Affinage

EDC4

Enhancer of mRNA-decapping protein 4 · UniProt Q6P2E9

Round 2 corrected
Length
1401 aa
Mass
151.7 kDa
Annotated
2026-04-28
57 papers in source corpus 16 papers cited in narrative 16 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EDC4 (Ge-1/Hedls) is a large scaffold protein that organizes the cytoplasmic mRNA decapping machinery within P-bodies, coupling 5′-cap removal by DCP2 to 5′-to-3′ exonucleolytic degradation by XRN1. Its C-terminal ARM/HEAT-repeat domain provides distinct binding sites for DCP1, DCP2, and XRN1 via short linear motifs, stimulates DCP2 catalytic activity, drives EDC4 oligomerization and phase separation required for P-body formation, and is regulated by the microprotein NBDY which inhibits EDC4 self-association to dissolve P-bodies and activate p53-dependent gene expression (PMID:16364915, PMID:24510189, PMID:18755833, PMID:37621215, PMID:40360209). Beyond mRNA decay, EDC4 represses MARF1 endoribonuclease activity by blocking LOTUS-domain RNA binding (PMID:32510323) and participates in homologous recombination as part of the BRCA1-BRIP1-TOPBP1 complex, where its loss phenocopies BRCA1 deficiency with impaired DNA end resection, genome instability, and hypersensitivity to PARP inhibitors and interstrand cross-linking agents (PMID:29511213). EDC4 is also co-opted by Ebola virus VP35, which binds its C-terminal domain to promote viral RNA synthesis (PMID:41006235).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2005 High

    Identification of EDC4 as a central P-body scaffold upstream of DCP2 resolved how decapping factors are spatially organized: EDC4 is required for P-body integrity, whereas DCP2 is dispensable for EDC4-containing foci.

    Evidence siRNA knockdown and confocal co-localization in human cells; independently, in vitro decapping assays showed EDC4 enhances DCP2 activity and promotes DCP1–DCP2 complex formation

    PMID:16314453 PMID:16364915

    Open questions at the time
    • Structural basis for EDC4–DCP2 enhancement unknown at this stage
    • Whether EDC4 scaffolding is required for all mRNA decay substrates or a subset
  2. 2008 High

    Crystal structure of the C-terminal domain revealed an ARM/HEAT-repeat fold that mediates oligomerization and P-body targeting, providing the first structural framework for understanding EDC4 scaffold function.

    Evidence X-ray crystallography of Drosophila Ge-1 C-terminal domain with structure-guided mutagenesis validating P-body localization residues

    PMID:18755833

    Open questions at the time
    • Full-length human EDC4 structure not determined
    • Oligomerization stoichiometry and its regulation unclear
  3. 2014 High

    Mapping of distinct SLiM-mediated binding sites for DCP1, DCP2, and XRN1 on the EDC4 C-terminal domain established how EDC4 physically couples decapping to 5′-to-3′ degradation, with DCP2 activation occurring preferentially on the EDC4 scaffold.

    Evidence Binding assays, co-immunoprecipitation, and mutational analysis with in vivo decapping reporters

    PMID:24510189

    Open questions at the time
    • Structural detail of simultaneous DCP2–XRN1 binding not resolved at atomic level
    • Contribution of EDC3 versus EDC4 to DCP2 activation in different cellular contexts
  4. 2016 Medium

    Discovery that the microprotein NBDY interacts with EDC4 and that NBDY levels inversely control P-body numbers revealed an endogenous regulatory mechanism for P-body assembly operating through the EDC4 scaffold.

    Evidence Co-immunoprecipitation, live-cell P-body quantification, and NMD reporter assays in human cells

    PMID:27918561

    Open questions at the time
    • Direct binding site on EDC4 not yet mapped at this point
    • Physiological signals controlling NBDY expression unknown
  5. 2016 Medium

    Genetic analysis in Drosophila showed a natural 26-amino-acid deletion in the Ge-1 serine-rich linker confers sigma virus resistance independently of the siRNA pathway, linking EDC4-mediated mRNA decay to antiviral defense.

