Component
Beta-tubulin carrying glycine at position 198
Beta-tubulin carrying glycine at position 198. Species, exposure and limitations are retained in each linked claim.
1 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)
Expressing beta-tubulin as a fusion with maltose binding protein produced a soluble protein and confirmed for the first time using a gel filtration assay that benzimidazoles indeed bind to beta-tubulin, with binding reduced by the mutation glutamate 198 to glycine which also confers resistance, while binding of phenylcarbamates was the complete opposite, reflecting their biological activity and the negative cross-resistance.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/mebendazole-research/9736529.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ee7cd2a364b52ba75f6f19da6935c7311ae80f514a223a50b17dbd6bbaf929d4", "start_char": 0, "end_char": 1053, "text_sha256": "ee7cd2a364b52ba75f6f19da6935c7311ae80f514a223a50b17dbd6bbaf929d4"}
- experimental_model
- Fungal beta-tubulin expressed as a maltose binding protein fusion, assayed by gel filtration
- exposure
- Benzimidazole and phenylcarbamate binding to wild-type and Glu198Gly fusion protein
- limitations
- The first direct confirmation by binding assay that benzimidazoles bind beta-tubulin itself. It is a fusion protein rather than native tubulin, which the authors address by the internal consistency of the two ligand classes.
- nutrient_topic
- Mebendazole research collection; topical membership is not evidence of a direct clinical effect, and mebendazole is recorded separately from albendazole, from the benzimidazole class and from its own crystal forms. · Mebendazole
- organism
- Fungus
- plain_language
- The drug really does stick to this protein, and the mutation that resists it loosens the grip.
- primary_references
- [mbz-p9736529] Fungal beta-tubulin, expressed as a fusion protein, binds benzimidazole and phenylcarbamate fungicides. (1998). https://pubmed.ncbi.nlm.nih.gov/9736529/ DOI: 10.1128/aac.42.9.2171
- tissue_or_cell_type
- Beta-tubulin
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fungal beta-tubulin expressed as a maltose binding protein fusion, assayed by gel filtration · source_derived_draft · unverified_draft
### mbz-direct-binding-and-glu198 Expressing beta-tubulin as a fusion with maltose binding protein produced a soluble protein and confirmed for the first time using a gel filtration assay that benzimidazoles indeed bind to beta-tubulin, with binding reduced by the mutation glutamate 198 to glycine which also confers resistance, while binding of phenylcarbamates was the complete opposite, reflecting their biological activity and the negative cross-resistance. Condition category: normal nutrient_topic: Mebendazole research collection; topical membership is not evidence of a direct clinical effect, and mebendazole is recorded separately from albendazole, from the benzimidazole class and from its own crystal forms. plain_language: The drug really does stick to this protein, and the mutation that resists it loosens the grip. organism: Fungus tissue_or_cell_type: Beta-tubulin experimental_model: Fungal beta-tubulin expressed as a maltose binding protein fusion, assayed by gel filtration limitations: The first direct confirmation by binding assay that benzimidazoles bind beta-tubulin itself. It is a fusion protein rather than native tubulin, which the authors address by the internal consistency of the two ligand classes. exposure: Benzimidazole and phenylcarbamate binding to wild-type and Glu198Gly fusion protein evidence_span: {"source_cache": "artifacts/mebendazole-research/9736529.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ee7cd2a364b52ba75f6f19da6935c7311ae80f514a223a50b17dbd6bbaf929d4", "start_char": 0, "end_char": 1053, "text_sha256": "ee7cd2a364b52ba75f6f19da6935c7311ae80f514a223a50b17dbd6bbaf929d4"} [mbz-p9736529] Fungal beta-tubulin, expressed as a fusion protein, binds benzimidazole and phenylcarbamate fungicides. (1998). https://pubmed.ncbi.nlm.nih.gov/9736529/ DOI: 10.1128/aac.42.9.2171
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.