Component

Human ERK1/ERK2 kinases

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

4 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. Oxidative-stress experiments identified ERK-dependent MARS1 phosphorylation at Ser209 and Ser825.

    Human ERK1/ERK2 kinases → Human cytosolic methionyl-tRNA synthetase / MARS1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human HeLa/HEK293T cells, kinase assays and site-directed mutants.
    limitations
    Arsenite/peroxide and engineered constructs do not represent routine dietary exposure.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Stress signaling changes how the charging enzyme behaves.
    primary_references
    Promiscuous methionyl-tRNA synthetase mediates adaptive mistranslation to protect cells against oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25097229/ · DOI 10.1242/jcs.152470

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 68–74

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human HeLa/HEK293T cells, kinase assays and site-directed mutants. · source_derived_draft · unverified_draft

    ## methionine-mars-phosphorylation Stress signaling changes how the charging enzyme behaves. Oxidative-stress experiments identified ERK-dependent MARS1 phosphorylation at Ser209 and Ser825. Model: Human HeLa/HEK293T cells, kinase assays and site-directed mutants. Limitations: Arsenite/peroxide and engineered constructs do not represent routine dietary exposure. Evidence access: Primary full text Promiscuous methionyl-tRNA synthetase mediates adaptive mistranslation to protect cells against oxidative stress. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25097229/ · DOI 10.1242/jcs.152470
    Complete structured claim and evidence

What acts on it

  1. Fulvic pretreatment reduced homocysteine-stimulated ERK phosphorylation.

    Esther Material Technology fulvic preparation, 2015 study → Human ERK1/ERK2 kinases source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human primary monocytes and U937 cells; Esther 20% stock diluted to 0.5-10 micrograms/mL, 4-hour pretreatment; homocysteine stimulation.
    limitations
    Cell exposure does not establish oral exposure, homocysteine removal or cardiovascular benefit. Results text reports homocysteine 200 micromolar, while figure captions say 200 micrograms/mL; dose units are unresolved. Inhibitor concentrations also need original-record clarification.
    nutrient_topic
    Fulvic acid collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Fulvic acid (heterogeneous humic fraction)
    plain_language
    The preparation dampened the ERK response.
    primary_references
    Fulvic acid attenuates homocysteine-induced cyclooxygenase-2 expression in human monocytes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25888188/ · DOI 10.1186/s12906-015-0583-x

    Fulvic acid: mixture identity, mineral chemistry, signaling and cross-nutrient mechanisms (2026-09-19) · lines 36–42

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human primary monocytes and U937 cells; Esther 20% stock diluted to 0.5-10 micrograms/mL, 4-hour pretreatment; homocysteine stimulation. · source_derived_draft · unverified_draft

    ## fulvic-acid-fa-erk The preparation dampened the ERK response. Fulvic pretreatment reduced homocysteine-stimulated ERK phosphorylation. Model: Human primary monocytes and U937 cells; Esther 20% stock diluted to 0.5-10 micrograms/mL, 4-hour pretreatment; homocysteine stimulation. Limitations: Cell exposure does not establish oral exposure, homocysteine removal or cardiovascular benefit. Results text reports homocysteine 200 micromolar, while figure captions say 200 micrograms/mL; dose units are unresolved. Inhibitor concentrations also need original-record clarification. Evidence access: Primary full text Fulvic acid attenuates homocysteine-induced cyclooxygenase-2 expression in human monocytes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25888188/ · DOI 10.1186/s12906-015-0583-x
    Complete structured claim and evidence

  2. Added homocysteine increased ERK phosphorylation in U937 cells.

    Homocysteine → Human ERK1/ERK2 kinases source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Human primary monocytes and U937 cells; Esther 20% stock diluted to 0.5-10 micrograms/mL, 4-hour pretreatment; homocysteine stimulation.
    limitations
    Cell exposure does not establish oral exposure, homocysteine removal or cardiovascular benefit. Results text reports homocysteine 200 micromolar, while figure captions say 200 micrograms/mL; dose units are unresolved. Inhibitor concentrations also need original-record clarification.
    nutrient_topic
    Fulvic acid collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Fulvic acid (heterogeneous humic fraction)
    plain_language
    Homocysteine activated an inflammatory signaling branch.
    primary_references
    Fulvic acid attenuates homocysteine-induced cyclooxygenase-2 expression in human monocytes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25888188/ · DOI 10.1186/s12906-015-0583-x

    Fulvic acid: mixture identity, mineral chemistry, signaling and cross-nutrient mechanisms (2026-09-19) · lines 20–26

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human primary monocytes and U937 cells; Esther 20% stock diluted to 0.5-10 micrograms/mL, 4-hour pretreatment; homocysteine stimulation. · source_derived_draft · unverified_draft

    ## fulvic-acid-hcy-erk Homocysteine activated an inflammatory signaling branch. Added homocysteine increased ERK phosphorylation in U937 cells. Model: Human primary monocytes and U937 cells; Esther 20% stock diluted to 0.5-10 micrograms/mL, 4-hour pretreatment; homocysteine stimulation. Limitations: Cell exposure does not establish oral exposure, homocysteine removal or cardiovascular benefit. Results text reports homocysteine 200 micromolar, while figure captions say 200 micrograms/mL; dose units are unresolved. Inhibitor concentrations also need original-record clarification. Evidence access: Primary full text Fulvic acid attenuates homocysteine-induced cyclooxygenase-2 expression in human monocytes. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25888188/ · DOI 10.1186/s12906-015-0583-x
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Bromelain dose-dependently blocked Salmonella Typhimurium-induced ERK1/2 and JNK activation in human Caco-2 cells.

    Bromelain → Salmonella-induced ERK/JNK activation in Caco-2 cells source_derived_draftungraded
    Experimental context and source evidence
    dose
    Bromelain with Salmonella Typhimurium
    duration
    Acute infection assay
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    evidence_scope
    literature_reviewed; model-specific source-derived curation
    experimental_model
    Human Caco-2 intestinal epithelial cells
    limitations
    Blocking these kinase signals did not prevent invasion or barrier-resistance loss in the same study.
    nutrient_topic
    Bromelain chapter; interacting nutrients, drugs, peptides and proteins retain their experimental settings. · Bromelain
    organism
    Human Caco-2 intestinal epithelial cells
    plain_language
    Bromelain dose-dependently blocked Salmonella Typhimurium-induced ERK1/2 and JNK activation in human Caco-2 cells.
    primary_references
    Proteolytic inhibition of Salmonella enterica serovar typhimurium-induced activation of the mitogen-activated protein kinases ERK and JNK in cultured human intestinal cells. (2002). https://pubmed.ncbi.nlm.nih.gov/11748167/ DOI: 10.1128/IAI.70.1.86-95.2002
    route
    In vitro
    tissue
    ERK1/2 and JNK phosphorylation

    Bromelain: mechanism of action and interactions (2026-09-20) · lines 77–86

    Original AI-assisted source-specific curation with primary-study citations, model, exposure, route, duration, negative findings and limitations preserved. Not publisher full text. · supports · Human Caco-2 intestinal epithelial cells · source_derived_draft · unverified_draft

    ## bromelain-mapk-blockade Bromelain dose-dependently blocked Salmonella Typhimurium-induced ERK1/2 and JNK activation in human Caco-2 cells. Model/species: Human Caco-2 intestinal epithelial cells Tissue/system: ERK1/2 and JNK phosphorylation Exposure: Bromelain with Salmonella Typhimurium Route: In vitro Duration: Acute infection assay Limits: Blocking these kinase signals did not prevent invasion or barrier-resistance loss in the same study. Primary reference: Proteolytic inhibition of Salmonella enterica serovar typhimurium-induced activation of the mitogen-activated protein kinases ERK and JNK in cultured human intestinal cells. (2002). https://pubmed.ncbi.nlm.nih.gov/11748167/ DOI: 10.1128/IAI.70.1.86-95.2002 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    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