Affinage

EXOSC10

Exosome complex component 10 · UniProt Q01780

Round 2 corrected
Length
885 aa
Mass
100.8 kDa
Annotated
2026-04-28
130 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EXOSC10 is the nucleus-restricted catalytic subunit of the RNA exosome, performing distributive 3′→5′ exoribonuclease activity essential for RNA surveillance, quality control, and regulated gene expression across multiple nuclear RNA classes. Its RNase D-family active site processes rRNA precursors, snoRNAs, telomerase RNA (hTR) precursors, promoter-upstream transcripts (PROMPTs), and ARE-containing mRNAs, and it participates in nonsense-mediated mRNA decay (PMID:17174896, PMID:21705430, PMID:19056938, PMID:14527413, PMID:30575725). EXOSC10 is recruited to the exosome core via its N-terminal PMC2NT domain, which together with cofactor Rrp47 forms a composite surface that docks the Mtr4 helicase; the TRAMP complex stimulates EXOSC10 hydrolytic activity, and cold-induced SUMO1 conjugation downregulates EXOSC10 abundance to reduce ribosome biogenesis (PMID:25319414, PMID:19955569, PMID:26857222). Beyond RNA metabolism, EXOSC10 localizes to DNA double-strand breaks where its ribonucleolytic clearance of damage-induced lncRNAs and R-loops is required for RPA recruitment and controlled DNA end resection during homologous recombination, and conditional knockouts demonstrate essential roles in both oogenesis and spermatogenesis (PMID:31086179, PMID:25632158, PMID:32313933, PMID:29118343).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 1999 High

    Identifying EXOSC10 as the nuclear-specific exosome subunit established that the RNA exosome exists in functionally distinct nuclear and cytoplasmic forms, with PM/Scl-100 (RRP6) exclusively marking the nuclear complex.

    Evidence Biochemical fractionation and immunofluorescence in human cells, with genetic complementation in yeast

    PMID:10465791

    Open questions at the time
    • Human-specific interaction partners beyond the core exosome were not identified
    • Catalytic activity of the human protein was not directly demonstrated
  2. 2001 High

    Demonstrating exosome recruitment to ARE-containing mRNAs via AU-rich element binding proteins revealed that EXOSC10 functions not only in rRNA processing but in regulated mRNA turnover.

    Evidence Mass spectrometry identification of purified mammalian exosome and cell-free ARE-mRNA decay assay

    PMID:11719186

    Open questions at the time
    • Direct contribution of EXOSC10 catalytic activity versus core exosome activity on ARE substrates was not separated
  3. 2003 High

    Linking EXOSC10 to nonsense-mediated mRNA decay expanded its role from general RNA surveillance to a specialized quality-control pathway by showing that its depletion stabilizes premature-termination-codon-containing mRNAs.

    Evidence RNAi knockdown with mRNA decay rate measurement and co-IP with Upf1/Upf2/Upf3X in human cells

    PMID:14527413

    Open questions at the time
    • Whether EXOSC10 is rate-limiting for NMD versus redundant with DIS3 was not resolved
  4. 2006 High

    Crystal structures of the yeast Rrp6 RNase D domain and reconstitution of multisubunit exosomes defined EXOSC10 as a distributive hydrolytic 3′→5′ exoribonuclease mechanistically distinct from the processive activities of other exosome catalytic subunits.

    Evidence X-ray crystallography of Rrp6 with product-bound complexes; in vitro reconstitution of 9-, 10-, and 11-subunit exosomes with activity assays

    PMID:16882719 PMID:17174896

    Open questions at the time
    • Human EXOSC10 structure had not yet been solved
    • How the distributive mechanism operates on structured substrates was unclear
  5. 2008 High

    Discovery that exosome depletion uncovers PROMPTs—short polyadenylated transcripts upstream of promoters—revealed a pervasive nuclear RNA surveillance function for EXOSC10 beyond characterized coding and ribosomal substrates.

    Evidence siRNA depletion of exosome subunits in human cells with tiling microarray detection of unstable transcripts

    PMID:19056938

    Open questions at the time
    • Whether EXOSC10 catalytic activity specifically or the core exosome is responsible for PROMPT clearance was not distinguished
  6. 2009 High

    Reconstituting TRAMP-mediated stimulation of Rrp6 activity identified a direct enzymatic partnership: TRAMP enhances Rrp6 hydrolytic activity ~10-fold independently of its own poly(A) polymerase and helicase functions.

