Component
Calmodulin
A calcium-binding signaling protein.
4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
Coexpressing human calmodulin stabilized eNOS and raised its specific activity; later calmodulin addition did not reproduce the gain.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/citrulline-research/8951046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f5c5176d8e2b671f5311c529c09abe80b8661050e73c156ee2916959aa5030cb", "start_char": 0, "end_char": 1362, "text_sha256": "f5c5176d8e2b671f5311c529c09abe80b8661050e73c156ee2916959aa5030cb"}
- experimental_model
- Recombinant coexpression and enzyme activity comparison
- exposure
- Calmodulin coexpression versus adding calmodulin after expression
- limitations
- Expression-system result; not a test of dietary calcium or calmodulin supplementation.
- nutrient_topic
- Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
- organism
- Human NOS3 and human calmodulin expressed in E. coli
- plain_language
- How the enzyme assembles with its regulatory protein mattered.
- primary_references
- [citrulline-p8951046] Human endothelial nitric oxide synthase: expression in Escherichia coli, coexpression with calmodulin, and characterization. (1996). https://pubmed.ncbi.nlm.nih.gov/8951046/ DOI: 10.1006/abbi.1996.0543
- tissue_or_cell_type
- NOS expression and catalytic function
Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 593–604
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant coexpression and enzyme activity comparison · source_derived_draft · unverified_draft
### citrulline-calmodulin-nos Coexpressing human calmodulin stabilized eNOS and raised its specific activity; later calmodulin addition did not reproduce the gain. Condition category: normal nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: How the enzyme assembles with its regulatory protein mattered. organism: Human NOS3 and human calmodulin expressed in E. coli tissue_or_cell_type: NOS expression and catalytic function experimental_model: Recombinant coexpression and enzyme activity comparison limitations: Expression-system result; not a test of dietary calcium or calmodulin supplementation. exposure: Calmodulin coexpression versus adding calmodulin after expression evidence_span: {"source_cache": "artifacts/citrulline-research/8951046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f5c5176d8e2b671f5311c529c09abe80b8661050e73c156ee2916959aa5030cb", "start_char": 0, "end_char": 1362, "text_sha256": "f5c5176d8e2b671f5311c529c09abe80b8661050e73c156ee2916959aa5030cb"} [citrulline-p8951046] Human endothelial nitric oxide synthase: expression in Escherichia coli, coexpression with calmodulin, and characterization. (1996). https://pubmed.ncbi.nlm.nih.gov/8951046/ DOI: 10.1006/abbi.1996.0543
Complete structured claim and evidence
What acts on it
Calcium-loaded calmodulin forms the Ca2+/CaM regulatory complex resolved with a myosin-light-chain-kinase target peptide.
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
Where it participates (unsigned role)
Calmodulin increases apparent calcium affinity and ATPase activity of the erythrocyte calcium pump.
Experimental context and source evidence
- compartment_description
- Plasma membrane
- experimental_model
- Human erythrocyte membrane ghosts with purified human or bovine calmodulin
- limitations
- Membrane ghosts with controlled additions; pump isoforms were not resolved and this is not an intact-cell dose response.
- nutrient_topic
- Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
- organism
- Homo sapiens
- plain_language
- Calmodulin makes the red-cell calcium pump respond more strongly to calcium.
- primary_references
- [ca-roufogalis1980] Regulation by calmodulin of the calcium affinity of the calcium-transport ATPase in human erythrocytes (1980). https://pubmed.ncbi.nlm.nih.gov/6109558/ DOI: 10.1139/o80-126
- research_relationship_category
- regulation
- tissue_or_cell_type
- Erythrocyte membranes
Calcium: mechanism-first literature curation (2026-09-17) · lines 612–623
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocyte membrane ghosts with purified human or bovine calmodulin · source_derived_draft · unverified_draft
### ca-calmodulin-pmca-affinity Calmodulin increases apparent calcium affinity and ATPase activity of the erythrocyte calcium pump. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Calmodulin makes the red-cell calcium pump respond more strongly to calcium. organism: Homo sapiens tissue_or_cell_type: Erythrocyte membranes experimental_model: Human erythrocyte membrane ghosts with purified human or bovine calmodulin limitations: Membrane ghosts with controlled additions; pump isoforms were not resolved and this is not an intact-cell dose response. research_relationship_category: regulation compartment_description: Plasma membrane [ca-roufogalis1980] Regulation by calmodulin of the calcium affinity of the calcium-transport ATPase in human erythrocytes (1980). https://pubmed.ncbi.nlm.nih.gov/6109558/ DOI: 10.1139/o80-126
Complete structured claim and evidenceCalcium binding forms the calcium/calmodulin signaling complex.
Experimental context and source evidence
- cell_type
- · T cell
- evidence_scope
- Source-derived draft; primary-source verification required
- organism
- · Human
Selenium in immune cells · lines 30–38
Selenium immune-cell mechanism draft · supports · Source draft; model details require primary-source verification · source_derived_draft · unverified_draft
5. TCR → LCK → ZAP70 → LAT → PLCγ1 → PIP₂ → IP₃ + DAG 6. IP₃ → IP3R → ER Ca²⁺ release → store depletion 7. STIM1 oligomerizes → ORAI1 → CRAC channel → sustained Ca²⁺ entry 8. Ca²⁺/calmodulin → CALCINEURIN (PP2B) → dephosphorylates NFAT 9. NFAT → nucleus → partners with AP-1 → IL2, IFNG, CD25 transcription
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.