Affinage

DEDD

Death effector domain-containing protein · UniProt O75618

Length
318 aa
Mass
36.8 kDa
Annotated
2026-04-28
35 papers in source corpus 17 papers cited in narrative 17 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

DEDD is a death effector domain (DED)-containing scaffold protein that integrates apoptotic signaling, cell cycle control, and autophagy-mediated suppression of epithelial-mesenchymal transition. In apoptosis, DEDD interacts with FADD and caspase-8/10 via its DED, recruits pro-caspase-3 to keratin 8/18 intermediate filaments for proximity-induced activation, activates caspase-6, and inhibits RNA polymerase I transcription upon nucleolar translocation—a process regulated by cIAP-1/2-mediated monoubiquitination that shuttles DEDD between the nucleolus and cytoplasm (PMID:9774341, PMID:11753564, PMID:12235123, PMID:16235027). Beyond apoptosis, DEDD directly binds and inhibits mitotic Cdk1/cyclin B1 kinase activity, thereby supporting S6K1 and Akt stability and controlling cell size and organ growth, as demonstrated by decreased body weight, glucose intolerance, and female infertility in DEDD-knockout mice (PMID:17283331, PMID:19106089, PMID:21135503). DEDD also activates autophagy by binding the PI3KC3/Beclin1 complex, promoting lysosomal degradation of Snail and Twist to suppress invasion and metastasis, and its own stability is regulated by ZIPK-mediated phosphorylation at S9 (PMID:22719072, PMID:40032841).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1998 High

    Identification of DEDD as a DED-containing protein that interacts with FADD and caspase-8, translocates to the nucleolus upon death receptor signaling, binds DNA/nucleosomes, and directly inhibits RNA Pol I transcription established DEDD as a nuclear apoptosis effector linking death receptor signaling to transcriptional shutdown.

    Evidence Co-IP, immunofluorescence co-localization with UBF, in vitro Pol I transcription reconstitution, and DNA/nucleosome binding assays in human cells

    PMID:9774341

    Open questions at the time
    • Identity of DEDD's nucleolar target beyond UBF co-localization not resolved
    • Endogenous stoichiometry of DEDD–FADD complex unclear
    • No structural data for DEDD-DED interactions
  2. 2001 High

    Demonstrating that all three NLS motifs are required for nuclear translocation and that the DED alone suffices for caspase-6 activation and Pol I repression established that DEDD's apoptotic function is nuclear and that its DED is the minimal functional unit for transcriptional inhibition.

    Evidence NLS mutagenesis (DEDD-ΔNLS1-3), BrUTP incorporation (in vivo Pol I activity), caspase-6 activity assay

    PMID:11753564

    Open questions at the time
    • Direct Pol I subunit target not identified
    • How caspase-6 activation by DEDD DED is mechanistically achieved remains unresolved
  3. 2002 High

    Discovery that diubiquitinated DEDD scaffolds pro-caspase-3 to K8/18 intermediate filaments, directing effector caspase activation to specific substrates, revealed a non-nuclear cytoplasmic apoptotic function for DEDD as a spatial organizer of caspase activity.

    Evidence Reciprocal co-IP of DEDD with K18 and pro-caspase-3, siRNA knockdown blocking staurosporine-induced DNA degradation, kinetic analysis of caspase-3 activation

    PMID:12235123

    Open questions at the time
    • Whether DEDD directly contacts both K18 and caspase-3 simultaneously or sequentially is unknown
    • Ubiquitin linkage type on DEDD not determined
  4. 2005 Medium

    Showing that cIAP-1/2-mediated monoubiquitination relocates DEDD from nucleolus to cytosol and that a ubiquitin-DEDD fusion enhances pro-apoptotic potential established ubiquitination as the switch governing DEDD's compartment-specific functions.

    Evidence Lysine mutagenesis, cIAP-1/2 co-transfection, ubiquitin-DEDD C-terminal fusion construct, immunofluorescence localization

    PMID:16235027

    Open questions at the time
    • Specific lysine residue(s) ubiquitinated not pinpointed
    • No deubiquitinase identified
    • In vivo relevance of cIAP-mediated ubiquitination not tested in KO model
  5. 2007 High

    Demonstration that DEDD directly binds cyclin B1 and inhibits Cdk1/cyclin B1 kinase activity, with DEDD-knockout mice showing accelerated mitosis, reduced rRNA, and decreased body/organ size, revealed an unexpected cell-cycle regulatory role independent of apoptosis.

