Component
Ribosomal protein S6 phosphorylation
Ribosomal protein S6 phosphorylation. 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 acts on it
Regulation of S6 phosphorylation was prevented only by direct modification of the metal-liganding groups of the biguanide structure, supporting that AMPK and S6 phosphorylation are regulated independently by biguanides.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/metformin-research/22492524.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a0b1587d871d78b3bccefc5a47b277191faf6bc3b070dbe43295a0b21a633c56", "start_char": 0, "end_char": 1526, "text_sha256": "a0b1587d871d78b3bccefc5a47b277191faf6bc3b070dbe43295a0b21a633c56"}
- experimental_model
- Copper sequestration and biguanide analogues in cells, with mitochondrial measurements
- exposure
- Metformin and analogues with and without copper sequestration
- limitations
- A metal-dependence result using chemical sequestration and structural analogues. It does not establish that copper status in a person changes the drug’s effect.
- nutrient_topic
- Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. · Metformin
- organism
- Cultured cells
- plain_language
- Two of the drug’s effects depend on the metal in different ways, so they are separate routes.
- primary_references
- [metformin-p22492524] Cellular responses to the metal-binding properties of metformin. (2012). https://pubmed.ncbi.nlm.nih.gov/22492524/ DOI: 10.2337/db11-0961
- tissue_or_cell_type
- Mitochondria and cytoplasm
Metformin: transport, molecular targets, gut mechanisms and nutrient interactions (2026-09-19) · lines 1360–1371
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Copper sequestration and biguanide analogues in cells, with mitochondrial measurements · source_derived_draft · unverified_draft
### metformin-copper-s6-independent Regulation of S6 phosphorylation was prevented only by direct modification of the metal-liganding groups of the biguanide structure, supporting that AMPK and S6 phosphorylation are regulated independently by biguanides. Condition category: normal nutrient_topic: Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. plain_language: Two of the drug’s effects depend on the metal in different ways, so they are separate routes. organism: Cultured cells tissue_or_cell_type: Mitochondria and cytoplasm experimental_model: Copper sequestration and biguanide analogues in cells, with mitochondrial measurements limitations: A metal-dependence result using chemical sequestration and structural analogues. It does not establish that copper status in a person changes the drug’s effect. exposure: Metformin and analogues with and without copper sequestration evidence_span: {"source_cache": "artifacts/metformin-research/22492524.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a0b1587d871d78b3bccefc5a47b277191faf6bc3b070dbe43295a0b21a633c56", "start_char": 0, "end_char": 1526, "text_sha256": "a0b1587d871d78b3bccefc5a47b277191faf6bc3b070dbe43295a0b21a633c56"} [metformin-p22492524] Cellular responses to the metal-binding properties of metformin. (2012). https://pubmed.ncbi.nlm.nih.gov/22492524/ DOI: 10.2337/db11-0961
Complete structured claim and evidencePost-exercise mTORC1 signalling measured as rps6 phosphorylation was blunted at 1 and 48 hours after training, basal FOXO1 protein content increased 1.3-fold, and training-induced increases in heat shock protein 27 were attenuated with reduced total heat shock protein 72.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/cold-research/31513450.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f39d3b6bef4879805e7aab7b14df67921ac12765af5d4466836936039ad7a872", "start_char": 0, "end_char": 2195, "text_sha256": "f39d3b6bef4879805e7aab7b14df67921ac12765af5d4466836936039ad7a872"}
- experimental_model
- Sixteen men completing seven weeks of whole-body resistance training with immersion or passive recovery
- exposure
- 15 minutes at 10 degrees C after each session, three days a week for seven weeks
- limitations
- A second training study with molecular endpoints. It reproduces the fibre-size result but not the strength result, which is the disagreement recorded in this collection.
- nutrient_topic
- Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Cold water immersion
- organism
- Human
- plain_language
- The building signal was turned down, the breakdown marker went up, and the muscle stress proteins did not accumulate.
- primary_references
- [cold-p31513450] Cold water immersion attenuates anabolic signaling and skeletal muscle fiber hypertrophy, but not strength gain, following whole-body resistance training. (2019). https://pubmed.ncbi.nlm.nih.gov/31513450/ DOI: 10.1152/japplphysiol.00127.2019
- tissue_or_cell_type
- Skeletal muscle
Cold water immersion: cold sensing, heat production, the catecholamine axis and what repeated exposure changes (2026-09-19) · lines 845–856
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Sixteen men completing seven weeks of whole-body resistance training with immersion or passive recovery · source_derived_draft · unverified_draft
### cold-cwi-anabolic-catabolic Post-exercise mTORC1 signalling measured as rps6 phosphorylation was blunted at 1 and 48 hours after training, basal FOXO1 protein content increased 1.3-fold, and training-induced increases in heat shock protein 27 were attenuated with reduced total heat shock protein 72. Condition category: normal nutrient_topic: Cold water immersion research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: The building signal was turned down, the breakdown marker went up, and the muscle stress proteins did not accumulate. organism: Human tissue_or_cell_type: Skeletal muscle experimental_model: Sixteen men completing seven weeks of whole-body resistance training with immersion or passive recovery limitations: A second training study with molecular endpoints. It reproduces the fibre-size result but not the strength result, which is the disagreement recorded in this collection. exposure: 15 minutes at 10 degrees C after each session, three days a week for seven weeks evidence_span: {"source_cache": "artifacts/cold-research/31513450.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f39d3b6bef4879805e7aab7b14df67921ac12765af5d4466836936039ad7a872", "start_char": 0, "end_char": 2195, "text_sha256": "f39d3b6bef4879805e7aab7b14df67921ac12765af5d4466836936039ad7a872"} [cold-p31513450] Cold water immersion attenuates anabolic signaling and skeletal muscle fiber hypertrophy, but not strength gain, following whole-body resistance training. (2019). https://pubmed.ncbi.nlm.nih.gov/31513450/ DOI: 10.1152/japplphysiol.00127.2019
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.