    Evidence In vitro assay with purified TRAMP and recombinant Rrp6, abolished by active-site mutation

    PMID:19955569

    Open questions at the time
    • The molecular basis of stimulation (conformational change vs. substrate delivery) was not determined
    • Whether this mechanism is conserved for human EXOSC10 was not tested
  7. 2011 High

    Solving the human EXOSC10 crystal structure revealed a more exposed active site than the yeast ortholog, explaining its enhanced activity on structured RNA substrates and confirming the conserved RNase D mechanism.

    Evidence X-ray crystallography of human RRP6 exoribonuclease/HRDC domains with comparative in vitro exonuclease assays

    PMID:21705430

    Open questions at the time
    • Structure of the full-length human EXOSC10 in complex with the exosome core was not obtained
  8. 2011 High

    The exosome's association with AID at immunoglobulin switch regions revealed an unexpected role in adaptive immunity, where the exosome enables AID access to both DNA strands during class switch recombination.

    Evidence Co-IP, ChIP at IgH switch regions, and in vitro DNA deamination assay with recombinant exosome in activated B cells

    PMID:21255825

    Open questions at the time
    • Specific catalytic contribution of EXOSC10 versus DIS3 to CSR was not delineated
  9. 2012 High

    Demonstrating that Rrp6 processes Microprocessor-generated TAR stem-loop cleavage products into small RNAs for transcriptional silencing linked EXOSC10 to RNA-mediated chromatin remodeling at the HIV-1 promoter and cellular gene targets.

    Evidence ChIP-seq, RNAi, and reporter assays at HIV-1 promoter and genome-wide cellular targets

    PMID:22980978

    Open questions at the time
    • Whether EXOSC10 directly generates the small RNAs or acts on intermediates was not fully resolved
    • Generalizability beyond HIV-associated and select cellular loci not established
  10. 2014 High

    The crystal structure of the 10-subunit exosome (Exo9+Rrp6) with bound RNA delineated the RNA path to the EXOSC10 active site through the S1/KH ring, and the Rrp6-Rrp47-Mtr4 interface structure explained how EXOSC10 recruits the Mtr4 helicase to the complex.

    Evidence 3.3 Å crystal structure of yeast Exo10-RNA; crystal structure of Rrp6-Rrp47-Mtr4 N-terminus with mutagenesis validation in yeast and human systems

    PMID:25043052 PMID:25319414

    Open questions at the time
    • Full cryo-EM structure of the complete TRAMP-exosome supercomplex with EXOSC10 was not available
    • Kinetic partitioning of substrates between Rrp6 and Dis3 pathways was not quantified
  11. 2015 High

    Showing that EXOSC10 is recruited to DNA double-strand breaks and that its catalytic activity is required for RAD51 recruitment extended its role from RNA metabolism to the DNA damage response and homologous recombination.

    Evidence Co-IP of EXOSC10 with RAD51, dominant-negative catalytic mutant, immunofluorescence at DSBs, and radiation sensitivity in human and Drosophila cells

    PMID:25632158

    Open questions at the time
    • The RNA substrate at DSBs whose clearance enables RAD51 loading was not identified
  12. 2016 High

    Identification of cold-induced SUMO1 conjugation to EXOSC10 as a mechanism to reduce its abundance established the first post-translational regulatory pathway controlling exosome function and connecting environmental stress to ribosome biogenesis.

    Evidence SUMO site mutagenesis, SUMO1 overexpression, RNAi phenocopy of rRNA processing defects and ribosomal subunit ratio shifts

    PMID:26857222

    Open questions at the time
    • Identity of the SUMO E3 ligase targeting EXOSC10 was not determined
    • Whether SUMOylation affects EXOSC10 functions beyond rRNA processing is unknown
  13. 2018 High

    Reconstituting RRP6-dependent trimming of telomerase RNA precursors showed that EXOSC10 acts in the first step of a two-step hTR maturation pathway modulated by RNA tertiary structure and H/ACA RNP assembly.

    Evidence In vitro processing assays with purified RRP6 and PARN on defined hTR precursor substrates with structural analysis

    PMID:30575725

    Open questions at the time
    • Whether this pathway is rate-limiting for telomerase assembly in vivo was not tested
  14. 2019 High

    Mechanistic dissection of the DSB repair defect revealed that EXOSC10 clears damage-induced lncRNAs and DNA-RNA hybrids at break sites, and that failure to do so causes uncontrolled DNA end resection and loss of RPA recruitment—a defect rescued by RNase H1.

