Component
Human endoplasmic reticulum oxidoreductin 1 alpha / ERO1A
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
Human ERO1A targets PDI through contacts with its b-prime substrate-binding domain, supporting the disulfide-forming pathway for protein folding.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human ERO1A structural and biochemical study.
- limitations
- Protein-residue oxidation is separate from free cystine reduction; dietary cysteine effects were not tested.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- Cysteines already incorporated into proteins are joined and rearranged during folding.
- primary_references
- Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20834232/ · DOI 10.1038/emboj.2010.222
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 484–490
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human ERO1A structural and biochemical study. · source_derived_draft · unverified_draft
## l-cysteine-ero1-pdi-targeting Cysteines already incorporated into proteins are joined and rearranged during folding. Human ERO1A targets PDI through contacts with its b-prime substrate-binding domain, supporting the disulfide-forming pathway for protein folding. Model: Human ERO1A structural and biochemical study. Limitations: Protein-residue oxidation is separate from free cystine reduction; dietary cysteine effects were not tested. Evidence access: Primary abstract Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20834232/ · DOI 10.1038/emboj.2010.222
Complete structured claim and evidence
What acts on it
Regulatory cysteines in a flexible ERO1A loop change disulfide arrangements and electron transfer, restraining its oxidative activity.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human ERO1A hyperactive and inactive crystal structures.
- limitations
- This is enzyme regulation, not proof that additional cysteine increases protein folding or antioxidant capacity.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- Cysteine bonds can regulate an enzyme as well as stabilize folded proteins.
- primary_references
- Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20834232/ · DOI 10.1038/emboj.2010.222
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 492–498
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human ERO1A hyperactive and inactive crystal structures. · source_derived_draft · unverified_draft
## l-cysteine-ero1-regulatory-disulfides Cysteine bonds can regulate an enzyme as well as stabilize folded proteins. Regulatory cysteines in a flexible ERO1A loop change disulfide arrangements and electron transfer, restraining its oxidative activity. Model: Human ERO1A hyperactive and inactive crystal structures. Limitations: This is enzyme regulation, not proof that additional cysteine increases protein folding or antioxidant capacity. Evidence access: Primary abstract Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20834232/ · DOI 10.1038/emboj.2010.222
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.