Affinage

AEBP2

Zinc finger protein AEBP2 · UniProt Q6ZN18

Length
517 aa
Mass
54.5 kDa
Annotated
2026-06-09
42 papers in source corpus 24 papers cited in narrative 24 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

AEBP2 is a zinc-finger accessory subunit of Polycomb Repressive Complex 2 (PRC2) that modulates the deposition and genomic targeting of repressive H3K27 methylation (PMID:15225548, PMID:27317809, PMID:29628311). First characterized as a zinc-finger DNA-binding transcriptional repressor acting at the aP2 promoter (PMID:10329662), AEBP2 was subsequently shown to enhance the histone methyltransferase activity of the EED-EZH2-SUZ12 core above its minimal baseline through a mechanism independent of and additive to H3K27me3-driven allosteric activation (PMID:15225548, PMID:29681498). Together with JARID2, AEBP2 defines the PRC2.2 subcomplex, which is mutually exclusive and antagonistic to the PCL/PALI1-containing PRC2.1 assembly (PMID:29628311). Structural studies place AEBP2 in contact with the RBBP4 subunit, where it mimics an unmodified H3 tail and progressively blocks H3K4 binding, and show that AEBP2 and JARID2 each engage a ubiquitin moiety and the H2A-H2B surface of H2AK119ub1 nucleosomes to stimulate methylation and partly override the inhibitory effect of active marks H3K4me3 and H3K36me3 (PMID:29348366, PMID:29499137, PMID:33479123). This nucleosomal engagement is the structural basis of a positive feedback loop in which PRC1-deposited H2Aub recruits JARID2-AEBP2-PRC2 to establish H3K27me3 domains, a relationship demonstrated in vitro and through in vivo epistasis at zebrafish zygotic genome activation (PMID:24837194, PMID:34982026, PMID:36610636). AEBP2 controls PRC2 genomic localization by binding the non-canonical SUZ12 C2 domain, where it competes with PHF19, disrupts the intrinsic PRC2 dimer, blocks C2-DNA contacts, and thereby regulates cooperative DNA looping and chromatin residence (PMID:29499137, PMID:29891558, PMID:31959557, PMID:32043141). AEBP2 exists as two developmentally regulated isoforms with opposing effects on PRC2: the embryo-specific short isoform stimulates DNA binding and de novo repression, while the broadly expressed long isoform inhibits PRC2 DNA binding and methyltransferase activity through a recently evolved, negatively charged N-terminal region (PMID:41168462). In vivo, Aebp2 is essential for embryogenesis and neural crest development, with knockouts co-occupying and regulating neural crest migration genes alongside PRC2 (PMID:21949878, PMID:27317809). AEBP2 is itself a substrate of SCF-β-TrCP-mediated ubiquitin-proteasomal degradation, and its abundance influences cisplatin sensitivity in cancer cells (PMID:31864706).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1999 High

    Established AEBP2 as a sequence-specific zinc-finger transcriptional repressor before any link to chromatin complexes was known, defining its DNA-binding and repressive activities.

    Evidence Reporter and Gal4-fusion repression assays with zinc-finger mutagenesis and recombinant DNA-binding assay at the aP2 promoter

    PMID:10329662

    Open questions at the time
    • No connection to PRC2 or chromatin modification yet
    • Physiological target genes not defined
  2. 2004 High

    Placed AEBP2 as a stimulatory cofactor of the PRC2 methyltransferase, distinguishing the minimal active core (EZH2-EED-SUZ12) from the optimal complex.

    Evidence In vitro HMTase reconstitution with defined subunit combinations

    PMID:15225548

    Open questions at the time
    • Mechanism of stimulation not resolved
    • Did not address genomic targeting
  3. 2009 Medium

    Connected AEBP2's DNA binding to PRC2 by showing a bipartite recognition motif, two developmental isoforms, and genomic co-occupancy with SUZ12, framing it as a candidate PRC2 targeting factor.

