Component
Tetrathiomolybdate-copper-yeast Atx1 cluster
Tetrathiomolybdate-copper-yeast Atx1 cluster. 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
The drug-Atx1 complex inhibited copper transfer between copper-trafficking proteins in the experimental system.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"}
- experimental_model
- Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments
- exposure
- Tetrathiomolybdate exposure
- limitations
- Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins.
- nutrient_topic
- Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
- organism
- Saccharomyces cerevisiae proteins; comparison with animal drug complexes
- plain_language
- Trapping the copper interrupted its handoff to another protein.
- primary_references
- [mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
- tissue_or_cell_type
- Purified copper chaperones
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1613–1624
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments · source_derived_draft · unverified_draft
### mo-ttm-copper-transfer The drug-Atx1 complex inhibited copper transfer between copper-trafficking proteins in the experimental system. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Trapping the copper interrupted its handoff to another protein. organism: Saccharomyces cerevisiae proteins; comparison with animal drug complexes tissue_or_cell_type: Purified copper chaperones experimental_model: Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments limitations: Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins. exposure: Tetrathiomolybdate exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"} [mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
Complete structured claim and evidence
Where it participates (unsigned role)
Tetrathiomolybdate formed a stable sulfur-bridged copper-molybdenum cluster with yeast Atx1.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"}
- experimental_model
- Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments
- exposure
- Tetrathiomolybdate exposure
- limitations
- Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins.
- nutrient_topic
- Molybdenum research collection; topical membership is not evidence of a direct dietary effect. · Molybdenum
- organism
- Saccharomyces cerevisiae proteins; comparison with animal drug complexes
- plain_language
- A sulfur-rich molybdenum drug can trap copper in a protein complex.
- primary_references
- [mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
- tissue_or_cell_type
- Purified copper chaperones
Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1600–1611
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments · source_derived_draft · unverified_draft
### mo-ttm-copper-cluster Tetrathiomolybdate formed a stable sulfur-bridged copper-molybdenum cluster with yeast Atx1. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: A sulfur-rich molybdenum drug can trap copper in a protein complex. organism: Saccharomyces cerevisiae proteins; comparison with animal drug complexes tissue_or_cell_type: Purified copper chaperones experimental_model: Yeast Atx1 crystallography, spectroscopy and copper-transfer experiments limitations: Drug and yeast-protein chemistry; not evidence that normal human dietary molybdate strips copper from proteins. exposure: Tetrathiomolybdate exposure evidence_span: {"source_cache": "artifacts/molybdenum-research/19965379.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57", "start_char": 0, "end_char": 950, "text_sha256": "166eb55335870bc9843fdb0c61becaa318603b25c601bbfa8f69a469dab89e57"} [mo-p19965379] Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation. (2010). https://pubmed.ncbi.nlm.nih.gov/19965379/ DOI: 10.1126/science.1179907
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.