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DDX39A

ATP-dependent RNA helicase DDX39A · UniProt O00148

Length
427 aa
Mass
49.1 kDa
Annotated
2026-06-09
37 papers in source corpus 24 papers cited in narrative 23 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DDX39A is an ATP-dependent DEAD-box RNA helicase that binds RNA, hydrolyzes NTPs in an RNA-dependent manner, and bidirectionally unwinds double-stranded RNA, functioning principally in nuclear mRNA and snRNA export (PMID:17548965, PMID:16949217). It is the paralog of UAP56/DDX39B and assembles a distinct export complex, the AREX complex, with CIP29 — separate from the canonical UAP56-based TREX complex — and the two complexes regulate distinct genome-wide subsets of mRNAs; depletion of DDX39A causes chromosome arm resolution defects and cytokinesis failure linked to its mitotic-regulator target mRNAs (PMID:17196963, PMID:20573985). Complex identity is determined by ATP state and by unique structural features of each helicase, particularly the C-terminus of DDX39A, with the apo-AREX complex remodeling into a TREX-like complex containing THO, ALYREF, and CIP29 upon ATP addition; export ultimately proceeds through the NXF1 receptor (PMID:31917363, PMID:38225262, PMID:38377942). Beyond bulk mRNA export, DDX39A performs a protein-loading reaction, stimulating ATP-dependent loading of PHAX onto spliceosomal U snRNAs to drive their nuclear export, and contributes non-redundantly with DDX39B to alternative pre-mRNA splicing (PMID:39011894, PMID:38801080). DDX39A also acts on genome maintenance: upon replication stress it is recruited to stalled forks via RAD51 to resolve fork-associated RNA-DNA hybrids and license regulated DNA2 nuclease access and fork restart, with loss causing excessive fork protection and chemoresistance in BRCA1/2-deficient cells (PMID:39706186, PMID:39706185). It modulates telomere length through direct interaction with TRF2 and association with telomerase, and Erk2 phosphorylation at Y132/Y138 controls its telomeric and differentiation functions (PMID:21388492, PMID:39107495). In antiviral defense, DDX39A relocates from nucleus to cytoplasm upon infection and restricts alphaviruses by binding the CHIKV 5' conserved sequence element in an interferon-independent manner, and is itself targeted by the antiviral GTPase MxA (PMID:21859714, PMID:37949067). A pathogenic p.Lys137Gln variant causes nuclear clumping of the protein and abolishes its interaction with THOC1, impairing TREX integrity and producing severe nuclear morphological abnormalities and increased cell death in patient cells (PMID:40726340).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 2004 Medium

    Established that DDX39A is a functional ortholog of the yeast mRNA export helicase Sub2/UAP56, defining its baseline role in mRNA splicing and nuclear export.

    Evidence Yeast complementation of Sub2p loss and Aly interaction assay

    PMID:15047853

    Open questions at the time
    • Did not establish whether DDX39A functions independently of UAP56 in human cells
    • No biochemical demonstration of helicase activity
  2. 2006 Medium

    Identified CIP29 as a principal DDX39A partner that stimulates its unwinding activity and showed DDX39A interacts with ALY, beginning the definition of its export-complex composition.

    Evidence Co-IP/mass spectrometry, in vivo binding, RNA unwinding stimulation, and ubiquitylation assays in human cells

    PMID:17196963

    Open questions at the time
    • Did not yet distinguish DDX39A complexes from UAP56/TREX
    • Functional consequence of ubiquitylation on activity unresolved
  3. 2006 Medium

    Showed by RNA localization that DDX39A is required for mRNA nuclear export and that it shares essential, partly overlapping function with UAP56.

    Evidence siRNA knockdown with poly(A)+ RNA FISH in HeLa cells

    PMID:16949217

    Open questions at the time
    • Did not identify which specific mRNAs depend on DDX39A versus UAP56
    • Mechanism of selectivity unaddressed
  4. 2007 High

    Confirmed DDX39A is a bona fide ATP-dependent RNA helicase, providing the biochemical foundation for all downstream activities.

