ArticleThe Journal of biological chemistry2014
Insight into the architecture of the NuRD complex: structure of the RbAp48-MTA1 subcomplex.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
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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Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 83 citations in OpenAlex.
- The potential role of PHF6 as an oncogene: a genotranscriptomic/proteomic meta-analysis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Pooled it
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- Multicomplex Integrative Structural Modeling of a Human Histone Deacetylase Interactome.bioRxiv : the preprint server for biology · 2026Article
- Proteome-wide model for human disease genetics.Nature genetics · 2025Article
- The dual guardians of cellular stability: exploring nesprin and lamin in senescence.Cell death & disease · 2025Review
- SMARCB1-driven EGFR-GLI1 epigenetic alterations in lung cancer progression and therapy are differentially modulated by MEOX2 and GLI-1.Cancer gene therapy · 2025Article
- Systemic identification and characterization of the conserved core NuRD complex in planarian.Frontiers in aging · 2025Article
- Analysis of the complex between MBD2 and the histone deacetylase core of NuRD reveals key interactions critical for gene silencing.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Caf1 regulates the histone methyltransferase activity of Ash1 by sensing unmodified histone H3.Epigenetics & chromatin · 2023Article
- Two assembly modes for SIN3 histone deacetylase complexes.Cell discovery · 2023Article
- Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination.Protein science : a publication of the Protein Society · 2022Article
- Rbbp4 loss disrupts neural progenitor cell cycle regulation independent of Rb and leads to Tp53 acetylation and apoptosis.Developmental dynamics : an official publication of the American Association of Anatomists · 2022Article
- Chromatin remodelling complexes in cerebral cortex development and neurodevelopmental disorders.Neurochemistry international · 2021Article
- Structural insights into the recognition of histone H3Q5 serotonylation by WDR5.Science advances · 2021Article
- Structure Based Design of Bicyclic Peptide Inhibitors of RbAp48.Angewandte Chemie (International ed. in English) · 2021Article
- The topology of chromatin-binding domains in the NuRD deacetylase complex.Nucleic acids research · 2020Article
- The Nucleosome Remodeling and Deacetylase Complex Has an Asymmetric, Dynamic, and Modular Architecture.Cell reports · 2020Article
- NuRD mediates mitochondrial stress-induced longevity via chromatin remodeling in response to acetyl-CoA level.Science advances · 2020Article
- Metastasis-associated protein 1 promotes epithelial-mesenchymal transition in idiopathic pulmonary fibrosis by up-regulating Snail expression.Journal of cellular and molecular medicine · 2020Article
- The multifaceted histone chaperone RbAp46/48 in Plasmodium falciparum: structural insights, production, and characterization.Parasitology research · 2020Article
Corrections and comments
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Authors and funding
18 authors at 4 institutions in 3 countries.
Funding
Abstract
The nucleosome remodeling and deacetylase (NuRD) complex is a widely conserved transcriptional co-regulator that harbors both nucleosome remodeling and histone deacetylase activities. It plays a critical role in the early stages of ES cell differentiation and the reprogramming of somatic to induced pluripotent stem cells. Abnormalities in several NuRD proteins are associated with cancer and aging. We have investigated the architecture of NuRD by determining the structure of a subcomplex comprising RbAp48 and MTA1. Surprisingly, RbAp48 recognizes MTA1 using the same site that it uses to bind histone H4, showing that assembly into NuRD modulates RbAp46/48 interactions with histones. Taken together with other results, our data show that the MTA proteins act as scaffolds for NuRD complex assembly. We further show that the RbAp48-MTA1 interaction is essential for the in vivo integration of RbAp46/48 into the NuRD complex.
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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.