Affinage

DAP3

Small ribosomal subunit protein mS29 · UniProt P51398

Length
398 aa
Mass
45.6 kDa
Annotated
2026-06-09
32 papers in source corpus 18 papers cited in narrative 18 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DAP3 (MRPS29) is a GTP-binding protein of the mitoribosomal small subunit that supports mitochondrial translation and a death-promoting signaling protein that mediates extrinsic apoptosis (PMID:7499268, PMID:17135360). A conserved N-terminal sequence targets DAP3 to mitochondria, where it is required for synthesis of mitochondrial genome-encoded proteins and oxidative phosphorylation: dap3-null mouse embryos die at ~E9.5 with abnormal mitochondria and reduced COX-I, and DAP3 promotes complex I activity by controlling translation of MT-ND5 (PMID:11162496, PMID:17135360, PMID:39080251). Bi-allelic loss-of-function variants reduce DAP3 protein, impair small-subunit assembly, and cause combined OXPHOS complex I/IV deficiency, establishing DAP3 as a Mendelian mitochondrial disease gene (PMID:39701103). The death-promoting activity of DAP3 acts downstream of death receptors (Fas, TNF-α) and during anoikis in a caspase-dependent manner, requiring an intact P-loop and full-length protein, and depends on partners including FADD, caspase-8, and the IPS-1/MAVS scaffold (PMID:9889192, PMID:15302871, PMID:19644511). DAP3 function is gated by phosphorylation: PKA and PKCδ phosphorylate residues clustered around its GTP-binding motifs, and AKT phosphorylation at Ser185 controls both its mitochondrial localization and its suppression of apoptosis (PMID:18227431, PMID:15302871, PMID:39080251). Independently, DAP3 acts as an RNA-binding regulator in cancer, repressing A-to-I editing by disrupting ADAR2–substrate contacts, reshaping alternative splicing through ribonucleoprotein complexes, and sustaining m6A methylation by facilitating METTL3 binding and MAT2A splicing (PMID:32596459, PMID:35379802, PMID:39316047).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 1995 High

    Established DAP3 as a required positive mediator of cytokine-induced cell death, defining its founding pro-apoptotic identity and flagging a nucleotide-binding motif as functionally central.

    Evidence Antisense functional selection screen and overexpression in HeLa cells

    PMID:7499268

    Open questions at the time
    • Molecular mechanism of death promotion unresolved
    • P-loop function not yet tested by mutagenesis
  2. 1999 High

    Localized DAP3 action downstream of death receptors and showed its death activity is P-loop- and caspase-dependent, mapping where in the apoptotic cascade it operates.

    Evidence Dominant-negative/truncation and P-loop mutagenesis, caspase inhibitor epistasis, cross-species complementation

    PMID:9889192

    Open questions at the time
    • Direct binding partners in the receptor complex not identified
    • Biochemical role of nucleotide binding unknown
  3. 2000 Medium

    Identified DAP3 as a ligand-dependent glucocorticoid receptor coactivator, suggesting a nuclear-receptor regulatory role distinct from apoptosis.

    Evidence Yeast two-hybrid, in vitro binding, co-transfection reporter and Co-IP

    PMID:10903152

    Open questions at the time
    • Single lab; physiological relevance unconfirmed
    • Reconciliation with mitochondrial localization not addressed
  4. 2001 Medium

    Demonstrated a conserved N-terminal mitochondrial targeting sequence, placing DAP3 in mitochondria and reframing its biology around organellar function.

    Evidence N-terminal DAP3-EGFP fusion and confocal microscopy in human fibroblasts

    PMID:11162496

    Open questions at the time
    • Submitochondrial location not defined
    • Function within mitochondria not yet shown
  5. 2002 Medium

    Clarified that the DAP3-FADD interaction reported in lysates is a compartment-disruption artifact and that TRAIL/DR4 apoptosis can proceed independently of DAP3, tempering the death-receptor model.

    Evidence Intact vs. disrupted compartment Co-IP and TRAIL apoptosis assays in Jurkat cells

    PMID:12359235

    Open questions at the time
    • Context-dependence of DAP3-FADD interaction unresolved
    • Single cell type tested
  6. 2004 High

    Connected DAP3 to anoikis and identified AKT phosphorylation as a switch suppressing its death function, linking integrin/survival signaling to DAP3 regulation.

    Evidence Antisense knockdown, overexpression, DAP3-FADD Co-IP, AKT site mutagenesis and integrin ligation

    PMID:15302871

    Open questions at the time
    • Exact AKT site not yet mapped
    • How phosphorylation alters DAP3 activity mechanistically unknown
  7. 2006 High

    Proved DAP3 is essential for embryonic viability and mitochondrial protein synthesis/respiration, and that its requirement is specific to extrinsic apoptosis, unifying its mitochondrial and death roles in vivo.

    Evidence dap3 knockout mice, TEM, COX-I western, siRNA respiration assay, pathway-specific apoptosis assays

    PMID:17135360

    Open questions at the time
    • Specific mitoribosomal substrates not defined
    • Molecular link between translation defect and apoptosis sensitivity unclear
  8. 2008 High

    Mapped DAP3 phosphosites clustering around its GTP-binding motifs and identified PKA/PKCδ as kinases, showing phosphorylation tunes proliferation and caspase activation.

    Evidence Tandem MS phosphosite mapping, in vitro kinase assays, mutagenesis with PARP cleavage readout

    PMID:18227431

    Open questions at the time
    • In vivo stoichiometry and regulation of each site unknown
    • Functional consequence per site not fully dissected
  9. 2008 Medium

    Identified hNOA1 as a matrix-facing mitochondrial GTPase partner of DAP3 with a corresponding apoptosis phenotype, expanding the mitochondrial interactome.

    Evidence IP-MS from mitochondrial fractions, immuno-EM, subfractionation, siRNA apoptosis assay

    PMID:19103604

    Open questions at the time
    • Functional consequence of the interaction for translation not shown
    • Single lab
  10. 2009 High

    Placed IPS-1/MAVS as a required partner in DAP3-mediated anoikis, providing a scaffold for caspase-8 recruitment during detachment.

    Evidence Co-IP, IPS-1 KO MEFs, siRNA/overexpression, caspase-3/8/9 assays, anoikis assay

    PMID:19644511

    Open questions at the time
    • Direct vs. indirect DAP3-IPS-1 binding not resolved
    • How mitochondrial DAP3 engages IPS-1 spatially unclear
  11. 2010 Medium

    Identified DELE as a DAP3-binding sensitizer of death-receptor apoptosis, adding a partner that amplifies caspase activation.

    Evidence Yeast two-hybrid, Co-IP, overexpression/knockdown, caspase assays

    PMID:20563667

    Open questions at the time
    • Mechanism of sensitization undefined
    • Single lab
  12. 2020 Medium

    Revealed an extra-mitochondrial RNA-regulatory function: DAP3 represses A-to-I editing by binding ADAR2 and displacing it from substrates, promoting tumorigenic unedited transcripts.

    Evidence Co-IP, domain mapping, RNA-IP, editome sequencing, PDZD7 recoding assays

    PMID:32596459

    Open questions at the time
    • Subcellular site of DAP3-ADAR2 action not pinned
    • Relation to mitochondrial pool unclear
  13. 2022 Medium

    Showed DAP3 acts as a splicing regulatory RNA-binding protein, reshaping splicing both directly and via splicing factors, with WSB1 mis-splicing as a tumorigenic output.

    Evidence RNA-seq, RNA-IP, RNP Co-IP, TCGA analysis, WSB1 splicing validation

    PMID:35379802

    Open questions at the time
    • RNP complex composition not fully defined
    • Direct vs. indirect splicing targets not separated
  14. 2023 Medium

    Linked DAP3 to the CHK1-dependent G2/M checkpoint in the radiation response, implicating it in cell-cycle control of cancer cells.

