Component
Vardenafil
Study-scoped entity; inspect species, exposure, model and limitations 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.
What it acts on
PDE5 inhibition with vardenafil potentiated EGCG-dependent apoptosis and prolonged survival in a mouse xenograft experiment.
Experimental context and source evidence
- experimental_model
- Cancer-cell experiments and mouse xenografts in the 2013 study.
- limitations
- Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety.
- nutrient_topic
- EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
- plain_language
- Blocking the opposing enzyme strengthened the response in these models.
- primary_references
- 67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 92–98
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cancer-cell experiments and mouse xenografts in the 2013 study. · source_derived_draft · unverified_draft
## egcg-vardenafil Blocking the opposing enzyme strengthened the response in these models. PDE5 inhibition with vardenafil potentiated EGCG-dependent apoptosis and prolonged survival in a mouse xenograft experiment. Model: Cancer-cell experiments and mouse xenografts in the 2013 study. Limitations: Preclinical combination experiments; normal-cell selectivity in tested preparations is not universal safety. Evidence access: primary abstract. 67-kDa laminin receptor increases cGMP to induce cancer-selective apoptosis. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23348740/ · DOI 10.1172/jci64768
Complete structured claim and evidence
Where it participates (unsigned role)
Three-dimensional structures of the catalytic domain of human PDE5, residues 537 to 860, were determined in complex with sildenafil, tadalafil and vardenafil.
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
- Human PDE5 catalytic domain
- exposure
- Each of the three drug molecules complexed with the enzyme
- limitations
- The catalytic domain alone was crystallised, not the full-length regulated enzyme, so the structures do not describe the allosteric cGMP-binding GAF domains.
- organism
- Human PDE5 catalytic domain
- plain_language
- Three-dimensional structures of the catalytic domain of human PDE5, residues 537 to 860, were determined in complex with sildenafil, tadalafil and vardenafil.
- primary_references
- Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. (2003). https://pubmed.ncbi.nlm.nih.gov/12955149/ DOI: 10.1038/nature01914
- route
- Structural
- tissue
- Inhibitor binding at the catalytic site
Tadalafil: PDE5 occupancy, the cGMP route and three measured endpoints (2026-09-22) · lines 35–44
Original AI-assisted curation of seven primary studies resolved by PubMed title search, with every abstract read and all DOIs cross-checked against live PubMed metadata. Two references carry an unresolvable erratum and are recorded as corrected. Study-specific doses, effect sizes and limitations retained. Not publisher full text. · supports · · source_derived_draft · unverified_draft
## pde5-binding-site-resolved-with-tadalafil Three-dimensional structures of the catalytic domain of human PDE5, residues 537 to 860, were determined in complex with sildenafil, tadalafil and vardenafil. Model/species: Human PDE5 catalytic domain Tissue/system: Inhibitor binding at the catalytic site Exposure: Each of the three drug molecules complexed with the enzyme Route: Structural Duration: Not applicable Limits: The catalytic domain alone was crystallised, not the full-length regulated enzyme, so the structures do not describe the allosteric cGMP-binding GAF domains. Primary reference: Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. (2003). https://pubmed.ncbi.nlm.nih.gov/12955149/ DOI: 10.1038/nature01914 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.