    Evidence In vitro RNA binding, NTPase, and bidirectional unwinding assays with recombinant protein plus nuclear foci imaging

    PMID:17548965

    Open questions at the time
    • In vitro substrate specificity relative to cellular targets not defined
    • Link between enzymatic activity and export not directly tested
  5. 2010 High

    Defined DDX39A as the core of a distinct AREX complex with CIP29, separate from UAP56's TREX, regulating distinct mRNA subsets and a specific mitotic function.

    Evidence Reciprocal Co-IP, genome-wide expression analysis, and siRNA knockdown with mitotic phenotyping

    PMID:20573985

    Open questions at the time
    • Determinants of mRNA target selectivity between the two complexes unresolved
    • How AREX engages export receptors not yet shown
  6. 2011 Medium

    Extended DDX39A function to telomere homeostasis through direct TRF2 binding and telomerase association.

    Evidence Co-IP with FXLXP motif domain mapping, shRNA knockdown, telomere length and DNA-damage foci assays

    PMID:21388492

    Open questions at the time
    • Mechanism by which DDX39A promotes telomere elongation without altering telomerase activity unclear
    • Single-lab finding
  7. 2011 Medium

    Showed DDX39A is directly targeted by the antiviral GTPase MxA and undergoes intrinsic CRM1-independent nucleocytoplasmic shuttling, linking its helicase activity to antiviral interference and defining shuttling determinants.

    Evidence In vitro binding with recombinant proteins, immunofluorescence, and deletion/domain-mapping shuttling assays

    PMID:21799930 PMID:21859714

    Open questions at the time
    • Functional consequence of MxA binding on DDX39A activity not directly measured
    • Shuttling regions mapped largely on UAP56 numbering
  8. 2018 Medium

    Connected DDX39A to oncogenic alternative splicing and Wnt/β-catenin signaling, broadening its role to cancer-relevant gene-expression programs.

    Evidence Knockdown of AR-V7 in prostate cells and overexpression/epistasis with TCF4/LEF1 in hepatocellular carcinoma

    PMID:28025139 PMID:29867138

    Open questions at the time
    • Whether effects are direct splicing/export functions or indirect not fully resolved
    • Direct RNA targets not all defined
  9. 2020 Medium

    Resolved the ATP-dependent assembly logic of the AREX complex and demonstrated that DDX39A-dependent export uses the same NXF1 receptor as the UAP56 pathway.

    Evidence Co-IP under ATP-depleted/replete conditions with mRNA export assays

    PMID:31917363

    Open questions at the time
    • Structural basis of apo-complex divergence not yet shown
    • Trigger for in vivo remodeling unclear
  10. 2021 Medium

    Identified ECD as a required cofactor for DDX39A-mediated mRNA export, with export depending on the ECD–DDX39A interaction.

    Evidence Co-IP, siRNA knockdown, FISH export assay, and rescue with an interaction-defective ECD mutant

    PMID:33941617

    Open questions at the time
    • Mechanistic role of ECD in the helicase cycle undefined
    • Single-lab finding
  11. 2023 High

    Established DDX39A as an interferon-independent antiviral effector that relocalizes to the cytoplasm and binds a defined viral RNA structure to restrict alphaviruses.

    Evidence Genetic screen, CRISPR/siLoss-of-function, biochemical RNA-binding, imaging, and viral replication assays mapping the CHIKV 5'CSE

    PMID:37949067

    Open questions at the time
    • How RNA binding mechanistically blocks replication unresolved
    • Trigger for nuclear-to-cytoplasmic relocation not defined
  12. 2024 High

    Revealed a non-canonical protein-loading helicase activity in which DDX39A loads PHAX onto U snRNAs for snRNA export, and clarified non-redundant splicing roles relative to DDX39B.

