Component

Purified G-actin in cucurbitacin assays, species as reported

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.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What acts on it

  1. The cucurbitacin E actin study reported binding to filamentous actin but not globular actin.

    Cucurbitacin E → Purified G-actin in cucurbitacin assays, species as reported source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Same purified-actin experiments.
    limitations
    Member-specific assay result; cannot be transferred to cucurbitacin I.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    The physical state of the protein changes the result.
    primary_references
    The natural product cucurbitacin E inhibits depolymerization of actin filaments. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22724897/ · DOI 10.1021/cb300254s

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 60–66

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Same purified-actin experiments. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-no-g-actin-binding The physical state of the protein changes the result. The cucurbitacin E actin study reported binding to filamentous actin but not globular actin. Model: Same purified-actin experiments. Limitations: Member-specific assay result; cannot be transferred to cucurbitacin I. Evidence access: Primary abstract The natural product cucurbitacin E inhibits depolymerization of actin filaments. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22724897/ · DOI 10.1021/cb300254s
    Complete structured claim and evidence

  2. Docking and molecular dynamics proposed cucurbitacin I contacts involving actin residues I136, I175, D154 and A138.

    Cucurbitacin I → Purified G-actin in cucurbitacin assays, species as reported source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Computational structural modeling in the 2024 actin paper.
    limitations
    No ligand-bound experimental structure or covalent mapping was established by this computation.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    The proposed contact map is a prediction.
    primary_references
    Depolymerization of actin filaments by Cucurbitacin I through binding G-actin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38370084/ · DOI 10.1002/fsn3.3804

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 100–106

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Computational structural modeling in the 2024 actin paper. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-docking The proposed contact map is a prediction. Docking and molecular dynamics proposed cucurbitacin I contacts involving actin residues I136, I175, D154 and A138. Model: Computational structural modeling in the 2024 actin paper. Limitations: No ligand-bound experimental structure or covalent mapping was established by this computation. Evidence access: Primary abstract Depolymerization of actin filaments by Cucurbitacin I through binding G-actin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38370084/ · DOI 10.1002/fsn3.3804
    Complete structured claim and evidence

  3. Cucurbitacin I at 1–200 nM increased G-actin thermal stability in a thermal-shift assay, supporting an interaction in that preparation.

    Cucurbitacin I → Purified G-actin in cucurbitacin assays, species as reported source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    2024 G-actin thermal-shift experiment; protein species not established by the accessed abstract.
    limitations
    A thermal shift is not an affinity measurement, covalent-site map or proof of selectivity.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    A later experiment found evidence of interaction with actin monomers.
    primary_references
    Depolymerization of actin filaments by Cucurbitacin I through binding G-actin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38370084/ · DOI 10.1002/fsn3.3804

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 84–90

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · 2024 G-actin thermal-shift experiment; protein species not established by the accessed abstract. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-g-actin-shift A later experiment found evidence of interaction with actin monomers. Cucurbitacin I at 1–200 nM increased G-actin thermal stability in a thermal-shift assay, supporting an interaction in that preparation. Model: 2024 G-actin thermal-shift experiment; protein species not established by the accessed abstract. Limitations: A thermal shift is not an affinity measurement, covalent-site map or proof of selectivity. Evidence access: Primary abstract Depolymerization of actin filaments by Cucurbitacin I through binding G-actin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38370084/ · DOI 10.1002/fsn3.3804
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Adding cucurbitacin I inhibited actin polymerization in the 2024 in-vitro experiment.

    Cucurbitacin I → Purified actin polymerization in the 2024 cucurbitacin I assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified actin plus endothelial-cell experiments; cell species not resolved in this abstract-based record.
    limitations
    Concentration-dependent and assay-dependent findings require matched replication before declaring a resolved direct-target disagreement.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Filament assembly is a separate endpoint from filament breakdown.
    primary_references
    Depolymerization of actin filaments by Cucurbitacin I through binding G-actin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38370084/ · DOI 10.1002/fsn3.3804

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 92–98

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified actin plus endothelial-cell experiments; cell species not resolved in this abstract-based record. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-polymerization Filament assembly is a separate endpoint from filament breakdown. Adding cucurbitacin I inhibited actin polymerization in the 2024 in-vitro experiment. Model: Purified actin plus endothelial-cell experiments; cell species not resolved in this abstract-based record. Limitations: Concentration-dependent and assay-dependent findings require matched replication before declaring a resolved direct-target disagreement. Evidence access: Primary abstract Depolymerization of actin filaments by Cucurbitacin I through binding G-actin. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38370084/ · DOI 10.1002/fsn3.3804
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards