Component

Human cofilin 1 / CFL1

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

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

    Cucurbitacin D → 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 12–18

    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-d-cofilin-adduct Protein cysteines can become chemical attachment sites. Incubating purified human cofilin 1 with cucurbitacin D 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

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

    Cucurbitacin E → 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 20–26

    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-e-cofilin-adduct Protein cysteines can become chemical attachment sites. Incubating purified human cofilin 1 with cucurbitacin E 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. Mass spectrometry localized cucurbitacin E modification to cofilin Cys39, Cys80 and Cys139, with weaker evidence for Cys147.

    Cucurbitacin E → Human cofilin 1 / CFL1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text PMC3751690
    experimental_model
    Purified human cofilin 1 biochemical mapping.
    limitations
    A protein cysteine residue is not equivalent to free dietary cysteine; these data do not quantify nutritional depletion.
    nutrient_topic
    Cucurbitacins collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Cucurbitacins
    plain_language
    The study identifies individual protein 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 36–42

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human cofilin 1 biochemical mapping. · source_derived_draft · unverified_draft

    ## cucurbitacin-e-cofilin-sites The study identifies individual protein attachment sites. Mass spectrometry localized cucurbitacin E modification to cofilin Cys39, Cys80 and Cys139, with weaker evidence for Cys147. Model: Purified human cofilin 1 biochemical mapping. Limitations: A protein cysteine residue is not equivalent to free dietary cysteine; these data do not quantify nutritional depletion. 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

  4. 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

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