    Evidence Co-IP of DEDD with Cdk1/cyclin B1, kinase activity assay in DEDD−/− vs. wild-type MEFs, DEDD−/− mouse phenotyping including cell cycle analysis

    PMID:17283331

    Open questions at the time
    • Binding interface between DEDD and cyclin B1 not mapped
    • Whether DEDD inhibits Cdk1 catalytically or by sequestering cyclin B1 is unresolved
  6. 2008 High

    Finding that DEDD associates with S6K1 and protects it from Cdk1-dependent inhibitory phosphorylation, with DEDD-knockout mice phenocopying S6K1 knockouts in glucose intolerance and reduced islet mass, connected DEDD's Cdk1 inhibition to growth/metabolic signaling via mTOR-S6K1.

    Evidence Co-IP of DEDD with S6K1, phosphorylation analysis (Thr-389 vs. Cdk1 sites) in DEDD−/− cells and tissues, metabolic phenotyping of DEDD−/− mice

    PMID:19106089

    Open questions at the time
    • Whether DEDD–S6K1 interaction is direct or bridged by cyclin B1/Cdk1 not fully resolved
    • Tissue-specific requirements not mapped
  7. 2009 Medium

    Showing that DEDD complexes with Akt and Hsp90 and that Cdk1 inhibition restores Akt levels in DEDD−/− cells established that DEDD stabilizes Akt indirectly through Cdk1 suppression, explaining impaired insulin-stimulated GLUT4 translocation in knockout tissues.

    Evidence Co-IP of DEDD with Akt and Hsp90, DEDD−/− mouse skeletal muscle/adipose analysis, Cdk1 siRNA rescue of Akt levels, GLUT4 translocation assay

    PMID:20043882

    Open questions at the time
    • Whether DEDD directly contacts Akt or only through Hsp90 not determined
    • Contribution of Hsp90 chaperone activity versus Cdk1 suppression not separated
  8. 2010 High

    Linking DEDD to cyclin D3 stabilization and Akt-dependent polyploidization during decidualization, with DEDD−/− female infertility rescued by cyclin D3 or Akt overexpression, demonstrated a physiological non-apoptotic role for DEDD in reproductive biology.

    Evidence DEDD−/− mouse fertility and decidualization analysis, co-IP of DEDD with cyclin D3, rescue by cyclin D3 or Akt overexpression, polyploidization assay

    PMID:21135503

    Open questions at the time
    • Mechanism by which DEDD stabilizes cyclin D3 (proteasome protection vs. other) not defined
    • Whether male DEDD−/− fertility phenotypes exist not explored
  9. 2012 High

    Discovery that DEDD binds PI3KC3/Beclin1 to activate autophagy and promote lysosomal degradation of Snail and Twist, suppressing EMT and metastasis both in vitro and in vivo, established DEDD as a metastasis suppressor acting through autophagy.

    Evidence Co-IP of DEDD with PI3KC3/Beclin1, autophagy induction assay, invasion/metastasis assays in vitro and in vivo, Western blot for Snail/Twist degradation, siRNA knockdown

    PMID:22719072

    Open questions at the time
    • Selectivity mechanism for Snail/Twist as autophagy cargo not identified
    • Whether DEDD activates PI3KC3 enzymatically or by stabilization not distinguished
  10. 2020 Medium

    Identification of DEDD as a stabilizer of Bcl-2 protein, with DEDD knockdown accelerating Bcl-2 degradation and altering drug sensitivity, added an anti-apoptotic regulatory dimension to DEDD's functions.

    Evidence Co-IP of DEDD with Bcl-2, siRNA knockdown and overexpression, drug sensitivity assays in breast cancer cells

    PMID:32113682

    Open questions at the time
    • Mechanism of Bcl-2 stabilization (proteasomal vs. other) not determined
    • Paradox of a pro-apoptotic DED protein stabilizing anti-apoptotic Bcl-2 not reconciled
    • Single cell-type study
  11. 2025 Medium

    Demonstration that ZIPK phosphorylates DEDD at S9 to enhance its stability and promote caspase-3-dependent neuronal apoptosis after traumatic brain injury identified the first upstream kinase controlling DEDD protein levels.