    Evidence In vitro reconstitution of ATP-dependent PHAX-RNA loading, Co-IP, and paralog complementation splicing assays with sequence analysis

    PMID:38801080 PMID:39011894

    Open questions at the time
    • Structural basis of PHAX loading not defined
    • Full target spectrum of DDX39A-specific splicing events unmapped
  13. 2024 High

    Provided the structural and C-terminal sequence determinants that explain how DDX39A and UAP56 form distinct apo-complexes, grounding their functional divergence.

    Evidence Structural analysis with chimeric and alanine-substitution mutagenesis and Co-IP/export assays

    PMID:38225262 PMID:38377942

    Open questions at the time
    • Atomic-resolution structure of full AREX complex not reported
    • How structural features dictate mRNA selectivity unresolved
  14. 2024 High

    Defined a genome-maintenance role: DDX39A resolves RNA-DNA hybrids at stalled forks via RAD51 recruitment to control DNA2 access, with loss conferring chemoresistance in BRCA1/2-deficient cells.

    Evidence Co-IP, chromatin fractionation, R-loop and fork-protection assays with BRCA1/2 epistasis, replicated across two independent reports

    PMID:39706185 PMID:39706186

    Open questions at the time
    • How DDX39A choice between RNA and DNA-hybrid substrates is regulated unclear
    • Relationship between export function and fork function not integrated
  15. 2024 Medium

    Placed DDX39A under Erk2 phosphorylation control (Y132/Y138) governing differentiation gene activation and TRF1-dependent suppression of alternative lengthening of telomeres.

    Evidence Erk2 substrate Co-IP/MS, knockout ESCs, phosphosite mutagenesis, ChIP, and ALT assays in mouse cells

    PMID:39107495

    Open questions at the time
    • Whether human DDX39A is regulated identically not shown
    • Mechanism by which DDX39A disrupts TRF1 DNA loops undefined
  16. 2024 Medium

    Implicated DDX39A intron retention and a short variant in an oncogenic MYC-export feedback loop, connecting its splicing/export biology to cancer gene circuits.

    Evidence RNA-seq/splicing analysis, SNRPD2/HNRNPL knockdown, MYC mRNA export assay, and ChIP/luciferase in human cells

    PMID:39018261

    Open questions at the time
    • Direct role of the short variant in selective MYC export mechanistically unresolved
    • Single-lab finding
  17. 2025 Medium

    Linked a DDX39A missense variant to disease by showing p.Lys137Gln disrupts THOC1 binding and TREX integrity with severe nuclear abnormalities in patient cells.

    Evidence Patient fibroblast studies, Co-IP, structural modeling, and nuclear morphology/viability assays

    PMID:40726340

    Open questions at the time
    • Genotype-phenotype scope beyond single proband unresolved
    • Whether export defect alone explains nuclear lamina disruption unclear
  18. 2025 Medium

    Demonstrated DDX39A directly binds and stabilizes specific mRNAs (SP1) to drive downstream programs, including a Ku70/NHEJ-mediated radioresistance axis.

    Evidence RIP-qPCR, ChIP-qPCR, luciferase, knockdown/rescue, and xenograft in human cancer models

    PMID:41984289

    Open questions at the time
    • Generality of mRNA-stabilization activity beyond SP1 unclear
    • Single-lab finding
  19. 2026 Medium

    Showed DDX39A stabilizes WISP1 pre-mRNA to activate AKT signaling and immunosuppressive macrophage polarization, and is a druggable target inhibited by fluphenazine.

    Evidence RNA-seq, RIP-seq, knockdown/overexpression, in vivo tumor models, and drug-binding assay in glioblastoma

    PMID:41772197

    Open questions at the time
    • Specificity of fluphenazine for DDX39A not fully established
    • Mechanistic distinction between splicing and stabilization roles unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • How DDX39A's many activities — selective mRNA/snRNA export, splicing, fork R-loop resolution, telomere regulation, and antiviral RNA binding — are coordinated and how its complex choice and substrate selectivity are regulated in vivo remains unresolved.
  • No unifying model integrating nuclear export and genome-maintenance roles
  • Determinants of mRNA target selectivity between AREX and TREX undefined
  • No high-resolution structure of the full AREX complex

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0140098 catalytic activity, acting on RNA 2 GO:0140657 ATP-dependent activity 2 GO:0016787 hydrolase activity 1 GO:0060090 molecular adaptor activity 1
Localization
GO:0005634 nucleus 3 GO:0000228 nuclear chromosome 1 GO:0005829 cytosol 1
Pathway
R-HSA-8953854 Metabolism of RNA 4 R-HSA-9609507 Protein localization 3 R-HSA-168256 Immune System 2 R-HSA-74160 Gene expression (Transcription) 2 R-HSA-73894 DNA Repair 1
Partners
ALYREFCIP29ECDMXAPHAXRAD51THOC1TRF2
Complex memberships
AREX complexTREX complex