    Evidence siRNA knockdown, S9.6 antibody detection of R-loops, DNA end resection assay, RNase H1 rescue, and transcription inhibitor epistasis in human cells

    PMID:31086179

    Open questions at the time
    • The specific dilncRNA species targeted by EXOSC10 at breaks were not sequenced
    • How EXOSC10 is recruited to DSBs remains unclear
  15. 2020 High

    Conditional knockout in oocytes demonstrated that EXOSC10 sculpts the maternal transcriptome to enable germinal vesicle breakdown, linking its RNA degradation activity to CDK1 activation, nuclear lamina disassembly, endomembrane integrity, and female fertility.

    Evidence CRISPR/Cas9 conditional KO with single-oocyte RNA-seq, live-cell imaging of GVBD, and phenotypic characterization

    PMID:32313933

    Open questions at the time
    • Direct RNA targets whose degradation is rate-limiting for GVBD were not functionally validated individually
    • Whether EXOSC10 acts independently of the core exosome in oocytes is unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis for substrate partitioning between EXOSC10 and DIS3 within the intact nuclear exosome, the mechanism by which EXOSC10 is recruited to DNA damage sites, and whether its roles in gametogenesis and DNA repair require core-exosome association or reflect exosome-independent functions.
  • No full structural model of human nuclear exosome with both catalytic subunits and substrates
  • Recruitment mechanism of EXOSC10 to DSBs undefined
  • Exosome-dependent versus independent functions in germ cells not separated

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140098 catalytic activity, acting on RNA 6 GO:0003723 RNA binding 3 GO:0016787 hydrolase activity 3
Localization
GO:0005634 nucleus 3 GO:0005694 chromosome 1 GO:0005730 nucleolus 1
Pathway
R-HSA-8953854 Metabolism of RNA 7 R-HSA-1640170 Cell Cycle 2 R-HSA-73894 DNA Repair 2 R-HSA-168256 Immune System 1 R-HSA-392499 Metabolism of proteins 1
Complex memberships
RNA exosome (nuclear form)TRAMP complex (functional partner)

