Component
Mammalian thioredoxin reductases, isoform unspecified
Mammalian thioredoxin reductases, isoform unspecified. Species, exposure and limitations are retained in each linked claim.
1 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
Purified mammalian thioredoxin reductases, including enzyme from human placenta, catalyzed NADPH-dependent lipoic-acid reduction.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/ala-research/8769129.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9ba6524ef04fdc03c0a6d108325b8a96fe7ad0748be4d7056e694b5afa2a8499", "start_char": 0, "end_char": 1307, "text_sha256": "9ba6524ef04fdc03c0a6d108325b8a96fe7ad0748be4d7056e694b5afa2a8499"}
- experimental_model
- Purified mammalian thioredoxin reductase assays
- exposure
- NADPH-dependent lipoate/lipoamide reduction
- limitations
- Isoform identity was not resolved as a specific human TXNRD gene in the indexed abstract; assay rate comparisons are not tissue-wide flux rankings.
- nutrient_topic
- Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
- organism
- Human placenta, calf tissues and rat liver
- plain_language
- The thioredoxin system provides another route to DHLA.
- primary_references
- [ala-p8769129] Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. (1996). https://pubmed.ncbi.nlm.nih.gov/8769129/ DOI: 10.1006/bbrc.1996.1165
- tissue_or_cell_type
- Purified thioredoxin reductases
Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 754–765
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian thioredoxin reductase assays · source_derived_draft · unverified_draft
### ala-thioredoxin-reductase-dhla Purified mammalian thioredoxin reductases, including enzyme from human placenta, catalyzed NADPH-dependent lipoic-acid reduction. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The thioredoxin system provides another route to DHLA. organism: Human placenta, calf tissues and rat liver tissue_or_cell_type: Purified thioredoxin reductases experimental_model: Purified mammalian thioredoxin reductase assays limitations: Isoform identity was not resolved as a specific human TXNRD gene in the indexed abstract; assay rate comparisons are not tissue-wide flux rankings. exposure: NADPH-dependent lipoate/lipoamide reduction evidence_span: {"source_cache": "artifacts/ala-research/8769129.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9ba6524ef04fdc03c0a6d108325b8a96fe7ad0748be4d7056e694b5afa2a8499", "start_char": 0, "end_char": 1307, "text_sha256": "9ba6524ef04fdc03c0a6d108325b8a96fe7ad0748be4d7056e694b5afa2a8499"} [ala-p8769129] Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. (1996). https://pubmed.ncbi.nlm.nih.gov/8769129/ DOI: 10.1006/bbrc.1996.1165
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.