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2006 DDX39A (DDX39) physically interacts with ALY (an essential mRNA export factor) in vivo, and co-immunoprecipitation with mass spectrometry identified CIP29 as a main DDX39-interacting protein; CIP29 binds RNA independently and enhances the RNA unwinding activity of DDX39A. DDX39A also undergoes heavy ubiquitylation and its stability is regulated via the ubiquitin-proteasome pathway. Co-immunoprecipitation, mass spectrometry, in vivo binding assay, ubiquitylation assay Experimental cell research Medium 17196963
2007 Recombinant DDX39A (DDX39-L isoform) binds RNA, hydrolyzes NTPs in an RNA-dependent manner, and unwinds double-stranded RNA bidirectionally, establishing it as a bona fide RNA helicase. DDX39A localizes to distinct punctate nuclear foci consistent with a role in RNA splicing/export. In vitro RNA binding assay, NTPase assay, RNA unwinding (helicase) assay, fluorescence microscopy Cancer biology & therapy High 17548965
2004 DDX39A (URH49) interacts with the mRNA export factor Aly and can rescue loss of Sub2p (the yeast homolog of UAP56) in Saccharomyces cerevisiae, demonstrating functional conservation in mRNA splicing and nuclear export. Yeast complementation assay, interaction assay with Aly Nucleic acids research Medium 15047853
2006 siRNA-mediated knockdown of DDX39A (URH49) alone in HeLa cells causes nuclear accumulation of poly(A)+ RNA in a speckled pattern, indicating a role in mRNA nuclear export. Simultaneous knockdown of DDX39A and UAP56 results in major reduction of reporter gene expression, loss of cytoplasmic poly(A)+ RNA, and cell death, demonstrating largely overlapping but essential functions. RNA interference (siRNA), fluorescence in situ hybridization (FISH) for poly(A)+ RNA localization Gene Medium 16949217
2010 DDX39A (URH49) forms a distinct complex termed the AREX (alternative mRNA export) complex with CIP29, whereas its paralog UAP56 forms the canonical human TREX complex. These two complexes regulate distinct subsets of mRNAs genome-wide. Depletion of URH49 causes chromosome arm resolution defects and cytokinesis failure, linked to its specific target mRNAs encoding mitotic regulators. Co-immunoprecipitation, genome-wide mRNA expression analysis, siRNA knockdown with mitotic phenotyping Molecular biology of the cell High 20573985
2011 DDX39A directly interacts with TRF2 via a FXLXP motif in DDX39A binding to the TREX homology domain of TRF2. DDX39A also associates with catalytically competent telomerase through hTERT interaction but does not affect telomerase activity. Overexpression of DDX39A leads to progressive telomere elongation, while shRNA-mediated depletion causes telomere shortening and DNA-damage response foci at both internal genome sites and telomeres (telomere dysfunction-induced foci). Co-immunoprecipitation, domain mapping (FXLXP motif mutagenesis), shRNA knockdown, telomere length analysis, immunofluorescence for DNA damage foci Aging cell Medium 21388492
2011 The antiviral GTPase MxA directly binds DDX39A (URH49) in vitro using purified recombinant proteins, forming a complex in the perinuclear region of infected cells. Mouse Mx1 also binds URH49/UAP56 in distinct nuclear dots, suggesting Mx proteins exert antiviral activity by interfering with the RNA helicase functions of URH49 and UAP56. Immunoprecipitation, in vitro binding assay with purified recombinant proteins, immunofluorescence/subcellular localization The Journal of biological chemistry Medium 21859714
2011 DDX39A (URH49) exhibits intrinsic CRM1-independent nucleocytoplasmic shuttling activity. Mapping studies identified distinct regions for intranuclear localization (aa 81–381 of UAP56) and the C-terminus (aa 195–428) as responsible for nucleocytoplasmic shuttling, which is independent of Rae1 interaction. Shuttling assay, deletion/domain mapping, co-immunoprecipitation PloS one Medium 21799930
2016 Simultaneous knockdown of DDX39A and its paralog DDX39B drastically and selectively downregulates AR-V7 splice variant mRNA expression in AR-V7-positive prostate cancer cell lines, indicating that DDX39A (together with DDX39B) regulates alternative splicing to generate the AR-V7 mRNA. shRNA library screen, siRNA knockdown, RT-PCR/qPCR for AR-V7 mRNA Biochemical and biophysical research communications Medium 28025139
2018 DDX39A overexpression increases nuclear β-catenin levels and upregulates Wnt/β-catenin pathway target genes in hepatocellular carcinoma cells; knockdown of TCF4 and LEF1 (Wnt/β-catenin co-activators) in DDX39A-overexpressing cells reverses this effect and reduces invasion, placing DDX39A upstream of the Wnt/β-catenin pathway. Overexpression and siRNA knockdown, Western blot for β-catenin nuclear localization, reporter assay, epistasis by co-knockdown Cell death & disease Medium 29867138
2020 In the ATP-depleted state, DDX39A (URH49) forms an apo-AREX complex containing CIP29 but lacking ALYREF and the THO subcomplex, distinct from UAP56's apo-TREX complex. Upon ATP addition, the apo-AREX complex is remodeled into an ATP-TREX-like complex containing THO subcomplex, ALYREF, and CIP29. URH49-dependent mRNA export is achieved through NXF1, the same export receptor as the UAP56 pathway. Co-immunoprecipitation under ATP-depleted and ATP-replete conditions, siRNA knockdown, mRNA export assay Biochimica et biophysica acta. Gene regulatory mechanisms Medium 31917363
2021 The mammalian ecdysoneless protein (ECD) physically interacts with DDX39A and is required for mRNA nuclear export; ECD knockdown blocks mRNA export from nucleus to cytoplasm, and this block is rescued by full-length ECD but not by an ECD mutant defective in DDX39A interaction. Co-immunoprecipitation, siRNA knockdown, mRNA export assay (FISH for poly(A)+ RNA), rescue with ECD mutant Molecular and cellular biology Medium 33941617
2023 DDX39A is an antiviral protein against chikungunya virus (CHIKV) and other alphaviruses. Upon infection, predominantly nuclear DDX39A relocates to the cytoplasm, where it inhibits alphavirus replication independently of the canonical interferon pathway. DDX39A biochemically binds CHIKV genomic RNA at the 5' conserved sequence element (5'CSE), and this RNA structure is essential for DDX39A's antiviral activity. Genetic screen, loss-of-function (siRNA/CRISPR), RNA-binding assay (biochemical), subcellular localization (imaging), viral replication assay, structural element mapping Molecular cell High 37949067
2024 DDX39A (URH49) stimulates loading of PHAX onto U snRNA in an ATP-dependent manner, thereby facilitating nuclear export of spliceosomal U snRNAs. ALYREF acts as a bridge between PHAX and UAP56/DDX39B in this reaction, revealing a protein-loading helicase activity distinct from classical RNA unwinding. In vitro reconstitution assay for ATP-dependent PHAX-RNA loading, co-immunoprecipitation, nuclear export assay Nucleic acids research High 39011894
2024 DDX39A and DDX39B have significant but not fully redundant roles in alternative pre-mRNA splicing. DDX39A cannot complement DDX39B-specific targets such as IL7R exon 6 splicing. Cassette exons specifically dependent on DDX39B (but not DDX39A) have U-poor/C-rich polypyrimidine tracts in the upstream intron, which is a sequence determinant of DDX39B dependency. siRNA knockdown of individual and combined paralogs, RT-PCR splicing assays, sequence analysis of polypyrimidine tracts Nucleic acids research Medium 38801080
2024 DDX39A (URH49) and UAP56 have unique structural features that determine their distinct apo-complex formation. Chimeric mutant analysis identified specific structural regions in each helicase responsible for forming the respective TREX or AREX apo-complexes, providing a molecular basis for functional divergence from their common ancestral gene Sub2. Structural comparison (crystal/structural analysis), chimeric mutant construction and functional analysis, co-immunoprecipitation Nature communications High 38225262
