ArticleStructure (London, England : 1993)2013
Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
72 citing papers in PubMed, 118 citations in OpenAlex.
- More than SAM: mechanisms of action of the Polycomb group protein polyhomeotic.Nucleus (Austin, Tex.) · 2026Review
- PCGF1 Promotes the Tumorigenesis of Malignancies Through Upregulating CCDC34 in Glioma.Annals of clinical and translational neurology · 2026Article
- Cryo-EM structure, enzymatic activity and genome targeting of canonical PRC1.Nature structural & molecular biology · 2026Article
- Inhibition of USP7 Destabilizes the Noncanonical PRC1.1 Complex and Induces Neuroblastoma Differentiation.Molecular cancer research : MCR · 2026Article
- Epigenetic corepressor BCORL1 predominates as a driver of clonal hematopoiesis of indeterminate potential in patients undergoing chronic hemodialysis: a multicenter cohort study.Human genomics · 2026Article
- Genetic analysis and clinical characteristics of sporadic and familial congenital cataracts in southern Chinese families.Frontiers in genetics · 2026Article
- Analysis of a BCOR internal tandem duplication in mouse embryonic stem cell to neuronal precursor differentiation.Genetics · 2025Article
- CNS Tumor with BCOR/BCORL1 Fusion: A Rare Tumor Entity.International journal of molecular sciences · 2025Article
- DNA demethylating agents suppress preclinical models of synovial sarcoma.The Journal of clinical investigation · 2025Article
- Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes.Science advances · 2025Article
- Targeted disruption of PRC1.1 complex enhances bone remodeling.Nature communications · 2025Article
- Unravelling the impact of the chromobox proteins in human cancers.Cell death & disease · 2025Review
- Paediatric renal tumours: an update on challenges and recent developments.Virchows Archiv : an international journal of pathology · 2025Review
- PRC1 Protein Subcomplexes Architecture: Focus on the Interplay between Distinct PCGF Subunits in Protein Interaction Networks.International journal of molecular sciences · 2024Article
- Genomic context- and H2AK119 ubiquitination-dependent inheritance of human Polycomb silencing.Science advances · 2024Article
- BCOR::CREBBP fusion in malignant neuroepithelial tumor of CNS expands the spectrum of methylation class CNS tumor with BCOR/BCOR(L1)-fusion.Acta neuropathologica communications · 2024Review
- H2A monoubiquitination: insights from human genetics and animal models.Human genetics · 2024Review
- Article
- Non-synonymous, synonymous, and non-coding nucleotide variants contribute to recurrently altered biological processes during retinoblastoma progression.Genes, chromosomes & cancer · 2023Article
- Targeting Menin disrupts the KMT2A/B and polycomb balance to paradoxically activate bivalent genes.Nature cell biology · 2023Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Polycomb-group RING finger homologs (PCGF1, PCGF2, PCGF3, PCGF4, PCGF5, and PCGF6) are critical components in the assembly of distinct Polycomb repression complex 1 (PRC1)-related complexes. Here, we identify a protein interaction domain in BCL6 corepressor, BCOR, which binds the RING finger- and WD40-associated ubiquitin-like (RAWUL) domain of PCGF1 (NSPC1) and PCGF3 but not of PCGF2 (MEL18) or PCGF4 (BMI1). Because of the selective binding, we have named this domain PCGF Ub-like fold discriminator (PUFD). The structure of BCOR PUFD bound to PCGF1 reveals that (1) PUFD binds to the same surfaces as observed for a different Polycomb group RAWUL domain and (2) the ability of PUFD to discriminate among RAWULs stems from the identity of specific residues within these interaction surfaces. These data show the molecular basis for determining the binding preference for a PCGF homolog, which ultimately helps determine the identity of the larger PRC1-like assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.