Affinage

DDX46

Probable ATP-dependent RNA helicase DDX46 · UniProt Q7L014

Length
1031 aa
Mass
117.4 kDa
Annotated
2026-06-09
33 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DDX46 (the yeast Prp5 ortholog) is a DEAD-box RNA-dependent ATPase that performs two distinct nuclear functions: assembly and fidelity control of the spliceosome, and post-transcriptional control of innate-immune gene expression (PMID:2349233, PMID:8969184, PMID:28846086). In splicing, it is required for spliceosome assembly (PMID:2349233) and bridges U1 and U2 snRNPs through distinct domains in an ATP-dependent manner to drive pre-spliceosome (complex A) formation (PMID:14713954). As an RNA-dependent ATPase with selectivity for U2 snRNA, it catalyzes a conformational change in U2 snRNP that exposes the branch-point pairing sequence (PMID:8969184, PMID:11927574), a switch in its RecA-like domains that occurs only when both ATP and RNA are bound (PMID:31712821). DDX46 anchors on the SF3b component SF3B1/Hsh155 through its N-terminal sequences, with its N-plug occupying the SF3B1 RNA path; cancer-associated SF3B1 mutations map to residues that contact DDX46 and alter branch-site selection (PMID:36797247, PMID:28087715). Mechanistically it enforces branch-site fidelity: its ATPase activity gates branch region–U2 duplex formation, it binds U2 RNA flanking the branchpoint-interacting stem-loop, and it is released only upon correct U2–branch-site base-pairing—a proofreading step that licenses tri-snRNP recruitment (PMID:18082608, PMID:25561497, PMID:34349264). In antiviral innate immunity, nuclear DDX46 binds MAVS, TRAF3 and TRAF6 transcripts via a CCGGUU element and recruits the m6A eraser ALKBH5 through its DEAD helicase domain to demethylate and nuclearly retain these transcripts, suppressing type I interferon; RNA virus infection triggers caspase-dependent cleavage and nuclear-to-cytoplasmic translocation of DDX46, releasing the retained transcripts to potentiate the IFN response (PMID:28846086, PMID:41854249). Loss-of-function studies in zebrafish establish in vivo requirements for DDX46 in pre-mRNA splicing during digestive-organ and brain development and in multilineage hematopoietic stem-cell differentiation (PMID:22442707, PMID:23635340).

Mechanistic history

Synthesis pass · year-by-year structured walk · 21 steps
  1. 1990 High

    Established that the DDX46 ortholog Prp5 is essential for spliceosome assembly, defining the gene as a core splicing factor before any biochemical activity was known.

    Evidence genetic complementation of a temperature-sensitive yeast mutant with splicing assays

    PMID:2349233

    Open questions at the time
    • Did not define the molecular activity
    • No partner proteins identified
    • No mechanism for how assembly fails
  2. 1993 High

    Placed Prp5 in a functional module with SF3a-type factors acting on U2 snRNA, and first implicated ATP and helicase activity in promoting a U1/U2 snRNP conformational change.

    Evidence genetic epistasis and biochemical complementation with in vitro splicing in yeast

    PMID:8405998

    Open questions at the time
    • ATPase activity not directly demonstrated
    • Which snRNP is remodeled left ambiguous
    • No structural basis
  3. 1996 High

    Demonstrated that Prp5 is itself an RNA-dependent ATPase with selectivity for U2 snRNA that drives an ATP-dependent conformational change exposing the branch point, converting the genetic inference into a defined enzymatic activity.

    Evidence in vitro ATPase assay with purified protein and RNaseH probing in extracts

    PMID:8969184

    Open questions at the time
    • RNA-binding sites on U2 not mapped
    • Did not address fidelity/proofreading
  4. 2002 Medium

    Mapped the conformational-change function to the ATP-binding helicase domain by linking a temperature-sensitive mutation in motif I to reduced U2 snRNP remodeling.

    Evidence 2'-O-methyl oligonucleotide binding and physical association assays with ts-mutant inactivation in yeast

    PMID:11927574

    Open questions at the time
    • Single lab
    • Structural detail of the conformational change absent
  5. 2004 High

    Showed that Prp5 physically bridges U1 and U2 snRNPs through distinct domains and that ATP binding/hydrolysis is required for complex A formation, generalizing the mechanism across human and S. pombe.

    Evidence depletion-reconstitution, reciprocal Co-IP, domain mapping and native complex isolation across organisms

    PMID:14713954

    Open questions at the time
    • Structural geometry of the bridge unknown
    • Domain boundaries for each snRNP contact coarse
  6. 2007 High

    Defined Prp5 ATPase activity as a branch-site fidelity checkpoint by showing ATPase-weakening mutations rescue suboptimal branch sites in a manner reversed by compensatory U2 mutations.

    Evidence alanine scanning, in vivo and in vitro ATPase/splicing assays, genetic epistasis with U2 snRNA mutations

    PMID:18082608

    Open questions at the time
    • Physical basis of gating not yet shown
    • Release step not directly observed
  7. 2009 Medium

    Extended Prp5 association beyond early assembly, showing it accompanies pre-mRNA from the commitment complex through disassembly with both ATP-independent and ATP-dependent roles.

    Evidence GST pulldown with radiolabeled pre-mRNA, glycerol gradient sedimentation, ATP-depletion in vitro

    PMID:19451545

    Open questions at the time
    • Functional role at later stages undefined
    • Single lab
  8. 2015 High

    Resolved the proofreading mechanism: Prp5 binds U2 RNA flanking the branchpoint-interacting stem-loop and is released only upon correct U2-branch-site pairing, coupling fidelity to tri-snRNP recruitment.

    Evidence prespliceosome isolation, RNA-protein crosslinking and mutant functional analysis

    PMID:25561497

    Open questions at the time
    • Atomic structure of bound state absent
    • Coupling to ATP cycle not visualized
  9. 2016 High

    Identified SF3B1/Hsh155 HEAT-domain contacts as the physical determinant of branch-site selectivity, explaining how cancer-associated SF3B1 mutations phenocopy Prp5 fidelity mutations.

    Evidence two-hybrid, pulldown/Co-IP, in vivo/in vitro splicing and yeast genetics

    PMID:28087715

    Open questions at the time
    • Structural interface only inferred at this stage
    • Human cancer relevance correlative
  10. 2016 High

    Showed U2 snRNA pseudouridylation tunes Prp5 enzymatic output, linking an RNA modification to ATPase activity, U2 binding and spliceosome assembly fidelity.

    Evidence in vitro ATPase/RNA-binding assays, designer snoRNA rescue, DMS probing and in vivo splicing

    PMID:26873591

    Open questions at the time
    • Mechanism by which pseudouridines stimulate ATPase unresolved
    • Conservation to human DDX46 not tested here
  11. 2019 Medium

    Linked RecA-domain dynamics to fidelity by showing the open/closed conformational switch requires simultaneous ATP and RNA, and that fidelity-altering mutations change switch dynamics.

    Evidence single-molecule FRET with mutagenesis

    PMID:31712821

    Open questions at the time
    • Single lab
    • Direct correlation to in vivo proofreading kinetics incomplete
  12. 2021 High

    Provided the structural mechanism for indirect proofreading: cryo-EM of a pre-A intermediate showed Prp5 blocks U1/U2 repositioning until Hsh155 HEAT closure on the bulged branch adenosine destabilizes Prp5.

    Evidence cryo-EM of stalled spliceosome intermediates with branch-adenosine deletion and mutagenesis

    PMID:34349264

    Open questions at the time
    • Human DDX46 complex not resolved in this study
    • ATP hydrolysis coupling to release timing
  13. 2023 High

    Defined the human DDX46-SF3b interface structurally, showing N-terminal anchoring on SF3B1 with the N-plug in the RNA path, mutual exclusivity with DDX42, and direct contact with cancer-mutated SF3B1 residues.

