Component

Quinolinic acid

Kynurenine-pathway intermediate feeding de novo NAD synthesis.

9 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. Quinolinate at 75 micromolar opened NMDA channels in cultured rat hippocampal neurons in calcium-containing, magnesium-free recording solution.

    Quinolinic acid → Rat NMDA-type glutamate receptors, subunits unresolved source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat CA1 neuronal single-channel recording; 1.8 mM calcium.
    limitations
    Quinolinate is not tryptophan itself; bath concentration is not a dietary dose.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    One downstream metabolite activates an excitatory receptor.
    primary_references
    Quinolinate activation of N-methyl-D-aspartate ion channels in rat hippocampal neurons. · 1990 · https://pubmed.ncbi.nlm.nih.gov/1700844/ · DOI 10.1016/0304-3940(90)90098-t

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 274–280

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Rat CA1 neuronal single-channel recording; 1.8 mM calcium. · source_derived_draft · unverified_draft

    ## tryptophan-quinolinate-nmda One downstream metabolite activates an excitatory receptor. Quinolinate at 75 micromolar opened NMDA channels in cultured rat hippocampal neurons in calcium-containing, magnesium-free recording solution. Model: Rat CA1 neuronal single-channel recording; 1.8 mM calcium. Limitations: Quinolinate is not tryptophan itself; bath concentration is not a dietary dose. Evidence access: Primary abstract Quinolinate activation of N-methyl-D-aspartate ion channels in rat hippocampal neurons. · 1990 · https://pubmed.ncbi.nlm.nih.gov/1700844/ · DOI 10.1016/0304-3940(90)90098-t
    Complete structured claim and evidence

What acts on it

  1. Kmo knockout reduced quinolinate to about 3% of wild-type liver content but about 80% of wild-type brain content.

    Mouse kynurenine 3-monooxygenase / Kmo → Quinolinic acid source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    A B2-dependent step feeds the tryptophan-to-niacin pathway with tissue-specific dependence.
    evidence_location
    Results: liver Fig 4 and brain Fig 7; matching abstract conclusion
    experimental_model
    Constitutive Kmo knockout and wild-type mice, approximately two months old; liver and brain metabolite assays.
    exposure
    Constitutive Kmo deletion
    limitations
    Genetic deletion; alternative routes were proposed but not all directly traced.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Mus musculus
    plain_language
    Removing this enzyme affected downstream metabolites differently across tissues.
    primary_references
    [giorgini2013] Targeted deletion of kynurenine 3-monooxygenase in mice: a new tool for studying kynurenine pathway metabolism in periphery and brain. (2013). https://pubmed.ncbi.nlm.nih.gov/24189070/ DOI: 10.1074/jbc.m113.503813
    tissue_or_cell_type
    Liver and brain
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1248–1260

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Constitutive Kmo knockout and wild-type mice, approximately two months old; liver and brain metabolite assays. · source_derived_draft · unverified_draft

    ### b2-kmo-loss-quinolinate-tissue Kmo knockout reduced quinolinate to about 3% of wild-type liver content but about 80% of wild-type brain content. Condition category: machinery_impairment nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing this enzyme affected downstream metabolites differently across tissues. organism: Mus musculus tissue_or_cell_type: Liver and brain experimental_model: Constitutive Kmo knockout and wild-type mice, approximately two months old; liver and brain metabolite assays. limitations: Genetic deletion; alternative routes were proposed but not all directly traced. exposure: Constitutive Kmo deletion cross_nutrient: A B2-dependent step feeds the tryptophan-to-niacin pathway with tissue-specific dependence. evidence_location: Results: liver Fig 4 and brain Fig 7; matching abstract conclusion [giorgini2013] Targeted deletion of kynurenine 3-monooxygenase in mice: a new tool for studying kynurenine pathway metabolism in periphery and brain. (2013). https://pubmed.ncbi.nlm.nih.gov/24189070/ DOI: 10.1074/jbc.m113.503813
    Complete structured claim and evidence

  2. Human HAAO expressed in HEK-293 cells was enzymatically active toward 3-hydroxyanthranilate, with an apparent substrate Km near 2 micromolar in the study of the quinolinate-producing pathway step.

    Human 3-hydroxyanthranilate 3,4-dioxygenase / HAAO → Quinolinic acid source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    This step follows the canonical PLP-dependent KYNU reaction and uses a nonheme iron enzyme.
    evidence_span
    {"source_cache": "artifacts/niacin-precursors-sources/haao1994.abstract.txt", "locator": "Indexed primary abstract", "start_char": 0, "end_char": 1874, "file_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8", "text_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8"}
    experimental_model
    Human HAAO cDNA from HepG2 library, expressed in HEK-293 cells and assayed biochemically
    exposure
    Biochemical or structural assay; no dietary intervention
    limitations
    The immediate HAAO product is ACMS, which cyclizes to quinolinate; the indexed abstract uses pathway-level quinolinate wording. This claim does not assert direct NAD+ synthesis.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Homo sapiens
    plain_language
    Expressed human HAAO processed the product made by B6-dependent KYNU.
    primary_references
    [b3-pre-haao1994] Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase. (1994). https://pubmed.ncbi.nlm.nih.gov/7514594/ DOI: 10.1016/s0021-9258(17)36717-0 [b3-pre-haao2017] Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site. (2017). https://pubmed.ncbi.nlm.nih.gov/28375145/ DOI: 10.1107/s2059798317002029
    supporting_evidence_spans
    [{"source_cache": "artifacts/niacin-precursors-sources/haao2017.paragraphs.txt", "locator": "Normalized full-text paragraphs 14–14 (0-based)", "start_char": 4395, "end_char": 7197, "file_sha256": "d02386a59595104ccae2e62943e69030930da86ec005769b469f2001e31a6eb5", "text_sha256": "3b52b56d1b671c24721b47204cd30d19cd004f8a461fecd4875e94d3f491dbf6"}]
    tissue_or_cell_type
    HEK-293 cells expressing human HAAO; biochemical activity assay

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 521–535

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human HAAO cDNA from HepG2 library, expressed in HEK-293 cells and assayed biochemically · source_derived_draft · unverified_draft

    ### b3-pre-haao-human-activity Human HAAO expressed in HEK-293 cells was enzymatically active toward 3-hydroxyanthranilate, with an apparent substrate Km near 2 micromolar in the study of the quinolinate-producing pathway step. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Expressed human HAAO processed the product made by B6-dependent KYNU. organism: Homo sapiens tissue_or_cell_type: HEK-293 cells expressing human HAAO; biochemical activity assay experimental_model: Human HAAO cDNA from HepG2 library, expressed in HEK-293 cells and assayed biochemically limitations: The immediate HAAO product is ACMS, which cyclizes to quinolinate; the indexed abstract uses pathway-level quinolinate wording. This claim does not assert direct NAD+ synthesis. exposure: Biochemical or structural assay; no dietary intervention cross_nutrient: This step follows the canonical PLP-dependent KYNU reaction and uses a nonheme iron enzyme. evidence_span: {"source_cache": "artifacts/niacin-precursors-sources/haao1994.abstract.txt", "locator": "Indexed primary abstract", "start_char": 0, "end_char": 1874, "file_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8", "text_sha256": "a79697b138bcb2957b0eff9580266c7879a1c5853aba34898f891559b4e435f8"} supporting_evidence_spans: [{"source_cache": "artifacts/niacin-precursors-sources/haao2017.paragraphs.txt", "locator": "Normalized full-text paragraphs 14–14 (0-based)", "start_char": 4395, "end_char": 7197, "file_sha256": "d02386a59595104ccae2e62943e69030930da86ec005769b469f2001e31a6eb5", "text_sha256": "3b52b56d1b671c24721b47204cd30d19cd004f8a461fecd4875e94d3f491dbf6"}] [b3-pre-haao1994] Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase. (1994). https://pubmed.ncbi.nlm.nih.gov/7514594/ DOI: 10.1016/s0021-9258(17)36717-0 [b3-pre-haao2017] Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site. (2017). https://pubmed.ncbi.nlm.nih.gov/28375145/ DOI: 10.1107/s2059798317002029
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human ACMSD decarboxylates unstable ACMS, competing with its spontaneous conversion toward quinolinate in the NAD synthesis pathway.

    Human ACMS decarboxylase / ACMSD → 2-Aminomuconate-6-semialdehyde / AMS source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text, pathway and enzyme results
    experimental_model
    Human recombinant enzyme biochemistry.
    limitations
    Not evidence that zinc intake universally lowers NAD or that inhibiting this branch is always desirable.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    A branch enzyme diverts material away from the quinolinate-to-NAD route.
    primary_references
    Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveiling. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25392945/ · DOI 10.1002/prot.24722

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 226–232

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant enzyme biochemistry. · source_derived_draft · unverified_draft

    ## tryptophan-acmsd-diversion A branch enzyme diverts material away from the quinolinate-to-NAD route. Human ACMSD decarboxylates unstable ACMS, competing with its spontaneous conversion toward quinolinate in the NAD synthesis pathway. Model: Human recombinant enzyme biochemistry. Limitations: Not evidence that zinc intake universally lowers NAD or that inhibiting this branch is always desirable. Evidence access: Primary full text, pathway and enzyme results Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveiling. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25392945/ · DOI 10.1002/prot.24722
    Complete structured claim and evidence

  2. ACMSD inhibition increased de novo NAD synthesis and SIRT1-related mitochondrial function in the mouse experiments.

    Mouse ACMS decarboxylase / Acmsd → NAD+ source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Mouse genetic/pharmacological work within a study also using C. elegans.
    limitations
    Not a human longevity outcome or evidence for tryptophan megadoses.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    Restricting one exit route increased flow toward NAD in a preclinical model.
    primary_references
    De novo NAD+ synthesis enhances mitochondrial function and improves health. · 2018 · https://pubmed.ncbi.nlm.nih.gov/30356218/ · DOI 10.1038/s41586-018-0645-6

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 234–240

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse genetic/pharmacological work within a study also using C. elegans. · source_derived_draft · unverified_draft

    ## tryptophan-acmsd-inhibition-nad Restricting one exit route increased flow toward NAD in a preclinical model. ACMSD inhibition increased de novo NAD synthesis and SIRT1-related mitochondrial function in the mouse experiments. Model: Mouse genetic/pharmacological work within a study also using C. elegans. Limitations: Not a human longevity outcome or evidence for tryptophan megadoses. Evidence access: Primary abstract De novo NAD+ synthesis enhances mitochondrial function and improves health. · 2018 · https://pubmed.ncbi.nlm.nih.gov/30356218/ · DOI 10.1038/s41586-018-0645-6
    Complete structured claim and evidence

  3. Adding 30 micromolar magnesium reduced quinolinate-activated NMDA channel mean open time to about one-third at minus 100 mV.

    Mg2+ → Rat NMDA-type glutamate receptors, subunits unresolved source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat hippocampal patch-clamp experiment.
    limitations
    Does not establish that oral magnesium prevents quinolinate-related disease.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    Magnesium and membrane voltage changed the receptor response.
    primary_references
    Quinolinate activation of N-methyl-D-aspartate ion channels in rat hippocampal neurons. · 1990 · https://pubmed.ncbi.nlm.nih.gov/1700844/ · DOI 10.1016/0304-3940(90)90098-t

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 282–288

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Rat hippocampal patch-clamp experiment. · source_derived_draft · unverified_draft

    ## tryptophan-magnesium-nmda Magnesium and membrane voltage changed the receptor response. Adding 30 micromolar magnesium reduced quinolinate-activated NMDA channel mean open time to about one-third at minus 100 mV. Model: Rat hippocampal patch-clamp experiment. Limitations: Does not establish that oral magnesium prevents quinolinate-related disease. Evidence access: Primary abstract Quinolinate activation of N-methyl-D-aspartate ion channels in rat hippocampal neurons. · 1990 · https://pubmed.ncbi.nlm.nih.gov/1700844/ · DOI 10.1016/0304-3940(90)90098-t
    Complete structured claim and evidence

  4. Qprt-heterozygous mice had higher quinolinate, lower NAD and greater acute kidney injury susceptibility.

    Mouse quinolinate phosphoribosyltransferase / Qprt → Mouse acute kidney injury susceptibility source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Mouse Qprt heterozygous deletion.
    limitations
    No inference that more tryptophan fixes the blocked step.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    Less conversion machinery increased vulnerability despite accumulated precursor.
    primary_references
    De novo NAD+ biosynthetic impairment in acute kidney injury in humans. · 2018 · https://pubmed.ncbi.nlm.nih.gov/30127395/ · DOI 10.1038/s41591-018-0138-z
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 250–256

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse Qprt heterozygous deletion. · source_derived_draft · unverified_draft

    ## tryptophan-qprt-dosage Less conversion machinery increased vulnerability despite accumulated precursor. Qprt-heterozygous mice had higher quinolinate, lower NAD and greater acute kidney injury susceptibility. Model: Mouse Qprt heterozygous deletion. Limitations: No inference that more tryptophan fixes the blocked step. Evidence access: Primary abstract De novo NAD+ biosynthetic impairment in acute kidney injury in humans. · 2018 · https://pubmed.ncbi.nlm.nih.gov/30127395/ · DOI 10.1038/s41591-018-0138-z
    Complete structured claim and evidence

  5. Mouse acute kidney injury reduced renal QPRT and NAD while quinolinate accumulated.

    Mouse quinolinate phosphoribosyltransferase / Qprt → Mouse renal NAD abundance source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Mouse acute kidney injury measurements.
    limitations
    Co-occurrence alone is not the complete causal test; Qprt dosage manipulation is recorded separately.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    An upstream metabolite can rise while the useful downstream product falls.
    primary_references
    De novo NAD+ biosynthetic impairment in acute kidney injury in humans. · 2018 · https://pubmed.ncbi.nlm.nih.gov/30127395/ · DOI 10.1038/s41591-018-0138-z
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 242–248