    Evidence siRNA, cell-cycle flow cytometry post-irradiation, phospho-CHK1/cdc2 westerns, CHK1 inhibitor epistasis

    PMID:37023702

    Open questions at the time
    • Molecular mechanism connecting DAP3 to CHK1 unknown
    • Single lung adenocarcinoma context
  15. 2024 Medium

    Defined the mitochondrial molecular role: DAP3 promotes complex I via MT-ND5 translation, with AKT phosphorylation at Ser185 controlling its mitochondrial localization and function.

    Evidence Knockdown/overexpression, complex I assay, MT-ND5 western, Ser185 mutagenesis, fractionation, tumor models

    PMID:39080251

    Open questions at the time
    • Whether DAP3 directly templates MT-ND5 translation not shown
    • Generality beyond HCC untested
  16. 2024 High

    Established DAP3 as a Mendelian mitochondrial disease gene, with loss-of-function variants impairing small-subunit assembly, OXPHOS, GTPase activity, and apoptotic sensitivity, rescuable by wild-type cDNA.

    Evidence Patient fibroblast proteomics, respiratory chain assays, lentiviral rescue, GTPase/thermal stability assays, structural modeling

    PMID:39701103

    Open questions at the time
    • Genotype-phenotype correlations across patients limited
    • Structural basis of GTPase defect modeled but not solved
  17. 2024 Medium

    Showed DAP3 sustains m6A methylation by facilitating METTL3 binding and promoting MAT2A splicing/SAM production, tying its RNA functions to tumorigenesis.

    Evidence m6A-seq, RNA-IP, METTL3 RIP, MAT2A splicing/SAM assays, MAT2A rescue, tumor growth

    PMID:39316047

    Open questions at the time
    • Whether m6A and mitochondrial functions are coupled unknown
    • Single lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • How a single mitoribosomal GTPase coordinates its mitochondrial translation role with its nuclear/cytoplasmic RNA-regulatory and pro-apoptotic activities remains unresolved.
  • Pool partitioning between organelle and cytoplasm undefined
  • No structure of full-length human DAP3 in the mitoribosome reported
  • Causal link between translation function and RNA-editing/splicing roles unestablished

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 3 GO:0005198 structural molecule activity 2 GO:0140110 transcription regulator activity 2 GO:0003924 GTPase activity 1
Localization
GO:0005739 mitochondrion 4 GO:0005634 nucleus 2 GO:0005840 ribosome 2
Pathway
R-HSA-5357801 Programmed Cell Death 5 R-HSA-392499 Metabolism of proteins 3 R-HSA-8953854 Metabolism of RNA 3 R-HSA-1640170 Cell Cycle 1 R-HSA-1643685 Disease 1
Partners
ADAR2CASP8DELE1FADDMAVSMETTL3NOA1NR3C1
Complex memberships
mitochondrial small ribosomal subunit (mitoribosome)

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 DAP3 was identified as a positive mediator of interferon-gamma-induced cell death in HeLa cells. Antisense RNA-mediated inactivation of DAP3 protected cells from IFN-γ-induced cell death, and ectopic overexpression was incompatible with cell growth. The protein carries a potential P-loop (nucleotide-binding) motif. Antisense cDNA library functional selection screen; antisense RNA knockdown; ectopic overexpression with colony-formation assay The Journal of biological chemistry High 7499268
1999 Structure-function analysis showed that the intact full-length DAP3 protein is required for apoptosis induction when overexpressed, while the N-terminal 230 amino acids act in a dominant-negative fashion. Both activities depend on the integrity of the nucleotide-binding (P-loop) motif. Antisense DAP3 and the dominant-negative form protected cells from Fas- and TNF-α-induced apoptosis, placing DAP3 downstream of the receptor signaling complex; its death-promoting effect is caspase-dependent. A C. elegans ortholog induced cell death in mammalian cells upon overexpression. Antisense RNA knockdown; truncation/dominant-negative mutant overexpression; P-loop mutagenesis; caspase inhibitor epistasis; cross-species functional complementation The EMBO journal High 9889192
2000 DAP3 interacts with the glucocorticoid receptor (GR) ligand-binding domain in a ligand-dependent manner, identified by yeast two-hybrid and confirmed in vitro. The main interaction domain maps to the N-terminal region of DAP3. Co-transfection showed DAP3 stimulates ligand-induced GR transcriptional activation and increases steroid sensitivity. DAP3 also formed complexes with other nuclear receptors, bHLH/PAS proteins, and Hsp90. Yeast two-hybrid; in vitro binding assay; co-transfection transcriptional reporter assay; co-immunoprecipitation The Biochemical journal Medium 10903152
2001 A conserved N-terminal sequence targets DAP3 to mitochondria. GFP fusion with the N-terminal region of human DAP3 localized exclusively to mitochondria in transfected human fibroblasts, confirmed by confocal microscopy. The mitochondrial targeting sequence is conserved in mouse, Drosophila, and C. elegans orthologs. N-terminal DAP3–EGFP fusion protein; confocal fluorescence microscopy in transfected human fibroblasts; in silico targeting prediction (MITOPROT, TargetP) with experimental validation Biochemical and biophysical research communications Medium 11162496
2002 Co-expression of DAP3 and GR results in increased cellular GR protein levels and partial translocation of DAP3 to the nucleus. The full-length DAP3 (not just the N-terminal domain) is required to efficiently increase GR levels and enhance GR transcriptional activity, indicating interplay between N- and C-termini for DAP3 cellular function. Co-transfection; western blot; subcellular fractionation/immunofluorescence for DAP3 localization; transcriptional reporter assay Biochemical and biophysical research communications Medium 12099703
2002 DAP3 remains intra-mitochondrial during TRAIL-induced apoptosis and does not interact with FADD when subcellular compartments are intact. Interaction between DAP3 and FADD was only detectable in whole-cell lysate co-immunoprecipitation (i.e., an in vitro artifact after compartment disruption). TRAIL-induced, DR4-mediated apoptosis in Jurkat cells was found to be independent of DAP3. Cell fractionation; immunoprecipitation with intact vs. disrupted compartments; TRAIL-induced apoptosis in Jurkat cells with DAP3 analysis Biochemical and biophysical research communications Medium 12359235
2004 DAP3 is critical for anoikis induction. DAP3 knockdown (antisense oligonucleotides) inhibited anoikis, while overexpression augmented caspase activation upon cell detachment. Upon detachment, DAP3 associates with FADD and caspase-8 is activated. DAP3 is phosphorylated by Akt (PKB), and active Akt suppresses DAP3-induced apoptosis; mutation of the Akt phosphorylation consensus site in DAP3 renders it resistant to Akt suppression. Integrin ligation activates Akt, which phosphorylates DAP3 and suppresses anoikis. Antisense oligonucleotide knockdown; overexpression; co-immunoprecipitation (DAP3-FADD); caspase activation assay; Akt phosphorylation site mutagenesis; integrin ligation experiments The Journal of biological chemistry High 15302871
2006 DAP3 is essential for embryonic viability in mice; dap3-/- embryos die at ~E9.5 with arrested development, shrunken mitochondria with swollen cristae (by TEM), and reduced cytochrome c oxidase-I (mitochondrial genome-encoded), consistent with a role in mitochondrial protein synthesis. siRNA knockdown reduced oxygen consumption in cultured cells. Cultured dap3-/- embryonic cells showed impaired apoptosis in response to extrinsic stimuli (TNFα, TRAIL, anti-Fas) but not intrinsic (mitochondrial) pathway stimuli. Knockout mouse generation; transmission electron microscopy; western blot for mtDNA-encoded protein (COX-I); siRNA knockdown + oxygen consumption measurement; cultured embryonic cell apoptosis assays with death receptor stimuli FASEB journal High 17135360
2008 DAP3 (mitochondrial ribosomal small subunit protein MRPS29) is phosphorylated in situ at Ser215 or Thr216, Ser220, Ser251 or Ser252, and Ser280, mapped by tandem mass spectrometry. Protein kinase A and Protein kinase Cδ can phosphorylate recombinant DAP3 at these same residues in vitro. Phosphorylation sites cluster around the conserved GTP-binding motifs. Site-directed mutagenesis of selected phosphorylation sites affected cell proliferation and PARP cleavage (caspase activation). Tandem mass spectrometry of immunopurified mitochondrial ribosomal DAP3; in vitro kinase assay with PKA and PKCδ; site-directed mutagenesis; PARP cleavage assay Protein science High 18227431
2008 hNOA1 (human homolog of AtNOA1, a large mitochondrial GTPase) physically interacts with DAP3 in mitochondria, identified by immunoprecipitation-mass spectrometry from enriched mitochondrial fractions. hNOA1 is peripherally associated with the inner mitochondrial membrane facing the matrix. Knockdown of hNOA1 renders cells more resistant to apoptotic stimuli (IFN-γ, staurosporine), consistent with a functional link through its DAP3 interaction. Immunoprecipitation-mass spectrometry from mitochondrial fractions; immunofluorescence; immunoelectron microscopy; mitochondrial subfractionation; siRNA knockdown + apoptosis assay The Journal of biological chemistry Medium 19103604
2009 IPS-1 (interferon-beta promoter stimulator 1, also known as MAVS) binds DAP3 and is required for DAP3-mediated anoikis. Cell detachment induces IPS-1 expression, recruitment of caspase-8 to IPS-1, and caspase-8 activation. IPS-1 knockout mouse embryonic fibroblasts are resistant to anoikis. Knockdown of IPS-1 inhibits DAP3-mediated anoikis, placing IPS-1 downstream of or in concert with DAP3 in this pathway. Co-immunoprecipitation (IPS-1/DAP3 interaction); IPS-1 KO MEFs; siRNA knockdown of IPS-1; overexpression of IPS-1; caspase-3/-8/-9 activation assays; anoikis assay Cell death and differentiation High 19644511
2010 Yeast two-hybrid screening identified DELE (death ligand signal enhancer) as a novel DAP3-binding protein. DELE interaction with DAP3 was confirmed in mammalian cells by co-immunoprecipitation. Stable DELE expression sensitized cells to TNF-α- and TRAIL-induced apoptosis; DELE knockdown rescued HeLa cells from apoptosis and significantly inhibited activation of caspase-3, -8, and -9 induced by TNF-α, anti-Fas, or TRAIL. Yeast two-hybrid screening; co-immunoprecipitation in mammalian cells; stable overexpression; siRNA knockdown; caspase activation assays Apoptosis Medium 20563667
2020 DAP3 functions as a potent repressor of A-to-I RNA editing in cancer by directly interacting with the deaminase domain of ADAR2, disrupting ADAR2's association with its target transcripts. This suppression of editing leads to accumulation of unedited, more tumorigenic forms of target transcripts (e.g., PDZD7 without stop-codon recoding). Co-immunoprecipitation (DAP3-ADAR2 interaction); domain-mapping pulldown; RNA immunoprecipitation; editome sequencing; functional assays of PDZD7 recoding Science advances Medium 32596459
2022 DAP3 functions as a splicing regulatory RNA-binding protein in cancer. It coordinates splicing regulatory networks by mediating formation of ribonucleoprotein complexes to induce substrate-specific splicing changes, and also modulates splicing of splicing factors themselves, causing indirect widespread alternative splicing effects. Non-productive splicing of WSB1 was demonstrated as a causal DAP3-modulated mis-splicing event in tumorigenesis. RNA-seq splicing analysis; RNA immunoprecipitation; ribonucleoprotein complex co-immunoprecipitation; TCGA pan-cancer splicing analysis; functional WSB1 splicing validation Nature communications Medium 35379802
2024 DAP3 promotes mitochondrial complex I activity in HCC cells by regulating translation and expression of the mitochondrial genome-encoded MT-ND5. AKT-mediated phosphorylation of DAP3 at Ser185 is the key event mediating its mitochondrial localization and function in HCC cells. siRNA knockdown; overexpression; mitochondrial complex I activity assay; western blot for MT-ND5; Ser185 phosphorylation site mutagenesis; subcellular fractionation; in vitro and in vivo tumor models Cell death & disease Medium 39080251
2024 Bi-allelic loss-of-function variants in DAP3 reduce MRPS29 (DAP3) protein levels, causing decreased assembly of the mitoribosomal small subunit and combined deficiency of oxidative phosphorylation complexes I and IV. Lentiviral rescue with wild-type DAP3 cDNA partially restored MRPS7, MRPS9, and complex I/IV subunit levels. In vitro assays showed DAP3 disease variants reduce GTPase activity, thermal stability, and both intrinsic and extrinsic apoptotic sensitivity. Protein modeling suggested variants impact ADP binding. Proteomic profiling of patient fibroblasts; respiratory chain activity measurement; lentiviral cDNA rescue; in vitro GTPase activity assay; thermal stability assay; apoptosis sensitivity assays; protein structural modeling American journal of human genetics High 39701103
2024 DAP3 preserves m6A RNA methylation levels through two mechanisms: (1) it directly binds to m6A target regions on RNA, facilitating METTL3 binding to these sites; and (2) it promotes MAT2A last-intron splicing, increasing MAT2A protein, cellular SAM (methyl donor), and m6A levels. DAP3 silencing impairs tumorigenesis, which can be rescued by MAT2A overexpression. m6A sequencing; RNA immunoprecipitation; METTL3 ChIP/RIP; MAT2A splicing assay; SAM quantification; MAT2A overexpression rescue; tumor growth assays Proceedings of the National Academy of Sciences of the United States of America Medium 39316047
2023 DAP3 knockdown attenuated radiation-induced G2/M cell cycle arrest in human lung adenocarcinoma cells and decreased expression of phosphorylated cdc2 (Tyr15) and phosphorylated CHK1 (Ser296). A CHK1 inhibitor phenocopied DAP3 loss in abrogating G2 arrest, placing DAP3 upstream of CHK1-mediated G2/M checkpoint regulation in the radiation response. siRNA knockdown of DAP3; flow cytometry cell cycle analysis after irradiation; western blot for phospho-cdc2, phospho-CHK1; CHK1 inhibitor epistasis; radiosensitivity assay Journal of radiation research Medium 37023702