    Evidence cryo-EM of DDX46-SF3b and DDX46-U2 intermediates with in vitro binding and mutagenesis

    PMID:36797247

    Open questions at the time
    • Functional consequence of DDX46/DDX42 exchange in cells unresolved
    • Dynamics of N-plug displacement not captured
  14. 2020 Medium

    Connected splicing-factor function to transcription by showing Prp5 directly binds the SAGA component Spt8p, coupling pre-spliceosome assembly to Pol II recruitment at intron-containing genes.

    Evidence in vitro interaction, ChIP/ChIP-seq, suppressor genetics and in vivo splicing

    PMID:32399566

    Open questions at the time
    • Single lab
    • Conservation of Spt8p coupling to human DDX46 untested
  15. 2025 Medium

    Refined the early prespliceosome network, implicating Prp5 in displacing Cus2 and revealing ATP-independent assembly routes when Sub2 or Cus2 is absent.

    Evidence in vitro splicing with ATP depletion and genetic deletion of splicing factors

    PMID:41027713

    Open questions at the time
    • No replication yet
    • Order of Cus2 displacement versus ATPase cycle unclear
  16. 2017 High

    Revealed a second, splicing-independent role: nuclear DDX46 binds MAVS/TRAF3/TRAF6 transcripts via a CCGGUU element and recruits ALKBH5 through its DEAD domain to demethylate and retain them, suppressing interferon.

    Evidence RIP, Co-IP, m6A sequencing, nuclear retention assays and in vivo viral infection models

    PMID:28846086

    Open questions at the time
    • How DDX46 selects CCGGUU targets mechanistically unclear
    • Relationship to its splicing role not addressed
  17. 2025 Medium

    Completed the antiviral switch by showing RNA virus infection induces caspase-dependent DDX46 cleavage and nuclear export, releasing retained immune transcripts to amplify IFN responses.

    Evidence RNA-binding protein knockout screen, caspase cleavage assays, fractionation/imaging and IFN reporter assays

    PMID:41854249

    Open questions at the time
    • Cleavage site and responsible caspase detail limited
    • Single lab
  18. 2025 Medium

    Extended the ALKBH5-coupled demethylation role to lymphocyte biology, showing DDX46/ALKBH5/treRNA1 demethylates BCR-signaling transcripts handed to HuR for export and translation.

    Evidence Co-IP, nuclear fractionation, m6A analysis and loss-of-function assays

    PMID:39987653

    Open questions at the time
    • treRNA1 role mechanistically thin
    • Limited methodological detail
  19. 2013 Medium

    Established an in vivo developmental requirement, showing zebrafish Ddx46 is needed for multilineage HSC differentiation via gata1a-dependent erythro/lymphopoiesis.

    Evidence zebrafish mutant analysis, in situ hybridization and lineage marker expression

    PMID:23635340

    Open questions at the time
    • Whether phenotype reflects splicing or immune role untested
    • Direct targets unknown
  20. 2019 Medium

    Demonstrated in vivo splicing function in vertebrates, with zebrafish Ddx46 mutants accumulating unspliced pre-mRNA in digestive organs and brain.

    Evidence forward genetic screen with RT-PCR splicing analysis and in situ hybridization

    PMID:22442707

    Open questions at the time
    • Tissue specificity of splicing dependence unexplained
    • Affected introns not catalogued
  21. 2025 Medium

    Implicated DDX46 in cancer via O-GlcNAcylation at Ser257 by OGT, which stabilizes the protein and drives PI3K/Akt-dependent hepatocellular carcinoma growth.

