Component

Adenosine

Study-scoped entity; inspect species, exposure, model and limitations on each claim.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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. ADK variants impaired recombinant enzyme activity and were linked to increased adenosine excretion and SAM/SAH/methionine accumulation.

    Human adenosine kinase / ADK → Adenosine removal coupled to the human methionine cycle source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Six affected individuals from three families; exome sequencing and recombinant variant assays.
    limitations
    A functional block of SAH hydrolysis from adenosine accumulation is the mechanistic interpretation; this is not primary AHCY deficiency.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Removing one reaction product helps keep the recycling pathway moving.
    primary_references
    Adenosine kinase deficiency disrupts the methionine cycle and causes hypermethioninemia, encephalopathy, and abnormal liver function. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21963049/ · DOI 10.1016/j.ajhg.2011.09.004
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 196–202

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Six affected individuals from three families; exome sequencing and recombinant variant assays. · source_derived_draft · unverified_draft

    ## methionine-adk-product-removal Removing one reaction product helps keep the recycling pathway moving. ADK variants impaired recombinant enzyme activity and were linked to increased adenosine excretion and SAM/SAH/methionine accumulation. Model: Six affected individuals from three families; exome sequencing and recombinant variant assays. Limitations: A functional block of SAH hydrolysis from adenosine accumulation is the mechanistic interpretation; this is not primary AHCY deficiency. Evidence access: Primary abstract Adenosine kinase deficiency disrupts the methionine cycle and causes hypermethioninemia, encephalopathy, and abnormal liver function. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21963049/ · DOI 10.1016/j.ajhg.2011.09.004
    Complete structured claim and evidence

  2. AHCY catalyzes reversible conversion between SAH and adenosine plus homocysteine; product clearance favors net SAH removal.

    Human adenosylhomocysteinase / AHCY → S-Adenosyl-L-homocysteine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Established reaction in the human AHCY-deficiency investigation.
    limitations
    Reaction equilibrium and cellular product removal matter; plasma concentrations do not uniquely define tissue flux.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    After methyl transfer, the spent donor must be processed.
    primary_references
    S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15024124/ · DOI 10.1073/pnas.0400658101

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 172–178

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Established reaction in the human AHCY-deficiency investigation. · source_derived_draft · unverified_draft

    ## methionine-ahcy-reaction After methyl transfer, the spent donor must be processed. AHCY catalyzes reversible conversion between SAH and adenosine plus homocysteine; product clearance favors net SAH removal. Model: Established reaction in the human AHCY-deficiency investigation. Limitations: Reaction equilibrium and cellular product removal matter; plasma concentrations do not uniquely define tissue flux. Evidence access: Primary abstract S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. · 2004 · https://pubmed.ncbi.nlm.nih.gov/15024124/ · DOI 10.1073/pnas.0400658101
    Complete structured claim and evidence

  3. Crystallography resolved caffeine in a thermostabilized A2A receptor with an inactive-state conformation.

    Caffeine → Thermostabilized human A2A receptor crystallography construct source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Engineered human receptor construct; crystallographic comparison with XAC and ZM241385.
    limitations
    Engineered inactive-state structure, not a measurement of native receptor signaling in a person.
    nutrient_topic
    Caffeine collection; salts, coffee, species and coexposure contexts retain their identities. · Caffeine
    plain_language
    A receptor structure shows where caffeine binds.
    primary_references
    Structure of the adenosine A(2A) receptor in complex with ZM241385 and the xanthines XAC and caffeine. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21885291/ · DOI 10.1016/j.str.2011.06.014

    Caffeine: receptors, metabolism, nutrient interactions, adaptation and discovery questions (2026-09-18) · lines 28–34

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Engineered human receptor construct; crystallographic comparison with XAC and ZM241385. · source_derived_draft · unverified_draft

    ## caf-a2a-structure A receptor structure shows where caffeine binds. Crystallography resolved caffeine in a thermostabilized A2A receptor with an inactive-state conformation. Model: Engineered human receptor construct; crystallographic comparison with XAC and ZM241385. Limitations: Engineered inactive-state structure, not a measurement of native receptor signaling in a person. Evidence access: Primary abstract Structure of the adenosine A(2A) receptor in complex with ZM241385 and the xanthines XAC and caffeine. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21885291/ · DOI 10.1016/j.str.2011.06.014
    Complete structured claim and evidence

  4. Ethanol increased extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter.

    Ethanol → Cellular adenosine uptake by the nucleoside transporter source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/alcohol-research/2298733.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3933013c774b52112ebb838291e240d625dbf664faa2e94db35204bc38fb73d9", "start_char": 0, "end_char": 1419, "text_sha256": "3933013c774b52112ebb838291e240d625dbf664faa2e94db35204bc38fb73d9"}
    experimental_model
    Nucleoside transport and adenosine measurement in cultured cells during ethanol exposure
    exposure
    Ethanol exposure with adenosine uptake measurement
    limitations
    A transport mechanism for an indirect target: the effect is on adenosine handling, not on a receptor. Cultured cells.
    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
    Cultured cells
    plain_language
    Alcohol raises a natural sedative by blocking its reuptake.
    primary_references
    [alcohol-p2298733] Ethanol increases extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter. (1990). https://pubmed.ncbi.nlm.nih.gov/2298733/ DOI: 10.1016/s0021-9258(19)39923-5
    tissue_or_cell_type
    Nucleoside transporter

    Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 410–421

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Nucleoside transport and adenosine measurement in cultured cells during ethanol exposure · source_derived_draft · unverified_draft

    ### alcohol-ent1-inhibition Ethanol increased extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter. 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 raises a natural sedative by blocking its reuptake. organism: Cultured cells tissue_or_cell_type: Nucleoside transporter experimental_model: Nucleoside transport and adenosine measurement in cultured cells during ethanol exposure limitations: A transport mechanism for an indirect target: the effect is on adenosine handling, not on a receptor. Cultured cells. exposure: Ethanol exposure with adenosine uptake measurement evidence_span: {"source_cache": "artifacts/alcohol-research/2298733.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3933013c774b52112ebb838291e240d625dbf664faa2e94db35204bc38fb73d9", "start_char": 0, "end_char": 1419, "text_sha256": "3933013c774b52112ebb838291e240d625dbf664faa2e94db35204bc38fb73d9"} [alcohol-p2298733] Ethanol increases extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter. (1990). https://pubmed.ncbi.nlm.nih.gov/2298733/ DOI: 10.1016/s0021-9258(19)39923-5
    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.

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