{
  "title": "What this review means",
  "includeSubclaimIllustrations": false,
  "redteamReviewed": true,
  "accessNotice": "Source checking used complete abstracts/status records and selected original partial-body passages. No complete-paper audit or independent scientific peer review is claimed. Detailed access counts and limitations appear in the review.",
  "overview": "Histone proteins carry chemical modifications that can affect gene activity. This review asks whether combinations form instructions beyond the effects of each individual mark.",
  "implications": "The preregistered SC3 gate returns Γ. Structural recognition, cellular recruitment and engineered reporter combinations make the mechanism plausible, while direct endogenous factorial mark dependence beyond individual effects remains unresolved. This is not a refutation of histone function: SC2 reaches Ζ on independent mark/reader perturbations with functional outcomes, and the observational SC1 stays Β on its own evidence class. Recent bivalent-reader and NURF results are included rather than inheriting the index grade uncritically.",
  "limitations": "62 primary reports with 9 selected partial-body examinations; density, heterogeneous controls and incomplete access set the confidence, not correctness. The grade applies to the exact registered claim; stronger findings for narrower subclaims remain separate. No complete-paper audit or blinded calibration is claimed. This educational review does not establish an individual treatment recommendation."
}