Component
Zinc-bound disulfide-reduced human SOD1
Human SOD1 intermediate with one zinc ion per subunit, without copper and with reduced Cys57/Cys146.
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
In zinc-supplemented HEK293T cells, CCS coexpression promoted SOD1 disulfide oxidation without detectable additional SOD1 copper loading.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- Transient expression of human SOD1 and CCS in human HEK293T cells; in-cell NMR
- exposure
- 10 µM ZnSO4 and SOD1/CCS coexpression; no added CuCl2 in this comparison.
- limitations
- HEK293T cells overexpressed SOD1/CCS above endogenous levels; these medium concentrations are experimental exposures, not dietary targets. Copper transfer and disulfide oxidation need not occur in a fixed coupled step in every cellular context. This is not proof that all copper is absent from the cell.
- nutrient_topic
- Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
- organism
- Homo sapiens
- plain_language
- CCS can help form the SOD1 disulfide before copper is inserted.
- primary_references
- [zinc-enz-sod1-live2013] Atomic-resolution monitoring of protein maturation in live human cells by NMR. (2013). https://pubmed.ncbi.nlm.nih.gov/23455544/ DOI: 10.1038/nchembio.1202
- tissue_or_cell_type
- Human HEK293T cytoplasm
Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 755–766
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transient expression of human SOD1 and CCS in human HEK293T cells; in-cell NMR · source_derived_draft · unverified_draft
### zinc-enz-sod1-disulfide-independent In zinc-supplemented HEK293T cells, CCS coexpression promoted SOD1 disulfide oxidation without detectable additional SOD1 copper loading. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: CCS can help form the SOD1 disulfide before copper is inserted. organism: Homo sapiens tissue_or_cell_type: Human HEK293T cytoplasm experimental_model: Transient expression of human SOD1 and CCS in human HEK293T cells; in-cell NMR limitations: HEK293T cells overexpressed SOD1/CCS above endogenous levels; these medium concentrations are experimental exposures, not dietary targets. Copper transfer and disulfide oxidation need not occur in a fixed coupled step in every cellular context. This is not proof that all copper is absent from the cell. exposure: 10 µM ZnSO4 and SOD1/CCS coexpression; no added CuCl2 in this comparison. cross_nutrient: true [zinc-enz-sod1-live2013] Atomic-resolution monitoring of protein maturation in live human cells by NMR. (2013). https://pubmed.ncbi.nlm.nih.gov/23455544/ DOI: 10.1038/nchembio.1202
Complete structured claim and evidenceAdding 10 µM ZnSO4 during human SOD1 expression in HEK293T cells promoted site-selective binding of one zinc ion per SOD1 subunit and the zinc-containing dimer.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Transient expression of human SOD1 and CCS in human HEK293T cells; in-cell NMR
- exposure
- 10 µM ZnSO4 immediately after transfection; 48 h expression before later copper manipulations.
- limitations
- HEK293T cells overexpressed SOD1/CCS above endogenous levels; these medium concentrations are experimental exposures, not dietary targets. Copper transfer and disulfide oxidation need not occur in a fixed coupled step in every cellular context.
- nutrient_topic
- Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
- organism
- Homo sapiens
- plain_language
- Zinc binding helps the cellular SOD1 protein reach a dimeric maturation intermediate.
- primary_references
- [zinc-enz-sod1-live2013] Atomic-resolution monitoring of protein maturation in live human cells by NMR. (2013). https://pubmed.ncbi.nlm.nih.gov/23455544/ DOI: 10.1038/nchembio.1202
- tissue_or_cell_type
- Human HEK293T cytoplasm
Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 729–740
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transient expression of human SOD1 and CCS in human HEK293T cells; in-cell NMR · source_derived_draft · unverified_draft
### zinc-enz-sod1-zinc-binding Adding 10 µM ZnSO4 during human SOD1 expression in HEK293T cells promoted site-selective binding of one zinc ion per SOD1 subunit and the zinc-containing dimer. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Zinc binding helps the cellular SOD1 protein reach a dimeric maturation intermediate. organism: Homo sapiens tissue_or_cell_type: Human HEK293T cytoplasm experimental_model: Transient expression of human SOD1 and CCS in human HEK293T cells; in-cell NMR limitations: HEK293T cells overexpressed SOD1/CCS above endogenous levels; these medium concentrations are experimental exposures, not dietary targets. Copper transfer and disulfide oxidation need not occur in a fixed coupled step in every cellular context. exposure: 10 µM ZnSO4 immediately after transfection; 48 h expression before later copper manipulations. cross_nutrient: false [zinc-enz-sod1-live2013] Atomic-resolution monitoring of protein maturation in live human cells by NMR. (2013). https://pubmed.ncbi.nlm.nih.gov/23455544/ DOI: 10.1038/nchembio.1202
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.