Component

Cucurbitacin I

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

10 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 it acts on

  1. Adding cucurbitacin I rapidly reduced motility and produced actin aggregates in canine MDCK cells.

    Cucurbitacin I → Canine MDCK cell motility during cucurbitacin I exposure source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC2991314
    experimental_model
    Canine MDCK cellular experiments; also mouse B16-F1 experiments in the paper.
    limitations
    Cellular phenotype does not identify a direct molecular binding target.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Cell movement changes along with filament organization.
    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 68–74

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Canine MDCK cellular experiments; also mouse B16-F1 experiments in the paper. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-canine-motility Cell movement changes along with filament organization. Adding cucurbitacin I rapidly reduced motility and produced actin aggregates in canine MDCK cells. Model: Canine MDCK cellular experiments; also mouse B16-F1 experiments in the paper. Limitations: Cellular phenotype does not identify a direct molecular binding target. 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

  2. Incubating purified human cofilin 1 with cucurbitacin I produced covalent adducts; mass shifts were compatible with about four compound molecules per cofilin under the tested excess-compound conditions.

    Cucurbitacin I → Human cofilin 1 / CFL1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC3751690
    experimental_model
    Purified human cofilin 1, 5 micromolar; up to 1:100 protein:compound molar ratio, 16 hours.
    limitations
    Long, high-excess biochemical incubation; does not establish selectivity or occupancy after human ingestion.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Protein cysteines can become chemical attachment sites.
    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 28–34

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human cofilin 1, 5 micromolar; up to 1:100 protein:compound molar ratio, 16 hours. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-cofilin-adduct Protein cysteines can become chemical attachment sites. Incubating purified human cofilin 1 with cucurbitacin I produced covalent adducts; mass shifts were compatible with about four compound molecules per cofilin under the tested excess-compound conditions. Model: Purified human cofilin 1, 5 micromolar; up to 1:100 protein:compound molar ratio, 16 hours. Limitations: Long, high-excess biochemical incubation; does not establish selectivity or occupancy after human ingestion. 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

  3. 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

  4. 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

  5. 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

  6. 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

  7. Cucurbitacin I reduced heregulin-evoked Rac1 activation in human breast-cancer cells.

    Cucurbitacin I → RAC1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human breast-cancer cell experiments; representative 0.1 micromolar exposure for 1 hour.
    limitations
    Activity change is not direct Rac1 binding.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    A movement-control switch became less active.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 156–162

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human breast-cancer cell experiments; representative 0.1 micromolar exposure for 1 hour. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-rac1 A movement-control switch became less active. Cucurbitacin I reduced heregulin-evoked Rac1 activation in human breast-cancer cells. Model: Human breast-cancer cell experiments; representative 0.1 micromolar exposure for 1 hour. Limitations: Activity change is not direct Rac1 binding. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    Complete structured claim and evidence

  8. Cucurbitacin I activated RhoA/ROCK signaling; disrupting this pathway prevented the observed Rac1 inhibition.

    Cucurbitacin I → Human RhoA / RHOA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human breast-cancer cellular perturbation experiments.
    limitations
    ROCK isoform is not resolved in this record; pathway dependence does not establish a direct cucurbitacin target.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    One cytoskeletal pathway helped suppress another.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 164–170

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human breast-cancer cellular perturbation experiments. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-rhoa-rock One cytoskeletal pathway helped suppress another. Cucurbitacin I activated RhoA/ROCK signaling; disrupting this pathway prevented the observed Rac1 inhibition. Model: Human breast-cancer cellular perturbation experiments. Limitations: ROCK isoform is not resolved in this record; pathway dependence does not establish a direct cucurbitacin target. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Silencing STAT3 or JAK2 did not reproduce cucurbitacin I-mediated Rac1 inhibition in the tested human breast-cancer cells.

    STAT3 → RAC1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    RNA interference in human breast-cancer cells.
    limitations
    Negative pathway test is limited to these endpoints and cells; it does not show that all JAK/STAT effects are absent.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Removing the familiar signaling pathway did not explain this movement effect.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 172–178

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · RNA interference in human breast-cancer cells. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-jak-stat-knockdown Removing the familiar signaling pathway did not explain this movement effect. Silencing STAT3 or JAK2 did not reproduce cucurbitacin I-mediated Rac1 inhibition in the tested human breast-cancer cells. Model: RNA interference in human breast-cancer cells. Limitations: Negative pathway test is limited to these endpoints and cells; it does not show that all JAK/STAT effects are absent. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    Complete structured claim and evidence

  2. Mito-TEMPO and NAC prevented tested cucurbitacin I effects on Rac1 activation, supporting mitochondrial ROS involvement alongside the thiol-interception caveat for NAC.

    Mito-TEMPO → RAC1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human breast-cancer pharmacology.
    limitations
    Probe rescue does not identify the ROS-generating enzyme or prove the same route after human ingestion.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    Two different probes help test the oxidative-stress route.
    primary_references
    Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293

    Cucurbitacins: thiol chemistry, cytoskeleton, metabolic dependencies and signaling (2026-09-20) · lines 180–186

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human breast-cancer pharmacology. · source_derived_draft · unverified_draft

    ## cucurbitacin-i-mitoros-rescue Two different probes help test the oxidative-stress route. Mito-TEMPO and NAC prevented tested cucurbitacin I effects on Rac1 activation, supporting mitochondrial ROS involvement alongside the thiol-interception caveat for NAC. Model: Human breast-cancer pharmacology. Limitations: Probe rescue does not identify the ROS-generating enzyme or prove the same route after human ingestion. Evidence access: Primary abstract Cucurbitacin I inhibits Rac1 activation in breast cancer cells by a reactive oxygen species-mediated mechanism and independently of Janus tyrosine kinase 2 and P-Rex1. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23478800/ · DOI 10.1124/mol.112.084293
    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