Component
Human alpha1 homomeric glycine receptor
Context-specific entity; species, compartment and exposure are stated on each claim.
4 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.
What acts on it
Applied taurine activated recombinant human alpha1 homomeric glycine receptors in oocytes and HEK293 cells; its potency and efficacy varied with the experimental receptor response.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human receptor expressed in Xenopus oocytes or human cells; electrophysiology.
- limitations
- Not a clinical sedative effect; chloride gradient and receptor composition shape cellular response.
- nutrient_topic
- Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Taurine
- plain_language
- Taurine can activate a receptor named for glycine.
- primary_references
- Activation of human alpha1 and alpha2 homomeric glycine receptors by taurine and GABA. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11559772/ · DOI 10.1111/j.1469-7793.2001.t01-1-00741.x
Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19) · lines 417–423
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human receptor expressed in Xenopus oocytes or human cells; electrophysiology. · source_derived_draft · unverified_draft
## taurine-glycine-receptor-alpha1 Taurine can activate a receptor named for glycine. Applied taurine activated recombinant human alpha1 homomeric glycine receptors in oocytes and HEK293 cells; its potency and efficacy varied with the experimental receptor response. Model: Human receptor expressed in Xenopus oocytes or human cells; electrophysiology. Limitations: Not a clinical sedative effect; chloride gradient and receptor composition shape cellular response. Evidence access: Primary abstract Activation of human alpha1 and alpha2 homomeric glycine receptors by taurine and GABA. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11559772/ · DOI 10.1111/j.1469-7793.2001.t01-1-00741.x
Complete structured claim and evidenceAt saturating 30 mM agonist, human alpha1 glycine-receptor activation rose faster with glycine than beta-alanine or taurine, and glycine responses decayed more slowly after removal.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human recombinant receptor comparison using high agonist concentrations.
- limitations
- Not equivalent to relative sedative potency after oral intake.
- nutrient_topic
- Glycine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Glycine
- plain_language
- Related molecules activate the same receptor with different timing.
- primary_references
- Kinetic determinants of agonist action at the recombinant human glycine receptor. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12679369/ · DOI 10.1113/jphysiol.2002.037796
Glycine: supply, one-carbon allocation, receptors and cross-nutrient mechanisms (2026-09-19) · lines 202–208
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant receptor comparison using high agonist concentrations. · source_derived_draft · unverified_draft
## glycine-glyr-ligand-kinetics Related molecules activate the same receptor with different timing. At saturating 30 mM agonist, human alpha1 glycine-receptor activation rose faster with glycine than beta-alanine or taurine, and glycine responses decayed more slowly after removal. Model: Human recombinant receptor comparison using high agonist concentrations. Limitations: Not equivalent to relative sedative potency after oral intake. Evidence access: Primary abstract Kinetic determinants of agonist action at the recombinant human glycine receptor. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12679369/ · DOI 10.1113/jphysiol.2002.037796
Complete structured claim and evidenceGlycine opened recombinant human alpha1 homomeric glycine receptors in HEK293 cells; rapid-application and single-channel assays resolved activation kinetics.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human alpha1 receptor, rapid agonist application and patch recording.
- limitations
- Homomeric experimental receptor differs from native heteromeric receptor mixtures; chloride gradient determines current consequences.
- nutrient_topic
- Glycine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Glycine
- plain_language
- Glycine can directly open a receptor channel.
- primary_references
- Kinetic determinants of agonist action at the recombinant human glycine receptor. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12679369/ · DOI 10.1113/jphysiol.2002.037796
Glycine: supply, one-carbon allocation, receptors and cross-nutrient mechanisms (2026-09-19) · lines 194–200
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human alpha1 receptor, rapid agonist application and patch recording. · source_derived_draft · unverified_draft
## glycine-glyr-opening Glycine can directly open a receptor channel. Glycine opened recombinant human alpha1 homomeric glycine receptors in HEK293 cells; rapid-application and single-channel assays resolved activation kinetics. Model: Human alpha1 receptor, rapid agonist application and patch recording. Limitations: Homomeric experimental receptor differs from native heteromeric receptor mixtures; chloride gradient determines current consequences. Evidence access: Primary abstract Kinetic determinants of agonist action at the recombinant human glycine receptor. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12679369/ · DOI 10.1113/jphysiol.2002.037796
Complete structured claim and evidenceIvermectin irreversibly activated human alpha1 homomeric and alpha1beta heteromeric glycine receptors at concentrations at or above 0.03 micromolar, through a site that is not the glycine site.
Experimental context and source evidence
- duration
- Acute and irreversible within the experiment
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Recombinant human alpha1 homomeric and alpha1beta heteromeric glycine receptors
- exposure
- 0.03 micromolar potentiation and higher-concentration irreversible activation
- limitations
- Ivermectin-gated currents showed markedly reduced sensitivity to strychnine, picrotoxin and zinc, so the pharmacology of this activation differs from ordinary glycinergic transmission.
- organism
- Recombinant human alpha1 homomeric and alpha1beta heteromeric glycine receptors
- plain_language
- Ivermectin irreversibly activated human alpha1 homomeric and alpha1beta heteromeric glycine receptors at concentrations at or above 0.03 micromolar, through a site that is not the glycine site.
- primary_references
- Ivermectin, an unconventional agonist of the glycine receptor chloride channel. (2001). https://pubmed.ncbi.nlm.nih.gov/11278873/ DOI: 10.1074/jbc.M011264200
- route
- In vitro
- tissue
- Inhibitory chloride channel gating
Ivermectin: mechanism of action across parasite, host barrier and mammalian targets (2026-09-22) · lines 112–121
Original AI-assisted curation of sixteen primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Study-specific citations, concentrations, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## ivermectin-glycine-receptor-activation Ivermectin irreversibly activated human alpha1 homomeric and alpha1beta heteromeric glycine receptors at concentrations at or above 0.03 micromolar, through a site that is not the glycine site. Model/species: Recombinant human alpha1 homomeric and alpha1beta heteromeric glycine receptors Tissue/system: Inhibitory chloride channel gating Exposure: 0.03 micromolar potentiation and higher-concentration irreversible activation Route: In vitro Duration: Acute and irreversible within the experiment Limits: Ivermectin-gated currents showed markedly reduced sensitivity to strychnine, picrotoxin and zinc, so the pharmacology of this activation differs from ordinary glycinergic transmission. Primary reference: Ivermectin, an unconventional agonist of the glycine receptor chloride channel. (2001). https://pubmed.ncbi.nlm.nih.gov/11278873/ DOI: 10.1074/jbc.M011264200 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
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.