    Evidence DNA-binding assays, ChIP co-occupancy, isoform RT-PCR and Western blot

    PMID:19293275

    Open questions at the time
    • Targeting function inferred from co-occupancy, not causal recruitment
    • Functional difference between isoforms not yet defined
  4. 2011 High

    Demonstrated an essential in vivo role, with Aebp2 required for embryogenesis and neural crest development through co-regulation of migration genes with PRC2.

    Evidence Targeted mouse knockout with phenotypic analysis, ChIP, and expression profiling

    PMID:21949878

    Open questions at the time
    • Direct molecular mechanism linking AEBP2 loss to gene dysregulation unresolved
    • Isoform-specific contributions not separated
  5. 2012 High

    Provided the first structural placement of AEBP2 within PRC2, indicating a stabilizing and potentially allosteric position.

    Evidence Electron microscopy with cross-linking mass spectrometry and internal protein tagging

    PMID:23110252

    Open questions at the time
    • Resolution insufficient for atomic contacts
    • Nucleosome-bound state not captured
  6. 2014 High

    Defined a PRC1-PRC2 feedback loop in which H2Aub recruits JARID2-AEBP2-PRC2 to promote H3K27me3, and confirmed AEBP2 associates exclusively with PRC2 while defining mutually exclusive subcomplex composition; an unexpected Trithorax phenotype emerged from Aebp2 loss.

    Evidence Biochemical binding and HMTase assays on H2Aub nucleosomes; quantitative proteomics, IF/ChIP localization, ChIP-seq, and mouse mutants

    PMID:24837194 PMID:25451679 PMID:27317809

    Open questions at the time
    • Structural basis of ubiquitin reading not yet defined
    • Reconciling repressive cofactor role with Trithorax loss-of-function phenotype unresolved
  7. 2018 High

    Resolved the atomic architecture and competitive logic of AEBP2 within PRC2 — RBBP4 contact mimicking an unmodified H3 tail, competition with PHF19 for the SUZ12 C2 domain, definition of the PRC2.2 subcomplex, allosteric-independent stimulation, and a dominant contribution to chromatin residence.

    Evidence Cryo-EM and X-ray crystallography of holo-complexes, HMTase and nucleosome-binding assays, live-cell single-particle tracking with SUZ12 separation-of-function mutants

    PMID:29348366 PMID:29499137 PMID:29628311 PMID:29681498 PMID:29891558

    Open questions at the time
    • Isoform-specific structural differences not addressed
    • Quantitative balance of PRC2.1 vs PRC2.2 at individual loci unresolved
  8. 2020 High

    Mechanistically linked AEBP2's SUZ12 C2-domain binding to control of PRC2 dimerization, DNA looping, and CpG-island engagement, explaining how it tunes genomic localization.

    Evidence X-ray crystallography, in vitro DNA binding, ChIP-seq in mESCs, and single-molecule AFM/force spectroscopy with molecular dynamics

    PMID:31959557 PMID:32043141

    Open questions at the time
    • In vivo consequence of looping modulation at native loci not fully mapped
    • Interplay with isoform identity not tested
  9. 2021 High

    Captured AEBP2 bound to an H2AK119ub1 nucleosome, defining its ubiquitin and H2A-H2B contacts and a scaffolding role that, with JARID2, partly overrides inhibitory active marks; in vivo epistasis confirmed H2Aub1 acts upstream of Aebp2-PRC2.

    Evidence Cryo-EM and HMTase assays on modified nucleosomes; Rnf2 inhibition in zebrafish with ChIP-seq and RNA-seq; single-molecule force spectroscopy with simulation

    PMID:33479123 PMID:34057467 PMID:34982026

    Open questions at the time
    • Relative contribution of AEBP2 vs JARID2 ubiquitin reading not separated
    • Mammalian ZGA generalization untested
  10. 2023 High

    Showed H2A ubiquitination remodels H3-tail/DNA contacts and synergizes with linker DNA to enhance PRC2-AEBP2-JARID2 catalysis, providing the biophysical basis for activation.

