Component
Caenorhabditis elegans glutamate-gated chloride channel alpha / GluCl
Invertebrate anion-selective Cys-loop receptor; the avermectin-sensitive channel.
3 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
An avermectin-sensitive glutamate-gated chloride channel was cloned from Caenorhabditis elegans and shown to be a new member of the ligand-gated ion channel superfamily.
Experimental context and source evidence
- duration
- Acute
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Caenorhabditis elegans complementary DNAs expressed in Xenopus oocytes
- exposure
- Avermectin applied to the expressed channel
- limitations
- The same report notes that avermectins also interact with vertebrate and invertebrate GABA receptors, so an invertebrate-only target cannot be inferred from this channel alone.
- organism
- Caenorhabditis elegans complementary DNAs expressed in Xenopus oocytes
- plain_language
- An avermectin-sensitive glutamate-gated chloride channel was cloned from Caenorhabditis elegans and shown to be a new member of the ligand-gated ion channel superfamily.
- primary_references
- Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans. (1994). https://pubmed.ncbi.nlm.nih.gov/7935817/ DOI: 10.1038/371707a0
- route
- In vitro
- tissue
- Expression cloning and electrophysiology of a glutamate-gated chloride channel
Ivermectin: mechanism of action across parasite, host barrier and mammalian targets (2026-09-22) · lines 13–22
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-glucl-cloning An avermectin-sensitive glutamate-gated chloride channel was cloned from Caenorhabditis elegans and shown to be a new member of the ligand-gated ion channel superfamily. Model/species: Caenorhabditis elegans complementary DNAs expressed in Xenopus oocytes Tissue/system: Expression cloning and electrophysiology of a glutamate-gated chloride channel Exposure: Avermectin applied to the expressed channel Route: In vitro Duration: Acute Limits: The same report notes that avermectins also interact with vertebrate and invertebrate GABA receptors, so an invertebrate-only target cannot be inferred from this channel alone. Primary reference: Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans. (1994). https://pubmed.ncbi.nlm.nih.gov/7935817/ DOI: 10.1038/371707a0 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidenceIvermectin binds in the transmembrane domain of the Caenorhabditis elegans glutamate-gated chloride channel and stabilises an open-pore conformation.
Experimental context and source evidence
- duration
- Not applicable
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Homopentameric Caenorhabditis elegans GluCl alpha, X-ray structure at 3.3 angstrom resolution
- exposure
- GluCl-Fab complex determined with ivermectin as allosteric agonist, and separately with L-glutamate and picrotoxin
- limitations
- A structure establishes a binding site and a stabilised conformation; it does not establish the concentration at which this occurs in a living parasite.
- organism
- Homopentameric Caenorhabditis elegans GluCl alpha, X-ray structure at 3.3 angstrom resolution
- plain_language
- Ivermectin binds in the transmembrane domain of the Caenorhabditis elegans glutamate-gated chloride channel and stabilises an open-pore conformation.
- primary_references
- Principles of activation and permeation in an anion-selective Cys-loop receptor. (2011). https://pubmed.ncbi.nlm.nih.gov/21572436/ DOI: 10.1038/nature10139
- route
- Structural
- tissue
- Anion-selective Cys-loop receptor gating and permeation
Ivermectin: mechanism of action across parasite, host barrier and mammalian targets (2026-09-22) · lines 24–33
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-glucl-open-pore Ivermectin binds in the transmembrane domain of the Caenorhabditis elegans glutamate-gated chloride channel and stabilises an open-pore conformation. Model/species: Homopentameric Caenorhabditis elegans GluCl alpha, X-ray structure at 3.3 angstrom resolution Tissue/system: Anion-selective Cys-loop receptor gating and permeation Exposure: GluCl-Fab complex determined with ivermectin as allosteric agonist, and separately with L-glutamate and picrotoxin Route: Structural Duration: Not applicable Limits: A structure establishes a binding site and a stabilised conformation; it does not establish the concentration at which this occurs in a living parasite. Primary reference: Principles of activation and permeation in an anion-selective Cys-loop receptor. (2011). https://pubmed.ncbi.nlm.nih.gov/21572436/ DOI: 10.1038/nature10139 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
Complete structured claim and evidence
Where it participates (unsigned role)
Ivermectin exposure decreased the amount of protein released from the excretory-secretory apparatus of Brugia malayi microfilariae.
Experimental context and source evidence
- duration
- Acute
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Brugia malayi microfilariae
- exposure
- Ivermectin in vitro
- limitations
- The link from reduced secretion to rapid microfilarial clearance in the host is proposed by the authors, not measured in this work.
- organism
- Brugia malayi microfilariae
- plain_language
- Ivermectin exposure decreased the amount of protein released from the excretory-secretory apparatus of Brugia malayi microfilariae.
- primary_references
- Ivermectin disrupts the function of the excretory-secretory apparatus in microfilariae of Brugia malayi. (2010). https://pubmed.ncbi.nlm.nih.gov/21041637/ DOI: 10.1073/pnas.1011983107
- route
- In vitro
- tissue
- Excretory-secretory vesicle and the muscle structure surrounding it, where GluCl expression was localised
Ivermectin: mechanism of action across parasite, host barrier and mammalian targets (2026-09-22) · lines 35–44
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-es-protein-release Ivermectin exposure decreased the amount of protein released from the excretory-secretory apparatus of Brugia malayi microfilariae. Model/species: Brugia malayi microfilariae Tissue/system: Excretory-secretory vesicle and the muscle structure surrounding it, where GluCl expression was localised Exposure: Ivermectin in vitro Route: In vitro Duration: Acute Limits: The link from reduced secretion to rapid microfilarial clearance in the host is proposed by the authors, not measured in this work. Primary reference: Ivermectin disrupts the function of the excretory-secretory apparatus in microfilariae of Brugia malayi. (2010). https://pubmed.ncbi.nlm.nih.gov/21041637/ DOI: 10.1073/pnas.1011983107 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.