Component

NaV1.4 / SCN4A

NaV1.4 / SCN4A; interpretation depends on linked experimental context.

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 it acts on

  1. Analysis of the Nav1.4 structure and previously characterized residues supported an allosteric blocking mechanism of fast inactivation.

    NaV1.4 / SCN4A → Nav1.4 fast inactivation source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sodium-research/30190309.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436", "start_char": 0, "end_char": 876, "text_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436"}
    experimental_model
    Cryo-EM reconstruction at 3.2 angstrom resolution
    exposure
    Purified Nav1.4–beta1 structure
    limitations
    Structural support for permeation and inactivation; this experiment did not test dietary sodium or clinical supplementation.
    nutrient_topic
    Sodium research collection; topical membership is not evidence of a direct dietary effect. · Sodium
    organism
    Human channel complex
    plain_language
    The channel has a mechanism to stop sodium flow rapidly after activation.
    primary_references
    [sodium-p30190309] Structure of the human voltage-gated sodium channel Nav1.4 in complex with β1. (2018). https://pubmed.ncbi.nlm.nih.gov/30190309/ DOI: 10.1126/science.aau2486
    tissue_or_cell_type
    Skeletal-muscle Nav1.4 with beta1

    Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17) · lines 356–367

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM reconstruction at 3.2 angstrom resolution · source_derived_draft · unverified_draft

    ### sodium-nav14-inactivation Analysis of the Nav1.4 structure and previously characterized residues supported an allosteric blocking mechanism of fast inactivation. Condition category: normal nutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The channel has a mechanism to stop sodium flow rapidly after activation. organism: Human channel complex tissue_or_cell_type: Skeletal-muscle Nav1.4 with beta1 experimental_model: Cryo-EM reconstruction at 3.2 angstrom resolution limitations: Structural support for permeation and inactivation; this experiment did not test dietary sodium or clinical supplementation. exposure: Purified Nav1.4–beta1 structure evidence_span: {"source_cache": "artifacts/sodium-research/30190309.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436", "start_char": 0, "end_char": 876, "text_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436"} [sodium-p30190309] Structure of the human voltage-gated sodium channel Nav1.4 in complex with β1. (2018). https://pubmed.ncbi.nlm.nih.gov/30190309/ DOI: 10.1126/science.aau2486
    Complete structured claim and evidence

  2. The human Nav1.4–beta1 structure resolved its pore and voltage-sensing domains, supporting a molecular account of sodium permeation.

    NaV1.4 / SCN4A → Sodium ion source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sodium-research/30190309.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436", "start_char": 0, "end_char": 876, "text_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436"}
    experimental_model
    Cryo-EM reconstruction at 3.2 angstrom resolution
    exposure
    Purified Nav1.4–beta1 structure
    limitations
    Structural support for permeation and inactivation; this experiment did not test dietary sodium or clinical supplementation.
    nutrient_topic
    Sodium research collection; topical membership is not evidence of a direct dietary effect. · Sodium
    organism
    Human channel complex
    plain_language
    A dedicated sodium-channel protein helps electrically excitable cells generate signals.
    primary_references
    [sodium-p30190309] Structure of the human voltage-gated sodium channel Nav1.4 in complex with β1. (2018). https://pubmed.ncbi.nlm.nih.gov/30190309/ DOI: 10.1126/science.aau2486
    tissue_or_cell_type
    Skeletal-muscle Nav1.4 with beta1

    Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17) · lines 343–354

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM reconstruction at 3.2 angstrom resolution · source_derived_draft · unverified_draft

    ### sodium-nav14-pore The human Nav1.4–beta1 structure resolved its pore and voltage-sensing domains, supporting a molecular account of sodium permeation. Condition category: normal nutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect. plain_language: A dedicated sodium-channel protein helps electrically excitable cells generate signals. organism: Human channel complex tissue_or_cell_type: Skeletal-muscle Nav1.4 with beta1 experimental_model: Cryo-EM reconstruction at 3.2 angstrom resolution limitations: Structural support for permeation and inactivation; this experiment did not test dietary sodium or clinical supplementation. exposure: Purified Nav1.4–beta1 structure evidence_span: {"source_cache": "artifacts/sodium-research/30190309.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436", "start_char": 0, "end_char": 876, "text_sha256": "2c9e7fceab1407740b539362913e9f97227515a9a7d9439ce57113545d2f7436"} [sodium-p30190309] Structure of the human voltage-gated sodium channel Nav1.4 in complex with β1. (2018). https://pubmed.ncbi.nlm.nih.gov/30190309/ DOI: 10.1126/science.aau2486
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. At 2 mM bath K, R528H muscle paradoxically depolarized and lost force while wild-type fibers hyperpolarized.

    CaV1.1 R528H variant → Skeletal muscle excitability source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    A calcium-channel genetic defect changes potassium sensitivity of sodium-dependent muscle excitability.
    experimental_model
    4.75 to 2 mM K challenge; mouse muscle recordings.
    limitations
    Sex/genotype influenced susceptibility; no general dietary-paralysis claim.
    nutrient_topic
    Potassium research collection; topical membership is not evidence of a direct dietary effect. · Potassium
    organism
    Mouse
    plain_language
    The same low-potassium exposure acted differently with inherited channel impairment.
    primary_references
    [wu-2012-hypopp] A calcium channel mutant mouse model of hypokalemic periodic paralysis (2012). https://pmc.ncbi.nlm.nih.gov/articles/PMC3533564/ DOI: 10.1172/JCI66091
    tissue_or_cell_type
    Skeletal muscle
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 762–772

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · 4.75 to 2 mM K challenge; mouse muscle recordings. · source_derived_draft · unverified_draft

    ### k-hypopp-low-k-depolarization At 2 mM bath K, R528H muscle paradoxically depolarized and lost force while wild-type fibers hyperpolarized. Condition category: machinery_impairment nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same low-potassium exposure acted differently with inherited channel impairment. organism: Mouse tissue_or_cell_type: Skeletal muscle experimental_model: 4.75 to 2 mM K challenge; mouse muscle recordings. limitations: Sex/genotype influenced susceptibility; no general dietary-paralysis claim. cross_nutrient: A calcium-channel genetic defect changes potassium sensitivity of sodium-dependent muscle excitability. [wu-2012-hypopp] A calcium channel mutant mouse model of hypokalemic periodic paralysis (2012). https://pmc.ncbi.nlm.nih.gov/articles/PMC3533564/ DOI: 10.1172/JCI66091
    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