Component
Prenylation of Rho-family GTPases
Attachment of an isoprenoid lipid anchor to Rho-family GTPases.
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.
What acts on it
Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects.
Experimental context and source evidence
- duration
- Not stated here
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Live-cell high-content screen in human cell culture
- exposure
- Statins, and separately perillyl alcohol as a geranylgeranyltransferase inhibitor
- limitations
- The screen tested statins as a class without attributing the result to atorvastatin, and respiratory syncytial virus infection itself globally upregulated prenylation, so the baseline was not a resting cell.
- organism
- Live-cell high-content screen in human cell culture
- plain_language
- Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects.
- primary_references
- Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2
- route
- In vitro
- tissue
- Host protein prenylation and virus production
Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 89–98
Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## statin-reduces-rho-gtpase-prenylation Statin treatment reduced host protein prenylation including prenylation of Rho GTPases, and reduced respiratory syncytial virus infection in vitro through combined cholesterol and isoprenoid effects. Model/species: Live-cell high-content screen in human cell culture Tissue/system: Host protein prenylation and virus production Exposure: Statins, and separately perillyl alcohol as a geranylgeranyltransferase inhibitor Route: In vitro Duration: Not stated here Limits: The screen tested statins as a class without attributing the result to atorvastatin, and respiratory syncytial virus infection itself globally upregulated prenylation, so the baseline was not a resting cell. Primary reference: Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2 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)
Loss of Rac1 activity strongly inhibited respiratory syncytial virus through a decrease in F protein surface expression.
Experimental context and source evidence
- duration
- Not stated here
- evidence_access
- Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
- experimental_model
- Human cell culture
- exposure
- Rac1 activity loss under statin or geranylgeranyltransferase inhibition
- limitations
- Rac1 was the strongest of the Rho-family GTPases assayed in that study; the others were not equivalent.
- organism
- Human cell culture
- plain_language
- Loss of Rac1 activity strongly inhibited respiratory syncytial virus through a decrease in F protein surface expression.
- primary_references
- Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2
- route
- In vitro
- tissue
- Rho-family GTPase activity and viral fusion protein surface expression
Atorvastatin: mechanism of action from target occupancy to isoprenoids, transport, muscle and metabolism (2026-09-22) · lines 100–109
Original AI-assisted curation of twelve primary studies resolved by PubMed title search and cross-checked against live PubMed metadata. Findings obtained with mevastatin, simvastatin or the statin class are recorded against those subjects. Study-specific citations, doses, negative findings and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## rac1-supports-viral-f-protein-surface-expression Loss of Rac1 activity strongly inhibited respiratory syncytial virus through a decrease in F protein surface expression. Model/species: Human cell culture Tissue/system: Rho-family GTPase activity and viral fusion protein surface expression Exposure: Rac1 activity loss under statin or geranylgeranyltransferase inhibition Route: In vitro Duration: Not stated here Limits: Rac1 was the strongest of the Rho-family GTPases assayed in that study; the others were not equivalent. Primary reference: Statin-mediated disruption of Rho GTPase prenylation and activity inhibits respiratory syncytial virus infection. (2021). https://pubmed.ncbi.nlm.nih.gov/34716403/ DOI: 10.1038/s42003-021-02754-2 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.