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 Human EXOSC10 (PM/Scl-100/RRP6) was identified as a component of the human PM-Scl complex, which is the functional equivalent of the yeast exosome. The nuclear form of the complex in both yeast and humans contains Rrp6p/PM-Scl100 exclusively, distinguishing the nuclear from cytoplasmic exosome. Human homologs complemented mutations in respective yeast exosome genes. Biochemical fractionation, indirect immunofluorescence, genetic complementation Genes & development High 10465791
2001 PM/Scl100 (EXOSC10) was identified as a component of the human exosome required for rapid degradation of ARE-containing mRNAs. AU-rich element binding proteins recruit the exosome (including PM/Scl100) to unstable RNAs to promote their degradation. The mammalian exosome was purified and characterized by mass spectrometry. Mass spectrometry, cell-free RNA decay assay, immunoprecipitation Cell High 11719186
2003 Downregulating PM/Scl100 (EXOSC10) significantly increases the abundance of nonsense-containing mRNAs and slows their decay rate, demonstrating its role in nonsense-mediated mRNA decay (NMD). NMD factors Upf1, Upf2, and Upf3X co-immunopurify with PM/Scl100 and other exosomal components, linking EXOSC10 to both 3'→5' degradation and the NMD pathway. RNAi knockdown, mRNA decay rate assay, co-immunoprecipitation Molecular cell High 14527413
2006 The crystal structure of yeast Rrp6p (ortholog of EXOSC10) reveals a conserved RNase D core with an HRDC domain in an unusual conformation important for RNA processing. Co-crystals with AMP and UMP products reveal how the protein specifically recognizes ribonucleotides. In vivo mutational studies show domain contacts are critical for the processing function, highlighting differences from prokaryotic RNase D counterparts. X-ray crystallography, in vitro exonuclease assay, in vivo mutagenesis Proceedings of the National Academy of Sciences of the United States of America High 16882719
2006 Reconstitution of 9-, 10-, and 11-subunit eukaryotic exosomes established that human Rrp41/Rrp45 has processive phosphorolytic activity, yeast Rrp44 has processive hydrolytic activity, and Rrp6 (EXOSC10 ortholog) has distributive hydrolytic 3'→5' exoribonuclease activity. The 3.35 Å X-ray structure of the 9-subunit human exosome was also determined, revealing the conserved architecture. In vitro reconstitution, exonuclease assays with multiple RNA substrates, X-ray crystallography Cell High 17174896
2008 Rrp6p (EXOSC10 ortholog) can carry out some RNA 3'-end processing functions (5.8S rRNA, snoRNAs) and degrade certain rRNA intermediates independently of physical association with the core exosome. However, Rrp6p–core exosome interaction is required for efficient degradation of poly(A)+ rRNA processing products that require combined activities of Dis3p and Rrp6p. Truncation mutants, co-purification assays, in vivo RNA analysis Nucleic acids research Medium 18940861
2008 Depletion of the RNA exosome (including its nuclear component equivalent to EXOSC10) from human cells revealed a class of short, polyadenylated, highly unstable promoter upstream transcripts (PROMPTs) produced ~0.5–2.5 kb upstream of active transcription start sites, demonstrating that EXOSC10/exosome normally degrades these bidirectional transcripts. siRNA depletion, tiling microarray, nuclear RNA analysis Science High 19056938
2009 The TRAMP complex enhances RNA degradation by the nuclear exosome specifically through stimulation of Rrp6 (EXOSC10 ortholog) activity. Purified TRAMP incubated with recombinant Rrp6 results in a 10-fold enhancement of RNA degradation rate via the hydrolytic activity of Rrp6; an Rrp6 active-site mutant abolishes this enhancement. This enhancement is independent of TRAMP's poly(A) polymerase or helicase activities. In vitro reconstituted RNA degradation assay with purified components, active-site mutagenesis The Journal of biological chemistry High 19955569
2011 Human RRP6 (EXOSC10/PM-Scl100) was characterized biochemically; full-length enzyme and truncation mutants retaining catalytic activity were expressed, and the X-ray structure of the human RRP6 exoribonuclease and HRDC domain was determined. Human RRP6 degrades structured RNA substrates more effectively than yeast Rrp6 due to a more exposed active site. Human RRP6 catalyzes distributive 3'→5' exoribonuclease activity on nuclear transcripts including ribosomal RNA precursors. X-ray crystallography, in vitro exonuclease assays, truncation mutagenesis RNA (New York, N.Y.) High 21705430
2011 The RNA exosome (with EXOSC10 contributing to both strands access) associates with AID (activation-induced cytidine deaminase) in B cells activated for class switch recombination. The exosome complex accumulates on IgH switch regions in an AID-dependent fashion and is required for optimal class switch recombination. A recombinant RNA exosome core complex imparts robust AID- and transcription-dependent DNA deamination of both strands in vitro, revealing a role for the exosome in targeting AID to template DNA strand. Co-immunoprecipitation, ChIP, in vitro DNA deamination assay with recombinant exosome, RNAi Cell High 21255825
2011 Drosophila Rrp6 (ortholog of EXOSC10) is required for cell proliferation and error-free mitosis independently of the core exosome subunit Rrp40. Depletion of dRrp6 increases cell cycle- and mitosis-related transcripts, decreases mitotic frequency, and causes chromosome congression/separation/segregation defects. dRrp6 dynamically redistributes to condensed chromosomes during mitosis, while core subunits localize to microtubules. RNAi knockdown in S2 cells, microarray, live-cell imaging, phospho-histone H3 analysis Molecular biology of the cell Medium 19225159
