Version history

{
  "description": "The debate identified chaperone system differences as a key mechanism but failed to establish which specific chaperone components drive tissue selectivity. Understanding these networks is essential for developing tissue-targeted protein folding therapies.\n\nSource: Debate session sess_SDA-2026-04-08-gap-pubmed-20260406-062222-b5f44522 (Analysis: SDA-2026-04-08-gap-pubmed-20260406-062222-b5f44522)",
  "domain": "protein folding",
  "status": "open",
  "priority_score": 0.85,
  "source": "debate:sess_SDA-2026-04-08-gap-pubmed-20260406-062222-b5f44522",
  "resolution_criteria": "Gap closes when: (1) A proteomics study comparing chaperone network compositions across at least three CNS cell types (neurons, astrocytes, oligodendrocytes) identifies >=5 chaperone components with >= 2-fold expression differences between vulnerable and resistant cell types; and (2) siRNA/CRISPR knockdown of the top candidate chaperones in iPSC-derived neurons and astrocytes reproduces >=30% differential aggregation of the misfolding-prone protein; and (3) results are replicated in at least one independent in vivo model (mouse or human postmortem tissue). Accepted deliverable: peer-reviewed publication or preprint with raw proteomics and aggregation quantification data publicly deposited.",
  "market_price": 0.5
}