The review centers on cytosolic NADP-dependent glucose-6-phosphate oxidation. G6PD performs the entry reaction of the oxidative pentose-phosphate pathway and directly reduces NADP+. Downstream glutathione recycling, lipid synthesis and redox-sensitive signaling depend on its products but are carried out by other enzymes. The annotation rationales distinguish direct catalysis from those contextual contributions.
The review YAML contains the current judgments and 39 manual reference assessments. The source-evidence archive retains the 66 original contexts and their current joins, three natural-product sequences, inherited review and journal, source-access records, and quotation locators. Its compact PAINT section includes the four literal ancestral assertions, target lineage, retained negative assertions and original book URLs/hashes. The single urine extension remains in its original context; it is not reconstructed from the older auxiliary projection.
PMID:15858258, original publisher was read in selected sections 1, 2 and 3.1–3.5 through the indexed publisher text. The normal cache is abstract-only, and the direct local HTTP request returned 403; the failed response is not a full-text source. Human engineered ΔN25 protein and disease-variant structures must be distinguished from natural splice products. The selected sections establish G6P contacts, catalytic and structural NADP sites, and active dimeric/tetrameric assemblies. The free-glucose discrimination discussion includes a bacterial Leuconostoc H178N mutant, which does not settle a human free-D-glucose binding assertion.
PMID:38066190(https://pubmed.ncbi.nlm.nih.gov/38066190/) has genuine full text in the retained normal cache. Selected Results, Table 1, size-exclusion chromatography descriptions, figure captions and Methods were read. His-tagged human wild type and R219G were expressed in bacteria; NADPH formation was measured with G6P and NADP+. Wild type predominated as a dimer under the reported conditions, whereas the mutant had dimeric and monomeric populations. Michaelis constants are kinetic parameters rather than direct binding dissociation constants. Transcript Arg249 and canonical Arg219 numbering are distinct. Figure captions were read; this is not a new image audit.
The canonical P11413-1 product is 515 residues. P11413-2 is 561 residues and P11413-3 is 545 residues, with all three sequences preserved from direct official FASTA responses. Engineered deletions, substitutions and tags do not establish equal activity or localization of these natural products. The core describes the established enzyme, not experimentally demonstrated equivalence of all products.
PMID:21157431(https://pubmed.ncbi.nlm.nih.gov/21157431/) has native full text. Its human reciprocal Hsp27/G6PD co-immunoprecipitations in irradiated AG02603 fibroblasts are distinct from initial extract assays and recombinant Xenopus G6PD experiments. Association and activity regulation do not give G6PD Hsp27 chaperone or DNA-repair catalytic activity.
PMID:24769394, original PMC text was successfully recovered as HTML and read in selected Results, Methods and figure legends. The normal cache remains abstract-only; a failed Europe PMC response is excluded. SIRT2 association and G6PD Lys403 acetylation affect dimerization and activity. G6PD is the regulated enzyme, not the deacetylase. A cytosolic redox sensor is not itself a G6PD localization measurement.
PMID:35122041(https://pubmed.ncbi.nlm.nih.gov/35122041/) was read as authentic abstract and publisher preview. It supports an ALDOB–G6PD–p53 complex while separating human tumor observations from mouse genetic experiments. Exact human construct and microscopy details remain inaccessible. A later correction replaces an Extended Data 4d image and source-data item; it is not a retraction. Current P04637 and P05062 partners remain separate. Two historical machine-only joins are ambiguous because the old rows omit donors; literal historical summaries independently resolve TP53 versus ALDOB without rewriting that machine ambiguity.
The four positive generic-binding contexts are retained as non-core under the standing project instructions. No additional partner function is inferred from association alone.
Human PBMC studies 12027950 and 17361089 support contextual lipid/cholesterol effects. The authentic 2420826 abstract separates oxidative pentose production from glutathione-dependent PRPP-synthetase effects in infected human erythrocytes. These sources do not make G6PD a sterol-synthetic enzyme, glutathione reductase or PRPP synthetase.
The actual PTHR23429 tree contains the human target AN68/PTN002512035 with its exact 515-residue sequence. Activity, glucose metabolism and oxidative PPP assertions originate at AN0/PTN000604427; cytosol originates at AN2/PTN000604429. The retained cytosol-loss assertion is on the separate H6PD lineage. No target-path loss was found. A target self-donor is legitimate descendant experimental evidence, not circularity.
Rat P05370/ENSRNOP00000075297 is the literal electronic source. Ten actual donor papers were read as authentic abstracts, with selected complete cardiac originals and the soluble-versus-microsomal distinction read separately. PMID:24190878(https://pmc.ncbi.nlm.nih.gov/articles/PMC3886755/) reports neonatal rat ventricular myocytes, phenylephrine-induced enlargement, HK2-associated G6PD activity and DHEA-sensitive protection. That positive perturbation does not by itself establish the initial-to-mature developmental scope of GO:0061052. PMID:23071515(https://pmc.ncbi.nlm.nih.gov/articles/PMC3465299/) combines rat G6PD/NADPH/current experiments with separate deficient-mouse evidence; it supports indirect regulation of L-type current, not direct channel binding.
The reproduced original PMID:2843500 was read in selected JBC pages 12849–12851 Results/Discussion. It explicitly assays soluble G6PD separately from microsomal glucose/hexose-6-phosphate dehydrogenase. The endoplasmic-reticulum title is not evidence of a wrong-gene citation. The free-glucose passage concerns the microsomal enzyme; miniprint Methods and images were not independently read.
Official typed ancestry establishes oxidative PPP part_of PPP, with PPP is_a G6P metabolism. GO:0006006 glucose metabolism is absent from both tested ancestor closures, so a false ancestor argument is not used against those existing annotations. The broad catalytic-class and cytoplasm terms retain their existing granularity judgments. Direct human G6P-bound structures support non-core carbohydrate binding; a catalytic activity does not itself entail a binding term. Free D-glucose recognition remains unresolved and distinct from the observed G6P contacts.
The earlier OMICS manual membrane corrections and their history records are preserved. Cytosol and a nonexclusive peripheral membrane-associated pool can coexist. PMID:743300(https://pubmed.ncbi.nlm.nih.gov/743300/) remains title/metadata-only in the accessible cache; the exact fractionation controls and quantitative partitioning are not newly claimed. The YTS-specific G6PD peptide row in PMID:19946888(https://pubmed.ncbi.nlm.nih.gov/19946888/) was not recovered. Independent curated peripheral localization and the retained GO:0009898 annotation support refining both general membrane rows to the cytoplasmic side of the plasma membrane. Official ontology edges are GO:0009898 part_of GO:0005886, then GO:0005886 is_a GO:0016020. This refinement does not newly certify the YTS peptide assignment, a leaflet-specific assay in that paper, or integral topology. Short UniProt location excerpts remain in the validated review with their record sections.
PMID:19056867(https://pmc.ncbi.nlm.nih.gov/articles/PMC2637050/) has an independently retained expanded NHLBI urinary-exosome protein table. Its G6PD/NP_000393 entry appears at retained HTML row index 440 with the historical isoform-a label. The literal urine extension is conserved. No peptide dataset was recovered that would establish a unique present-day splice product.
PMID:23533145(https://pmc.ncbi.nlm.nih.gov/articles/PMC3773505/) has full main text in the normal cache and an independently retained authentic Supplemental Table 2 workbook. Sheet SI Table 2 row 675 contains P11413/G6PD. Both proteomic contexts support association with isolated fractions, not exosome biogenesis, mandatory intravesicular topology or a demonstrated extracellular catalytic role.
The three free-D-glucose binding assertions, original pentose-biosynthesis and erythrocyte-maturation assertions citing PMID:5643703(https://pubmed.ncbi.nlm.nih.gov/5643703/), and substantia-nigra development from PMID:22926577(https://pubmed.ncbi.nlm.nih.gov/22926577/) remain undecided. Unavailable target experiments are not treated as disproven. Established catalytic annotations can be retained from independent human experiments without claiming that every old experiment was read.
PMID:34784249(https://pubmed.ncbi.nlm.nih.gov/34784249/) explicitly assigns NAADP reduction to NAADPH to G6PD and the reverse oxidation to NOX/DUOX. The retained UniProt FUNCTION prose states the opposite G6PD direction, while its RHEA:86243 entry agrees with the paper. The source is preserved; a structured UNIPROT source defect on the NADP-metabolism row records the confirmed direction correction as not yet reported. Full G6PD reagent/construct details remain inaccessible; no new human T-cell calcium annotation is proposed. The R-HSA-9761849 display title says P6GD whereas its summary names G6PD; that fetched inconsistency is retained and recorded as a structured REACTOME title defect on its cytosol row. Neither source cache is edited.
All 52 inherited quotation associations remain intact in the archive. Six old occurrences contribute current support, including the NADP excerpt shortened to its complete first sentence; 46 remain historical-only. The separate wild-type assembly excerpt remains. Restored location and dimer excerpts support the same bounded claims: the dimer-loss quote concerns K403-acetylated G6PD, not wild type. Source-specific access limits still apply. Ontology-loaded target validation passed with four advisories, all for the generic protein-binding rows retained under project policy. Strict GOA matching passed for all 66 contexts. The computed status remains DRAFT; all 104 source files are unchanged.