2024 Upon replication stress, DDX39A acts as an RNA-DNA hybrid (R-loop) resolver at stalled replication forks by unwinding fork-associated RNA-DNA hybrids (RF-RDs). DDX39A is recruited to stalled forks via association with RAD51. This unwinding facilitates regulated DNA2 nuclease access and controlled fork restart; loss of DDX39A causes excessive fork protection and confers chemoresistance in BRCA1/2-deficient cells. Co-immunoprecipitation (RAD51 association), chromatin fractionation, R-loop resolution assay, fork protection assay, siRNA knockdown with defined phenotypic readouts, genetic epistasis with BRCA1/2 deficiency Molecular cell High 39706185 39706186
2024 SNRPD2 (an Sm protein) modulates DDX39A intron retention together with HNRNPL to sustain expression of a DDX39A short variant (39A_S). This short variant mediates MYC mRNA nuclear export to maintain high MYC protein levels, and MYC in turn potentiates SNRPD2 transcription, forming a positive feedback loop. RNA-seq/splicing analysis, knockdown of SNRPD2/HNRNPL, mRNA export assay for MYC mRNA, ChIP/luciferase for MYC→SNRPD2 transcription, rescue experiments Advanced science Medium 39018261
2024 Erk2 phosphorylates Ddx39 on Y132 and Y138. Phosphorylation of Ddx39 by Erk2 promotes recruitment of Hat1 to acetylate H3K27 and activate differentiation genes in mouse ESCs. Ddx39 is recruited to telomeres by Trf1, where it disrupts Trf1-mediated DNA loops and suppresses alternative lengthening of telomeres (ALT); Erk2 phosphorylation of Ddx39 weakens its interaction with Trf1, releasing it from telomeres and allowing enhanced ALT activity. Co-immunoprecipitation/mass spectrometry (Erk2 substrates), Ddx39 knockout ESCs, phosphorylation site mutagenesis (Y132/Y138), ChIP for Hat1 recruitment, telomere length analysis, ALT assay Cell death and differentiation Medium 39107495
2024 The C-terminal region of DDX39A (URH49) is indispensable for AREX complex formation, and a specific amino acid at the C-terminus of UAP56 (but not URH49) is critical for TREX complex formation; alanine substitution at this residue impairs complex formation and mRNA processing/export activity. Truncation and alanine substitution mutagenesis, co-immunoprecipitation, mRNA export assay Biochemical and biophysical research communications Medium 38377942
2025 A missense variant in DDX39A (p.Lys137Gln) causes aberrant nuclear clumping of the mutant protein and prevents its interaction with the TREX component THOC1, thereby impairing TREX complex integrity. Structural modeling shows Lys137 mediates critical inter- and intra-molecular interactions. Cells from the affected proband show severe nuclear morphological abnormalities, disrupted nuclear lamina organization, and increased cell death. Patient-derived fibroblast functional studies, co-immunoprecipitation (DDX39A-K137Q vs THOC1), structural modeling, immunofluorescence for nuclear morphology, cell viability assay Clinical genetics Medium 40726340
2025 DDX39A directly binds SP1 mRNA, stabilizing it and enhancing its translation efficiency without affecting SP1 transcription, as demonstrated by RIP-qPCR. Increased SP1 protein then binds the −223/−214 bp region of the Ku70 promoter (ChIP-qPCR, dual-luciferase assay), activating Ku70 expression and contributing to radioresistance via the non-homologous end-joining pathway. RIP-qPCR, ChIP-qPCR, dual-luciferase reporter assay, siRNA knockdown, rescue experiments, in vivo xenograft Cellular oncology Medium 41984289
2026 DDX39A stabilizes WISP1 pre-mRNA through alternative splicing regulation (identified by RNA-seq and RIP-seq), thereby activating AKT signaling. Secreted WISP1 acts as a paracrine signal promoting immunosuppressive tumor-associated macrophage polarization. The compound fluphenazine hydrochloride binds to and inhibits DDX39A, suppressing glioblastoma growth and macrophage immunosuppression. RNA-seq, RIP-seq, siRNA knockdown and overexpression, in vitro and in vivo tumor models, drug-binding assay Oncogene Medium 41772197

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 The closely related RNA helicases, UAP56 and URH49, preferentially form distinct mRNA export machineries and coordinately regulate mitotic progression. Molecular biology of the cell 87 20573985
2006 Intracellular characterization of DDX39, a novel growth-associated RNA helicase. Experimental cell research 70 17196963
2004 Growth-regulated expression and G0-specific turnover of the mRNA that encodes URH49, a mammalian DExH/D box protein that is highly related to the mRNA export protein UAP56. Nucleic acids research 66 15047853
2006 Nuclear localization of poly(A)+ mRNA following siRNA reduction of expression of the mammalian RNA helicases UAP56 and URH49. Gene 63 16949217
2011 Requirement of DDX39 DEAD box RNA helicase for genome integrity and telomere protection. Aging cell 55 21388492
2016 The RNA helicase DDX39B and its paralog DDX39A regulate androgen receptor splice variant AR-V7 generation. Biochemical and biophysical research communications 51 28025139
2007 DDX39, upregulated in lung squamous cell cancer, displays RNA helicase activities and promotes cancer cell growth. Cancer biology & therapy 51 17548965
2018 DDX39 promotes hepatocellular carcinoma growth and metastasis through activating Wnt/β-catenin pathway. Cell death & disease 50 29867138
2011 Interferon-induced antiviral protein MxA interacts with the cellular RNA helicases UAP56 and URH49. The Journal of biological chemistry 35 21859714
2011 The cellular DExD/H-box RNA-helicases UAP56 and URH49 exhibit a CRM1-independent nucleocytoplasmic shuttling activity. PloS one 22 21799930
2023 The RNA helicase DDX39A binds a conserved structure in chikungunya virus RNA to control infection. Molecular cell 20 37949067
2024 Intron Retention of DDX39A Driven by SNRPD2 is a Crucial Splicing Axis for Oncogenic MYC/Spliceosome Program in Hepatocellular Carcinoma. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 16 39018261
2013 Up-regulation of DDX39 in human malignant pleural mesothelioma cell lines compared to normal pleural mesothelial cells. Anticancer research 16 23749908
2024 Parsing the roles of DExD-box proteins DDX39A and DDX39B in alternative RNA splicing. Nucleic acids research 13 38801080
2021 The Mammalian Ecdysoneless Protein Interacts with RNA Helicase DDX39A To Regulate Nuclear mRNA Export. Molecular and cellular biology 13 33941617
2015 Identification of DDX39A as a Potential Biomarker for Unfavorable Neuroblastoma Using a Proteomic Approach. Pediatric blood & cancer 13 26469522
2024 Structural differences between the closely related RNA helicases, UAP56 and URH49, fashion distinct functional apo-complexes. Nature communications 12 38225262
2020 Phosphosite Analysis of the Cytomegaloviral mRNA Export Factor pUL69 Reveals Serines with Critical Importance for Recruitment of Cellular Proteins Pin1 and UAP56/URH49. Journal of virology 12 31969433
2013 Up-regulation of DDX39 in human pancreatic cancer cells with acquired gemcitabine resistance compared to gemcitabine-sensitive parental cells. Anticancer research 12 23898070
2010 Requirement of UAP56, URH49, RBM15, and OTT3 in the expression of Kaposi sarcoma-associated herpesvirus ORF57. Virology 12 20828777
2024 Dynamic control of RNA-DNA hybrid formation orchestrates DNA2 activation at stalled forks by RNAPII and DDX39A. Molecular cell 11 39706186
2020 URH49 exports mRNA by remodeling complex formation and mediating the NXF1-dependent pathway. Biochimica et biophysica acta. Gene regulatory mechanisms 11 31917363
2009 RNA helicase Ddx39 is expressed in the developing central nervous system, limb, otic vesicle, branchial arches and facial mesenchyme of Xenopus laevis. Gene expression patterns : GEP 11 19900578
2024 DDX39A resolves replication fork-associated RNA-DNA hybrids to balance fork protection and cleavage for genomic stability maintenance. Molecular cell 10 39706185
2010 Binding of the human cytomegalovirus (HCMV) tegument protein UL69 to UAP56/URH49 is not required for efficient replication of HCMV. Journal of virology 9 20610707
2024 The RNA helicase DDX39 contributes to the nuclear export of spliceosomal U snRNA by loading of PHAX onto RNA. Nucleic acids research 7 39011894
2024 Novel role for Ddx39 in differentiation and telomere length regulation of embryonic stem cells. Cell death and differentiation 4 39107495
2025 SNRPB-mediated regulation of DDX39A splicing promotes ovarian cancer progression by regulating α6 integrin subunit expression. Oncogene 3 40216968
2024 TRAIP enhances progression of tongue squamous cell carcinoma through EMT and Wnt/β-catenin signaling by interacting with DDX39A. BMC cancer 3 39623306
2025 Up-regulated DDX39 in Adrenocortical Carcinoma Is Associated With Patient Survival. Anticancer research 2 39890176
2024 Evaluation of protective efficacy of recombinant Toxoplasma gondii DDX39 protein vaccine against acute and chronic T. gondii infection in mice. Acta tropica 2 39461580
2025 DDX39 Is Down-regulated in Chromophobe Renal Cell Carcinoma Tissues, Whereas Overexpression Is Associated With Shorter Patient Survival. Anticancer research 1 41151902
2024 Terminal regions of UAP56 and URH49 are required for their distinct complex formation functioning to an essential role in mRNA processing and export. Biochemical and biophysical research communications 1 38377942
2026 The multifunctional RNA helicase DDX39A drives glioblastoma progression by modulating WISP1 alternative splicing that induces an immunosuppressive macrophage polarization. Oncogene 0 41772197
2026 Role of DDX39A in modulating the tumor progression and radiosensitivity in esophageal squamous cell carcinoma. Cellular oncology (Dordrecht, Netherlands) 0 41984289
2025 Pathogenic DDX39A Variant Disrupts Nuclear Homeostasis and Causes an Early-Onset Neurodegenerative Disorder With Cerebral Atrophy. Clinical genetics 0 40726340
2023 The Evil DExH/D: Chikungunya virus runs but cannot hide from DDX39A. Molecular cell 0 37977114

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