Component

Cytosol

Cytoplasmic compartment containing the translating ribosomes considered here.

14 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. FADS2 lacked mitochondrial import/localization in the experiments that imported and localized FADS1.

    Human FAD synthetase isoform 2 → Cytosol source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Abstract; FADS2 comparator
    experimental_model
    Parallel FADS1/FADS2 import and localization comparison
    exposure
    In vitro synthesized and transiently expressed human isoforms.
    limitations
    No import in this assay does not exclude condition-dependent localization outside the tested systems.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Human proteins in mammalian model preparations
    plain_language
    FLAD1 isoforms differ in access to the mitochondrial compartment.
    primary_references
    [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
    tissue_or_cell_type
    Rat liver mitochondria; BHK-21 and Caco-2 cells

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 360–371

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Parallel FADS1/FADS2 import and localization comparison · source_derived_draft · unverified_draft

    ### transport-flad1-isoform2-compartment FADS2 lacked mitochondrial import/localization in the experiments that imported and localized FADS1. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: FLAD1 isoforms differ in access to the mitochondrial compartment. organism: Human proteins in mammalian model preparations tissue_or_cell_type: Rat liver mitochondria; BHK-21 and Caco-2 cells experimental_model: Parallel FADS1/FADS2 import and localization comparison limitations: No import in this assay does not exclude condition-dependent localization outside the tested systems. exposure: In vitro synthesized and transiently expressed human isoforms. evidence_location: Abstract; FADS2 comparator [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. ANKH expression drove ATP release from HEK293 cells even when ENPP1 was absent.

    Progressive ankylosis protein homolog ANKH → ATP source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosol to extracellular medium
    experimental_model
    ANKH expression with ENPP1 deletion controls
    limitations
    Cellular export assay; it does not determine purified ANKH transport stoichiometry in every tissue.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    ANKH can provide extracellular ATP for subsequent PPi production.
    primary_references
    [szeri2022] The mineralization regulator ANKH mediates cellular efflux of ATP, not pyrophosphate (2022). https://pmc.ncbi.nlm.nih.gov/articles/PMC9098669/ DOI: 10.1002/jbmr.4528
    tissue_or_cell_type
    HEK293 cells

    Calcium: mechanism-first literature curation (2026-09-17) · lines 1000–1010

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · ANKH expression with ENPP1 deletion controls · source_derived_draft · unverified_draft

    ### ankh-atp-export ANKH expression drove ATP release from HEK293 cells even when ENPP1 was absent. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: ANKH can provide extracellular ATP for subsequent PPi production. organism: Homo sapiens tissue_or_cell_type: HEK293 cells experimental_model: ANKH expression with ENPP1 deletion controls limitations: Cellular export assay; it does not determine purified ANKH transport stoichiometry in every tissue. compartment_description: Cytosol to extracellular medium [szeri2022] The mineralization regulator ANKH mediates cellular efflux of ATP, not pyrophosphate (2022). https://pmc.ncbi.nlm.nih.gov/articles/PMC9098669/ DOI: 10.1002/jbmr.4528
    Complete structured claim and evidence

  2. ANKH-expressing HEK293 cells released citrate; Ank-mutant mice also had depleted bone-matrix citrate.

    Progressive ankylosis protein homolog ANKH → Citrate source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosol to extracellular space
    experimental_model
    Metabolomics and Ank-mutant tissue measurements
    limitations
    Citrate is a separate substrate; these findings do not prove that citrate alone explains altered bone strength.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens cells; Mus musculus
    plain_language
    ANKH affects a mineral-associated organic component as well as PPi supply.
    primary_references
    [szeri2020] The membrane protein ANKH is crucial for bone mechanical performance by mediating cellular export of citrate and ATP (2020). https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1008884 DOI: 10.1371/journal.pgen.1008884
    tissue_or_cell_type
    Cell medium and bone matrix

    Calcium: mechanism-first literature curation (2026-09-17) · lines 1024–1034

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Metabolomics and Ank-mutant tissue measurements · source_derived_draft · unverified_draft

