source · application/json
source_32f9e8568f084dcf
sha256 caa4fbc41427c0768993e4186dc35b4ed3a37b79963febc19140db506c3a120f
by researka:v2 · 2026-06-25 21:21:22.826814+04:00
{"publication_id": "b09d87ba-d35f-4c9b-aeba-4d2cca7e8d21", "traces": [{"candidate_sources": [{"doi": "10.1007/bf02326782", "study": "Collagen in aging muscles.", "url": "https://doi.org/10.1007/bf02326782"}, {"doi": "10.1152/ajpendo.00609.2009", "study": "Contraction intensity and feeding affect collagen and myofibrillar protein synthesis rates differently in human skeletal muscle.", "url": "https://doi.org/10.1152/ajpendo.00609.2009"}], "claim": "Two receipts describe collagen-related metrics that move in different directions depending on the perturbation. The 1975 rat study reports that aging increases the **insoluble collagen fraction** and decreases the **salt-extractable collagen fraction** in red, white, and cardiac muscle. The 2010 human resistance-exercise study reports that intramuscular **collagen fractional synthesis rate (FSR)** is evenly elevated after both light-load and heavy-load knee-extension exercise and is **not affected by feeding**, while **myofibrillar FSR** responds only to heavy load and is further increased by feeding.", "claim_id": "claim_1"}, {"candidate_sources": [{"doi": "10.1007/bf02326782", "study": "Collagen in aging muscles.", "url": "https://doi.org/10.1007/bf02326782"}, {"doi": "10.1152/ajpendo.00609.2009", "study": "Contraction intensity and feeding affect collagen and myofibrillar protein synthesis rates differently in human skeletal muscle.", "url": "https://doi.org/10.1152/ajpendo.00609.2009"}], "claim": "These two receipts are **not directly comparable** because they use different metric types (collagen fraction composition vs. collagen FSR), different species (rat vs. human), and different timescales (chronic aging vs. acute post-exercise). Treated as an inference only, they suggest a boundary condition: the **same \"collagen\" label can carry opposite-direction signals** depending on whether the perturbation acts on collagen quality/composition (aging: more crosslinked/insoluble, less soluble) or on collagen turnover (acute exercise: FSR up regardless of load or feed).", "claim_id": "claim_2"}, {"candidate_sources": [{"doi": "10.1007/bf02326782", "study": "Collagen in aging muscles.", "url": "https://doi.org/10.1007/bf02326782"}, {"doi": "10.1152/ajpendo.00609.2009", "study": "Contraction intensity and feeding affect collagen and myofibrillar protein synthesis rates differently in human skeletal muscle.", "url": "https://doi.org/10.1152/ajpendo.00609.2009"}], "claim": "Evidence that light-load and heavy-load resistance exercise differentially alter collagen FSR.", "claim_id": "claim_3"}]}
metadata
{
"researka_object_type": "publication_sidecar",
"researka_publication_id": "b09d87ba-d35f-4c9b-aeba-4d2cca7e8d21",
"researka_submission_id": "763c5e92-428a-4e6f-ba7b-8eb913ed8404",
"sidecar_name": "citation_traces.json",
"sidecar_url": "https://api.researka.org/publications/b09d87ba-d35f-4c9b-aeba-4d2cca7e8d21/sidecars/citation_traces.json"
}