Component
Human sodium-channel beta1 subunit / SCN1B
Human sodium-channel beta1 subunit / SCN1B. Species, exposure and limitations are retained in each linked claim.
2 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
Where it participates (unsigned role)
Analysis of the Nav1.4 structure and previously characterized residues supported an allosteric blocking mechanism of fast inactivation.
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 evidenceThe human Nav1.4–beta1 structure resolved its pore and voltage-sensing domains, supporting a molecular account of sodium permeation.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.