Component
Human C-lobe-ferric transferrin Tyr188-linked divanadate(V) adduct
Context-specific entity; species, compartment and exposure are stated on each claim.
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 it acts on
The vanadium adduct retained an open N-lobe and closed iron-containing C-lobe with little overall structural change.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Human transferrin crystal comparison.
- limitations
- Compatibility with receptor recognition is a structural interpretation, not a completed cellular uptake cycle; not a contradiction of the A549 transport study.
- nutrient_topic
- Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
- plain_language
- A binding structure alone does not demonstrate successful cellular delivery.
- primary_references
- First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 222–228
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transferrin crystal comparison. · source_derived_draft · unverified_draft
## vanadium-tf-open-lobe A binding structure alone does not demonstrate successful cellular delivery. The vanadium adduct retained an open N-lobe and closed iron-containing C-lobe with little overall structural change. Model: Human transferrin crystal comparison. Limitations: Compatibility with receptor recognition is a structural interpretation, not a completed cellular uptake cycle; not a contradiction of the A549 transport study. Evidence access: Primary full text First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
Complete structured claim and evidence
What acts on it
Crystals of C-lobe-ferric human transferrin exposed to vanadyl acetylacetonate contained a two-vanadium(V) unit linked to Tyr188 rather than intact V(IV) acetylacetonate.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Human protein crystallography; 5 mM compound and crystallization conditions.
- limitations
- Reaction/crystal structure does not demonstrate the same species dominates human blood.
- nutrient_topic
- Vanadium collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Vanadium
- plain_language
- The species bound to a protein can differ from the compound originally added.
- primary_references
- First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
Vanadium: speciation, phosphate-sensitive enzymes and cross-nutrient mechanisms (2026-09-19) · lines 214–220
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human protein crystallography; 5 mM compound and crystallization conditions. · source_derived_draft · unverified_draft
## vanadium-tf-crystal-transformation The species bound to a protein can differ from the compound originally added. Crystals of C-lobe-ferric human transferrin exposed to vanadyl acetylacetonate contained a two-vanadium(V) unit linked to Tyr188 rather than intact V(IV) acetylacetonate. Model: Human protein crystallography; 5 mM compound and crystallization conditions. Limitations: Reaction/crystal structure does not demonstrate the same species dominates human blood. Evidence access: Primary full text First crystal structure of an adduct formed upon reaction of a vanadium compound with human serum transferrin. · 2026 · https://pubmed.ncbi.nlm.nih.gov/41545537/ · DOI 10.1038/s42004-026-01891-1
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.