Component
Human histone deacetylase 1
Human histone deacetylase 1. Species, exposure and limitations are retained in each linked 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
DIM promoted proteasomal depletion of HDAC1 in the colon-cancer study.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/dim-research/20068155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bbb7efbd817b44da2771c9dac2c27d0bf4fe3db97ad9452a93eefc97319ebab9", "start_char": 0, "end_char": 862, "text_sha256": "bbb7efbd817b44da2771c9dac2c27d0bf4fe3db97ad9452a93eefc97319ebab9"}
- experimental_model
- Protein degradation and cell-cycle studies
- exposure
- DIM; proteasome-mediated protein depletion
- limitations
- Preclinical concentration/model dependence. The mechanism is loss of HDAC protein, not established direct inhibition of every HDAC catalytic site.
- nutrient_topic
- Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
- organism
- Human colon-cancer cells and xenografts
- plain_language
- This mechanism removes an epigenetic regulatory protein rather than merely blocking its active site.
- primary_references
- [dim-p20068155] Chemopreventive agent 3,3'-diindolylmethane selectively induces proteasomal degradation of class I histone deacetylases. (2010). https://pubmed.ncbi.nlm.nih.gov/20068155/ DOI: 10.1158/0008-5472.can-09-1924
- tissue_or_cell_type
- Class I HDAC regulation
Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 1364–1375
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein degradation and cell-cycle studies · source_derived_draft · unverified_draft
### dim-hdac-hdac1 DIM promoted proteasomal depletion of HDAC1 in the colon-cancer study. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: This mechanism removes an epigenetic regulatory protein rather than merely blocking its active site. organism: Human colon-cancer cells and xenografts tissue_or_cell_type: Class I HDAC regulation experimental_model: Protein degradation and cell-cycle studies limitations: Preclinical concentration/model dependence. The mechanism is loss of HDAC protein, not established direct inhibition of every HDAC catalytic site. exposure: DIM; proteasome-mediated protein depletion evidence_span: {"source_cache": "artifacts/dim-research/20068155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bbb7efbd817b44da2771c9dac2c27d0bf4fe3db97ad9452a93eefc97319ebab9", "start_char": 0, "end_char": 862, "text_sha256": "bbb7efbd817b44da2771c9dac2c27d0bf4fe3db97ad9452a93eefc97319ebab9"} [dim-p20068155] Chemopreventive agent 3,3'-diindolylmethane selectively induces proteasomal degradation of class I histone deacetylases. (2010). https://pubmed.ncbi.nlm.nih.gov/20068155/ DOI: 10.1158/0008-5472.can-09-1924
Complete structured claim and evidence
Where it participates (unsigned role)
Butyrate inhibited histone decrotonylation in the study linking class-I HDAC activity to crotonylation; separate mouse microbiota depletion altered colonic crotonyl marks.
Experimental context and source evidence
- evidence_access
- Primary abstract and full-text HCT116/HDAC assay results
- experimental_model
- Human cell/biochemical assays and separately analyzed mouse colon.
- limitations
- Crotonylation is a distinct modification from acetylation, butyrylation and beta-hydroxybutyrylation.
- nutrient_topic
- Butyrate collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Butyrate
- plain_language
- Its epigenetic effects extended beyond acetylation.
- primary_references
- Microbiota derived short chain fatty acids promote histone crotonylation in the colon through histone deacetylases. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29317660/ · DOI 10.1038/s41467-017-02651-5
Butyrate: microbial production, fuel use, signaling and nutrient interactions (2026-09-19) · lines 302–308
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human cell/biochemical assays and separately analyzed mouse colon. · source_derived_draft · unverified_draft
## butyrate-decrotonylation Its epigenetic effects extended beyond acetylation. Butyrate inhibited histone decrotonylation in the study linking class-I HDAC activity to crotonylation; separate mouse microbiota depletion altered colonic crotonyl marks. Model: Human cell/biochemical assays and separately analyzed mouse colon. Limitations: Crotonylation is a distinct modification from acetylation, butyrylation and beta-hydroxybutyrylation. Evidence access: Primary abstract and full-text HCT116/HDAC assay results Microbiota derived short chain fatty acids promote histone crotonylation in the colon through histone deacetylases. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29317660/ · DOI 10.1038/s41467-017-02651-5
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.