Source papers

Stage 0 corpus · 32 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1995 Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death. The Journal of biological chemistry 102 7499268
1999 Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-alpha- and Fas-induced cell death. The EMBO journal 97 9889192
2001 Death-associated protein 3 (Dap-3) is overexpressed in invasive glioblastoma cells in vivo and in glioma cell lines with induced motility phenotype in vitro. Clinical cancer research : an official journal of the American Association for Cancer Research 72 11489830
2006 Mammalian dap3 is an essential gene required for mitochondrial homeostasis in vivo and contributing to the extrinsic pathway for apoptosis. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 49 17135360
2004 Functional role of death-associated protein 3 (DAP3) in anoikis. The Journal of biological chemistry 47 15302871
2008 hNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis. The Journal of biological chemistry 43 19103604
2013 Discovery of Dap-3 polymyxin analogues for the treatment of multidrug-resistant Gram-negative nosocomial infections. Journal of medicinal chemistry 42 23735048
2020 Suppression of adenosine-to-inosine (A-to-I) RNA editome by death associated protein 3 (DAP3) promotes cancer progression. Science advances 38 32596459
2008 Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3. Protein science : a publication of the Protein Society 36 18227431
2010 Identification of DELE, a novel DAP3-binding protein which is crucial for death receptor-mediated apoptosis induction. Apoptosis : an international journal on programmed cell death 30 20563667
2009 IPS-1 is crucial for DAP3-mediated anoikis induction by caspase-8 activation. Cell death and differentiation 29 19644511
2012 The mRNA expression of DAP3 in human breast cancer: correlation with clinicopathological parameters. Anticancer research 26 22287761
2000 The pro-apoptotic protein death-associated protein 3 (DAP3) interacts with the glucocorticoid receptor and affects the receptor function. The Biochemical journal 24 10903152
2022 Multilayered control of splicing regulatory networks by DAP3 leads to widespread alternative splicing changes in cancer. Nature communications 21 35379802
2004 Arg and DAP3 expression was correlated with human thymoma stage. Clinical & experimental metastasis 19 15679048
2001 A conserved N-terminal sequence targets human DAP3 to mitochondria. Biochemical and biophysical research communications 15 11162496
2002 TRAIL-induced apoptosis is independent of the mitochondrial apoptosis mediator DAP3. Biochemical and biophysical research communications 12 12359235
2021 DAP3 Is Involved in Modulation of Cellular Radiation Response by RIG-I-Like Receptor Agonist in Human Lung Adenocarcinoma Cells. International journal of molecular sciences 11 33401559
2024 DAP3 promotes mitochondrial activity and tumour progression in hepatocellular carcinoma by regulating MT-ND5 expression. Cell death & disease 10 39080251
2002 Functional interaction between the pro-apoptotic DAP3 and the glucocorticoid receptor. Biochemical and biophysical research communications 10 12099703
2022 Death associated protein‑3 (DAP3) and DAP3 binding cell death enhancer‑1 (DELE1) in human colorectal cancer, and their impacts on clinical outcome and chemoresistance. International journal of oncology 9 36382667
2010 Regulation of mitochondrial ribosomal protein S29 (MRPS29) expression by a 5'-upstream open reading frame. Mitochondrion 9 20079882
2024 Death-associated protein 3 in cancer-discrepant roles of DAP3 in tumours and molecular mechanisms. Frontiers in oncology 8 38352299
2004 Association between genetic variation in the gene for death-associated protein-3 (DAP3) and adult asthma. Journal of human genetics 8 15179560
2021 Expression of Death Associated Proteins DAP1 and DAP3 in Human Pancreatic Cancer. Anticancer research 7 33952460
1992 Transfection of HLA-DR-expressing DAP.3 cells with a cDNA clone encoding the glycosyl phosphatidylinositol-linked form of lymphocyte function associated antigen-3: biochemical features and functional consequences. International immunology 7 1377490
2024 DNA methylation of microRNA-365-1 induces apoptosis of hair follicle stem cells by targeting DAP3. Non-coding RNA research 6 38616861
2024 Bi-allelic variants in DAP3 result in reduced assembly of the mitoribosomal small subunit with altered apoptosis and a Perrault-syndrome-spectrum phenotype. American journal of human genetics 6 39701103
2004 Altered expression of Tfg and Dap3 in Ikaros-defective T-cell lymphomas induced by X-irradiation in B6C3F1 mice. British journal of haematology 6 14687027
2024 Modulation of m6A RNA modification by DAP3 in cancer cells. Proceedings of the National Academy of Sciences of the United States of America 5 39316047
2023 DAP3-mediated cell cycle regulation and its association with radioresistance in human lung adenocarcinoma cell lines. Journal of radiation research 5 37023702
2024 Biallelic variants in DAP3 result in reduced assembly of the mitoribosomal small subunit with altered intrinsic and extrinsic apoptosis and a Perrault syndrome-spectrum phenotype. medRxiv : the preprint server for health sciences 1 39371131

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