    Evidence In vitro HMTase assays with defined nucleosomes and NMR/biophysical H3-tail dynamics measurements

    PMID:36610636

    Open questions at the time
    • Cellular relevance of linker-DNA contribution untested
    • Isoform dependence not examined
  11. 2025 High

    Resolved the long-standing isoform puzzle by demonstrating that the long isoform inhibits PRC2 via a recently evolved negatively charged N-terminal region while the short isoform stimulates DNA binding and de novo repression, and extended AEBP2 function to JARID2-independent PRC2.2 maintaining intergenic H3K27me2 in cancer.

    Evidence Cryo-EM, mutagenesis, HMTase and DNA-binding assays, ChIP-seq and ESC differentiation (peer-reviewed); triple-KO complementation and DLBCL CRISPR/ChIP-seq with drug sensitivity (preprints)

    PMID:41168462 PMID:bio_10.1101_2025.10.14.682307 PMID:bio_10.1101_2025.11.09.687442

    Open questions at the time
    • JARID2-independent PRC2.2 mechanism reported only in preprints
    • Physiological switch governing isoform choice undefined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How AEBP2 isoform selection is regulated developmentally and how the opposing isoforms are coordinated at specific loci to set H3K27me2 versus H3K27me3 boundaries remains open.
  • Upstream control of isoform expression unknown
  • Locus-level rules distinguishing AEBP2L inhibition from AEBP2S stimulation undefined
  • Link between AEBP2 degradation by SCF-β-TrCP and chromatin output not mechanistically established

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003677 DNA binding 4 GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3 GO:0042393 histone binding 2 GO:0140110 transcription regulator activity 2
Localization
GO:0005634 nucleus 2 GO:0000228 nuclear chromosome 1
Pathway
R-HSA-4839726 Chromatin organization 4 R-HSA-1266738 Developmental Biology 3 R-HSA-74160 Gene expression (Transcription) 3
Partners
EEDEZH2JARID2PHF19RBBP4SUZ12
Complex memberships
PRC2PRC2.2

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 AEBP2 is a zinc finger transcriptional repressor that binds to the AE-1 regulatory sequence in the aP2 gene promoter; the zinc finger motif plays a direct role in transcriptional repression (but not DNA binding), as mutation of a conserved histidine and flanking serine in the middle zinc finger abolished repression without affecting nuclear localization or DNA binding. Co-transfection reporter assay, Gal4-fusion repression assay, site-directed mutagenesis of zinc finger, recombinant protein DNA-binding assay The Journal of biological chemistry High 10329662
2004 AEBP2 is required for optimal (but not minimal) histone methyltransferase activity of the EED-EZH2-SUZ12 PRC2 complex; the minimum active complex requires EZH2, EED, and SUZ12, while AEBP2 enhances enzymatic activity above this baseline. In vitro histone methyltransferase (HMTase) reconstitution assay with defined subunit combinations Molecular cell High 15225548
2009 AEBP2 is an evolutionarily conserved zinc finger protein that binds DNA via a bipartite motif (CTT(N)15-23cagGCC), exists as two developmental-stage-specific isoforms (adult 51 kDa and embryo 32 kDa), and co-occupies genomic loci with SUZ12, functioning as a potential targeting factor for mammalian PRC2. DNA-binding assays, ChIP, promoter-GFP reporter, RT-PCR isoform characterization, Western blot Nucleic acids research Medium 19293275
2011 In developing mouse embryos, Aebp2 is expressed mainly in neural crest-derived cells; homozygous Aebp2 knockout is embryonic lethal, and heterozygotes display neural crest defects (enlarged colon, hypopigmentation). ChIP analyses showed that AEBP2 and PRC2 co-occupy promoters of genes involved in neural crest cell migration and development, and expression of these genes is altered in Aebp2 heterozygotes. Targeted mouse knockout, phenotypic analysis, ChIP, expression analysis PloS one High 21949878
2012 The first 3D electron microscopy structure of human PRC2 bound to cofactor AEBP2 revealed that AEBP2 stabilizes the complex and occupies a position suggesting an allosteric role in regulating gene silencing; cross-linking mass spectrometry and internal protein tagging localized all PRC2 subunits and mapped AEBP2 interactions within the assembly. Electron microscopy, cross-linking mass spectrometry, internal protein tagging eLife High 23110252
2014 Monoubiquitination of histone H2A by PRC1 (H2Aub) creates a binding site for Jarid2-Aebp2-containing PRC2, promoting H3K27 trimethylation on H2Aub nucleosomes; Jarid2, Aebp2, and H2Aub constitute a positive feedback loop establishing H3K27me3 chromatin domains. Biochemical binding assays, in vitro HMTase assay with H2Aub nucleosomes, mass spectrometry Nature structural & molecular biology High 24837194
2014 AEBP2 localizes specifically to PRC2 target loci including the inactive X chromosome; proteomic analysis confirmed AEBP2 associates exclusively with PRC2 complexes. In Aebp2 mutant ESCs, elevated H3K27 methylation at target loci was observed and atypical hybrid PRC2 subcomplexes assembled, suggesting AEBP2 normally defines mutually exclusive PRC2 subcomplex composition. Unexpectedly, homozygous Aebp2 mutant embryos display a Trithorax (anti-Polycomb) phenotype. Targeted mouse mutation, immunofluorescence/ChIP localization, quantitative proteomics (mass spectrometry), ChIP-seq H3K27me3 profiling Development (Cambridge, England) High 27317809
