Component
Rhodopsin
Rod opsin RHO carrying its 11-cis-retinal chromophore.
2 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
Bovine rhodopsin crystallography identifies 11-cis-retinal within the inactive seven-helix receptor.
Experimental context and source evidence
- experimental_model
- 2.8-angstrom crystal structure
- limitations
- A static ground-state structure does not measure dietary requirements.
- nutrient_topic
- Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
- organism
- Bos taurus
- plain_language
- The cis retinal isomer is the rod pigment chromophore.
- primary_references
- [palczewski-2000] Crystal structure of rhodopsin: A G protein-coupled receptor (2000). https://pubmed.ncbi.nlm.nih.gov/10926528/ DOI: 10.1126/science.289.5480.739
- tissue_or_cell_type
- Rod photopigment
Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 644–653
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · 2.8-angstrom crystal structure · source_derived_draft · unverified_draft
### a-vision-chromophore Bovine rhodopsin crystallography identifies 11-cis-retinal within the inactive seven-helix receptor. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cis retinal isomer is the rod pigment chromophore. organism: Bos taurus tissue_or_cell_type: Rod photopigment experimental_model: 2.8-angstrom crystal structure limitations: A static ground-state structure does not measure dietary requirements. [palczewski-2000] Crystal structure of rhodopsin: A G protein-coupled receptor (2000). https://pubmed.ncbi.nlm.nih.gov/10926528/ DOI: 10.1126/science.289.5480.739
Complete structured claim and evidence
Where it participates (unsigned role)
Light activation changes rhodopsin-bound 11-cis-retinal into its all-trans geometry, coupled to receptor activation.
Experimental context and source evidence
- experimental_model
- Solid-state NMR before/after illumination
- limitations
- Bound chromophore conversion precedes release of free retinal.
- nutrient_topic
- Vitamin A research collection; topical membership is not evidence of a direct dietary effect. · Vitamin A
- organism
- Bos taurus
- plain_language
- A photon changes the bound retinoid shape and starts the signal.
- primary_references
- [grobner-2000] Observations of light-induced structural changes of retinal within rhodopsin (2000). https://www.nature.com/articles/35015604 DOI: 10.1038/35015604
- tissue_or_cell_type
- Purified rhodopsin
Vitamin A: forms, mechanisms, deficiency and excess (2026-09-17) · lines 655–664
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Solid-state NMR before/after illumination · source_derived_draft · unverified_draft
### a-vision-photoisomerization Light activation changes rhodopsin-bound 11-cis-retinal into its all-trans geometry, coupled to receptor activation. Condition category: normal nutrient_topic: Vitamin A research collection; topical membership is not evidence of a direct dietary effect. plain_language: A photon changes the bound retinoid shape and starts the signal. organism: Bos taurus tissue_or_cell_type: Purified rhodopsin experimental_model: Solid-state NMR before/after illumination limitations: Bound chromophore conversion precedes release of free retinal. [grobner-2000] Observations of light-induced structural changes of retinal within rhodopsin (2000). https://www.nature.com/articles/35015604 DOI: 10.1038/35015604
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.