    Evidence Co-IP, site-specific mutagenesis, ubiquitination and PI3K/Akt signaling assays

    PMID:41176131

    Open questions at the time
    • Whether oncogenic effect derives from splicing or immune role unknown
    • Single lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how DDX46's spliceosomal proofreading function and its ALKBH5-coupled m6A/innate-immune RNA-retention function are partitioned or co-regulated within the same nuclear protein.
  • No structural model of the DDX46-ALKBH5 complex
  • Determinants directing DDX46 to splicing versus immune transcripts unknown
  • Human cancer mechanism not linked to either defined activity

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 4 GO:0140657 ATP-dependent activity 4 GO:0016787 hydrolase activity 2 GO:0060090 molecular adaptor activity 2 GO:0140098 catalytic activity, acting on RNA 2
Localization
GO:0005634 nucleus 3 GO:0005829 cytosol 1
Pathway
R-HSA-8953854 Metabolism of RNA 4 R-HSA-168256 Immune System 3 R-HSA-1266738 Developmental Biology 2
Partners
ALKBH5JMJD6OGTPRP11PRP21PRP9SF3B1SPT8
Complex memberships
SF3bU2 snRNPpre-spliceosome (complex A)

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 DDX46 binds MAVS, TRAF3, and TRAF6 antiviral transcripts via their conserved CCGGUU element and recruits the m6A eraser ALKBH5 through its DEAD helicase domain to demethylate these transcripts, causing their nuclear retention and preventing their translation, thereby inhibiting type I interferon production after viral infection. RNA immunoprecipitation, Co-IP, m6A sequencing, nuclear retention assays, in vivo viral infection models Nature immunology High 28846086
2023 Cryo-EM structures of the DDX46-SF3b complex and DDX46-U2 snRNP assembly intermediate reveal that DDX46 is anchored on SF3B1 through its N-terminal sequences with its N-plug occupying the RNA path of SF3B1; DDX46 and DDX42 are mutually exclusive for SF3B1 binding, and cancer-driving SF3B1 mutations target residues that directly interact with DDX46. Cryo-electron microscopy (cryo-EM), in vitro binding assays, structural analysis with mutagenesis Nature communications High 36797247
1990 Yeast Prp5 (DDX46 ortholog) is a DEAD-box helicase-like protein required for pre-mRNA splicing; spliceosome assembly does not occur in its absence. Genetic complementation of temperature-sensitive mutation, DNA sequencing, splicing assays Proceedings of the National Academy of Sciences of the United States of America High 2349233
1993 Yeast Prp5 (DDX46 ortholog) interacts with PRP9, PRP11, and PRP21, and all four proteins act concertedly with stem-loop IIa of U2 snRNA to promote U2 snRNP binding to pre-mRNA during spliceosome assembly; ATP and the helicase activity of Prp5 are required, suggesting it promotes a conformational change in U1 or U2 snRNP. Genetic epistasis analysis, biochemical complementation, in vitro splicing assays Genes & development High 8405998
1996 Yeast Prp5 (DDX46 ortholog) is an RNA-dependent ATPase with 7-fold specificity for U2 snRNA over other snRNAs; it mediates an ATP-dependent conformational change in the intact U2 snRNP, making the branch point pairing sequence accessible for pre-spliceosome formation. In vitro ATPase assay with purified protein, RNaseH assay in extracts The Journal of biological chemistry High 8969184
2004 Human and S. pombe Prp5 (DDX46 orthologs) physically associate with both U1 and U2 snRNPs through distinct domains; ATP binding and hydrolysis are required for pre-spliceosome complex A formation; Prp5 bridges U1 and U2 snRNPs, and a Prp5-associated U1/U2 complex was observed in S. pombe. Depletion-reconstitution from extracts, co-immunoprecipitation, domain mapping, native complex isolation The EMBO journal High 14713954
