ArticleNature communications2016
Insights into the activation mechanism of class I HDAC complexes by inositol phosphates.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
124 citing papers in PubMed, 1 synthesis or guideline pooled it, 245 citations in OpenAlex.
- Prognostic and clinical significance of metastasis-associated gene 1 overexpression in solid cancers: A meta-analysis.Medicine · 2018Pooled it
- Phosphoinositides and inositol phosphates as molecular glues.FEBS letters · 2026Review
- Design, Synthesis, and Antitumor Activities of Novel Coumarin-Based Histone Deacetylase Inhibitors.Biomolecules · 2026Article
- Multivalent interactions mediate SNAIL transcription factor stimulation of the nucleosome deacetylase activity of the CoREST complex.Nucleic acids research · 2026Article
- Cellular Target Engagement and Dissociation Kinetics of Class I-Selective Histone Deacetylase (HDAC) Inhibitors.International journal of molecular sciences · 2026Article
- Recommended Tool Compounds: Isoform- and Class-Specific Histone Deacetylase Inhibitors.ACS pharmacology & translational science · 2026Review
- The intracellular inositol (pyro)phosphate receptor AtSPX1 reciprocally binds to P1BS DNA.Nature communications · 2026Article
- Phytic acid (InsPNature communications · 2026Article
- Microbiota-driven epigenetic programming of local immunity.Frontiers in immunology · 2026Review
- Versatile roles of inositol hexakisphosphate in the ubiquitin-proteasome system.Essays in biochemistry · 2025Review
- Structure-based design of anticancer drugs based on β-elemene: Research foundations and development potential.Journal of pharmaceutical analysis · 2025Review
- The Allosteric Regulator Inositol Phosphate Dramatically Affects the Efficacy and Selectivity of Inhibitors for Different HDAC Complexes.Journal of the American Chemical Society · 2025Article
- Mutations on the surface of HDAC1 reveal molecular determinants of specific complex assembly and their requirement for gene regulation.Nucleic acids research · 2025Article
- Article
- Hispidulin: a potential alternative to vorinostat against HDAC1 for acute myeloid leukemia.Discover oncology · 2025Article
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- New potent N-hydroxycinnamamide-based histone deacetylase inhibitors suppress proliferation and trigger apoptosis in THP-1 leukaemia cells.Archiv der Pharmazie · 2025Article
- Article
- Article
- Towards Improved Bioavailability of Cereal Inositol Phosphates,Molecules (Basel, Switzerland) · 2025Review
64 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 3 institutions in 1 country.
Funding
Abstract
Histone deacetylases (HDACs) 1, 2 and 3 form the catalytic subunit of several large transcriptional repression complexes. Unexpectedly, the enzymatic activity of HDACs in these complexes has been shown to be regulated by inositol phosphates, which bind in a pocket sandwiched between the HDAC and co-repressor proteins. However, the actual mechanism of activation remains poorly understood. Here we have elucidated the stereochemical requirements for binding and activation by inositol phosphates, demonstrating that activation requires three adjacent phosphate groups and that other positions on the inositol ring can tolerate bulky substituents. We also demonstrate that there is allosteric communication between the inositol-binding site and the active site. The crystal structure of the HDAC1:MTA1 complex bound to a novel peptide-based inhibitor and to inositol hexaphosphate suggests a molecular basis of substrate recognition, and an entropically driven allosteric mechanism of activation.
Indexed as
Identifiers
What OpenQuestion holds
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.