    Evidence Genetic mapping, transgenic fly construction, and viral titre measurement with siRNA pathway epistasis

    PMID:26799957

    Open questions at the time
    • Mechanism by which the deletion alters viral mRNA handling not established
    • Whether mammalian EDC4 similarly restricts rhabdoviruses untested
  6. 2018 High

    Discovery of EDC4 as a member of the BRCA1-BRIP1-TOPBP1 complex that stimulates DNA end resection established a wholly unexpected role for EDC4 in homologous recombination, with EDC4 deficiency phenocopying BRCA1 loss.

    Evidence Co-immunoprecipitation, HR and DNA end resection assays, siRNA knockdown, PARP inhibitor and cross-linker sensitivity in human cells

    PMID:29511213

    Open questions at the time
    • Structural basis for EDC4 integration into the BRCA1 complex unknown
    • Whether mRNA decay and HR functions are separable or coordinate
  7. 2020 High

    EDC4 was shown to repress MARF1 endoribonuclease activity by preventing LOTUS-domain RNA binding, revealing that EDC4 acts as both an enhancer (DCP2) and a repressor (MARF1) of distinct mRNA decay pathways.

    Evidence Transcriptome-wide target identification, reciprocal co-immunoprecipitation, RNA binding assays, and mutagenesis

    PMID:32510323

    Open questions at the time
    • Conditions under which EDC4-MARF1 interaction is regulated not defined
    • MARF1 target overlap with DCP2 substrates not systematically assessed
  8. 2020 Medium

    EDC4 interaction with RPA and promotion of RPA phosphorylation extended its DNA damage response role, positioning EDC4 upstream of RPA-mediated cisplatin resistance.

    Evidence Co-immunoprecipitation, siRNA knockdown, γH2AX immunofluorescence, and RPA-knockdown rescue in cervical cancer cells

    PMID:33054858

    Open questions at the time
    • Whether EDC4-RPA interaction is part of the BRCA1 complex or an independent axis unclear
    • Kinase mediating RPA phosphorylation downstream of EDC4 not identified
  9. 2023 High

    Disruption of the EDC4-XRN1 interaction demonstrated that stoichiometric balance between scaffold and exonuclease controls P-body size, mRNA decapping rate, and miRNA-mediated silencing, with enlarged P-bodies supporting cell viability under XRN1-limiting conditions.

    Evidence EDC4-XRN1 interaction mutants, mRNA stability assays, P-body and stress granule quantification, and cell viability assays

    PMID:37621215

    Open questions at the time
    • In vivo physiological conditions that alter EDC4-XRN1 stoichiometry not identified
    • How enlarged P-bodies mechanistically prevent stress granule formation unclear
  10. 2024 Medium

    In C. elegans, EDC-4 counteracts EDC-3 and recruits DCP2 to the GID/CTLH ubiquitin ligase complex, linking P-body scaffold function to developmental mRNA clearance during the maternal-to-zygotic transition.

    Evidence Genetic epistasis, co-immunoprecipitation, proteomics, and embryonic mRNA quantification in C. elegans

    PMID:39331503

    Open questions at the time
    • Conservation of EDC4-GID/CTLH axis in mammals not tested
    • Whether this reflects ubiquitin-dependent or -independent DCP2 regulation unclear
  11. 2025 Medium

    Minimal mapping showed residues 1266–1401 drive EDC4 phase separation and P-body formation, and the NBDY peptide (residues 22–41) directly inhibits this self-association, dissolving P-bodies and activating p53-pathway transcripts.

    Evidence Deletion mapping, in vitro phase separation assays, NBDY peptide binding, transcriptome profiling, and p53 reporter assays

    PMID:40360209

    Open questions at the time
    • Atomic-resolution structure of NBDY–EDC4 complex not available
    • Whether p53 activation is a direct consequence of mRNA release from P-bodies or indirect
  12. 2025 Medium

    Ebola virus VP35 binds the EDC4 C-terminal domain and co-opts the decapping complex for viral RNA synthesis, demonstrating that pathogenic viruses exploit the EDC4 scaffold.

    Evidence Proximity-dependent biotinylation, co-localization in EBOV-infected cells, siRNA depletion with viral RNA synthesis measurement

    PMID:41006235

    Open questions at the time
    • Whether VP35 competes with endogenous EDC4 partners (DCP2, XRN1) for the same binding surface not resolved
    • Therapeutic potential of disrupting VP35-EDC4 not explored

Open questions

Synthesis pass · forward-looking unresolved questions
  • How EDC4 integrates its dual roles in cytoplasmic mRNA decay and nuclear DNA repair, whether these functions are mutually exclusive or dynamically coordinated, and the full-length human EDC4 structure remain unresolved.
  • Full-length human EDC4 structure not determined
  • Signals governing EDC4 partitioning between mRNA decay and DNA repair functions unknown
  • Systematic identification of EDC4-dependent mRNA substrates in physiological contexts lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 3 GO:0003723 RNA binding 1
Localization
GO:0031410 cytoplasmic vesicle 6 GO:0005829 cytosol 3
Pathway
R-HSA-8953854 Metabolism of RNA 5 R-HSA-73894 DNA Repair 2
Partners
BRCA1DCP1ADCP2EDC3MARF1NBDYRPA1XRN1
Complex memberships
BRCA1-BRIP1-TOPBP1 complexmRNA decapping complex (DCP1–DCP2–EDC4–XRN1)