    ### ankh-citrate-export ANKH-expressing HEK293 cells released citrate; Ank-mutant mice also had depleted bone-matrix citrate. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: ANKH affects a mineral-associated organic component as well as PPi supply. organism: Homo sapiens cells; Mus musculus tissue_or_cell_type: Cell medium and bone matrix experimental_model: Metabolomics and Ank-mutant tissue measurements limitations: Citrate is a separate substrate; these findings do not prove that citrate alone explains altered bone strength. compartment_description: Cytosol to extracellular space [szeri2020] The membrane protein ANKH is crucial for bone mechanical performance by mediating cellular export of citrate and ATP (2020). https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1008884 DOI: 10.1371/journal.pgen.1008884
    Complete structured claim and evidence

  3. Calcineurin binds NFAT1 and supports its reversible dephosphorylated, nuclear-active state during calcium stimulation.

    Calcineurin → NFAT1 / NFATC2 source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosol and nucleus
    experimental_model
    Murine T-cell experiments, inhibitor/chelation interventions and protein-binding assays
    limitations
    NFAT1-specific evidence; do not assign this calcium response to all NFAT proteins or NFAT5.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mus musculus
    plain_language
    Calcineurin connects calcium signaling to NFAT1 activation.
    primary_references
    [ca-loh1996] Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity (1996). https://pubmed.ncbi.nlm.nih.gov/8631904/ DOI: 10.1074/jbc.271.18.10884
    research_relationship_category
    regulation
    tissue_or_cell_type
    T lymphocytes

    Calcium: mechanism-first literature curation (2026-09-17) · lines 425–436

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Murine T-cell experiments, inhibitor/chelation interventions and protein-binding assays · source_derived_draft · unverified_draft

    ### ca-calcineurin-nfat1-regulation Calcineurin binds NFAT1 and supports its reversible dephosphorylated, nuclear-active state during calcium stimulation. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcineurin connects calcium signaling to NFAT1 activation. organism: Mus musculus tissue_or_cell_type: T lymphocytes experimental_model: Murine T-cell experiments, inhibitor/chelation interventions and protein-binding assays limitations: NFAT1-specific evidence; do not assign this calcium response to all NFAT proteins or NFAT5. research_relationship_category: regulation compartment_description: Cytosol and nucleus [ca-loh1996] Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity (1996). https://pubmed.ncbi.nlm.nih.gov/8631904/ DOI: 10.1074/jbc.271.18.10884
    Complete structured claim and evidence

  4. Calcium/calmodulin binding folds the human calcineurin regulatory region and supports displacement of autoinhibition.

    Calcium/calmodulin → Calcineurin source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosol
    experimental_model
    Recombinant human alpha-calcineurin, regulatory fragments and calmodulin; spectroscopy and exchange mass spectrometry
    limitations
    Fragment and biochemical data support a regulatory mechanism; not tissue-level output.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    Calcium-bound calmodulin helps switch on calcineurin.
    primary_references
    [ca-rumimasante2012] Structural basis for activation of calcineurin by calmodulin (2012). https://pubmed.ncbi.nlm.nih.gov/22100452/ DOI: 10.1016/j.jmb.2011.11.008
    research_relationship_category
    regulation
    tissue_or_cell_type
    Recombinant signaling proteins

    Calcium: mechanism-first literature curation (2026-09-17) · lines 412–423

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human alpha-calcineurin, regulatory fragments and calmodulin; spectroscopy and exchange mass spectrometry · source_derived_draft · unverified_draft

    ### ca-calmodulin-calcineurin-activation Calcium/calmodulin binding folds the human calcineurin regulatory region and supports displacement of autoinhibition. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium-bound calmodulin helps switch on calcineurin. organism: Homo sapiens tissue_or_cell_type: Recombinant signaling proteins experimental_model: Recombinant human alpha-calcineurin, regulatory fragments and calmodulin; spectroscopy and exchange mass spectrometry limitations: Fragment and biochemical data support a regulatory mechanism; not tissue-level output. research_relationship_category: regulation compartment_description: Cytosol [ca-rumimasante2012] Structural basis for activation of calcineurin by calmodulin (2012). https://pubmed.ncbi.nlm.nih.gov/22100452/ DOI: 10.1016/j.jmb.2011.11.008
    Complete structured claim and evidence

  5. Calcium-loaded calmodulin forms the Ca2+/CaM regulatory complex resolved with a myosin-light-chain-kinase target peptide.

    Calcium ion → Calmodulin source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic protein complex
    experimental_model
    Purified calcium-bound calmodulin and a chicken smooth-muscle myosin light-chain kinase peptide; crystallography
    limitations
    Structure of a peptide complex; not a measurement of dietary calcium effects or every calmodulin target.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Purified vertebrate proteins
    plain_language
    Calmodulin carries bound calcium while engaging a target protein.
    primary_references
    [ca-meador1992] Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex (1992). https://pubmed.ncbi.nlm.nih.gov/1519061/ DOI: 10.1126/science.1519061
    research_relationship_category
    binding
    tissue_or_cell_type
    Smooth-muscle target-peptide system

    Calcium: mechanism-first literature curation (2026-09-17) · lines 399–410

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified calcium-bound calmodulin and a chicken smooth-muscle myosin light-chain kinase peptide; crystallography · source_derived_draft · unverified_draft

    ### ca-calmodulin-calcium-complex Calcium-loaded calmodulin forms the Ca2+/CaM regulatory complex resolved with a myosin-light-chain-kinase target peptide. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calmodulin carries bound calcium while engaging a target protein. organism: Purified vertebrate proteins tissue_or_cell_type: Smooth-muscle target-peptide system experimental_model: Purified calcium-bound calmodulin and a chicken smooth-muscle myosin light-chain kinase peptide; crystallography limitations: Structure of a peptide complex; not a measurement of dietary calcium effects or every calmodulin target. research_relationship_category: binding compartment_description: Cytosolic protein complex [ca-meador1992] Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex (1992). https://pubmed.ncbi.nlm.nih.gov/1519061/ DOI: 10.1126/science.1519061
    Complete structured claim and evidence

  6. Partial autophosphorylation generates CaMKII activity that persists in the absence of calcium in the purified assay.

    Ca2+/calmodulin-dependent protein kinase II family → Autophosphorylated CaMKII with autonomous activity source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic kinase complex
    experimental_model
    Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays
    limitations
    Autonomy depends on phosphorylation conditions; not all self-phosphorylation activates and persistence in living cells is not quantified.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mammalia
    plain_language
    After activation, CaMKII can retain activity beyond the calcium pulse.
    primary_references
    [ca-miller1986] Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch (1986). https://pubmed.ncbi.nlm.nih.gov/3006921/ DOI: 10.1016/0092-8674(86)90008-5
    research_relationship_category
    protein_modification
    tissue_or_cell_type
    Brain enzyme preparation

    Calcium: mechanism-first literature curation (2026-09-17) · lines 451–462

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays · source_derived_draft · unverified_draft

    ### ca-camkii-autonomous-activity Partial autophosphorylation generates CaMKII activity that persists in the absence of calcium in the purified assay. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: After activation, CaMKII can retain activity beyond the calcium pulse. organism: Mammalia tissue_or_cell_type: Brain enzyme preparation experimental_model: Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays limitations: Autonomy depends on phosphorylation conditions; not all self-phosphorylation activates and persistence in living cells is not quantified. research_relationship_category: protein_modification compartment_description: Cytosolic kinase complex [ca-miller1986] Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch (1986). https://pubmed.ncbi.nlm.nih.gov/3006921/ DOI: 10.1016/0092-8674(86)90008-5
    Complete structured claim and evidence

  7. Calcium/calmodulin stimulates autophosphorylation of purified brain CaMKII.

    Calcium/calmodulin → Ca2+/calmodulin-dependent protein kinase II family source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic kinase complex
    experimental_model
    Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays
    limitations
    Brain holoenzyme assay; does not identify every isoform or phosphorylation site.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mammalia
    plain_language
    Calcium-bound calmodulin starts CaMKII self-phosphorylation.
    primary_references
    [ca-miller1986] Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch (1986). https://pubmed.ncbi.nlm.nih.gov/3006921/ DOI: 10.1016/0092-8674(86)90008-5
    research_relationship_category
    regulation
    tissue_or_cell_type
    Brain enzyme preparation