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse acute kidney injury measurements. · source_derived_draft · unverified_draft

    ## tryptophan-qprt-injury An upstream metabolite can rise while the useful downstream product falls. Mouse acute kidney injury reduced renal QPRT and NAD while quinolinate accumulated. Model: Mouse acute kidney injury measurements. Limitations: Co-occurrence alone is not the complete causal test; Qprt dosage manipulation is recorded separately. Evidence access: Primary abstract De novo NAD+ biosynthetic impairment in acute kidney injury in humans. · 2018 · https://pubmed.ncbi.nlm.nih.gov/30127395/ · DOI 10.1038/s41591-018-0138-z
    Complete structured claim and evidence

  6. Human QPRT converts quinolinate and PRPP toward nicotinic acid mononucleotide; the human enzyme structures resolve reactant quinolinate and product NaMN complexes.

    Human quinolinate phosphoribosyltransferase / QPRT → Nicotinic acid mononucleotide source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/niacin-precursors-sources/qprt2016.paragraphs.txt", "locator": "Normalized full-text paragraphs 13–15 (0-based)", "start_char": 10597, "end_char": 15612, "file_sha256": "85fcc4a79a17f4f3846301f67698a444c3c9930829e167d86a96adbb72d830e6", "text_sha256": "8da78d25a53af6507018eece4ce553705dc505d0b169f678affad49ee21b10f6"}
    experimental_model
    Purified recombinant human QPRT crystallography, calorimetry and oligomer studies
    exposure
    Biochemical or structural assay; no dietary intervention
    limitations
    Structural and biochemical enzyme study; does not establish how much dietary tryptophan becomes NAD in a person.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Homo sapiens
    plain_language
    Quinolinate enters the same deamidated mononucleotide route used by nicotinic acid.
    primary_references
    [b3-pre-qprt2016] Structural Insights into the Quaternary Catalytic Mechanism of Hexameric Human Quinolinate Phosphoribosyltransferase, a Key Enzyme in de novo NAD Biosynthesis. (2016). https://pubmed.ncbi.nlm.nih.gov/26805589/ DOI: 10.1038/srep19681
    supporting_evidence_spans
    [{"source_cache": "artifacts/niacin-precursors-sources/qprt2016.paragraphs.txt", "locator": "Normalized full-text paragraphs 4–4 (0-based)", "start_char": 1453, "end_char": 3871, "file_sha256": "85fcc4a79a17f4f3846301f67698a444c3c9930829e167d86a96adbb72d830e6", "text_sha256": "be14ed97ccf53b635f2cb35969188ce42c84dd739db897a24cbf3e65d8a3e3d1"}]
    tissue_or_cell_type
    Purified recombinant protein; no intact tissue

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 537–549

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human QPRT crystallography, calorimetry and oligomer studies · source_derived_draft · unverified_draft

    ### b3-pre-qprt-namn Human QPRT converts quinolinate and PRPP toward nicotinic acid mononucleotide; the human enzyme structures resolve reactant quinolinate and product NaMN complexes. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Quinolinate enters the same deamidated mononucleotide route used by nicotinic acid. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Purified recombinant human QPRT crystallography, calorimetry and oligomer studies limitations: Structural and biochemical enzyme study; does not establish how much dietary tryptophan becomes NAD in a person. exposure: Biochemical or structural assay; no dietary intervention evidence_span: {"source_cache": "artifacts/niacin-precursors-sources/qprt2016.paragraphs.txt", "locator": "Normalized full-text paragraphs 13–15 (0-based)", "start_char": 10597, "end_char": 15612, "file_sha256": "85fcc4a79a17f4f3846301f67698a444c3c9930829e167d86a96adbb72d830e6", "text_sha256": "8da78d25a53af6507018eece4ce553705dc505d0b169f678affad49ee21b10f6"} supporting_evidence_spans: [{"source_cache": "artifacts/niacin-precursors-sources/qprt2016.paragraphs.txt", "locator": "Normalized full-text paragraphs 4–4 (0-based)", "start_char": 1453, "end_char": 3871, "file_sha256": "85fcc4a79a17f4f3846301f67698a444c3c9930829e167d86a96adbb72d830e6", "text_sha256": "be14ed97ccf53b635f2cb35969188ce42c84dd739db897a24cbf3e65d8a3e3d1"}] [b3-pre-qprt2016] Structural Insights into the Quaternary Catalytic Mechanism of Hexameric Human Quinolinate Phosphoribosyltransferase, a Key Enzyme in de novo NAD Biosynthesis. (2016). https://pubmed.ncbi.nlm.nih.gov/26805589/ DOI: 10.1038/srep19681
    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