This is a new journal with no inherited notes. The genuine normal seed contains 74 original source assertions, two products and 21 reference identifier/title pairs. Every source object, including qualifiers, ortholog identifiers and the counterintuitive UniProt product numbering, remains unchanged. The displayed functional alpha product is P02708-2; P02708-1 is the P3A-containing alpha+ product. Genuine Falcon research timed out and the configured fallback returned a quota failure; these receipts are preserved and no provider report was invented. Manual primary reading supplies the review.
The integrated core is alpha1 contribution to acetylcholine-gated cation-channel activity in the muscle receptor pentamer. It performs ligand-interface and pore-gating work with beta/delta and gamma or epsilon, rather than merely being necessary for the receptor. The core uses contributes_to explicitly. Existing enables and contributes_to source qualifiers are retained: historical annotations are not silently rewritten, and the reviewed biology does not imply an isolated functional alpha1 homomer. The official acetylcholine-receptor activity term directs nicotinic channels to GO:0022848; broad receptor/channel entries and the contextual postsynaptic channel entry are refined accordingly. Broad ion/cation-transport entries are refined to the explicit cation-transmembrane process GO:0098655, preserving cation specificity rather than dropping it. No new annotation is added. [PMID:9221765; PMID:27375219]
The source organism and product distinctions matter. Original PMID:8872460 human patient muscle/endplate physiology is accompanied by mouse alpha/beta/delta/epsilon cDNAs expressed in HEK cells. Original PMID:9221765 instead explicitly uses human alpha/beta/delta/epsilon constructs. PMID:27375219 tests the human receptor and engineered alpha-pore valine, despite clinical emphasis on beta/epsilon variants. The approximately 4-Angstrom structure in PMID:15701510 concerns Torpedo marmorata postsynaptic membranes; it is positive conserved complex evidence, not a human structure. The precise older constructs were not aligned to every current product.
The genuine abstract of PMID:8788941 explicitly compares human alpha with alpha+ in Xenopus oocytes and reports that alpha+ does not enter functional channels in that system. Current UniProt identifies the P3A product consistently. Original full Methods could not be recovered, so exact details beyond the abstract/product record are not invented. No unscoped NOT annotation is added and normal alpha function is not assigned equally to both products.
Actual full PMID:16527851 Methods and Results directly establish calcium entry through human alpha-containing muscle receptors. Adult alpha/beta/delta/epsilon combinations were expressed in rat GH4C1 cells, giving a fractional calcium current near 7%; fetal combinations were around 2–3% and were corroborated in human myotubes. Intracellular-store controls and nontransfected controls support the measured conductance. Adult native-muscle fractional current was not directly measured. Epsilon largely explains the human–mouse adult difference, and the tested alpha mutations do not alter the calcium fraction. Alpha1 participation in transport is therefore supported, without assigning autonomous calcium selectivity. This same paper directly measures nicotine-evoked current, retained as a non-core pharmacological response. PMID:16527851
Presynaptic modulation and the derived presynapse location remain UNDECIDED. The corrected peer donor queries recover actual experimental grounding for other nicotinic subunits; failed direct MGI/RGD requests are not zero-hit evidence. The historical PAINT node and an alpha1-specific presynaptic function were not independently resolved. Postsynaptic muscle biology does not disprove an additional presynaptic pool. No donor-count, self-source, wrong-paralog or circularity objection is made. All IBA source node identifiers are retained with explicit uninspected historical placement.
PMID:8872460 measures compound muscle action potentials, endplate currents, muscle junctional-fold injury and postsynaptic depolarization block. It supports refining the original neuronal action-potential term to neuromuscular transmission, and neuronal cellular homeostasis to muscle-cell homeostasis. These changes identify the actual source endpoint rather than claiming that alpha1 can never be expressed or function in neurons. The existing muscle-maintenance assertion remains non-core. The original PMID:9221765 neuromuscular-junction-development term includes arrangement and disassembly by its current definition; observed fold loss supports a non-core maintenance/organization interpretation, not normal initiation of synaptogenesis.
The full PMID:18252226 study links biallelic human CHRNA1 defects to fetal akinesia and contractures, with mouse somite expression; Results explicitly report reduced muscle mass across affected individuals. A performed receptor-mediated excitatory step supports the existing movement assertion. In contrast, the muscle-growth term specifies changes in muscle size/mass via fiber number or size: the genuine reduced-mass observation does not separate such a CHRNA1-performed step from consequences of fetal immobility and explicitly treats early mesodermal participation as speculative. That annotation is marked over-annotated without denying secondary effects of immobility on growth. Its therapeutic response belongs to a RAPSN case and is not a CHRNA1 rescue experiment.
HPA's authentic CHRNA1 XML and actual Rh30/LHCN-M2 images corroborate plasma-membrane localization; they do not establish receptor electrophysiology or both-product localization. Four official Reactome reactions were traversed through their catalyst or receptor sets to explicit human P02708 entity480553 in the plasma membrane. The exact intermediate complex532595 is labeled homomeric and contains five copies of CHRNA1; this source representation is recorded rather than described as a heteropentamer. Independent human assays support the retained location. Neither this modeled composition nor the event titles are adopted as proof of a functional alpha1 homomer or alpha-specific calcium selectivity. The original cell-surface PMID:12928480 was recovered as authentic indexed author-uploaded Results/Methods: intact-cell toxin binding and extracellular delta-antibody detection concern the assembled receptor. These external readings do not overwrite normal abstract caches.
