GGCX performs protein glutamate carboxylation and vitamin K hydroquinone epoxidation as coupled chemistry at the endoplasmic-reticulum membrane. The evidence archive preserves original source contexts and the distinct sequence and assay records; it is provenance, not an independent experiment.
PMID:1749935(https://pubmed.ncbi.nlm.nih.gov/1749935/) links expression of cloned human GGCX to increased microsomal carboxylase activity. Its three-helix prediction and lipoxygenase similarity are historical observations, not additional enzyme functions. PMID:10910912(https://pubmed.ncbi.nlm.nih.gov/10910912/) reports terminal tags in 293 cells and reporter segments in canine microsomes; the authentic abstract supports amino-terminal cytoplasmic and carboxyl-terminal lumenal orientation. Neither original Methods section was recovered.
Selected full text of PMID:39880037(https://pubmed.ncbi.nlm.nih.gov/39880037/) separates full-length human enzyme from an engineered membrane-domain/BRIL fusion and directly tests carboxylation and vitamin K epoxidation. The nine-helix fold includes membrane-associated/reentrant structure; it should not be simplified into nine independent full bilayer crossings. PMID:41290650(https://pubmed.ncbi.nlm.nih.gov/41290650/) supplies human recognition and biochemical evidence for a bicarbonate-linked model. PMID:41888148(https://pubmed.ncbi.nlm.nih.gov/41888148/) examines five human substrates with separate carboxylation and epoxidation assays. An interface mutant's epoxide readout is not automatically a direct measurement of every carboxylated substrate residue. Proton transfer, substrate order, gas entry and unidentified peptide-like densities retain the papers' stated inferential limits.
The selected original PMID:12963724(https://pubmed.ncbi.nlm.nih.gov/12963724/) supports a structural Cys99–Cys450 disulfide, not free catalytic thiols; its topology diagram derives from earlier work. PMID:11570873(https://pubmed.ncbi.nlm.nih.gov/11570873/) remains abstract-only, with enzyme species/construct unverified. PMID:39880952(https://pubmed.ncbi.nlm.nih.gov/39880952/) has partial primary access: publisher abstract/extended captions, supplement and reporting summary, but not main Methods/Results. Modeled propeptides or a C-terminal peptide are distinct from solved complexes and demonstrated self-carboxylation.
PMID:17073445(https://pubmed.ncbi.nlm.nih.gov/17073445/) supports enzyme chemistry in its authentic abstract; original Methods/Results remain inaccessible. The curated UniProt FUNCTION record independently supports the osteocalcin input. The unresolved component of the conjunction is the neurotransmitter-suppression relationship. Its absence from an abstract or curated summary does not disprove it.
Selected mouse PMID:17327402(https://pubmed.ncbi.nlm.nih.gov/17327402/) demonstrates loss of fetal-liver microsomal enzyme activity after Ggcx deletion. GGCX performs precursor-modifying chemistry, so protein maturation is not merely a substrate-necessity inference. Microsomal enrichment alone does not determine membrane orientation. The human is_active_in ER-lumen assertion has positive curated topology support; the review retains it as a non-core compartment facet alongside the core ER-membrane location.
For PMID:25264202(https://pubmed.ncbi.nlm.nih.gov/25264202/), only the authentic abstract is available for assessment. The previously attributed publisher highlights could not be substantiated in the retained captures. Each unresolved endpoint remains distinct; no annotation is rejected from abstract omission. The human rows preserve their literal IEA provenance and genuine experimental mouse donor records. Clinical coagulation evidence (PMID:9845520(https://pubmed.ncbi.nlm.nih.gov/9845520/)) is retained without making GGCX a circulating coagulation protease; the codon/amino-acid wording discrepancy is explicit in its assessment.
Direct official FASTAs reconstruct P38435-1 at 758 residues and P38435-2 at 701 by deleting canonical positions 15–71. That deletion overlaps part of the first annotated membrane helix; its effects on activity or insertion remain unresolved. The declared initiator-cleaved chain 2–758 is not another splice product. The cDNA-resource attribution for VSP_046179 is distinct from PMID:9166845(https://pubmed.ncbi.nlm.nih.gov/9166845/), whose two transcripts differ in 3-prime untranslated sequence. Tagged constructs and engineered fusions are not extra natural products.
