Component
Human glycine receptor alpha1 / GLRA1
Context-specific entity; species, compartment and exposure are stated on each 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)
Human alpha1(K276E)/beta receptors expressed in Xenopus oocytes were about 29-fold less glycine-sensitive than wild type and had shorter channel openings.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Human disease-associated receptor constructs in frog oocytes; concentration-response and single-channel recording.
- limitations
- Modeling implicated impaired gating rather than simply loss of ligand binding; not dietary glycine deficiency.
- nutrient_topic
- Glycine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Glycine
- plain_language
- The receptor can respond poorly even when its ligand is supplied.
- primary_references
- Properties of human glycine receptors containing the hyperekplexia mutation alpha1(K276E), expressed in Xenopus oocytes. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9490812/ · DOI 10.1111/j.1469-7793.1998.025bu.x
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Glycine: supply, one-carbon allocation, receptors and cross-nutrient mechanisms (2026-09-19) · lines 210–216
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human disease-associated receptor constructs in frog oocytes; concentration-response and single-channel recording. · source_derived_draft · unverified_draft
## glycine-glyr-variant The receptor can respond poorly even when its ligand is supplied. Human alpha1(K276E)/beta receptors expressed in Xenopus oocytes were about 29-fold less glycine-sensitive than wild type and had shorter channel openings. Model: Human disease-associated receptor constructs in frog oocytes; concentration-response and single-channel recording. Limitations: Modeling implicated impaired gating rather than simply loss of ligand binding; not dietary glycine deficiency. Evidence access: Primary abstract Properties of human glycine receptors containing the hyperekplexia mutation alpha1(K276E), expressed in Xenopus oocytes. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9490812/ · DOI 10.1111/j.1469-7793.1998.025bu.x
Complete structured claim and evidenceEnhancement of glycine receptor function by ethanol was inversely correlated with the molecular volume at position alpha267, implying a size-limited site rather than a general membrane effect.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/alcohol-research/9452448.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec", "start_char": 0, "end_char": 1618, "text_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec"}
- experimental_model
- Site-directed mutagenesis of glycine receptor position alpha267 with alcohols of differing size
- exposure
- A series of alcohols against residue volume at alpha267
- limitations
- A volume-series experiment that argues for a discrete binding pocket rather than a membrane-disordering effect. It is recombinant receptor electrophysiology.
- 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
- Recombinant receptor
- plain_language
- Make the pocket smaller and alcohol works less, which is what a real binding site looks like.
- primary_references
- [alcohol-p9452448] Enhancement of glycine receptor function by ethanol is inversely correlated with molecular volume at position alpha267. (1998). https://pubmed.ncbi.nlm.nih.gov/9452448/ DOI: 10.1074/jbc.273.6.3314
- tissue_or_cell_type
- Glycine receptor
Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 345–356
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Site-directed mutagenesis of glycine receptor position alpha267 with alcohols of differing size · source_derived_draft · unverified_draft
### alcohol-glycine-receptor-pocket Enhancement of glycine receptor function by ethanol was inversely correlated with the molecular volume at position alpha267, implying a size-limited site rather than a general membrane effect. 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: Make the pocket smaller and alcohol works less, which is what a real binding site looks like. organism: Recombinant receptor tissue_or_cell_type: Glycine receptor experimental_model: Site-directed mutagenesis of glycine receptor position alpha267 with alcohols of differing size limitations: A volume-series experiment that argues for a discrete binding pocket rather than a membrane-disordering effect. It is recombinant receptor electrophysiology. exposure: A series of alcohols against residue volume at alpha267 evidence_span: {"source_cache": "artifacts/alcohol-research/9452448.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec", "start_char": 0, "end_char": 1618, "text_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec"} [alcohol-p9452448] Enhancement of glycine receptor function by ethanol is inversely correlated with molecular volume at position alpha267. (1998). https://pubmed.ncbi.nlm.nih.gov/9452448/ DOI: 10.1074/jbc.273.6.3314
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.