    Evidence Co-IP and in vitro kinase assay (ZIPK–DEDD), S9 phosphosite mapping, ZIPK haploinsufficiency mouse model after TBI, pharmacological ZIPK inhibition

    PMID:40032841

    Open questions at the time
    • Whether S9 phosphorylation affects DEDD ubiquitination or other post-translational modifications not tested
    • Generality beyond neuronal TBI context unknown
    • Single lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • The structural basis for DEDD's multivalent scaffolding—simultaneously engaging Cdk1/cyclin B1, PI3KC3/Beclin1, caspase-3/K18, and Akt/Hsp90—and how cells select between DEDD's apoptotic versus growth-regulatory versus autophagy functions in a context-dependent manner remain unresolved.
  • No crystal or cryo-EM structure of DEDD or any DEDD complex
  • No systematic interactome under apoptotic vs. proliferative conditions
  • Regulatory logic integrating ubiquitination, phosphorylation, and localization not modeled

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 3 GO:0060090 molecular adaptor activity 2 GO:0003677 DNA binding 1
Localization
GO:0005730 nucleolus 3 GO:0005829 cytosol 3 GO:0005634 nucleus 2 GO:0005856 cytoskeleton 2
Pathway
R-HSA-5357801 Programmed Cell Death 4 R-HSA-162582 Signal Transduction 3 R-HSA-1640170 Cell Cycle 2 R-HSA-74160 Gene expression (Transcription) 2 R-HSA-9612973 Autophagy 1
Partners
AKT1CASP3CASP8CCNB1CDK1FADDKRT18RPS6KB1
Complex memberships
Cdk1/cyclin B1PI3KC3/Beclin1

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 DEDD contains an N-terminal death effector domain (DED) through which it interacts with FADD and caspase-8; endogenous DEDD resides in the cytoplasm and translocates to the nucleus/nucleolus upon CD95 stimulation, where it co-localizes with UBF; recombinant DEDD binds DNA and reconstituted mononucleosomes and inhibits RNA polymerase I transcription in a reconstituted in vitro system; overexpression induces apoptosis primarily through its DED. Co-immunoprecipitation, immunofluorescence/co-localization with UBF, in vitro transcription reconstitution assay, DNA/nucleosome binding assay, overexpression apoptosis assay The EMBO journal High 9774341
2001 Nuclear/nucleolar localization of DEDD is required for its apoptotic activity; DEDD activates caspase-6 through its DED domain; DEDD specifically inhibits RNA polymerase I-dependent transcription in vivo (blocking BrUTP incorporation); the DED alone is sufficient for DNA binding, caspase-6 activation, and Pol I transcriptional repression; mutation of all three nuclear localization signals (NLS) abolishes nuclear targeting and apoptosis induction. BrUTP incorporation assay (in vivo Pol I transcription), immunofluorescence with anti-DEDD antibody, NLS mutagenesis, caspase-6 activity assay, cytoplasmic DEDD (DEDD-ΔNLS1-3) functional analysis Cell death and differentiation High 11753564
2002 Diubiquitinated DEDD interacts with the K8/18 intermediate filament network and pro-caspase-3; early in apoptosis, DEDD and DEDD2 form filaments co-localizing with K8/18 in a caspase-3-dependent manner; these structures collapse into inclusions containing active caspase-3 and cleaved K18; cytosolic DEDD (DEDD-ΔNLS1-3) inhibits caspase-3 activation and K18 cleavage; siRNA-mediated DEDD knockdown inhibits staurosporine-induced DNA degradation; DEDD functions as a scaffold directing effector caspase-3 to specific substrates. Co-immunoprecipitation (DEDD with K18 and pro-caspase-3), immunofluorescence, siRNA knockdown, biochemical kinetics of caspase-3 activation and K18 cleavage The Journal of cell biology High 12235123
2002 DEDD interacts with the TFIIIC102 subunit of human transcription factor TFIIIC via its DED domain; co-expression of DEDD with hTFIIIC102 causes translocation of hTFIIIC102 to the nucleus; overexpression of DEDD inhibits NF-κB promoter-driven luciferase expression. Yeast two-hybrid identification of TFIIIC102 as DEDD interactor, co-immunoprecipitation, co-localization immunofluorescence, luciferase reporter assay Cell death and differentiation Medium 11965497
2003 DEDD and DEDD2 bind to caspase-8 and caspase-10 (tandem DED-containing caspases) and to each other and to each other's homologue; nuclear localization is required for DEDD/DEDD2-induced apoptosis; both the N-terminal DED and C-terminal region of DEDD2 can independently induce apoptosis. Co-immunoprecipitation/binding assays, deletion analysis, overexpression apoptosis assay in various cell types Oncogene Medium 12527898
2005 DEDD exists in non-, mono-, and diubiquitinated forms; monoubiquitination relocates DEDD from the nucleolus to the cytosol; a central region (aa 109–305) outside the DED is required for ubiquitination; cIAP-1 and cIAP-2 can catalyze both mono- and polyubiquitination of DEDD; fusion of ubiquitin to DEDD C-terminus (mimicking monoubiquitinated DEDD) increases its pro-apoptotic potential. Ubiquitin-DEDD fusion construct, mutagenesis of lysine residues, co-transfection with cIAP-1/2, immunofluorescence localization, apoptosis assay Apoptosis Medium 16235027
2007 DEDD associates with the mitotic Cdk1/cyclin B1 complex via direct binding to cyclin B1 and inhibits its kinase activity; DEDD-null embryonic fibroblasts show increased nuclear Cdk1/cyclin B1 kinase activity, accelerated mitotic progression, and shortened G2/M; DEDD-/- mice display decreased body and organ weights; absence of DEDD reduces rRNA amounts and cell volume due to rapid termination of rRNA synthesis before division. Co-immunoprecipitation (DEDD with Cdk1/cyclin B1), kinase activity assay in DEDD-/- vs. DEDD+/+ cells, DEDD-/- mouse model, cell cycle analysis Proceedings of the National Academy of Sciences of the United States of America High 17283331
2008 DEDD associates with S6K1 and supports S6K1 activity by preventing Cdk1-dependent inhibitory phosphorylation at the S6K1 C-terminus; DEDD-/- cells show reduced S6K1 activating phosphorylation (Thr-389) and increased inhibitory Cdk1-dependent phosphorylation; DEDD-/- mice show reduced pancreatic islet insulin mass and glucose intolerance, paralleling S6K1-/- phenotype. Co-immunoprecipitation (DEDD with S6K1), phosphorylation analysis in DEDD-/- cells/tissues, DEDD-/- mouse metabolic phenotyping, comparison with S6K1-/- mice The Journal of biological chemistry High 19106089