PMID:7619526, PMID:9546329 and PMID:21480901 remain original-abstract-only in this audit. Their authentic positive statements and independent full target experiments support clearly established receptor/neuromuscular biology, with construct, clinical-cohort and Torpedo/Xenopus limits made explicit. No inaccessible experimental assertion is rejected from its title. PMID:8872460 and PMID:12928480 full-body access was recovered externally and their review access flags reflect actual access, while selected cache bytes remain immutable.
The source artifact records meaningful authored evidence paraphrases, exact original source objects, official terms/domain records, literal current donor records, donor-request limitations, HPA images, Reactome target chains, source selections and the GO-CAM index lookup. These are reproducible provenance extracts, not a custom sequence or functional analysis. No NEW process, inferred missing family label or guessed ancestral placement is asserted. Primary quotations are deliberately short; the complete authored journal adds no quotations.
Removed 74 quotations of authored audit interpretations from file-reference supporting text. Bare file citations remain as links to the provenance index; they are not independent scientific support. The artifact reference no longer marks its own interpretations VERIFIED. Primary quotations, source-specific reasons, all annotation actions and the biological synthesis remain unchanged.
The three GO:0042391 assertions are refined to the existing GO:0060078 term. The human endplate measurements in PMID:8872460 and PMID:9221765 establish the postsynaptic membrane scope. The former reports endplate-potential summation in Results and predicts depolarization block in Discussion; the latter measures endplate amplitudes and decay and separately tests human alpha V249F receptors. The ARBA assertion is refined using this independent target evidence, with its source identifier unchanged. No new process assertion is added.
Annotation support now cites the primary publications, source GO_REF or Reactome records and, where used, the external InterPro, QuickGO, HPA or physical-entity records directly. The authored source index remains a provenance reference, with no per-row support pointers. Its historical annotation-fact prose is retained for audit and superseded by the current YAML reasons and this entry. In particular, the repeated PMID:9221765 wording did not identify the original source of GO_REF annotations. The current reasons distinguish family/domain transfer, ARBA inference, PAINT assertion, orthology and direct experiments. Historical PAINT node placement remains uninspected, and the two presynaptic assertions remain UNDECIDED; the logical presynapse inference follows its unresolved premise.
The captured UniProt P02709 record identifies bovine CHRNA1, correcting the prior Torpedo label in one ISS reason. No source accession is rewritten. The muscle-homeostasis refinement remains non-core, consistent with the independently retained assertion. The core's title fragment is replaced by a short Results anchor; a separate endplate-amplitude anchor supports the membrane-potential refinement. Existing notes and source bytes remain exact, and cumulative primary quotations across the YAML, notes and index are audited. The earlier notes' workflow-heavy wording remains historical provenance rather than being rewritten.
Reviewed all seeded assertions against human receptor reconstitution, calcium-current measurements and the existing source-specific audit. Original row payloads, product identifiers, signs and inherited proposals are retained. The core is a subunit contribution to the heteropentamer: alpha1 twice, beta1, delta and gamma or epsilon. Human PMID:27375219 / PMID:16527851 functional experiments are distinct from the native bovine structures in PMID:39085615 and Torpedo structural/pharmacological sources PMID:15701510 / PMID:21480901. The human calcium-current study independently supports complex-level calcium conduction and separates fetal/adult channels; no subunit alone is a calcium-selective channel.
Historical binding observations remain observations. Where old reviews kept uninformative GO:0005515 as non-core, the current binding policy requires removal of that annotation only; supported specific keratin binding remains refined, and historical notes/provenance are not rewritten. The inherited CHRNG acetylcholine-binding proposal is retained as an inherited claim based on complementary ligand-pocket contribution in the bovine structural comparison; it is not a new gap filled in this module audit. CHRNA1's displayed P02708-2 corresponds to named isoform1, while P02708-1 is the P3A-containing named isoform2: accession suffix and displayed name are not interchangeable.
Broad signaling, channel and transport assertions are resolved to measured receptor chemistry when warranted. Root organelle assertions are not replaced by subcompartments. Fetal akinesia establishes movement failure; reduced muscle mass does not independently prove a receptor-performed muscle growth program. Genuine presynaptic/homeostatic uncertainties in the prior fully sourced reviews remain explicit rather than being cleared mechanically. Provider/publication attempts are recorded by the shared normal acquisition job in acetylcholine-foundation-fetch; provider prose is not evidence.
Normalized human-facing citation identifiers and spacing, preserving every machine annotation field and existing supporting quotation. Removed exactly repeated summary prefixes from reasons where a separate substantive explanation remains. Removed 8 blanket reference-review templates; source-specific assessments and the underlying references/evidence remain available. All annotation actions remain unchanged for this gene.