Component
Human iNOS dimer stability
Human iNOS dimer stability. Species, exposure and limitations are retained in each linked claim.
1 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 acts on it
The NOS2 zinc-tetrathiolate center supported intersubunit contacts and integrity of the BH4-binding site.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/citrulline-research/10409685.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b", "start_char": 0, "end_char": 942, "text_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b"}
- experimental_model
- Crystal structures of zinc-free and zinc-bound heme domains
- exposure
- Zinc-free versus zinc-tetrathiolate-containing structures
- limitations
- Direct structure is NOS2; similarity to NOS3 does not justify silently treating the proteins as identical.
- nutrient_topic
- Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
- organism
- Human NOS2
- plain_language
- The structural metal and the pterin-binding region are connected.
- primary_references
- [citrulline-p10409685] Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. (1999). https://pubmed.ncbi.nlm.nih.gov/10409685/ DOI: 10.1074/jbc.274.30.21276
- tissue_or_cell_type
- NOS dimer interface and pterin-binding region
Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 606–617
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures of zinc-free and zinc-bound heme domains · source_derived_draft · unverified_draft
### citrulline-inos-zinc-interface The NOS2 zinc-tetrathiolate center supported intersubunit contacts and integrity of the BH4-binding site. Condition category: normal nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The structural metal and the pterin-binding region are connected. organism: Human NOS2 tissue_or_cell_type: NOS dimer interface and pterin-binding region experimental_model: Crystal structures of zinc-free and zinc-bound heme domains limitations: Direct structure is NOS2; similarity to NOS3 does not justify silently treating the proteins as identical. exposure: Zinc-free versus zinc-tetrathiolate-containing structures evidence_span: {"source_cache": "artifacts/citrulline-research/10409685.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b", "start_char": 0, "end_char": 942, "text_sha256": "c320fb6f3fd659a2e7df4a8ddd3467a902a07b84380075d429040eaf244ccf6b"} [citrulline-p10409685] Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. (1999). https://pubmed.ncbi.nlm.nih.gov/10409685/ DOI: 10.1074/jbc.274.30.21276
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.