Component

Borrelidin

Context-specific entity; species, compartment and exposure are stated on each 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

What it acts on

  1. Borrelidin-class inhibitor toxicity was linked to competition with threonine at TARS, provoking amino-acid-starvation responses and apoptosis in the studied systems.

    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Enzyme biochemistry, structures, cellular assays and zebrafish work.
    limitations
    Anti-angiogenic action could be separated from toxicity with selected derivatives; these are experimental agents, not routine nutrient interactions.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    Blocking amino-acid processing can mimic inadequate supply inside a cell.
    primary_references
    Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26271225/ · DOI 10.1038/srep13160

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 394–400

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Enzyme biochemistry, structures, cellular assays and zebrafish work. · source_derived_draft · unverified_draft

    ## l-threonine-borrelidin-competition Blocking amino-acid processing can mimic inadequate supply inside a cell. Borrelidin-class inhibitor toxicity was linked to competition with threonine at TARS, provoking amino-acid-starvation responses and apoptosis in the studied systems. Model: Enzyme biochemistry, structures, cellular assays and zebrafish work. Limitations: Anti-angiogenic action could be separated from toxicity with selected derivatives; these are experimental agents, not routine nutrient interactions. Evidence access: Primary abstract Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26271225/ · DOI 10.1038/srep13160
    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