Original evidence-method reference preserved. This identifies the annotation framework, not a reconstruction of every historical rule or PAINT ancestral node.

Original evidence-method reference preserved. This identifies the annotation framework, not a reconstruction of every historical rule or PAINT ancestral node.

Original evidence-method reference preserved. This identifies the annotation framework, not a reconstruction of every historical rule or PAINT ancestral node.

Original evidence-method reference preserved. This identifies the annotation framework, not a reconstruction of every historical rule or PAINT ancestral node.

Human recombinant 69- and 82-kDa ChAT products retain acetyltransferase activity and differ in localization; phosphorylation by particular kinases alters their activity. The enzyme is the kinase substrate, not itself a protein kinase.

Human ChAT binary structures with choline, CoA and an acetyl-CoA analogue support substrate recognition and a modeled direct acetyl-transfer mechanism; a ternary Michaelis complex is modeled rather than directly solved.

The original screen excluded autoactivating baits, used HIS3/URA3/lacZ reporters, repeated the search space and retested pooled positives pairwise. Its separate mammalian DULIP experiment tested a random subset; no individual CHAT pair is identified here as independently validated in that assay. Exact CHAT-3/partner records, including fragment boundaries, support assay-scoped associations rather than a native neuronal interaction network.

Authentic normal cache and official current event graph inspected. CHAT target membership and catalytic reaction are genuine; broad parent-pathway process transfer is assessed separately. The three entries share the same curated reaction and are not independent experimental evidence.

Authentic normal cache and official current event graph inspected. CHAT target membership and catalytic reaction are genuine; broad parent-pathway process transfer is assessed separately. The three entries share the same curated reaction and are not independent experimental evidence.

Authentic normal cache and official current event graph inspected. CHAT target membership and catalytic reaction are genuine; broad parent-pathway process transfer is assessed separately. The three entries share the same curated reaction and are not independent experimental evidence.

Normal cache is abstract-only; selected indexed original primary Results/localization context independently inspected. Human HEK293 constructs and large-product nuclear enrichment are resolved. Intact-cell acetylcholine measurements do not locate synthesis to a particular compartment.

Normal cache is abstract-only. Selected indexed original localization, mutant/shuttling Results and Discussion inspected. Nuclear activity with supplied substrates is reported, but detailed isolated-nuclei enzyme-assay Methods were not independently recovered; no claim of a resolved physiological nuclear reaction is made.

Authentic normal abstract and identifier inspected. It explicitly reports isoform-specific antibodies and nuclear 82-kDa ChAT in native human CNS tissue. Full antibody controls, Methods and figure pixels were not accessed; no stronger assay detail is claimed.

Human recombinant-enzyme kinetics distinguish an inactive E441K variant from eight mutants with reduced catalytic efficiency; the endplate phenotype is interpreted together with these direct enzyme measurements. Full primary Methods and Results were inspected externally, separately from the abstract-only normal cache.

Human ChAT-GFP increases SLC5A7 expression in the tested SH-SY5Y system, with nuclear targeting and catalytic competence required. The inactive nuclear mutant fails to induce the transcript; the downstream mechanism remains unresolved, so this is not assigned as direct DNA binding or coactivator activity.

Authored extraction of genuine database fields and source-access evidence, independently checked against the literal records in the campaign peer review. VERIFIED applies to the correctness of that extraction and its identified provenance, not to an independent biological experiment, provider report or certification of every physiological screen interaction. The added follow-up evidence paragraphs are explicitly authored paraphrases, not primary-source quotations.