2011 5-Fluorouracil (5FU) incorporation into RNA modifies Rrp6 (EXOSC10 ortholog in Drosophila) function in two ways: (1) it alters the repertoire of multimolecular complexes containing Rrp6, consistent with sequestration in ribonucleoprotein complexes; and (2) 5FU-containing RNA is less susceptible to degradation by Rrp6, as shown by in vitro activity assays. This reveals that RNA surveillance by EXOSC10 is compromised by 5FU. Gel filtration, in vitro Rrp6 exonuclease activity assay with 5FU-containing RNA Molecular cancer research : MCR Medium 21289297
2012 Microprocessor (Drosha/Dgcr8), Setx, Xrn2, and Rrp6 (EXOSC10 ortholog) co-operate to induce premature termination of RNAPII transcription at the HIV-1 promoter and cellular gene targets. Rrp6 processes the TAR stem-loop cleavage product to generate a small RNA required for transcriptional repression and chromatin remodeling. ChIP-seq identified genome-wide cellular gene targets whose transcription is modulated by this microprocessor-Rrp6 mechanism. ChIP-seq, RNAi knockdown, reporter assays, chromatin remodeling assays Cell High 22980978
2014 A 3.3 Å crystal structure of a ten-subunit yeast RNA exosome (Exo9 core + Rrp6) bound to poly(A) RNA showed that the Rrp6 catalytic domain rests atop the Exo9 S1/KH ring above the central channel, with the RNA 3' end anchored in the Rrp6 active site and remaining RNA traversing the S1/KH ring. Solution studies with human and yeast exosomes demonstrated that this RNA path to Rrp6 is conserved and dependent on S1/KH ring integrity. X-ray crystallography at 3.3 Å, solution biochemical studies with human exosome Nature High 25043052
2014 Rrp6 and its cofactor Rrp47 form a highly intertwined structural unit via their N-terminal domains. Together they create a composite conserved surface groove that binds the N-terminus of the Mtr4 helicase, thereby recruiting Mtr4 to the exosome. Mutations in conserved residues at the Rrp6–Mtr4 interface disrupt their interaction and inhibit cell growth, linking this structural interface to exosome function. X-ray crystallography, in vitro binding assays, mutagenesis, cell growth assays The EMBO journal High 25319414
2015 EXOSC10 (RRP6) and its Drosophila ortholog RRP6 are recruited to DNA double-strand breaks (DSBs). Depletion of RRP6/EXOSC10 does not affect H2AX phosphorylation but impairs RAD51 recruitment to DSBs without altering RAD51 levels. Catalytically inactive RRP6 (Y361A mutant) overexpression also inhibits RAD51 recruitment. EXOSC10 can be co-immunoprecipitated with RAD51, linking EXOSC10 to homologous recombination. EXOSC10-depleted cells show hypersensitivity to radiation. RNAi, co-immunoprecipitation, immunofluorescence at DSBs, dominant-negative mutagenesis, radiation sensitivity assay Journal of cell science High 25632158
2016 Cooling of mammalian cells triggers SUMOylation of EXOSC10 (hRrp6/PM/Scl-100), specifically conjugation of SUMO1 to defined sites on EXOSC10 identified by mutagenesis. This SUMOylation reduces EXOSC10 abundance. EXOSC10 knockdown by RNAi recapitulates the 3' pre-rRNA processing defects and reduced 40S:60S ribosomal subunit ratio seen in the cold. Overexpression of SUMO1 alone is sufficient to suppress EXOSC10 abundance, demonstrating that SUMOylation is a post-translational mechanism for downregulating EXOSC10 and thereby reducing ribosome biogenesis. SUMOylation site mutagenesis, RNAi, ribosomal subunit ratio analysis, in vivo cooling model RNA (New York, N.Y.) High 26857222
2017 EXOSC10 protein is detected in nucleoli and the cytoplasm of mitotic and meiotic male germ cells and transiently associates with the XY body (targeted by meiotic sex chromosome inactivation). EXOSC10 becomes unstable at later stages of gamete development, indicating post-translational regulation. Conditional knockout of Exosc10 in male germ cells using Stra8- or Vasa-cre results in small testes, impaired germ cell differentiation, and subfertility, establishing an essential role for EXOSC10 in germ cell growth and development. Conditional knockout (Cre-lox), immunofluorescence localization, testis histology Scientific reports High 29118343
2018 RRP6 (EXOSC10) participates in two-step processing of human telomerase RNA (hTR) precursor: longer extended forms are first trimmed by RRP6 and shorter forms are then processed by PARN. H/ACA RNP assembly promotes productive processing by disrupting tertiary RNA interactions (triplex) in longer precursors that otherwise favor RNA degradation. Thus EXOSC10 activity on hTR precursors is modulated by RNA structure and RNP assembly state. In vitro processing assays with RRP6 and PARN, RNA structure analysis, RNP assembly assays Nature communications High 30575725
2019 EXOSC10 is required for DNA double-strand break repair by homologous recombination. Depletion of EXOSC10 leads to increased damage-induced long non-coding RNA (dilncRNA) and DNA-RNA hybrid (R-loop) levels at DSBs. RPA targeting to DNA damage sites is impaired, while DNA end resection is hyper-stimulated in EXOSC10-depleted cells. The resection deregulation is abolished by transcription inhibitors, and RNase H1 overexpression restores RPA recruitment, demonstrating that EXOSC10-mediated RNA clearance of dilncRNAs is required for RPA assembly and controlled DNA end resection. siRNA knockdown, immunofluorescence at DSBs, DNA-RNA hybrid (S9.6) detection, end-resection assay, RNase H1 rescue Nature communications High 31086179
2020 EXOSC10 sculpts the oocyte transcriptome during the growth-to-maturation transition. Oocyte-specific conditional knockout of Exosc10 in mice causes female subfertility due to delayed germinal vesicle breakdown (GVBD). Single-oocyte RNA-seq revealed dysregulation of mRNAs encoding endomembrane trafficking proteins and meiotic cell cycle regulators. EXOSC10-depleted oocytes show impaired endomembrane components (endosomes, lysosomes, ER, Golgi), failure of CDK1 activation (due to persistent WEE1 activity), impaired lamina phosphorylation/disassembly, and rRNA processing defects causing higher rates of developmentally incompetent oocytes. CRISPR/Cas9 conditional knockout, single-oocyte RNA-seq, immunofluorescence, live-cell imaging of GVBD Nucleic acids research High 32313933

Source papers

Stage 0 corpus · 130 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
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2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2012 The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Molecular cell 973 22681889
2009 A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the Ras oncogene. Cell 843 19490893
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2008 Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication. Cell 787 18854154
2003 Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature genetics 754 14702039
2001 AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell 736 11719186
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2008 RNA exosome depletion reveals transcription upstream of active human promoters. Science (New York, N.Y.) 616 19056938
2004 Cellular distribution and functions of P2 receptor subtypes in different systems. International review of cytology 613 15548415
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2018 Extracellular ATP and P2 purinergic signalling in the tumour microenvironment. Nature reviews. Cancer 566 30006588
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2002 Functional proteomic analysis of human nucleolus. Molecular biology of the cell 391 12429849
1999 The yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases. Genes & development 390 10465791
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2010 Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 318 21145461
2003 Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Molecular cell 307 14527413
2007 P2 receptors in cardiovascular regulation and disease. Purinergic signalling 288 18368530
2008 Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Genes & development 282 18172165
2011 The RNA exosome targets the AID cytidine deaminase to both strands of transcribed duplex DNA substrates. Cell 248 21255825
2006 Regulation of platelet functions by P2 receptors. Annual review of pharmacology and toxicology 226 16402906
2010 The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L. The EMBO journal 224 20531386
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2006 Accumulation of unstable promoter-associated transcripts upon loss of the nuclear exosome subunit Rrp6p in Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America 196 16484372
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2014 Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA. Nature 126 25043052
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2008 Evidence for core exosome independent function of the nuclear exoribonuclease Rrp6p. Nucleic acids research 86 18940861
2019 EXOSC10 is required for RPA assembly and controlled DNA end resection at DNA double-strand breaks. Nature communications 85 31086179
2009 TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6. The Journal of biological chemistry 85 19955569
2006 Roles of P2 receptors in glial cells: focus on astrocytes. Purinergic signalling 82 18404462
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2008 Degradation of a polyadenylated rRNA maturation by-product involves one of the three RRP6-like proteins in Arabidopsis thaliana. Molecular and cellular biology 73 18285452
2019 Extracellular Nucleotides and P2 Receptors in Renal Function. Physiological reviews 72 31437091
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2011 Activities of human RRP6 and structure of the human RRP6 catalytic domain. RNA (New York, N.Y.) 63 21705430
2016 PtdIns(4,5)P2 signaling regulates ATG14 and autophagy. Proceedings of the National Academy of Sciences of the United States of America 60 27621469
2003 Contribution of domain structure to the RNA 3' end processing and degradation functions of the nuclear exosome subunit Rrp6p. RNA (New York, N.Y.) 58 12923258
2001 Glucose deprivation and chemical hypoxia: neuroprotection by P2 receptor antagonists. Neurochemistry international 57 11099776
1999 Salivary gland P2 nucleotide receptors. Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists 56 10759423
1996 Design and pharmacology of selective P2-purinoceptor antagonists. Journal of autonomic pharmacology 56 9131412
1990 Identification of protein components reactive with anti-PM/Scl autoantibodies. Clinical and experimental immunology 56 2199097
2016 Bacteriophage P2. Bacteriophage 55 27144088
1987 Both P1 and P2 protamine genes are expressed in mouse, hamster, and rat. Biology of reproduction 54 3676400
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