Component
Human ISCU
Human ISCU. Species, exposure and limitations are retained in each linked 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
[2Fe-2S]-loaded human ISCU and ISCA2 reconstituted catalytically active human LIAS in vitro.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/ala-research/33562493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac", "start_char": 0, "end_char": 1544, "text_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac"}
- experimental_model
- Recombinant human LIAS cluster reconstitution, EPR and LC-MS
- exposure
- [2Fe-2S]-loaded ISCU or ISCA2 donors
- limitations
- In vitro donor capacity does not establish a unique physiological donor or exclude other routes.
- nutrient_topic
- Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
- organism
- Human proteins
- plain_language
- These carrier proteins can help rebuild active enzyme under assay conditions.
- primary_references
- [ala-p33562493] Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly. (2021). https://pubmed.ncbi.nlm.nih.gov/33562493/ DOI: 10.3390/ijms22041598
- tissue_or_cell_type
- Two LIAS iron-sulfur sites
Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 390–401
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human LIAS cluster reconstitution, EPR and LC-MS · source_derived_draft · unverified_draft
### ala-iscu-isca2-reconstitution [2Fe-2S]-loaded human ISCU and ISCA2 reconstituted catalytically active human LIAS in vitro. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: These carrier proteins can help rebuild active enzyme under assay conditions. organism: Human proteins tissue_or_cell_type: Two LIAS iron-sulfur sites experimental_model: Recombinant human LIAS cluster reconstitution, EPR and LC-MS limitations: In vitro donor capacity does not establish a unique physiological donor or exclude other routes. exposure: [2Fe-2S]-loaded ISCU or ISCA2 donors evidence_span: {"source_cache": "artifacts/ala-research/33562493.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac", "start_char": 0, "end_char": 1544, "text_sha256": "4261f63098ce640cc87368d3f23f294441fdfa2a3f9b271086821fc1196bb3ac"} [ala-p33562493] Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly. (2021). https://pubmed.ncbi.nlm.nih.gov/33562493/ DOI: 10.3390/ijms22041598
Complete structured claim and evidence
Where it participates (unsigned role)
The NFS1–ISD11–ACP core associates with ISCU, frataxin and ferredoxin to support Fe-S cluster biosynthesis.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/iron-research/28634302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04", "start_char": 0, "end_char": 1850, "text_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04"}
- experimental_model
- Crystallography, electron microscopy, kinetics and cell studies
- exposure
- SDA-complex structural analysis
- limitations
- Hybrid structural system: bacterial ACP must not be silently labeled human NDUFAB1. Direct dietary B6/B5 effects were not tested.
- nutrient_topic
- Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
- organism
- Human NFS1/ISD11 with bacterial ACP in the recombinant structural complex
- plain_language
- Iron needs an assembly system and a sulfur supply before it becomes a working iron-sulfur cofactor.
- primary_references
- [iron-p28634302] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
- tissue_or_cell_type
- Mitochondrial Fe-S assembly machinery
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 1161–1172
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystallography, electron microscopy, kinetics and cell studies · source_derived_draft · unverified_draft
### iron-sda-assembly The NFS1–ISD11–ACP core associates with ISCU, frataxin and ferredoxin to support Fe-S cluster biosynthesis. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron needs an assembly system and a sulfur supply before it becomes a working iron-sulfur cofactor. organism: Human NFS1/ISD11 with bacterial ACP in the recombinant structural complex tissue_or_cell_type: Mitochondrial Fe-S assembly machinery experimental_model: Crystallography, electron microscopy, kinetics and cell studies limitations: Hybrid structural system: bacterial ACP must not be silently labeled human NDUFAB1. Direct dietary B6/B5 effects were not tested. exposure: SDA-complex structural analysis evidence_span: {"source_cache": "artifacts/iron-research/28634302.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04", "start_char": 0, "end_char": 1850, "text_sha256": "82faf07d78311d063c1d990ebb922062650054be372fb324fa67020790c9fa04"} [iron-p28634302] Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. (2017). https://pubmed.ncbi.nlm.nih.gov/28634302/ DOI: 10.1073/pnas.1702849114
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.