The review distinguishes human enzyme experiments from assays of mouse and fly Eogt. A human cell host does not establish that the expressed enzyme is human. Normal publication caches remain unchanged, including their original full-text flags.
| Source | Original access and precise locator | Evidence used and limits |
|---|---|---|
| PMID:23671640 | Original article; Results, Figures 1–2 and 5; Methods, Plasmids and Cell Culture; opening Discussion | The 527-residue human KC347596.1 clone, obtained from HEK293T, restores O-GlcNAc on fly Notch EGF repeats in S2 cells after fly Eogt depletion. Human DYD-to-AYA reduces rather than abolishes activity. Mutant-comparison constructs use a BiP signal sequence. Human-transgene rescue of fly lethality and wing blisters is a heterologous experiment. Short-transcript low activity is predicted, not directly assayed. Main text, relevant captions and tables were read; figure pixels and supplements were not independently inspected. |
| PMID:23522784 | Original article; main-text family mapping/variant paragraphs, mouse embryo in-situ-hybridization paragraph and closing Discussion | