Component
Class I histone deacetylase activity
Context-specific entity; species, compartment and exposure are stated on each claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
The later study detected no HDAC inhibition with 10 mM sodium R-BHB in its nuclear-extract assay; multiple cell models lacked histone hyperacetylation up to 40 mM.
Experimental context and source evidence
- evidence_access
- Primary abstract and indexed full-text Figure 2/Discussion, PMC6346118
- experimental_model
- Nuclear-extract assay and HEK293, HMEC-1, rat and human myotube experiments.
- limitations
- Different preparations/readouts may matter; the discrepancy is unresolved. Concentrations are experimental, not target blood levels.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- Another study did not reproduce the proposed direct effect.
- primary_references
- Prominent action of butyrate over β-hydroxybutyrate as histone deacetylase inhibitor, transcriptional modulator and anti-inflammatory molecule. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30679586/ · DOI 10.1038/s41598-018-36941-9
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 400–406
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Nuclear-extract assay and HEK293, HMEC-1, rat and human myotube experiments. · source_derived_draft · unverified_draft
## fast-hdac-negative Another study did not reproduce the proposed direct effect. The later study detected no HDAC inhibition with 10 mM sodium R-BHB in its nuclear-extract assay; multiple cell models lacked histone hyperacetylation up to 40 mM. Model: Nuclear-extract assay and HEK293, HMEC-1, rat and human myotube experiments. Limitations: Different preparations/readouts may matter; the discrepancy is unresolved. Concentrations are experimental, not target blood levels. Evidence access: Primary abstract and indexed full-text Figure 2/Discussion, PMC6346118 Prominent action of butyrate over β-hydroxybutyrate as histone deacetylase inhibitor, transcriptional modulator and anti-inflammatory molecule. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30679586/ · DOI 10.1038/s41598-018-36941-9
Complete structured claim and evidenceThe study reported direct class-I HDAC inhibition by D-beta-hydroxybutyrate, alongside increased histone acetylation in mouse tissues.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Biochemical/cellular experiments; mouse fasting, calorie restriction or exogenous BHB.
- limitations
- Later direct testing challenged HDAC inhibition; see the linked research disagreement.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- One study proposed a direct route from ketones to gene regulation.
- primary_references
- Suppression of oxidative stress by β-hydroxybutyrate, an endogenous histone deacetylase inhibitor. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23223453/ · DOI 10.1126/science.1227166
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 392–398
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Biochemical/cellular experiments; mouse fasting, calorie restriction or exogenous BHB. · source_derived_draft · unverified_draft
## fast-hdac-positive One study proposed a direct route from ketones to gene regulation. The study reported direct class-I HDAC inhibition by D-beta-hydroxybutyrate, alongside increased histone acetylation in mouse tissues. Model: Biochemical/cellular experiments; mouse fasting, calorie restriction or exogenous BHB. Limitations: Later direct testing challenged HDAC inhibition; see the linked research disagreement. Evidence access: Primary abstract Suppression of oxidative stress by β-hydroxybutyrate, an endogenous histone deacetylase inhibitor. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23223453/ · DOI 10.1126/science.1227166
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.