2014 The somatic (long, 52 kDa) isoform of AEBP2 acts as a transcriptional activator for Jarid2, Aebp2, and Snai2 target genes, whereas the embryonic (short, 32 kDa) isoform acts as a transcriptional repressor for Snai2; the somatic form also enhances cell migration. AEBP2 binds its own promoter and the promoters of Jarid2 and Snai2 as shown by ChIP. Reporter/transfection assays, ChIP, cell migration assay, RT-PCR isoform characterization Genomics Medium 25451679
2017 The AEBP2 subunit of PRC2 regulates preferential binding of PRC2 to methylated DNA (CpG-rich sequences); inclusion of AEBP2 in the PRC2 complex mediates this specificity for methylated DNA. In vitro binding assays with reconstituted PRC2 ± AEBP2, methylated vs. unmethylated DNA substrates Nature structural & molecular biology Medium 29058709
2018 Cryo-EM structures of human PRC2 with JARID2 and AEBP2 in basal and active states showed that AEBP2 interacts with the RBAP48 (RBBP4) subunit, mimicking an unmodified H3 tail. SUZ12 interacts with all other subunits; together these interactions define the complete architecture of the complex. Cryo-electron microscopy, cross-linking mass spectrometry Science (New York, N.Y.) High 29348366
2018 AEBP2 and PHF19 compete for binding to the non-canonical C2 domain of SUZ12; AEBP2 and JARID2 together enable nucleosome binding by the PRC2 complex. Crystal structures show that SUZ12 contains two structural platforms defining distinct PRC2 holo-complex classes. AEBP2 progressively blocks histone H3K4 binding to RBBP4 together with SUZ12. X-ray crystallography (crystal structures of heterotetrameric complexes), in vitro nucleosome binding assay Molecular cell High 29499137
2018 AEBP2 stimulates both PRC2-EZH1 and PRC2-EZH2 methyltransferase activity through a mechanism that is independent of and additive to allosteric activation (by H3K27me3), distinguishing AEBP2-mediated stimulation from the allosteric pathway. In vitro HMTase assay with defined subunit combinations, allosteric activator competition assays Molecular cell High 29681498
2018 AEBP2 and PCL homolog proteins make a major contribution to PRC2 chromatin binding in living human cells; SUZ12 separation-of-function mutants that cannot bind accessory proteins (including AEBP2) greatly reduce chromatin residence time of PRC2, as measured by single-particle tracking. CRISPR genome editing (HaloTag knock-in), single-particle tracking in live cells, SUZ12 separation-of-function mutants Genes & development High 29891558
2018 AEBP2 and JARID2 define the PRC2.2 subcomplex, which is mutually exclusive and antagonistic relative to the PRC2.1 subcomplex (containing PALI1/PCL proteins); the balance of PRC2.1 and PRC2.2 activities is required for appropriate regulation of polycomb target genes during differentiation. In vitro HMTase assay, co-immunoprecipitation, mouse genetic knockout, differentiation assays Molecular cell High 29628311
2019 AEBP2 contains a non-canonical phosphodegron and is targeted for ubiquitylation and proteasomal degradation by the SCF-β-TrCP E3 ubiquitin ligase complex; failure to degrade AEBP2 confers cisplatin resistance in ovarian cancer cells. Co-immunoprecipitation, ubiquitination assay, AEBP2 knockout cell lines, cisplatin sensitivity assay, phosphodegron mutagenesis Biochemical and biophysical research communications Medium 31864706
2020 AEBP2 binding to the C2 domain of SUZ12 disrupts the intrinsic PRC2 dimer (formed by domain swapping involving RBBP4 and the SUZ12 C2 domain), whereas MTF2/PHF19 stabilize the dimer; PRC2 dimerization enhances CpG island DNA binding, and loss of dimerization impairs H3K27me3 at developmental gene loci. X-ray crystallography, in vitro DNA binding assay, ChIP-seq in mouse ESCs Molecular cell High 31959557
