Component

Microsomal ethanol-oxidising activity

Microsomal ethanol-oxidising activity. Species, exposure and limitations are retained in each linked claim.

1 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.

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.

Recorded relationships

Where it participates (unsigned role)

  1. Ethanol induces CYP2E1 by protein stabilisation, slowing the ubiquitin-conjugation-dependent rapid degradation of the enzyme rather than raising its synthesis.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/alcohol-research/8530344.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689", "start_char": 0, "end_char": 909, "text_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689"}
    experimental_model
    Ethanol treatment with ubiquitin conjugation and degradation assays
    exposure
    Ethanol exposure with measurement of CYP2E1 turnover
    limitations
    A protein-turnover mechanism rather than a transcriptional one. It explains why the second oxidation route appears quickly without new transcription.
    nutrient_topic
    Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol
    organism
    Rat and cell systems
    plain_language
    Alcohol does not make more of this enzyme; it stops the cell destroying it.
    primary_references
    [alcohol-p8530344] Ethanol induces CYP2E1 by protein stabilization. Role of ubiquitin conjugation in the rapid degradation of CYP2E1. (1995). https://pubmed.ncbi.nlm.nih.gov/8530344/ DOI: 10.1074/jbc.270.50.29632
    tissue_or_cell_type
    Hepatic microsomes

    Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 137–148

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ethanol treatment with ubiquitin conjugation and degradation assays · source_derived_draft · unverified_draft

    ### alcohol-cyp2e1-stabilisation Ethanol induces CYP2E1 by protein stabilisation, slowing the ubiquitin-conjugation-dependent rapid degradation of the enzyme rather than raising its synthesis. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol does not make more of this enzyme; it stops the cell destroying it. organism: Rat and cell systems tissue_or_cell_type: Hepatic microsomes experimental_model: Ethanol treatment with ubiquitin conjugation and degradation assays limitations: A protein-turnover mechanism rather than a transcriptional one. It explains why the second oxidation route appears quickly without new transcription. exposure: Ethanol exposure with measurement of CYP2E1 turnover evidence_span: {"source_cache": "artifacts/alcohol-research/8530344.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689", "start_char": 0, "end_char": 909, "text_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689"} [alcohol-p8530344] Ethanol induces CYP2E1 by protein stabilization. Role of ubiquitin conjugation in the rapid degradation of CYP2E1. (1995). https://pubmed.ncbi.nlm.nih.gov/8530344/ DOI: 10.1074/jbc.270.50.29632
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards