Component
Cellular iron-responsive RNA binding
Cellular iron-responsive RNA binding. 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
Manipulations of the IRE-binding protein Fe-S cluster reciprocally altered RNA-binding and aconitase activities.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/iron-research/1502165.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1fc2a7abe3fbac12a5196a163c8d6f21f5847bd89c049958dfb4055302a14a56", "start_char": 0, "end_char": 1583, "text_sha256": "1fc2a7abe3fbac12a5196a163c8d6f21f5847bd89c049958dfb4055302a14a56"}
- experimental_model
- Iron-sulfur manipulation and enzyme/RNA-binding assays
- exposure
- Iron and Fe-S cluster manipulation
- limitations
- IRP1/aconitase switch; no assertion that IRP2 has the same catalytic switch.
- nutrient_topic
- Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
- organism
- Mammalian IRE-binding protein systems
- plain_language
- One protein can act as an enzyme or an iron-responsive RNA-binding regulator, depending on its cluster state.
- primary_references
- [iron-p1502165] Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster. (1992). https://pubmed.ncbi.nlm.nih.gov/1502165/ DOI: 10.1073/pnas.89.16.7536
- tissue_or_cell_type
- Purified/recombinant IRE-BP and cultured cells
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 667–678
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Iron-sulfur manipulation and enzyme/RNA-binding assays · source_derived_draft · unverified_draft
### iron-irp1-switch Manipulations of the IRE-binding protein Fe-S cluster reciprocally altered RNA-binding and aconitase activities. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: One protein can act as an enzyme or an iron-responsive RNA-binding regulator, depending on its cluster state. organism: Mammalian IRE-binding protein systems tissue_or_cell_type: Purified/recombinant IRE-BP and cultured cells experimental_model: Iron-sulfur manipulation and enzyme/RNA-binding assays limitations: IRP1/aconitase switch; no assertion that IRP2 has the same catalytic switch. exposure: Iron and Fe-S cluster manipulation evidence_span: {"source_cache": "artifacts/iron-research/1502165.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1fc2a7abe3fbac12a5196a163c8d6f21f5847bd89c049958dfb4055302a14a56", "start_char": 0, "end_char": 1583, "text_sha256": "1fc2a7abe3fbac12a5196a163c8d6f21f5847bd89c049958dfb4055302a14a56"} [iron-p1502165] Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster. (1992). https://pubmed.ncbi.nlm.nih.gov/1502165/ DOI: 10.1073/pnas.89.16.7536
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.