2020 PRC2 (five-subunit complex including AEBP2) bends DNA approximately 3-fold locally and mediates DNA looping via multiple PRC2 molecules binding cooperatively; AEBP2 regulates loop formation, in part by associating with the C2 domain of SUZ12 and blocking its DNA contact. Atomic force microscopy (single-molecule, in liquid), single-molecule force spectroscopy, molecular dynamics simulation Nucleic acids research Medium 32043141
2021 Cryo-EM structure of PRC2 with JARID2 and AEBP2 bound to an H2AK119ub1-containing nucleosome revealed: JARID2 and AEBP2 each contact one ubiquitin moiety and the H2A-H2B surface; JARID2 stimulates PRC2 via interactions with EED and H2AK119-ubiquitin; AEBP2 has an additional scaffolding role. The presence of both cofactors partially overcomes the inhibitory effect of H3K4me3 and H3K36me3 on PRC2 activity. Cryo-electron microscopy, in vitro HMTase assay, cross-linking mass spectrometry Science (New York, N.Y.) High 33479123
2021 AEBP2 regulates cooperative DNA looping by multiple PRC2 complexes; the association of AEBP2 with the C2 domain of SUZ12 blocks C2-DNA contacts, providing a mechanism by which AEBP2 modulates PRC2 genomic localization. Single-molecule force spectroscopy, coarse-grained/atomistic molecular dynamics simulations, free energy calculations Nucleic acids research Medium 34057467
2022 In zebrafish embryos, H2Aub1 deposition by PRC1 (Rnf2) during pre-ZGA stages enables recruitment of Aebp2-containing PRC2 and subsequent H3K27me3 deposition during post-ZGA; inhibition of Rnf2 eliminates both Aebp2-PRC2 recruitment and H3K27me3, demonstrating that H2Aub1 is required upstream of Aebp2-PRC2 for gene silencing at ZGA. Rnf2 small-molecule inhibition in zebrafish embryos, ChIP-seq (H2Aub1, H3K27me3), RNA-seq, Aebp2-PRC2 co-localization eLife High 34982026
2023 H2A ubiquitination by PRC1 alters contacts between the H3 tail and DNA on nucleosomes, improving the methyltransferase activity of the PRC2-AEBP2-JARID2 complex; linker DNA is equally important as H2Aub for H3K27 methylation, and these effects synergize. In vitro HMTase assay with defined nucleosomes (±H2Aub, ±linker DNA), NMR/biophysical H3-tail dynamics measurements Journal of molecular biology High 36610636
2025 The broadly expressed long isoform of AEBP2 (AEBP2L) inhibits PRC2, while the short isoform (AEBP2S) promotes PRC2 activity. AEBP2L inhibits PRC2 DNA binding, histone methyltransferase activity, and binding to target genes; AEBP2S promotes PRC2 DNA-binding and is essential for de novo repression during naïve-to-primed pluripotency transition. Cryo-EM and mutagenesis identified the negatively charged N-terminal region of AEBP2L as the inhibitory element, which is a recently evolved vertebrate feature. Cryo-EM, mutagenesis, in vitro HMTase assay, in vitro DNA binding assay, ChIP-seq, ESC differentiation assays The EMBO journal High 41168462
2025 AEBP2 long isoform N-terminal DE-rich motif inhibits both EZH2 automethylation and H3K27 methylation; AEBP2 short isoform enhances PRC2 catalytic activity and H3K27me3 spreading; re-expression of AEBP2L (but not AEBP2S) in Mtf2/Jarid2/Aebp2 triple-knockout mESCs failed to restore H3K27me3 and caused defective differentiation. In vitro HMTase assay, triple-knockout mESC complementation, H3K27me3 ChIP, differentiation assay bioRxivpreprint Medium bio_10.1101_2025.11.09.687442
2025 In EZH2-mutant DLBCL, AEBP2 functions within a PRC2.2 complex lacking JARID2, using its zinc-finger domains to sample intergenic chromatin and sustain H3K27me2 (not H3K27me3-mediated gene silencing). Loss of AEBP2 reduces intergenic H3K27me2 and sensitizes cells to PRC2 inhibitors. CRISPR knockout, ChIP-seq (H3K27me2, H3K27me3), co-immunoprecipitation, functional drug sensitivity assays bioRxivpreprint Medium bio_10.1101_2025.10.14.682307