The actual PTHR12639 book contains 67 nodes, 35 leaves and 1157 alignment columns. Exact human AN20/PTN002489209 descends from AN0/PTN002651685 for catalytic activity/vitamin binding and AN6/PTN000974017 for vitamin K metabolism. Literal donor sets and target sequence were replayed. Self-evidence and the single rat vitamin-binding donor are legitimate, and no retained target-path loss was found. The selected Lys218 alignment neighborhood supports only that bounded conservation check; it does not establish every catalytic residue or shorter-product activity.
Nine official Reactome reactions share catalyst 159812, linked through entity 159860 to human P38435 at the ER membrane. Eight model normal substrate modification. R-HSA-9673231 is a FailedReaction because F9 propeptide variants impair recognition, with normal GGCX retained; it is not a GGCX NOT assertion. Reaction lumen compartments do not automatically assign every participant as a freely soluble lumen resident.
All 39 original contexts and all 16 exporter columns are preserved. The genuine native seed has 38 keys, exactly matching the forecast: raw2 is omitted by key collapse with raw3. The actual 39-row review restores raw2 as an original at index 38. Both extension expressions contain one AND group, with three and two atoms respectively; no OR is flattened. BFO:0000050, RO:0002233 and RO:0002234 are the actual predicates. CHEBI:28433 is phyllohydroquinone, CHEBI:15759 is 2,3-epoxyphylloquinone, and P02818 is osteocalcin. The literal GO:0046929 label is negative regulation of neurotransmitter secretion.
The qualified union has 39 native source paths: 25 publications, 11 Reactome entries and three family files. All 39 are now present: 13 inherited sources are unchanged and 26 were acquired through the native helpers. All 39 export contexts match the private records; the 38 seed records and two product sequences were verified. Four publication excerpts retain their exact native byte offsets and eight public occurrences. One additional three-word UniProt excerpt occurs only in the review; its archive entry contains a hash and locator. The current total is five distinct excerpts and nine public occurrences, within the per-source budgets. Raw2 and all five flat atoms are now restored in the actual review. The genuine CREATE history and affected checks are complete; their outcomes are recorded in the archive.
Reference full_text_unavailable booleans describe the normal cached record. They do not claim that externally accessible full text was or was not read. Every reference_review states its actual reading scope, including abstract-only resources, selected original sections and partial access. A new native full-text cache must be inspected before any expanded source claim. No figure pixels, supplements or constructs are implied beyond the named reading scope.
The newly available native full-text caches for PMID:41290650(https://pubmed.ncbi.nlm.nih.gov/41290650/) and PMID:41888148(https://pubmed.ncbi.nlm.nih.gov/41888148/) were inspected in the selected functional Methods and Results passages already described above. Their cache-availability flags are now false for full_text_unavailable. No additional function, product or experimental scope is inferred from cache availability.
Initial default validation and strict GOA matching passed. The legacy term-action check emitted one advisory: the original neurotransmitter/osteocalcin conjunction is UNDECIDED while unqualified carboxylase activity is accepted elsewhere. The current action-consistency rules table contains no ACCEPT/UNDECIDED rule; no per-annotation exception is added. Computed DRAFT status retains all five scientific uncertainties. The genuine codex CREATE history, private rendering, local links and scoped authored whitespace checks passed. Local checks do not establish publication or integration acceptance.
The current reasons distinguish the complete contextual assertions and omit internal row keys. Natural-product entries retain identifiers and sequence provenance; functional limits remain in the biological notes above and the appended journal. All 39 original contexts, decisions, five extension atoms, four excerpts and 39 source files are unchanged. The four-file follow-up and genuine EDIT history are complete. Default validation and strict GOA matching passed for all 39 originals; computed DRAFT status retains five scientific UNDECIDED judgments. One legacy term-action advisory remains for accepted base catalysis versus the unresolved complete assertion. History, private rendering, local links and authored whitespace checks passed. All 39 sources and the ontology cache are unchanged. These follow-up outcomes are recorded separately from the initial execution record; publication and integration remain separate.
The qualified activity reason now credits the supported substrate atom and isolates the unresolved process relationship. The lumen reason cites actual curated topology. All 39 original contexts and actions, two products, five extension atoms and 39 source files remain unchanged. The prior four publication excerpts are unchanged. The four-file follow-up and genuine EDIT history are complete. Default validation and strict GOA matching passed for all 39 originals; computed DRAFT status retains five scientific UNDECIDED judgments. One legacy term-action advisory remains for accepted base catalysis versus the unresolved complete assertion. History, private rendering, local links and authored whitespace checks passed. All 39 sources and the ontology cache are unchanged. These follow-up outcomes are recorded separately from the initial execution record; publication and integration remain separate.