    Calcium: mechanism-first literature curation (2026-09-17) · lines 438–449

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays · source_derived_draft · unverified_draft

    ### ca-camkii-calmodulin-activation Calcium/calmodulin stimulates autophosphorylation of purified brain CaMKII. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium-bound calmodulin starts CaMKII self-phosphorylation. organism: Mammalia tissue_or_cell_type: Brain enzyme preparation experimental_model: Purified mammalian brain CaMKII; phosphorylation and substrate-kinase assays limitations: Brain holoenzyme assay; does not identify every isoform or phosphorylation site. research_relationship_category: regulation compartment_description: Cytosolic kinase complex [ca-miller1986] Regulation of brain type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: a Ca2+-triggered molecular switch (1986). https://pubmed.ncbi.nlm.nih.gov/3006921/ DOI: 10.1016/0092-8674(86)90008-5
    Complete structured claim and evidence

  8. Localized sarcoplasmic-reticulum calcium release generates brief calcium sparks in rat cardiac myocytes.

    Sarcoplasmic reticulum calcium release → Cardiac calcium sparks source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    SR to local cytosol
    experimental_model
    Quiescent rat cardiac myocytes; confocal calcium imaging with ryanodine and SR-loading manipulations
    limitations
    Imaging and ryanodine sensitivity establish localized release; the historical single-channel estimate is not encoded as settled channel stoichiometry.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Rattus norvegicus
    plain_language
    Heart cells release small local bursts of stored calcium.
    primary_references
    [ca-cheng1993] Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle (1993). https://pubmed.ncbi.nlm.nih.gov/8235594/ DOI: 10.1126/science.8235594
    research_relationship_category
    mechanism
    tissue_or_cell_type
    Cardiac myocytes
    transport_or_reaction_direction
    SR lumen to cytosol

    Calcium: mechanism-first literature curation (2026-09-17) · lines 809–821

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Quiescent rat cardiac myocytes; confocal calcium imaging with ryanodine and SR-loading manipulations · source_derived_draft · unverified_draft

    ### ca-cardiac-sr-sparks Localized sarcoplasmic-reticulum calcium release generates brief calcium sparks in rat cardiac myocytes. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Heart cells release small local bursts of stored calcium. organism: Rattus norvegicus tissue_or_cell_type: Cardiac myocytes experimental_model: Quiescent rat cardiac myocytes; confocal calcium imaging with ryanodine and SR-loading manipulations limitations: Imaging and ryanodine sensitivity establish localized release; the historical single-channel estimate is not encoded as settled channel stoichiometry. research_relationship_category: mechanism transport_or_reaction_direction: SR lumen to cytosol compartment_description: SR to local cytosol [ca-cheng1993] Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle (1993). https://pubmed.ncbi.nlm.nih.gov/8235594/ DOI: 10.1126/science.8235594
    Complete structured claim and evidence

  9. Applied IP3 releases calcium from a nonmitochondrial intracellular store in permeabilized pancreatic acinar cells.

    IP3 → ER calcium release source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Nonmitochondrial intracellular store to cytosol
    experimental_model
    Permeabilized rat pancreatic acinar cells
    limitations
    Permeabilized-cell application; receptor isoform and dietary status were not established.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Rattus norvegicus
    plain_language
    IP3 releases stored calcium inside acinar cells.
    primary_references
    [ca-streb1983] Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate (1983). https://pubmed.ncbi.nlm.nih.gov/6605482/ DOI: 10.1038/306067a0
    research_relationship_category
    mechanism
    tissue_or_cell_type
    Pancreatic acinar cells
    transport_or_reaction_direction
    Intracellular store to cytosol

    Calcium: mechanism-first literature curation (2026-09-17) · lines 464–476

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Permeabilized rat pancreatic acinar cells · source_derived_draft · unverified_draft

