Component
Protein-incorporated N-terminal cysteine residue
Context-specific entity; species, compartment and exposure are stated on each claim.
3 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
Human ADO oxidized exposed N-terminal cysteine residues in RGS4/5 peptides to the corresponding sulfinic-acid state using molecular oxygen.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Human ADO biochemistry, peptide substrates and human-cell experiments.
- limitations
- This is a protein-residue reaction, not evidence that ADO is the ordinary free-cysteine catabolic enzyme.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- A cysteine already built into a protein can serve as part of an oxygen-sensitive degradation signal.
- primary_references
- Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 420–426
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human ADO biochemistry, peptide substrates and human-cell experiments. · source_derived_draft · unverified_draft
## l-cysteine-ado-nterminal-oxidation A cysteine already built into a protein can serve as part of an oxygen-sensitive degradation signal. Human ADO oxidized exposed N-terminal cysteine residues in RGS4/5 peptides to the corresponding sulfinic-acid state using molecular oxygen. Model: Human ADO biochemistry, peptide substrates and human-cell experiments. Limitations: This is a protein-residue reaction, not evidence that ADO is the ordinary free-cysteine catabolic enzyme. Evidence access: Primary full text Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
Complete structured claim and evidence
Where it participates (unsigned role)
Manipulating ADO altered G-protein-coupled calcium signals and MAP-kinase activity in the studied human cells.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Human-cell functional signaling assays.
- limitations
- Not evidence of dietary calcium or cysteine requirements for this response.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- Protein turnover connected an oxygen-sensing step to signaling outputs.
- primary_references
- Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 436–442
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human-cell functional signaling assays. · source_derived_draft · unverified_draft
## l-cysteine-ado-calcium-signals Protein turnover connected an oxygen-sensing step to signaling outputs. Manipulating ADO altered G-protein-coupled calcium signals and MAP-kinase activity in the studied human cells. Model: Human-cell functional signaling assays. Limitations: Not evidence of dietary calcium or cysteine requirements for this response. Evidence access: Primary full text Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
Complete structured claim and evidenceADO-dependent N-terminal cysteine oxidation regulated RGS4/5 stability through the N-degron pathway in human cells.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Human-cell ADO and oxygen perturbations with N-degron readouts.
- limitations
- The downstream pathway requires additional machinery; dietary cysteine effects were not tested.
- nutrient_topic
- L-Cysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Cysteine
- plain_language
- Oxidation can mark a signaling regulator for degradation rather than merely damage it.
- primary_references
- Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
L-Cysteine: sulfur allocation, redox supply and cross-nutrient mechanisms (2026-09-19) · lines 428–434
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human-cell ADO and oxygen perturbations with N-degron readouts. · source_derived_draft · unverified_draft
## l-cysteine-ado-protein-stability Oxidation can mark a signaling regulator for degradation rather than merely damage it. ADO-dependent N-terminal cysteine oxidation regulated RGS4/5 stability through the N-degron pathway in human cells. Model: Human-cell ADO and oxygen perturbations with N-degron readouts. Limitations: The downstream pathway requires additional machinery; dietary cysteine effects were not tested. Evidence access: Primary full text Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31273118/ · DOI 10.1126/science.aaw0112
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.