Component

Amyloid-beta fibrils, sequence specified by study

Study-scoped entity; inspect species, exposure, model and limitations on each claim.

8 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. Nattokinase degraded amyloid fibrils in vitro, and the study determined the conditions under which it does so.

    Nattokinase / subtilisin NAT → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified fibril preparations
    exposure
    Nattokinase
    limitations
    In vitro proteolysis of a purified fibril preparation. It says nothing about oral dosing, brain entry or clinical benefit in any amyloid disease.
    organism
    Purified fibril preparations
    plain_language
    Nattokinase degraded amyloid fibrils in vitro, and the study determined the conditions under which it does so.
    primary_references
    Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. (2009) https://pubmed.ncbi.nlm.nih.gov/19117402/ DOI: 10.1021/jf803072r
    route
    In vitro
    tissue
    In vitro fibril proteolysis

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 202–202

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified fibril preparations · source_derived_draft · unverified_draft

    Nattokinase degraded amyloid fibrils in vitro, and the study determined the conditions under which it does so.
    Complete structured claim and evidence

  2. Plasmin did not degrade the fibrils that nattokinase, proteinase K and subtilisin Carlsberg degraded.

    Plasmin → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified fibril preparations
    exposure
    Plasmin
    limitations
    This measured null is the informative half of the comparison: the activity tracks the subtilisin family rather than proteolysis in general.
    organism
    Purified fibril preparations
    plain_language
    Plasmin did not degrade the fibrils that nattokinase, proteinase K and subtilisin Carlsberg degraded.
    primary_references
    Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. (2009) https://pubmed.ncbi.nlm.nih.gov/19117402/ DOI: 10.1021/jf803072r
    route
    In vitro
    tissue
    In vitro fibril proteolysis

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 235–235

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified fibril preparations · source_derived_draft · unverified_draft

    Plasmin did not degrade the fibrils that nattokinase, proteinase K and subtilisin Carlsberg degraded.
    Complete structured claim and evidence

  3. Proteinase K degraded the same amyloid fibrils.

    Proteinase K → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified fibril preparations
    exposure
    Proteinase K
    limitations
    As above.
    organism
    Purified fibril preparations
    plain_language
    Proteinase K degraded the same amyloid fibrils.
    primary_references
    Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. (2009) https://pubmed.ncbi.nlm.nih.gov/19117402/ DOI: 10.1021/jf803072r
    route
    In vitro
    tissue
    In vitro fibril proteolysis

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 224–224

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified fibril preparations · source_derived_draft · unverified_draft

    Proteinase K degraded the same amyloid fibrils.
    Complete structured claim and evidence

  4. Subtilisin Carlsberg degraded the same amyloid fibrils.

    Subtilisin Carlsberg → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified fibril preparations
    exposure
    Subtilisin Carlsberg
    limitations
    Recorded because it removes the uniqueness of the nattokinase result, not because subtilisin Carlsberg is of interest here in itself.
    organism
    Purified fibril preparations
    plain_language
    Subtilisin Carlsberg degraded the same amyloid fibrils.
    primary_references
    Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. (2009) https://pubmed.ncbi.nlm.nih.gov/19117402/ DOI: 10.1021/jf803072r
    route
    In vitro
    tissue
    In vitro fibril proteolysis

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 213–213

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified fibril preparations · source_derived_draft · unverified_draft

    Subtilisin Carlsberg degraded the same amyloid fibrils.
    Complete structured claim and evidence

  5. Trypsin likewise did not degrade the fibrils.

    Trypsin → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
    Experimental context and source evidence
    duration
    Not stated here
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    experimental_model
    Purified fibril preparations
    exposure
    Trypsin
    limitations
    The second measured null in the same comparison.
    organism
    Purified fibril preparations
    plain_language
    Trypsin likewise did not degrade the fibrils.
    primary_references
    Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. (2009) https://pubmed.ncbi.nlm.nih.gov/19117402/ DOI: 10.1021/jf803072r
    route
    In vitro
    tissue
    In vitro fibril proteolysis

    Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 246–246

    Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Purified fibril preparations · source_derived_draft · unverified_draft

    Trypsin likewise did not degrade the fibrils.
    Complete structured claim and evidence

  6. EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers.

    Epigallocatechin-3-gallate (EGCG) → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Mature amyloid-beta and alpha-synuclein fibril preparations.
    limitations
    This does not show removal of deposits from a human brain.
    nutrient_topic
    EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
    plain_language
    EGCG changed pre-existing aggregates in a laboratory experiment.
    primary_references
    EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107

    EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 356–362

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mature amyloid-beta and alpha-synuclein fibril preparations. · source_derived_draft · unverified_draft

    ## egcg-ab-remodel EGCG changed pre-existing aggregates in a laboratory experiment. EGCG bound mature fibrils and remodeled them into smaller amorphous aggregates without measured release of monomers or small diffusible oligomers. Model: Mature amyloid-beta and alpha-synuclein fibril preparations. Limitations: This does not show removal of deposits from a human brain. Evidence access: primary abstract. EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20385841/ · DOI 10.1073/pnas.0910723107
    Complete structured claim and evidence

  7. Remodeling of the tested mature amyloid preparations depended on EGCG autooxidation.

    Oxidized EGCG reaction products, unresolved mixture → Amyloid-beta fibrils, sequence specified by study source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Amyloid-beta 1–40 and IAPP/Sup35 fragment preparations.
    limitations
    Fragment and in-vitro oxidation contexts limit generalization.
    nutrient_topic
    EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
    plain_language
    The oxidation state helped determine aggregate remodeling.
    primary_references
    Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23611538/ · DOI 10.1021/ja3115696

    EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 380–386

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Amyloid-beta 1–40 and IAPP/Sup35 fragment preparations. · source_derived_draft · unverified_draft

    ## egcg-oxidation-remodel The oxidation state helped determine aggregate remodeling. Remodeling of the tested mature amyloid preparations depended on EGCG autooxidation. Model: Amyloid-beta 1–40 and IAPP/Sup35 fragment preparations. Limitations: Fragment and in-vitro oxidation contexts limit generalization. Evidence access: primary abstract. Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23611538/ · DOI 10.1021/ja3115696
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. EGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system.

    Epigallocatechin-3-gallate (EGCG) → Amyloid fibril formation in specified assays source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Biophysical and cell-based aggregation experiments.
    limitations
    Not evidence of preventing or treating human neurodegenerative disease.
    nutrient_topic
    EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
    plain_language
    EGCG changed how these proteins assembled.
    primary_references
    EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18511942/ · DOI 10.1038/nsmb.1437

    EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 348–354

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Biophysical and cell-based aggregation experiments. · source_derived_draft · unverified_draft

    ## egcg-amyloid-initiation EGCG changed how these proteins assembled. EGCG bound unfolded amyloid-beta and alpha-synuclein and redirected assembly toward unstructured, relatively nontoxic oligomers in the experimental system. Model: Biophysical and cell-based aggregation experiments. Limitations: Not evidence of preventing or treating human neurodegenerative disease. Evidence access: primary abstract. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. · 2008 · https://pubmed.ncbi.nlm.nih.gov/18511942/ · DOI 10.1038/nsmb.1437
    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