    ### ca-ip3-mobilizes-store Applied IP3 releases calcium from a nonmitochondrial intracellular store in permeabilized pancreatic acinar cells. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: IP3 releases stored calcium inside acinar cells. organism: Rattus norvegicus tissue_or_cell_type: Pancreatic acinar cells experimental_model: Permeabilized rat pancreatic acinar cells limitations: Permeabilized-cell application; receptor isoform and dietary status were not established. research_relationship_category: mechanism transport_or_reaction_direction: Intracellular store to cytosol compartment_description: Nonmitochondrial intracellular store to cytosol [ca-streb1983] Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate (1983). https://pubmed.ncbi.nlm.nih.gov/6605482/ DOI: 10.1038/306067a0
    Complete structured claim and evidence

  10. Calcium binding participates in ITPR3 gating after IP3/ATP priming, with both active and inactive calcium-bound conformations resolved.

    Calcium ion → Inositol 1,4,5-trisphosphate receptor type 3 / ITPR3 source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic regulatory regions of ER channel
    experimental_model
    Recombinant human ITPR3; cryo-EM in ligand-bound gating states
    limitations
    Structural populations do not define a universal calcium threshold or prove all calcium-bound channels are active.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    Calcium helps control ITPR3 opening; binding does not guarantee that the channel stays open.
    primary_references
    [ca-schmitz2022] Structural basis for activation and gating of IP3 receptors (2022). https://pubmed.ncbi.nlm.nih.gov/35301323/ DOI: 10.1038/s41467-022-29073-2
    research_relationship_category
    regulation
    tissue_or_cell_type
    Recombinant ITPR3

    Calcium: mechanism-first literature curation (2026-09-17) · lines 492–503

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human ITPR3; cryo-EM in ligand-bound gating states · source_derived_draft · unverified_draft

    ### ca-itpr3-calcium-coactivation Calcium binding participates in ITPR3 gating after IP3/ATP priming, with both active and inactive calcium-bound conformations resolved. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium helps control ITPR3 opening; binding does not guarantee that the channel stays open. organism: Homo sapiens tissue_or_cell_type: Recombinant ITPR3 experimental_model: Recombinant human ITPR3; cryo-EM in ligand-bound gating states limitations: Structural populations do not define a universal calcium threshold or prove all calcium-bound channels are active. research_relationship_category: regulation compartment_description: Cytosolic regulatory regions of ER channel [ca-schmitz2022] Structural basis for activation and gating of IP3 receptors (2022). https://pubmed.ncbi.nlm.nih.gov/35301323/ DOI: 10.1038/s41467-022-29073-2
    Complete structured claim and evidence

  11. Calcium binding to the cytosolic CBD2 regulatory domain disrupts an inactive NCX1 assembly and permits exchange.

    Calcium ion → Na+/Ca2+ exchanger 1 / SLC8A1 source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic regulatory domain of plasma-membrane exchanger
    experimental_model
    Human cardiac NCX1; cryo-EM and functional exchange assays
    limitations
    Regulatory calcium binding is distinct from calcium being transported; the measured splice form and assay conditions matter.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    Calcium also regulates NCX1 at a site separate from the transported-ion pathway.
    primary_references
    [ca-xue2023] Structural mechanisms of the human cardiac sodium-calcium exchanger NCX1 (2023). https://pubmed.ncbi.nlm.nih.gov/37794011/ DOI: 10.1038/s41467-023-41885-4
    research_relationship_category
    regulation
    tissue_or_cell_type
    Cardiac NCX1 expression system

    Calcium: mechanism-first literature curation (2026-09-17) · lines 639–650

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cardiac NCX1; cryo-EM and functional exchange assays · source_derived_draft · unverified_draft

    ### ca-ncx1-regulatory-calcium Calcium binding to the cytosolic CBD2 regulatory domain disrupts an inactive NCX1 assembly and permits exchange. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium also regulates NCX1 at a site separate from the transported-ion pathway. organism: Homo sapiens tissue_or_cell_type: Cardiac NCX1 expression system experimental_model: Human cardiac NCX1; cryo-EM and functional exchange assays limitations: Regulatory calcium binding is distinct from calcium being transported; the measured splice form and assay conditions matter. research_relationship_category: regulation compartment_description: Cytosolic regulatory domain of plasma-membrane exchanger [ca-xue2023] Structural mechanisms of the human cardiac sodium-calcium exchanger NCX1 (2023). https://pubmed.ncbi.nlm.nih.gov/37794011/ DOI: 10.1038/s41467-023-41885-4
    Complete structured claim and evidence

  12. Calcium binds an activating RyR1 site and primes gating; ATP and caffeine increase open-state representation in the experimental preparation.

    Calcium ion → Ryanodine receptor 1 / RYR1 source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Cytosolic channel-regulatory region
    experimental_model
    Purified rabbit skeletal-muscle RyR1 with calstabin2; cryo-EM and planar-bilayer recordings
    limitations
    Calcium is both a transported ion and a ligand; caffeine-assisted structures do not imply caffeine is required physiologically.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Oryctolagus cuniculus
    plain_language
    Calcium helps regulate the RyR1 gate.
    primary_references
    [ca-desgeorges2016] Structural Basis for Gating and Activation of RyR1 (2016). https://pubmed.ncbi.nlm.nih.gov/27662087/ DOI: 10.1016/j.cell.2016.08.075
    research_relationship_category
    regulation
    tissue_or_cell_type
    Skeletal-muscle channel preparation

    Calcium: mechanism-first literature curation (2026-09-17) · lines 666–677

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified rabbit skeletal-muscle RyR1 with calstabin2; cryo-EM and planar-bilayer recordings · source_derived_draft · unverified_draft

    ### ca-ryr1-calcium-gating Calcium binds an activating RyR1 site and primes gating; ATP and caffeine increase open-state representation in the experimental preparation. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calcium helps regulate the RyR1 gate. organism: Oryctolagus cuniculus tissue_or_cell_type: Skeletal-muscle channel preparation experimental_model: Purified rabbit skeletal-muscle RyR1 with calstabin2; cryo-EM and planar-bilayer recordings limitations: Calcium is both a transported ion and a ligand; caffeine-assisted structures do not imply caffeine is required physiologically. research_relationship_category: regulation compartment_description: Cytosolic channel-regulatory region [ca-desgeorges2016] Structural Basis for Gating and Activation of RyR1 (2016). https://pubmed.ncbi.nlm.nih.gov/27662087/ DOI: 10.1016/j.cell.2016.08.075
    Complete structured claim and evidence

  13. Increasing sarcoplasmic-reticulum calcium content raises spontaneous release activity and permits some sparks to initiate propagating calcium waves.

    Calcium ion → Propagating cardiac calcium waves source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    SR and cytosol
    experimental_model
    Quiescent rat cardiac myocytes; confocal calcium imaging with ryanodine and SR-loading manipulations
    limitations
    Experimental intracellular store loading, not dietary intake; normal schema category denotes a mechanistic experiment, not a healthy exposure.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Rattus norvegicus
    plain_language
    Heavily loaded stores can turn local calcium bursts into spreading waves.
    primary_references
    [ca-cheng1993] Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle (1993). https://pubmed.ncbi.nlm.nih.gov/8235594/ DOI: 10.1126/science.8235594
    research_relationship_category
    exposure_response
    tissue_or_cell_type
    Quiescent cardiac myocytes under experimental SR loading

    Calcium: mechanism-first literature curation (2026-09-17) · lines 823–834

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Quiescent rat cardiac myocytes; confocal calcium imaging with ryanodine and SR-loading manipulations · source_derived_draft · unverified_draft

    ### ca-sr-overload-propagating-waves Increasing sarcoplasmic-reticulum calcium content raises spontaneous release activity and permits some sparks to initiate propagating calcium waves. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Heavily loaded stores can turn local calcium bursts into spreading waves. organism: Rattus norvegicus tissue_or_cell_type: Quiescent cardiac myocytes under experimental SR loading experimental_model: Quiescent rat cardiac myocytes; confocal calcium imaging with ryanodine and SR-loading manipulations limitations: Experimental intracellular store loading, not dietary intake; normal schema category denotes a mechanistic experiment, not a healthy exposure. research_relationship_category: exposure_response compartment_description: SR and cytosol [ca-cheng1993] Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle (1993). https://pubmed.ncbi.nlm.nih.gov/8235594/ DOI: 10.1126/science.8235594
    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