2009 DEDD forms a complex with Akt and Hsp90 and supports the stability of both proteins; in DEDD-/- mice, Akt protein levels are diminished in skeletal muscle and adipose tissue, impairing GLUT4 translocation upon insulin stimulation; Cdk1 inhibition in DEDD-/- cells (via siRNA or inhibitor) restores Akt and Hsp90 levels, suggesting DEDD stabilizes Akt by suppressing Cdk1. Co-immunoprecipitation (DEDD with Akt and Hsp90), DEDD-/- mouse tissue analysis, Cdk1 siRNA knockdown, GLUT4 translocation assay Biochemical and biophysical research communications Medium 20043882
2010 Female DEDD-/- mice are infertile due to defective uterine decidualization; DEDD-deficient decidual cells show attenuated polyploidization; DEDD associates with and stabilizes cyclin D3 (important for polyploidization); overexpression of cyclin D3 rescues polyploidization in DEDD-deficient cells; decreased Akt levels in DEDD-/- uteri contribute to defective decidualization, and Akt overexpression restores polyploidization. DEDD-/- mouse model (fertility and decidualization phenotype), co-immunoprecipitation (DEDD with cyclin D3), rescue by cyclin D3 or Akt overexpression, cell polyploidization assay The Journal of clinical investigation High 21135503
2010 DEDD physically interacts with Smad3 and inhibits TGF-β1/Smad3-mediated transcription by preventing Smad3 phosphorylation and nuclear translocation, reducing formation of the Smad3-Smad4 complex; DEDD inhibits TGF-β1-mediated cell invasion. Co-immunoprecipitation (DEDD with Smad3), immunofluorescence (Smad3 localization), reporter assay for Smad3 transcriptional activity, invasion assay FEBS letters Medium 20553715
2012 DEDD directly interacts with the PI3KC3 (PIK3C3)/Beclin1 complex and activates autophagy; the DEDD-PI3KC3 interaction stabilizes PI3KC3; this autophagy activation leads to lysosomal degradation of Snail and Twist (EMT master regulators), thereby attenuating epithelial-to-mesenchymal transition; DEDD overexpression suppresses invasion in vitro and metastasis in vivo while DEDD silencing promotes invasion. Co-immunoprecipitation (DEDD with PI3KC3/Beclin1), in vitro and in vivo invasion/metastasis assays, autophagy induction assay, Western blot for Snail/Twist degradation, siRNA knockdown Cancer research High 22719072
2013 The N-terminal DED domain of DEDD is sufficient to inhibit TGF-β1-induced Smad3 nuclear translocation and Smad3-Smad4 complex formation; both full-length DEDD and its N-terminal (N-DEDD) and C-terminal (C-DEDD) truncation mutants can induce apoptosis and inhibit cell proliferation. Truncation mutant analysis, immunofluorescence, co-immunoprecipitation, flow cytometry (apoptosis), MTT assay (proliferation) Yao xue xue bao = Acta pharmaceutica Sinica Medium 23888690
2020 DEDD interacts with and stabilizes Bcl-2 protein; DEDD knockdown downregulates Bcl-2 transcriptional activity and accelerates Bcl-2 degradation; DEDD expression levels are positively correlated with Bcl-2 in breast cancer cells; knockdown of DEDD causes drug resistance to doxorubicin and paclitaxel, while overexpression increases sensitivity. Co-immunoprecipitation (DEDD with Bcl-2), Western blot, luciferase-based transcription assay, drug sensitivity assay (MTT), siRNA knockdown and overexpression Biochemical and biophysical research communications Medium 32113682
2025 ZIPK (zipper-interacting protein kinase) binds to and phosphorylates DEDD at the S9 residue, enhancing DEDD stability and leading to activation of caspase-3-mediated apoptosis in neurons; ZIPK haploinsufficiency reduces neuronal apoptosis, DEDD upregulation, and caspase-3 activation after traumatic brain injury; pharmacological ZIPK inhibition prior to TBI prevents DEDD upregulation and caspase-3 activation. Co-immunoprecipitation (ZIPK with DEDD), phosphorylation mapping (S9 site), ZIPK haploinsufficiency mouse model, in vitro kinase assay, caspase-3 activity assay, pharmacological ZIPK inhibitor Cell death & disease Medium 40032841
2006 DEDD co-purifies with CK18 in subcellular fractionation (Triton X-100 resistant fraction); mono- or diubiquitinated DEDD associates with K8/18 cytokeratin filaments; cells with filamentous DEDD distribution are more apoptosis-prone; DEDD is proposed to provide a scaffold for proximity-induced autocleavage and activation of procaspase-9 and -3 at the CK8/18 scaffold. Double immunofluorescence, Triton X-100 extraction and subcellular fractionation, co-purification with CK18, apoptosis sensitivity assay (M30 staining after roscovitine) Apoptosis Medium 16820959
2006 DEDDL, a longer human-specific isoform of DEDD produced by alternative splicing, is expressed in T lymphocytes and dendritic cells; DEDDL binds FADD and cFLIP more potently than DEDD in co-immunoprecipitation, and is a more potent apoptosis inducer than DEDD; both DEDD and DEDDL are substrates of active caspases. Co-immunoprecipitation (DEDDL vs. DEDD with FADD/cFLIP), overexpression apoptosis assay, RT-PCR expression analysis Gene expression Low 17193921

Source papers

Stage 0 corpus · 35 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 Self-enhanced accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction. Journal of bacteriology 165 19684127
2012 DEDD interacts with PI3KC3 to activate autophagy and attenuate epithelial-mesenchymal transition in human breast cancer. Cancer research 148 22719072
1998 DEDD, a novel death effector domain-containing protein, targeted to the nucleolus. The EMBO journal 110 9774341
2010 Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA. Journal of bacteriology 85 19880599
2002 DEDD regulates degradation of intermediate filaments during apoptosis. The Journal of cell biology 77 12235123
2016 miR-24-3p regulates bladder cancer cell proliferation, migration, invasion and autophagy by targeting DEDD. Oncology reports 71 28000900
2003 DEDD and DEDD2 associate with caspase-8/10 and signal cell death. Oncogene 62 12527898
2012 DEDD, a novel tumor repressor, reverses epithelial-mesenchymal transition by activating selective autophagy. Autophagy 52 22874565
2001 Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription. Cell death and differentiation 51 11753564
2010 Death effector domain-containing protein (DEDD) is required for uterine decidualization during early pregnancy in mice. The Journal of clinical investigation 47 21135503
2018 MicroRNA-17 inhibition overcomes chemoresistance and suppresses epithelial-mesenchymal transition through a DEDD-dependent mechanism in gastric cancer. The international journal of biochemistry & cell biology 31 29953965
2018 Long Noncoding RNA LINC00472 Inhibits Proliferation and Promotes Apoptosis of Lung Adenocarcinoma Cells via Regulating miR-24-3p/ DEDD. Technology in cancer research & treatment 27 30175664
2007 Death-effector domain-containing protein DEDD is an inhibitor of mitotic Cdk1/cyclin B1. Proceedings of the National Academy of Sciences of the United States of America 25 17283331
2006 DEDD association with cytokeratin filaments correlates with sensitivity to apoptosis. Apoptosis : an international journal on programmed cell death 25 16820959
2002 Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC. Cell death and differentiation 22 11965497
2019 Roles of the DedD Protein in Escherichia coli Cell Constriction. Journal of bacteriology 20 30692172
2017 De-immunized and Functional Therapeutic (DeFT) versions of a long lasting recombinant alpha interferon for antiviral therapy. Clinical immunology (Orlando, Fla.) 18 28089609
2005 Fusing DEDD with ubiquitin changes its intracellular localization and apoptotic potential. Apoptosis : an international journal on programmed cell death 16 16235027
2018 MicroRNA-24-3p regulates Hodgkin's lymphoma cell proliferation, migration and invasion by targeting DEDD. Oncology letters 14 30655776
2005 Piv site-specific invertase requires a DEDD motif analogous to the catalytic center of the RuvC Holliday junction resolvases. Journal of bacteriology 14 15866929
1998 DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells. Endocrinology 12 9832420
2023 POLD1 DEDD Motif Mutation Confers Hypermutation in Endometrial Cancer and Durable Response to Pembrolizumab. Cancers 10 38067377
2008 The death effector domain-containing DEDD supports S6K1 activity via preventing Cdk1-dependent inhibitory phosphorylation. The Journal of biological chemistry 10 19106089
2025 Zipper-interacting protein kinase mediates neuronal cell death and cognitive dysfunction in traumatic brain injury via regulating DEDD. Cell death & disease 9 40032841
2009 The death effector domain-containing DEDD forms a complex with Akt and Hsp90, and supports their stability. Biochemical and biophysical research communications 8 20043882
2019 MCL1 and DEDD Promote Urothelial Carcinoma Progression. Molecular cancer research : MCR 7 30777879
2013 [DEDD decreases Smad3 activity, promotes tumor cell apoptosis and inhibits proliferation]. Yao xue xue bao = Acta pharmaceutica Sinica 6 23888690
2010 DEDD negatively regulates transforming growth factor-beta1 signaling by interacting with Smad3. FEBS letters 6 20553715
2022 Contribution of domain structure to the function of the yeast DEDD family exoribonuclease and RNase T functional homolog, Rex1. RNA (New York, N.Y.) 4 35082142
2014 Development of deft amplification refractory mutation sequencing system (ARMSS) for discriminating Pilos antler based on a short cytochrome b (Cytb) gene. Mitochondrial DNA. Part A, DNA mapping, sequencing, and analysis 4 25090397
2020 Low DEDD expression in breast cancer cells indicates higher sensitivity to the Bcl-2-specific inhibitor ABT-199. Biochemical and biophysical research communications 2 32113682
2016 A requirement for cell elongation protein RodZ and cell division proteins FtsN and DedD to maintain the small rod morphology of Escherichia coli at growth temperatures near 8°C. The Journal of general and applied microbiology 1 27477251
2006 Identification and characterization of DEDDL, a human-specific isoform of DEDD. Gene expression 1 17193921
1996 Rapid identification of Escherichia coli O157:H7 in bovine feces using the antibody-direct epifluorescent filter technique (Ab-DEFT). Veterinary microbiology 1 8870195
2026 [Retracted] miR‑24‑3p regulates bladder cancer cell proliferation, migration, invasion and autophagy by targeting DEDD. Oncology reports 0 41952488