Component

Mouse eIF2α / Eif2s1

Mouse eIF2α / Eif2s1. Species, exposure and limitations are retained in each linked claim.

3 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

What acts on it

  1. Boric acid induced eIF2α Ser51 phosphorylation in wild-type mouse fibroblasts at one hour, but not in Perk-null cells tested for up to six hours.

    Mouse PERK / Eif2ak3 → Mouse eIF2α / Eif2s1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/boron-research/30196486.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e220df5fb0f9b8653035f7a144259ce66778467a7a72acbf7cd7d113f8b6030a", "start_char": 0, "end_char": 2006, "text_sha256": "e220df5fb0f9b8653035f7a144259ce66778467a7a72acbf7cd7d113f8b6030a"}
    experimental_model
    PERK knockout comparison, immunofluorescence and quantitative PCR
    exposure
    10 µM boric acid; 1–6 hour comparisons
    limitations
    Knockout dependence in mouse fibroblasts is separate from human tumor-cell transcription. Increased GCLC mRNA is not a measured increase in glutathione synthesis or clinical antioxidant benefit.
    nutrient_topic
    Boron research collection; topical membership is not evidence of a direct dietary effect. · Boron
    organism
    Mouse embryonic fibroblasts and human DU-145 cells
    plain_language
    Removing PERK blocked this step of the boric-acid response.
    primary_references
    [boron-p30196486] Boric Acid Activation of eIF2α and Nrf2 Is PERK Dependent: a Mechanism that Explains How Boron Prevents DNA Damage and Enhances Antioxidant Status. (2019). https://pubmed.ncbi.nlm.nih.gov/30196486/ DOI: 10.1007/s12011-018-1498-4
    tissue_or_cell_type
    Cell culture
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Boron: chemistry, nutrient interactions, low-intake studies and mechanistic uncertainties (2026-09-17) · lines 495–506

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · PERK knockout comparison, immunofluorescence and quantitative PCR · source_derived_draft · unverified_draft

    ### boron-perk-eif2alpha-dependence Boric acid induced eIF2α Ser51 phosphorylation in wild-type mouse fibroblasts at one hour, but not in Perk-null cells tested for up to six hours. Condition category: machinery_impairment nutrient_topic: Boron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing PERK blocked this step of the boric-acid response. organism: Mouse embryonic fibroblasts and human DU-145 cells tissue_or_cell_type: Cell culture experimental_model: PERK knockout comparison, immunofluorescence and quantitative PCR limitations: Knockout dependence in mouse fibroblasts is separate from human tumor-cell transcription. Increased GCLC mRNA is not a measured increase in glutathione synthesis or clinical antioxidant benefit. exposure: 10 µM boric acid; 1–6 hour comparisons evidence_span: {"source_cache": "artifacts/boron-research/30196486.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e220df5fb0f9b8653035f7a144259ce66778467a7a72acbf7cd7d113f8b6030a", "start_char": 0, "end_char": 2006, "text_sha256": "e220df5fb0f9b8653035f7a144259ce66778467a7a72acbf7cd7d113f8b6030a"} [boron-p30196486] Boric Acid Activation of eIF2α and Nrf2 Is PERK Dependent: a Mechanism that Explains How Boron Prevents DNA Damage and Enhances Antioxidant Status. (2019). https://pubmed.ncbi.nlm.nih.gov/30196486/ DOI: 10.1007/s12011-018-1498-4
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Exogenous proline reversed halofuginone-induced amino-acid response signaling and selected cellular effects in the study, consistent with competition at the prolyl-tRNA synthetase step.

    L-Proline → Mouse-cell amino acid response during halofuginone exposure source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Mouse embryonic fibroblast and immune-cell experiments with halofuginone; model and assay-specific concentrations.
    limitations
    Not every proline-processing defect is competitively reversible, and this is not a clinical drug-interaction dose recommendation.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    Restoring access to a blocked loading step can turn off a shortage-like signal.
    primary_references
    Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 238–244

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse embryonic fibroblast and immune-cell experiments with halofuginone; model and assay-specific concentrations. · source_derived_draft · unverified_draft

    ## l-proline-eprs-stress-rescue Restoring access to a blocked loading step can turn off a shortage-like signal. Exogenous proline reversed halofuginone-induced amino-acid response signaling and selected cellular effects in the study, consistent with competition at the prolyl-tRNA synthetase step. Model: Mouse embryonic fibroblast and immune-cell experiments with halofuginone; model and assay-specific concentrations. Limitations: Not every proline-processing defect is competitively reversible, and this is not a clinical drug-interaction dose recommendation. Evidence access: Primary full text Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22327401/ · DOI 10.1038/nchembio.790
    Complete structured claim and evidence

  2. When intracellular heme declined, HRI inhibited translation initiation and restrained both alpha- and beta-globin synthesis in erythroid precursors.

    Mouse heme-regulated eIF2 alpha kinase HRI / Eif2ak1 → Globin protein synthesis source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/11726526.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6182d43925454a0208a74bed0b7da46736b9ff456509b215aa87e3051fe92eb3", "start_char": 0, "end_char": 1056, "text_sha256": "6182d43925454a0208a74bed0b7da46736b9ff456509b215aa87e3051fe92eb3"}
    experimental_model
    Targeted gene disruption with iron-deficient feeding
    exposure
    Hri deletion crossed with iron deficiency
    limitations
    Combined gene-loss and nutritional stress; the unusual knockout anemia pattern is not the standard description of ordinary iron deficiency.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Mice
    plain_language
    Cells normally slow globin production when there is not enough heme to assemble hemoglobin.
    primary_references
    [iron-p11726526] Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency. (2001). https://pubmed.ncbi.nlm.nih.gov/11726526/ DOI: 10.1093/emboj/20.23.6909
    tissue_or_cell_type
    Erythroid precursors and red cells

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1109–1120

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Targeted gene disruption with iron-deficient feeding · source_derived_draft · unverified_draft

    ### iron-hri-translation When intracellular heme declined, HRI inhibited translation initiation and restrained both alpha- and beta-globin synthesis in erythroid precursors. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Cells normally slow globin production when there is not enough heme to assemble hemoglobin. organism: Mice tissue_or_cell_type: Erythroid precursors and red cells experimental_model: Targeted gene disruption with iron-deficient feeding limitations: Combined gene-loss and nutritional stress; the unusual knockout anemia pattern is not the standard description of ordinary iron deficiency. exposure: Hri deletion crossed with iron deficiency evidence_span: {"source_cache": "artifacts/iron-research/11726526.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6182d43925454a0208a74bed0b7da46736b9ff456509b215aa87e3051fe92eb3", "start_char": 0, "end_char": 1056, "text_sha256": "6182d43925454a0208a74bed0b7da46736b9ff456509b215aa87e3051fe92eb3"} [iron-p11726526] Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency. (2001). https://pubmed.ncbi.nlm.nih.gov/11726526/ DOI: 10.1093/emboj/20.23.6909
    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