Component

Mitochondrial matrix

Internal mitochondrial compartment where the curated NAD and thioredoxin reactions are situated.

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

Where it participates (unsigned role)

  1. MICU1 knockdown elevates basal matrix calcium through MCU-dependent uptake in the tested cells.

    Mitochondrial calcium uptake protein 1 / MICU1 → Mitochondrial calcium overload source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    compartment_description
    Mitochondrial matrix
    experimental_model
    HeLa, HEK293 and human endothelial-cell knockdown; calcium-flux and stress assays
    limitations
    Cell-specific knockdown response; does not imply high dietary calcium or all MICU1 variants behave identically.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    Loss of MICU1 can let mitochondria accumulate too much calcium at rest.
    primary_references
    [ca-mallilankaraman2012] MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca2+ uptake that regulates cell survival (2012). https://pubmed.ncbi.nlm.nih.gov/23101630/ DOI: 10.1016/j.cell.2012.10.011
    research_relationship_category
    loss_of_function
    tissue_or_cell_type
    HeLa and endothelial cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Calcium: mechanism-first literature curation (2026-09-17) · lines 719–730

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · HeLa, HEK293 and human endothelial-cell knockdown; calcium-flux and stress assays · source_derived_draft · unverified_draft

    ### ca-micu1-loss-overload MICU1 knockdown elevates basal matrix calcium through MCU-dependent uptake in the tested cells. Condition category: machinery_impairment nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Loss of MICU1 can let mitochondria accumulate too much calcium at rest. organism: Homo sapiens tissue_or_cell_type: HeLa and endothelial cells experimental_model: HeLa, HEK293 and human endothelial-cell knockdown; calcium-flux and stress assays limitations: Cell-specific knockdown response; does not imply high dietary calcium or all MICU1 variants behave identically. research_relationship_category: loss_of_function compartment_description: Mitochondrial matrix [ca-mallilankaraman2012] MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca2+ uptake that regulates cell survival (2012). https://pubmed.ncbi.nlm.nih.gov/23101630/ DOI: 10.1016/j.cell.2012.10.011
    Complete structured claim and evidence

  2. Calcium-overload conditions induce cyclophilin-D-sensitive mitochondrial permeability transition and swelling in the tested mouse preparations.

    Calcium ion → Mitochondrial permeability transition source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Inner mitochondrial membrane and matrix
    experimental_model
    Ppif-null and cyclophilin-D-overexpressing mice; isolated mitochondria, hepatocytes and fibroblasts
    limitations
    Experimental overload; not all apoptosis uses this pathway and the study does not settle the molecular identity of the pore.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mus musculus
    plain_language
    Excess mitochondrial calcium can trigger membrane permeability failure.
    primary_references
    [ca-baines2005] Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death (2005). https://pubmed.ncbi.nlm.nih.gov/15800627/ DOI: 10.1038/nature03434
    research_relationship_category
    exposure_response
    tissue_or_cell_type
    Isolated liver, heart and brain mitochondria

    Calcium: mechanism-first literature curation (2026-09-17) · lines 836–847

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ppif-null and cyclophilin-D-overexpressing mice; isolated mitochondria, hepatocytes and fibroblasts · source_derived_draft · unverified_draft

    ### ca-overload-permeability-transition Calcium-overload conditions induce cyclophilin-D-sensitive mitochondrial permeability transition and swelling in the tested mouse preparations. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Excess mitochondrial calcium can trigger membrane permeability failure. organism: Mus musculus tissue_or_cell_type: Isolated liver, heart and brain mitochondria experimental_model: Ppif-null and cyclophilin-D-overexpressing mice; isolated mitochondria, hepatocytes and fibroblasts limitations: Experimental overload; not all apoptosis uses this pathway and the study does not settle the molecular identity of the pore. research_relationship_category: exposure_response compartment_description: Inner mitochondrial membrane and matrix [ca-baines2005] Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death (2005). https://pubmed.ncbi.nlm.nih.gov/15800627/ DOI: 10.1038/nature03434
    Complete structured claim and evidence

  3. Reconstituted human SLC25A29 transports lysine by uniport and exchange, supporting lysine entry into the mitochondrial matrix.

    SLC25A29 → L-Lysine source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified recombinant carrier reconstituted in liposomes
    limitations
    Physiological import role is inferred from transport properties and localization; not a carnitine transporter.
    organism
    Homo sapiens
    plain_language
    SLC25A29 gives lysine access to mitochondrial metabolism.
    primary_references
    [porcelli2014] The Human Gene SLC25A29, of Solute Carrier Family 25, Encodes a Mitochondrial Transporter of Basic Amino Acids (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4036346/ DOI: 10.1074/jbc.M114.547448
    tissue_or_cell_type
    Inner mitochondrial membrane
    transport_effect
    raises Uniport and exchange supporting lysine entry into the matrix.
    transport_pool
    the mitochondrial matrix Uniport and exchange supporting lysine entry into the matrix.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 44–52

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant carrier reconstituted in liposomes · source_derived_draft · unverified_draft

    ### mitochondrial-lysine-transport Reconstituted human SLC25A29 transports lysine by uniport and exchange, supporting lysine entry into the mitochondrial matrix. Plain language: SLC25A29 gives lysine access to mitochondrial metabolism. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Inner mitochondrial membrane experimental_model: Purified recombinant carrier reconstituted in liposomes limitations: Physiological import role is inferred from transport properties and localization; not a carnitine transporter. [porcelli2014] The Human Gene SLC25A29, of Solute Carrier Family 25, Encodes a Mitochondrial Transporter of Basic Amino Acids (2014). https://pmc.ncbi.nlm.nih.gov/articles/PMC4036346/ DOI: 10.1074/jbc.M114.547448
    Complete structured claim and evidence

  4. Human MTHFD1L expressed in CHO cells behaves as a peripheral protein at the matrix face of the inner mitochondrial membrane.

    Human MTHFD1L → Inner mitochondrial membrane source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Tagged human protein, mitochondrial fractionation
    exposure
    Assay conditions described in the linked primary study.
    limitations
    Tagging and heterologous expression may affect localization.
    nutrient_topic
    Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
    organism
    Homo sapiens protein in Cricetulus griseus cells
    plain_language
    The formate-pathway enzyme sits on the mitochondrial inner surface.
    primary_references
    [prasannan-2009] Human mitochondrial C1-tetrahydrofolate synthase: submitochondrial localization of the full-length enzyme and characterization of a short isoform (2009). https://pubmed.ncbi.nlm.nih.gov/18996079/ DOI: 10.1016/j.abb.2008.10.028
    tissue_or_cell_type
    CHO cells

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 875–885

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Tagged human protein, mitochondrial fractionation · source_derived_draft · unverified_draft

    ### mthfd1l-matrix-face Human MTHFD1L expressed in CHO cells behaves as a peripheral protein at the matrix face of the inner mitochondrial membrane. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The formate-pathway enzyme sits on the mitochondrial inner surface. organism: Homo sapiens protein in Cricetulus griseus cells tissue_or_cell_type: CHO cells experimental_model: Tagged human protein, mitochondrial fractionation limitations: Tagging and heterologous expression may affect localization. exposure: Assay conditions described in the linked primary study. [prasannan-2009] Human mitochondrial C1-tetrahydrofolate synthase: submitochondrial localization of the full-length enzyme and characterization of a short isoform (2009). https://pubmed.ncbi.nlm.nih.gov/18996079/ DOI: 10.1016/j.abb.2008.10.028
    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