Component

Human microtubule-associated protein tau / MAPT

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

7 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. Lithium reduced tau phosphorylation through reversible GSK3 inhibition in human NT2N neurons.

    Lithium ion (Li+) → Human microtubule-associated protein tau / MAPT source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cultured human NT2N neurons.
    limitations
    Does not demonstrate dementia prevention in people.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    A signaling enzyme changes chemical marks on a structural protein.
    primary_references
    Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9312151/ · DOI 10.1074/jbc.272.40.25326

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 176–182

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cultured human NT2N neurons. · source_derived_draft · unverified_draft

    ## lithium-tau-phosphorylation A signaling enzyme changes chemical marks on a structural protein. Lithium reduced tau phosphorylation through reversible GSK3 inhibition in human NT2N neurons. Model: Cultured human NT2N neurons. Limitations: Does not demonstrate dementia prevention in people. Evidence access: Primary abstract Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9312151/ · DOI 10.1074/jbc.272.40.25326
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The reagent reduced tau HTRF aggregation signals, while tau BiFC-positive cell frequency was unchanged.

    Defined fungal fulvic acid / CAS 479-66-3 → Tau aggregation readouts in human HEK293 cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    2020 study; Cayman CAS 479-66-3 at 37 micromolar; HEK293 constructs or purified K18 tau as specified. Twelve-hour treatment following co-culture.
    limitations
    The methods identify a defined fungal compound, not an interchangeable environmental mixture. Supplier identity: https://www.caymanchem.com/product/19063/fulvic-acid . No clinical efficacy or CNS exposure was measured. Assay differences are retained rather than collapsed into universal suppression.
    nutrient_topic
    Fulvic acid collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Fulvic acid (heterogeneous humic fraction)
    plain_language
    Two assays measured different aspects of the tau response.
    primary_references
    Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32732936/ · DOI 10.1038/s41598-020-69744-y

    Fulvic acid: mixture identity, mineral chemistry, signaling and cross-nutrient mechanisms (2026-09-19) · lines 172–178

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · 2020 study; Cayman CAS 479-66-3 at 37 micromolar; HEK293 constructs or purified K18 tau as specified. Twelve-hour treatment following co-culture. · source_derived_draft · unverified_draft

    ## fulvic-acid-defined-cell-tau Two assays measured different aspects of the tau response. The reagent reduced tau HTRF aggregation signals, while tau BiFC-positive cell frequency was unchanged. Model: 2020 study; Cayman CAS 479-66-3 at 37 micromolar; HEK293 constructs or purified K18 tau as specified. Twelve-hour treatment following co-culture. Limitations: The methods identify a defined fungal compound, not an interchangeable environmental mixture. Supplier identity: https://www.caymanchem.com/product/19063/fulvic-acid . No clinical efficacy or CNS exposure was measured. Assay differences are retained rather than collapsed into universal suppression. Evidence access: Primary full text Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32732936/ · DOI 10.1038/s41598-020-69744-y
    Complete structured claim and evidence

  2. The specified reagent reduced K18 tau aggregation in RT-QuIC assays.

    Defined fungal fulvic acid / CAS 479-66-3 → Human tau K18 amplification assay source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    2020 study; Cayman CAS 479-66-3 at 37 micromolar; HEK293 constructs or purified K18 tau as specified.
    limitations
    The methods identify a defined fungal compound, not an interchangeable environmental mixture. Supplier identity: https://www.caymanchem.com/product/19063/fulvic-acid . No clinical efficacy or CNS exposure was measured.
    nutrient_topic
    Fulvic acid collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Fulvic acid (heterogeneous humic fraction)
    plain_language
    The defined research chemical slowed an in-vitro aggregation readout.
    primary_references
    Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32732936/ · DOI 10.1038/s41598-020-69744-y

    Fulvic acid: mixture identity, mineral chemistry, signaling and cross-nutrient mechanisms (2026-09-19) · lines 164–170

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · 2020 study; Cayman CAS 479-66-3 at 37 micromolar; HEK293 constructs or purified K18 tau as specified. · source_derived_draft · unverified_draft

    ## fulvic-acid-defined-tau-k18 The defined research chemical slowed an in-vitro aggregation readout. The specified reagent reduced K18 tau aggregation in RT-QuIC assays. Model: 2020 study; Cayman CAS 479-66-3 at 37 micromolar; HEK293 constructs or purified K18 tau as specified. Limitations: The methods identify a defined fungal compound, not an interchangeable environmental mixture. Supplier identity: https://www.caymanchem.com/product/19063/fulvic-acid . No clinical efficacy or CNS exposure was measured. Evidence access: Primary full text Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32732936/ · DOI 10.1038/s41598-020-69744-y
    Complete structured claim and evidence