2007 Prp5 ATPase activity gates branch region-U2 snRNA duplex formation as a fidelity checkpoint; reduced ATPase activity (SAT motif mutations in motif III) improves splicing of suboptimal branch-site substrates, and this effect is abrogated by compensatory U2 snRNA mutations that increase branch region-U2 pairing. Alanine scanning mutagenesis, in vivo splicing assays, in vitro ATPase assays, genetic epistasis with U2 snRNA mutations Molecular cell High 18082608
2015 Prp5 binds directly to U2 snRNA in regions flanking the branchpoint-interacting stem-loop (BSL); it stabilizes the BSL and is released upon U2-branch site base-pairing; mutations impairing U2-branch site pairing retard Prp5 release and impede tri-snRNP association, establishing a novel proofreading mechanism. Prespliceosome isolation, RNA-protein crosslinking, mutant Prp5 functional analysis, in vitro splicing Genes & development High 25561497
2016 SF3B1 (Hsh155) interacts directly with Prp5 through its HEAT motifs; cancer-associated SF3B1/hsh155 mutations alter this physical interaction, leading to altered branch site selectivity during pre-spliceosome formation, phenocopying Prp5 mutations. Directed two-hybrid, pulldown/Co-IP, in vivo and in vitro splicing assays, yeast genetics Genes & development High 28087715
2016 Pseudouridines at positions 42 and 44 of U2 snRNA stimulate Prp5 ATPase activity and Prp5 binding affinity for U2 snRNA; blocking pseudouridylation reduces Prp5 ATPase activity, impairs spliceosome assembly, and causes splicing deficiency. In vitro ATPase assays, RNA binding assays, designer snoRNA rescue, DMS probing, in vivo splicing analysis The EMBO journal High 26873591
2021 Cryo-EM structure of a pre-A spliceosome intermediate reveals that Prp5 blocks large-scale repositioning of U1 and U2 snRNPs required for tri-snRNP binding; binding of Hsh155HEAT to the bulged BS-A of the U2-BS helix triggers Hsh155HEAT closure, which destabilizes Prp5 binding, providing a structural mechanism for indirect branch-site proofreading by Prp5. Cryo-electron microscopy of stalled spliceosome assembly intermediates, branch-site adenosine deletion, mutational analysis Nature High 34349264
2002 Prp5 physically associates with U2 snRNP and promotes an ATP-enhanced conformational change in U2 snRNP that is required for branch-point region binding; the temperature-sensitive prp5-1 mutation maps to ATP-binding motif I within the helicase domain and reduces U2 snRNP conformational change. 2'-O-methyl oligonucleotide binding assay, gel electrophoresis, heat inactivation of temperature-sensitive mutants, physical association assays The Journal of biological chemistry Medium 11927574
2009 Prp5 associates with pre-mRNA from the commitment complex stage through spliceosome disassembly; it co-sediments with active spliceosomes and pulls down pre-mRNA, splicing intermediates, and lariat product but reduced amounts of spliced mRNA; Prp5 is an integral spliceosomal component with both ATP-independent and ATP-dependent functions at multiple stages. GST pulldown with radiolabeled pre-mRNA, glycerol gradient sedimentation, ATP-depletion experiments RNA (New York, N.Y.) Medium 19451545
2019 The Prp5 RecA-like domains undergo a large conformational rearrangement (open/closed) only when both ATP and RNA are bound simultaneously; fidelity-altering Prp5 mutations change the dynamics of this conformational switch, linking RecA domain movement to branch-site recognition during spliceosome assembly. Single-molecule FRET (smFRET), mutagenesis Nucleic acids research Medium 31712821
2020 Prp5 directly interacts with Spt8p (a TBP-binding module component of the SAGA complex), but not Spt3p; this interaction modulates Prp5's splicing proofreading function and mutually influences RNA Pol II recruitment to intron-containing genes, establishing a reciprocal coupling between transcription initiation/elongation and pre-spliceosome assembly. In vitro direct protein interaction assay, chromatin immunoprecipitation (ChIP), ChIP-seq, genetic epistasis (suppressor screen), in vivo splicing analysis Nucleic acids research Medium 32399566
2025 RNA virus infection induces caspase-dependent cleavage of DDX46, which triggers its translocation from the nucleus to the cytoplasm; this translocation releases nuclear-retained innate immune transcripts (previously sequestered by DDX46), licensing their rapid translation and potentiating robust IFN responses. RNA-binding protein knockout library screen, caspase cleavage assays, subcellular fractionation/imaging, IFN reporter assays mBio Medium 41854249
2025 DDX46 forms a functional complex with ALKBH5 and treRNA1 in the nucleus to orchestrate m6A demethylation of BCR signaling transcripts; demethylated transcripts interact with HuR for cytoplasmic export and translation; loss of DDX46 impairs transcript processing and BCR-related gene expression. Co-immunoprecipitation, nuclear fractionation, m6A analysis, loss-of-function assays Neoplasia (New York, N.Y.) Medium 39987653
2025 O-GlcNAcylation of DDX46 at Ser257 by OGT enhances DDX46 protein stability by impeding ubiquitin-mediated degradation; elevated DDX46 expression then activates the PI3K/Akt signaling pathway, promoting hepatocellular carcinoma cell proliferation and invasion. Co-IP (OGT-DDX46 interaction), site-specific mutagenesis (Ser257), ubiquitination assay, PI3K/Akt signaling readouts Biochimica et biophysica acta. Molecular cell research Medium 41176131
2013 Zebrafish Ddx46 is expressed in hematopoietic stem cells; loss-of-function mutants show suppressed erythropoiesis and lymphopoiesis with maintained myelopoiesis, correlating with downregulation of gata1a but not spi1 expression, indicating Ddx46 is required for multilineage HSC differentiation. Zebrafish genetic mutant analysis, whole-mount in situ hybridization, lineage marker expression Stem cells and development Medium 23635340
2012 Zebrafish Ddx46 is required for normal development of digestive organs and brain; Ddx46 mutants show accumulation of unspliced pre-mRNA forms in affected tissues, indicating Ddx46 is required for pre-mRNA splicing in vivo. Forward genetic screen, RT-PCR splicing analysis, whole-mount in situ hybridization PloS one Medium 22442707
2025 Prp5 (DDX46 ortholog) is implicated in displacing the U2 snRNP component Cus2; prespliceosome formation can proceed without ATP in the absence of either Sub2 or Cus2, revealing a coordinated interplay among Prp5, Sub2, Cus2, Mud2, and Msl5 during prespliceosome formation. In vitro splicing assays, ATP-depletion experiments, genetic deletion of splicing factors RNA (New York, N.Y.) Medium 41027713
2024 DDX46 binds JMJD6 and promotes the JMJD6/CDK4 signaling pathway in pancreatic cancer cells; DDX46 knockdown represses tumor growth and sensitizes cells to gemcitabine, and JMJD6 overexpression reverses the anti-tumor effect of DDX46 knockdown. Co-immunoprecipitation (DDX46-JMJD6), in vitro and in vivo tumor growth assays, drug sensitivity assays Neoplasia Low 38764294

Source papers

Stage 0 corpus · 33 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 The RNA helicase DDX46 inhibits innate immunity by entrapping m6A-demethylated antiviral transcripts in the nucleus. Nature immunology 319 28846086
1993 Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA. Genes & development 125 8405998
1990 PRP5: a helicase-like protein required for mRNA splicing in yeast. Proceedings of the National Academy of Sciences of the United States of America 116 2349233
2007 Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly. Molecular cell 109 18082608
1996 The Saccharomyces cerevisiae Prp5 protein has RNA-dependent ATPase activity with specificity for U2 small nuclear RNA. The Journal of biological chemistry 101 8969184
2004 Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA. The EMBO journal 89 14713954
2016 SF3B1/Hsh155 HEAT motif mutations affect interaction with the spliceosomal ATPase Prp5, resulting in altered branch site selectivity in pre-mRNA splicing. Genes & development 72 28087715
2015 A novel mechanism for Prp5 function in prespliceosome formation and proofreading the branch site sequence. Genes & development 69 25561497
2016 Pseudouridines in U2 snRNA stimulate the ATPase activity of Prp5 during spliceosome assembly. The EMBO journal 68 26873591
2021 Structural insights into how Prp5 proofreads the pre-mRNA branch site. Nature 53 34349264
2023 Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP assembly. Nature communications 48 36797247
2013 Cotton PRP5 gene encoding a proline-rich protein is involved in fiber development. Plant molecular biology 33 23625445
2015 Lentiviral DDX46 knockdown inhibits growth and induces apoptosis in human colorectal cancer cells. Gene 29 25680556
2013 Ddx46 is required for multi-lineage differentiation of hematopoietic stem cells in zebrafish. Stem cells and development 27 23635340
2002 Probing interactions between the U2 small nuclear ribonucleoprotein and the DEAD-box protein, Prp5. The Journal of biological chemistry 23 11927574
2012 DEAD-box protein Ddx46 is required for the development of the digestive organs and brain in zebrafish. PloS one 22 22442707
2009 DExD/H-box Prp5 protein is in the spliceosome during most of the splicing cycle. RNA (New York, N.Y.) 21 19451545
2016 Knockdown of DDX46 inhibits proliferation and induces apoptosis in esophageal squamous cell carcinoma cells. Oncology reports 18 27176873
2019 Dynamics of the DEAD-box ATPase Prp5 RecA-like domains provide a conformational switch during spliceosome assembly. Nucleic acids research 17 31712821
2016 Knockdown of DDX46 Inhibits the Invasion and Tumorigenesis in Osteosarcoma Cells. Oncology research 17 27697093
2020 Knockdown of DDX46 suppresses the proliferation and invasion of gastric cancer through inactivating Akt/GSK-3β/β-catenin pathway. Experimental cell research 15 33347858
2020 Prp5-Spt8/Spt3 interaction mediates a reciprocal coupling between splicing and transcription. Nucleic acids research 13 32399566
2017 Corrigendum: The RNA helicase DDX46 inhibits innate immunity by entrapping m6A-demethylated antiviral transcripts in the nucleus. Nature immunology 12 29144498
2020 DDX46 silencing inhibits cell proliferation by activating apoptosis and autophagy in cutaneous squamous cell carcinoma. Molecular medicine reports 10 33000271
2020 Knockdown of DDX46 inhibits trophoblast cell proliferation and migration through the PI3K/Akt/mTOR signaling pathway in preeclampsia. Open life sciences 9 33817228
2025 m6A eraser ALKBH5/treRNA1/DDX46 axis regulates BCR expression. Neoplasia (New York, N.Y.) 6 39987653
2021 DDX46 accelerates the proliferation of glioblastoma by activating the MAPK-p38 signaling. Journal of B.U.ON. : official journal of the Balkan Union of Oncology 5 34761620
2022 The role of DDX46 in breast cancer proliferation and invasiveness: A potential therapeutic target. Cell biology international 3 36200534
2019 Regulation of the Neurospora Circadian Clock by the Spliceosome Component PRP5. G3 (Bethesda, Md.) 3 31511298
2024 Oncogenic DDX46 promotes pancreatic cancer development and gemcitabine resistance by facilitating the JMJD6/CDK4 signaling pathway. Neoplasma 2 38764294
2025 O-GlcNAcylation of DDX46 promotes hepatocellular carcinoma progression by activating the PI3K/Akt signaling pathway. Biochimica et biophysica acta. Molecular cell research 1 41176131
2026 Caspase-mediated DDX46 cleavage unchains antiviral immunity. mBio 0 41854249
2025 New mechanistic insights into prespliceosome formation-roles of DEAD-box proteins Prp5 and Sub2. RNA (New York, N.Y.) 0 41027713

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