Component

Purified F-actin in cucurbitacin assays, species as reported

Context-specific entity; species, compartment and exposure are stated on each claim.

3 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. Cucurbitacin E covalently modified actin at Cys257 in F-actin and inhibited depolymerization, with effects at substoichiometric compound:actin ratios down to 1:6.

    Cucurbitacin E → Purified F-actin in cucurbitacin assays, species as reported source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified actin and cellular photoactivation experiments.
    limitations
    Purified actin species/isoform not established from the accessed abstract; not automatically human ACTB. This study did not find an effect on polymerization.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    The filament itself can be stabilized.
    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 52–58

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

    ## cucurbitacin-e-f-actin The filament itself can be stabilized. Cucurbitacin E covalently modified actin at Cys257 in F-actin and inhibited depolymerization, with effects at substoichiometric compound:actin ratios down to 1:6. Model: Purified actin and cellular photoactivation experiments. Limitations: Purified actin species/isoform not established from the accessed abstract; not automatically human ACTB. This study did not find an effect on polymerization. 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. In the 2010 purified-actin assays, cucurbitacin I did not change depolymerization rate at concentrations active in cells; high concentrations delayed polymerization initiation without changing its subsequent rate.

    Cucurbitacin I → Purified F-actin in cucurbitacin assays, species as reported source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC2991314
    experimental_model
    Purified-actin experiments alongside canine and mouse cell models.
    limitations
    Different member, concentration and endpoint from cucurbitacin E stabilization; not an automatic scientific contradiction.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    A dramatic cell phenotype was not reproduced by every purified-actin endpoint.
    primary_references
    Cucurbitacin I inhibits cell motility by indirectly interfering with actin dynamics. · 2010 · https://pubmed.ncbi.nlm.nih.gov/21124831/ · DOI 10.1371/journal.pone.0014039

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 76–82

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified-actin experiments alongside canine and mouse cell models. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-no-depolymerization-effect A dramatic cell phenotype was not reproduced by every purified-actin endpoint. In the 2010 purified-actin assays, cucurbitacin I did not change depolymerization rate at concentrations active in cells; high concentrations delayed polymerization initiation without changing its subsequent rate. Model: Purified-actin experiments alongside canine and mouse cell models. Limitations: Different member, concentration and endpoint from cucurbitacin E stabilization; not an automatic scientific contradiction. Evidence access: Primary full text PMC2991314 Cucurbitacin I inhibits cell motility by indirectly interfering with actin dynamics. · 2010 · https://pubmed.ncbi.nlm.nih.gov/21124831/ · DOI 10.1371/journal.pone.0014039
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Cucurbitacin E pretreatment inhibited the F-actin-severing activity of purified human cofilin 1.

    Cucurbitacin E → Human cofilin-mediated F-actin severing source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC3751690
    experimental_model
    Purified-protein functional assay.
    limitations
    Actin preparation species is not resolved in this record; broad thiol reactivity prevents assigning cofilin as the exclusive cellular target.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Modifying the cutting protein slows filament disassembly.
    primary_references
    Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 44–50

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified-protein functional assay. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-cofilin-severing Modifying the cutting protein slows filament disassembly. Cucurbitacin E pretreatment inhibited the F-actin-severing activity of purified human cofilin 1. Model: Purified-protein functional assay. Limitations: Actin preparation species is not resolved in this record; broad thiol reactivity prevents assigning cofilin as the exclusive cellular target. Evidence access: Primary full text PMC3751690 Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23945128/ · DOI 10.1186/1478-811X-11-58
    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