Evidence

Reading pass · 16 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 Ge-1 (EDC4) is a central scaffold component of mammalian P-bodies that co-localizes with DCP1a, DCP2, and GW182. Its C-terminal domain is necessary and sufficient for P-body targeting. siRNA-mediated knockdown of Ge-1 abolishes P-bodies containing Ge-1, DCP1a, and DCP2, while Ge-1-containing P-bodies persist despite DCP2 knockdown, placing Ge-1 upstream of the 5'-decapping step. siRNA knockdown, confocal co-localization, cDNA cloning via autoimmune patient serum RNA (New York, N.Y.) High 16314453
2005 Hedls (EDC4) enhances the catalytic activity of hDCP2 and promotes complex formation between hDCP2 and hDCP1. It exists in a complex with hDcp2, hDcp1, hEdc3, and Rck/p54. Overexpression of Hedls produces aberrant P-bodies and causes accumulation of a deadenylated ARE-mediated mRNA decay intermediate. Co-immunoprecipitation, in vitro decapping assay, overexpression phenotypic analysis, P-body localization Molecular cell High 16364915
2008 The C-terminal domain of Ge-1 (EDC4) adopts an all alpha-helical fold related to ARM/HEAT-repeat proteins. Structure-based mutagenesis identified an invariant surface residue required for P-body localization, and the domain mediates Ge-1 oligomerization. X-ray crystallography (Drosophila Ge-1 C-terminal domain), structure-based mutagenesis, P-body localization assays RNA (New York, N.Y.) High 18755833
2014 EDC4 serves as a scaffold for the human decapping complex, providing distinct binding sites for DCP1, DCP2, and XRN1. DCP2 and XRN1 bind simultaneously to the EDC4 C-terminal domain via short linear motifs (SLiMs). DCP1 and DCP2 form direct but weak interactions that are facilitated by EDC4. A conserved asparagine-arginine loop (NR-loop) in the DCP1 EVH1 domain is required for DCP2 activation, which occurs preferentially on the EDC4 scaffold, coupling decapping to 5'-to-3' degradation by XRN1. Binding assays, co-immunoprecipitation, mutational analysis, in vivo functional decapping assays Nucleic acids research High 24510189
2012 EDC4 forms a complex with Coenzyme A synthase (CoAsy) in a growth factor- and stress-regulated manner. EDC4 strongly inhibits the dephospho-CoA kinase activity of CoAsy in vitro, and transient overexpression of EDC4 decreases cell proliferation, an effect partially rescued by co-expression of CoAsy. Co-immunoprecipitation, in vitro kinase activity assay, overexpression/rescue experiments FEBS letters Medium 22982864
2014 CCHCR1 interacts with EDC4 as its major binding partner, as identified by co-immunoprecipitation with EGFP-tagged CCHCR1 and LC-MS/MS. The N-terminus of CCHCR1 is required for P-body localization, establishing CCHCR1 as a novel P-body component. Co-immunoprecipitation, LC-MS/MS, confocal imaging, stable cell line expression Experimental cell research Medium 24858563
2014 Edc4 interacts with the mTORC1 complex (via raptor) in human T lymphoblast cells, co-localizes with raptor in P-bodies, and undergoes serine phosphorylation that is reduced by rapamycin treatment. Rapamycin also increases total Edc4 protein while decreasing its interaction with mTORC1 and reducing total 5'-capped mRNA levels. Co-immunoprecipitation, quantitative co-localization by confocal microscopy, rapamycin treatment, immunoblotting International journal of molecular sciences Low 25514416
2016 A naturally occurring 26 amino acid deletion in the serine-rich linker region of Drosophila Ge-1 confers resistance to Drosophila melanogaster sigma virus. Knockdown of the susceptible allele reduces viral titre. Ge-1-based resistance is independent of the siRNA pathway. DCP1, which interacts with Ge-1 and commits mRNA to degradation by cap removal, also protects against sigma virus. Genetic mapping, transgenic fly construction, viral titre measurement, siRNA pathway epistasis PLoS pathogens Medium 26799957
2018 EDC4 is a member of the BRCA1-BRIP1-TOPBP1 complex and plays a role in homologous recombination by stimulating DNA end resection at double-strand breaks. EDC4 deficiency causes genome instability, hypersensitivity to DNA interstrand cross-linking drugs and PARP inhibitors, phenocopying BRCA1 deficiency. Co-immunoprecipitation, HR assays, DNA end resection assays, siRNA knockdown, drug sensitivity assays, patient mutation analysis Nature communications High 29511213
2020 EDC4 interacts with mammalian MARF1 endoribonuclease and impairs its activity by preventing MARF1's LOTUS domains from binding target mRNAs. MARF1 predominantly binds 3' UTRs of target mRNAs via its LOTUS domains to promote their decay, and a MARF1 RRM enhances its endonuclease activity. Thus EDC4 acts as a repressor of MARF1-mediated mRNA decay in addition to its role as an enhancer of DCP2-mediated decapping. RNA-seq/transcriptome-wide analysis, co-immunoprecipitation, RNA binding assays, mutagenesis eLife High 32510323
2020 EDC4 interacts with replication protein A (RPA) and promotes RPA phosphorylation. EDC4 knockdown enhances cisplatin sensitivity and cisplatin-induced DNA damage in cervical cancer cells. RPA knockdown reverses the protective effect of EDC4 overexpression on cisplatin-induced DNA damage, placing RPA downstream of EDC4 in this cisplatin resistance pathway. Co-immunoprecipitation, siRNA knockdown, MTT/colony assays, γH2AX immunofluorescence, overexpression rescue Hereditas Medium 33054858
2023 Disrupting the EDC4-XRN1 interaction or altering their stoichiometry inhibits mRNA decapping and stabilizes microRNA-targeted mRNAs in a translationally repressed state. This concomitantly leads to larger P-bodies that are responsible for preventing mRNA decapping. P-bodies support cell viability and prevent stress granule formation when XRN1 is limiting, demonstrating that the EDC4-XRN1 interaction regulates P-body dynamics to coordinate mRNA decapping with 5'-to-3' decay. Mutational disruption of EDC4-XRN1 interaction, mRNA stability assays, P-body size quantification, stress granule assays, cell viability assays The EMBO journal High 37621215
2024 In C. elegans, EDC-4 counteracts EDC-3 function and engenders the assembly of DCAP-2 (DCP2) with the GID/CTLH complex, a ubiquitin ligase involved in the maternal-to-zygotic transition, linking P-body scaffold function to developmental mRNA clearance. Genetic epistasis in C. elegans, co-immunoprecipitation, proteomics, embryonic mRNA quantification Cell reports Medium 39331503
2025 The EDC4 C-terminal domain (residues 1266-1401) is the minimal region required for P-body formation, driving phase separation and EDC4 condensation. The microprotein Nobody (NBDY) peptide (residues 22-41) directly binds the EDC4 C-terminal domain and inhibits its self-association, selectively dissolving P-bodies without affecting the canonical mRNA decay pathway. P-body disruption activates the p53 pathway and enhances stability of associated transcripts. Deletion mapping, phase separation assays, NBDY peptide binding assay, transcriptome profiling, p53 pathway reporter assays, cell proliferation/invasion assays RNA (New York, N.Y.) Medium 40360209
2025 Ebola virus VP35 binds directly to the C-terminal subdomain of EDC4, and both proteins co-localize in EBOV-infected cells. siRNA depletion of EDC4, DCP2, and EDC3 each reduce EBOV replication by inhibiting early viral RNA synthesis, demonstrating that EBOV co-opts the EDC4 scaffold of the mRNA decapping complex for its replication. Proximity-dependent biotinylation, co-localization in infected cells, siRNA depletion with viral RNA synthesis measurement Nature communications Medium 41006235
2016 NoBody (NBDY) microprotein interacts with mRNA decapping proteins including EDC4 and localizes to P-bodies. Modulation of NoBody levels is anticorrelated with cellular P-body numbers and alters steady-state levels of an NMD substrate, implicating NBDY as a novel component of the mRNA decapping complex that regulates P-body assembly. Co-immunoprecipitation, live-cell imaging, P-body quantification, NMD reporter assays Nature chemical biology Medium 27918561