Source papers

Stage 0 corpus · 42 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Molecular cell 652 15225548
2014 Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression. Nature structural & molecular biology 357 24837194
2021 JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications. Science (New York, N.Y.) 197 33479123
2012 Molecular architecture of human polycomb repressive complex 2. eLife 194 23110252
2017 Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA. Nature structural & molecular biology 178 29058709
2018 Structures of human PRC2 with its cofactors AEBP2 and JARID2. Science (New York, N.Y.) 168 29348366
2009 AEBP2 as a potential targeting protein for Polycomb Repression Complex PRC2. Nucleic acids research 150 19293275
2018 A Family of Vertebrate-Specific Polycombs Encoded by the LCOR/LCORL Genes Balance PRC2 Subtype Activities. Molecular cell 128 29628311
2018 Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. Molecular cell 121 29499137
2018 Distinct Stimulatory Mechanisms Regulate the Catalytic Activity of Polycomb Repressive Complex 2. Molecular cell 109 29681498
2011 Frequent deletions of JARID2 in leukemic transformation of chronic myeloid malignancies. American journal of hematology 91 22190018
2016 Functional analysis of AEBP2, a PRC2 Polycomb protein, reveals a Trithorax phenotype in embryonic development and in ESCs. Development (Cambridge, England) 86 27317809
2014 Reciprocal interactions of human C10orf12 and C17orf96 with PRC2 revealed by BioTAP-XL cross-linking and affinity purification. Proceedings of the National Academy of Sciences of the United States of America 80 24550272
2020 A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island Chromatin. Molecular cell 74 31959557
2018 Live-cell imaging reveals the dynamics of PRC2 and recruitment to chromatin by SUZ12-associated subunits. Genes & development 70 29891558
2014 Role of PRC2-associated factors in stem cells and disease. The FEBS journal 70 25271128
2012 Recruitment and biological consequences of histone modification of H3K27me3 and H3K9me3. ILAR journal 68 23744963
2019 Polycomb repressive 2 complex-Molecular mechanisms of function. Protein science : a publication of the Protein Society 64 31095801
2011 Aebp2 as an epigenetic regulator for neural crest cells. PloS one 45 21949878
1999 Cloning and characterization of a novel zinc finger transcriptional repressor. A direct role of the zinc finger motif in repression. The Journal of biological chemistry 45 10329662
2001 Jing: a downstream target of slbo required for developmental control of border cell migration. Development (Cambridge, England) 39 11152631
2022 The Role of Polycomb Proteins in Cell Lineage Commitment and Embryonic Development. Epigenomes 34 35997369
2022 Establishment of developmental gene silencing by ordered polycomb complex recruitment in early zebrafish embryos. eLife 32 34982026
2021 Cooperative DNA looping by PRC2 complexes. Nucleic acids research 25 34057467
2021 Genome-wide gene-air pollution interaction analysis of lung function in 300,000 individuals. Environment international 25 34923368
2019 β-TRCP-mediated AEBP2 ubiquitination and destruction controls cisplatin resistance in ovarian cancer. Biochemical and biophysical research communications 24 31864706
2023 Oncogenic miR-93-5p/Gal-9 axis drives CD8 (+) T-cell inactivation and is a therapeutic target for hepatocellular carcinoma immunotherapy. Cancer letters 18 37105392
2002 The jing Zn-finger transcription factor is a mediator of cellular differentiation in the Drosophila CNS midline and trachea. Development (Cambridge, England) 18 12015288
2021 SUMO pathway, blood coagulation and oxidative stress in SARS-CoV-2 infection. Biochemistry and biophysics reports 17 33558851
2014 AEBP2 as a transcriptional activator and its role in cell migration. Genomics 17 25451679
2023 H2A Ubiquitination Alters H3-tail Dynamics on Linker-DNA to Enhance H3K27 Methylation. Journal of molecular biology 15 36610636
2020 Bending and looping of long DNA by Polycomb repressive complex 2 revealed by AFM imaging in liquid. Nucleic acids research 15 32043141
2014 Profiling of embryonic stem cell differentiation. The review of diabetic studies : RDS 14 25148369
2021 Three genes associated with anterior and posterior cruciate ligament injury : a genome-wide association analysis. Bone & joint open 11 34169730
2016 The genetic landscape of paediatric de novo acute myeloid leukaemia as defined by single nucleotide polymorphism array and exon sequencing of 100 candidate genes. British journal of haematology 11 27022003
2021 AC092127.1-miR-451a-AE binding protein 2 Signaling Facilitates Malignant Properties of Breast Cancer. Journal of breast cancer 5 34352938
2024 A preliminary study unveils CISD2 as a ferroptosis-related therapeutic target for recurrent spontaneous abortion through immunological analysis and two-sample mendelian randomization. Journal of reproductive immunology 4 38678819
2024 Exploring the role of ferroptosis-related genes as biomarkers in acute kidney injury. PloS one 3 39042632
2025 Development and Validation of a Diagnostic Model for AKI Based on the Analysis of Ferroptosis-related Genes. Current medicinal chemistry 1 39572917
2025 Integrated miRNA-mRNA Analyses of Triple-Negative Breast Cancer in Black and White Patients with or Without Obesity. International journal of molecular sciences 0 41009685
2025 Auto-inhibition of PRC2 by the broadly expressed long isoform of AEBP2. The EMBO journal 0 41168462
2015 Retrotransposon-derived promoter of Mammalian Aebp2. PloS one 0 25915901

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