  3. The tested fulvic preparation reduced tau filament formation in vitro.

    Fulvic preparation in 2011 tau study, identity unresolved here → Tau paired-helical-filament assembly in vitro source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free tau aggregation and atomic-force microscopy.
    limitations
    Preparation identity and concentration are not resolved from the accessed abstract; no brain delivery or Alzheimer efficacy is demonstrated.
    nutrient_topic
    Fulvic acid collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Fulvic acid (heterogeneous humic fraction)
    plain_language
    One preparation interfered with fibril assembly.
    primary_references
    Fulvic acid inhibits aggregation and promotes disassembly of tau fibrils associated with Alzheimer's disease. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21785188/ · DOI 10.3233/JAD-2011-110623

    Fulvic acid: mixture identity, mineral chemistry, signaling and cross-nutrient mechanisms (2026-09-19) · lines 148–154

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free tau aggregation and atomic-force microscopy. · source_derived_draft · unverified_draft

    ## fulvic-acid-tau-assembly One preparation interfered with fibril assembly. The tested fulvic preparation reduced tau filament formation in vitro. Model: Cell-free tau aggregation and atomic-force microscopy. Limitations: Preparation identity and concentration are not resolved from the accessed abstract; no brain delivery or Alzheimer efficacy is demonstrated. Evidence access: Primary abstract Fulvic acid inhibits aggregation and promotes disassembly of tau fibrils associated with Alzheimer's disease. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21785188/ · DOI 10.3233/JAD-2011-110623
    Complete structured claim and evidence

  4. Exposure altered preformed tau fibrils, including shorter filaments.

    Fulvic preparation in 2011 tau study, identity unresolved here → Preformed tau paired-helical-filament length and morphology source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Cell-free atomic-force microscopy.
    limitations
    Proposed hydrophobic interaction is not a verified binding site; smaller structures need not be non-toxic.
    nutrient_topic
    Fulvic acid collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Fulvic acid (heterogeneous humic fraction)
    plain_language
    Already formed fibrils changed in the assay.
    primary_references
    Fulvic acid inhibits aggregation and promotes disassembly of tau fibrils associated with Alzheimer's disease. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21785188/ · DOI 10.3233/JAD-2011-110623

    Fulvic acid: mixture identity, mineral chemistry, signaling and cross-nutrient mechanisms (2026-09-19) · lines 156–162

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Cell-free atomic-force microscopy. · source_derived_draft · unverified_draft

    ## fulvic-acid-tau-disassembly Already formed fibrils changed in the assay. Exposure altered preformed tau fibrils, including shorter filaments. Model: Cell-free atomic-force microscopy. Limitations: Proposed hydrophobic interaction is not a verified binding site; smaller structures need not be non-toxic. Evidence access: Primary abstract Fulvic acid inhibits aggregation and promotes disassembly of tau fibrils associated with Alzheimer's disease. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21785188/ · DOI 10.3233/JAD-2011-110623
    Complete structured claim and evidence

  5. A 71-person ten-week AD trial found no treatment effect on CSF biomarkers or lymphocyte GSK3 activity.

    Lithium carbonate → Human AD trial CSF tau and lymphocyte GSK3 outcomes source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Mild AD; six-week titration; serum target 0.5–0.8 mmol/L.
    limitations
    Short duration and different disease stage; neither proves lifelong efficacy nor rules out every regimen.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    A cell mechanism did not translate into measured target effects in this trial.
    primary_references
    Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19573486/

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 552–558

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mild AD; six-week titration; serum target 0.5–0.8 mmol/L. · source_derived_draft · unverified_draft

    ## lithium-ad-short-null A cell mechanism did not translate into measured target effects in this trial. A 71-person ten-week AD trial found no treatment effect on CSF biomarkers or lymphocyte GSK3 activity. Model: Mild AD; six-week titration; serum target 0.5–0.8 mmol/L. Limitations: Short duration and different disease stage; neither proves lifelong efficacy nor rules out every regimen. Evidence access: Primary abstract Lithium trial in Alzheimer's disease: a randomized, single-blind, placebo-controlled, multicenter 10-week study. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19573486/
    Complete structured claim and evidence

  6. Lithium increased tau–microtubule binding and microtubule assembly in the NT2N study.

    Lithium ion (Li+) → Human NT2N tau binding to microtubules source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human neuron-like cell culture.
    limitations
    Same paper as the tau-phosphorylation result, not independent replication.
    nutrient_topic
    Lithium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Lithium
    plain_language
    The altered protein interacted more strongly with the cellular scaffold.
    primary_references
    Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9312151/ · DOI 10.1074/jbc.272.40.25326

    Lithium: metal-sensitive enzymes, transport and cross-nutrient mechanisms (2026-09-19) · lines 184–190

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human neuron-like cell culture. · source_derived_draft · unverified_draft

    ## lithium-tau-microtubules The altered protein interacted more strongly with the cellular scaffold. Lithium increased tau–microtubule binding and microtubule assembly in the NT2N study. Model: Human neuron-like cell culture. Limitations: Same paper as the tau-phosphorylation result, not independent replication. Evidence access: Primary abstract Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9312151/ · DOI 10.1074/jbc.272.40.25326
    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.

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