Source papers

Stage 0 corpus · 57 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 Biological insights from 108 schizophrenia-associated genetic loci. Nature 5878 25056061
2012 Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 1718 22658674
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2016 ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 1233 26777405
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2011 Global landscape of HIV-human protein complexes. Nature 593 22190034
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2010 Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science (New York, N.Y.) 421 20360068
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
2005 Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Molecular cell 389 16364915
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2014 A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 325 25036637
2020 Virus-Host Interactome and Proteomic Survey Reveal Potential Virulence Factors Influencing SARS-CoV-2 Pathogenesis. Med (New York, N.Y.) 291 32838362
2011 Mapping a dynamic innate immunity protein interaction network regulating type I interferon production. Immunity 286 21903422
2012 A high-throughput approach for measuring temporal changes in the interactome. Nature methods 273 22863883
2011 Genome-wide association study of coronary heart disease and its risk factors in 8,090 African Americans: the NHLBI CARe Project. PLoS genetics 258 21347282
2017 A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis. Molecular cell 248 28431233
2016 A human microprotein that interacts with the mRNA decapping complex. Nature chemical biology 236 27918561
2014 Proximity biotinylation and affinity purification are complementary approaches for the interactome mapping of chromatin-associated protein complexes. Journal of proteomics 215 25281560
2011 Toward an understanding of the protein interaction network of the human liver. Molecular systems biology 207 21988832
2013 PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry. Molecular cell 204 24332808
2015 A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning. eLife 198 26673895
2011 Protein interactome reveals converging molecular pathways among autism disorders. Science translational medicine 180 21653829
2012 Genome-wide screen for metabolic syndrome susceptibility Loci reveals strong lipid gene contribution but no evidence for common genetic basis for clustering of metabolic syndrome traits. Circulation. Cardiovascular genetics 163 22399527
2005 Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body. RNA (New York, N.Y.) 156 16314453
2014 The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1. Nucleic acids research 99 24510189
1987 Gerbich blood group deficiency of the Ge:-1,-2,-3 and Ge:-1,-2,3 types. Immunochemical study and genomic analysis with cDNA probes. European journal of biochemistry 50 3595602
2008 Electrodeposition of Ge, Si and Si x Ge 1-x from an air- and water-stable ionic liquid. Physical chemistry chemical physics : PCCP 38 18665315
2018 Decapping protein EDC4 regulates DNA repair and phenocopies BRCA1. Nature communications 36 29511213
2023 The EDC4-XRN1 interaction controls P-body dynamics to link mRNA decapping with decay. The EMBO journal 33 37621215
2008 The C-terminal region of Ge-1 presents conserved structural features required for P-body localization. RNA (New York, N.Y.) 31 18755833
2011 Drosophila Ge-1 promotes P body formation and oskar mRNA localization. PloS one 24 21655181
2016 A Polymorphism in the Processing Body Component Ge-1 Controls Resistance to a Naturally Occurring Rhabdovirus in Drosophila. PLoS pathogens 22 26799957
2014 CCHCR1 interacts with EDC4, suggesting its localization in P-bodies. Experimental cell research 20 24858563
2021 Photocatalytic and Photoelectrochemical Hydrogen Evolution from Water over Cu2SnGe1-S3 Particles. Journal of the American Chemical Society 18 33827207
2012 EDC4 interacts with and regulates the dephospho-CoA kinase activity of CoA synthase. FEBS letters 18 22982864
2020 A non-canonical role for the EDC4 decapping factor in regulating MARF1-mediated mRNA decay. eLife 13 32510323
2020 Enhancer of mRNA Decapping protein 4 (EDC4) interacts with replication protein a (RPA) and contributes to Cisplatin resistance in cervical Cancer by alleviating DNA damage. Hereditas 11 33054858
2020 Reducing interfacial resistance of a Li1.5Al0.5Ge1.5(PO4)3 solid electrolyte/electrode interface by polymer interlayer protection. RSC advances 9 35498566
2014 Crosstalk between Edc4 and mammalian target of rapamycin complex 1 (mTORC1) signaling in mRNA decapping. International journal of molecular sciences 6 25514416
2025 EDC4 C-terminal domain scaffolds P-body assembly and links P-body dynamics to p53-mediated tumor suppression. RNA (New York, N.Y.) 4 40360209
2024 Construction of SnO2 buffer layer and analysis of its interface modification for Li and Li1.5Al0.5Ge1.5(PO4)3 in solid-state batteries. Journal of colloid and interface science 4 38394818
2024 EDC-3 and EDC-4 regulate embryonic mRNA clearance and biomolecular condensate specialization. Cell reports 3 39331503
2023 Dynamic "Cap"-abilities of P-bodies and the XRN1-EDC4 axis. The EMBO journal 3 37750488
2025 A protein-proximity screen reveals Ebola virus co-opts the mRNA decapping complex through the scaffold protein EDC4. Nature communications 2 41006235
2024 A protein-proximity screen reveals Ebola virus co-opts the mRNA decapping complex through the scaffold protein EDC4. Research square 2 38352529
2017 Complete genome sequence of Thermus brockianus GE-1 reveals key enzymes of xylan/xylose metabolism. Standards in genomic sciences 2 28174620
2025 The molecular axis hnRNPU/circKCNK2/EDC4/IL-11 aggravates osteolytic bone metastasis of RCC. Oncogene 1 40640337
2022 Magnetic phase diagram of the solid solution LaMn2(Ge1-xSix)2 (0 ≤ x ≤ 1) unraveled by powder neutron diffraction. Scientific reports 1 35665754
2025 EDC4 enhances multi-drug chemosensitivity in pancreatic cancer via GR50-based profiling. Cancer cell international 0 41073999
2016 2D Tl-Pb compounds on Ge(1 1 1) surface: atomic arrangement and electronic band structure. Journal of physics. Condensed matter : an Institute of Physics journal 0 27845925