (NNF18OC0033380)
- Max-Planck-Institut für Bildungsforschung
- Medical Research Council
- H2020 European Research Council (740329)
- 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 › Nuclear Structure and Function
- Keywords
- RBM7, protein complex structure, RNA degradation
- MeSH terms
- Cell Nucleus, DNA Helicases, Humans, Protein Binding, RNA, RNA Helicases, RNA Stability, DEAD-box RNA Helicases, Exosomes, 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
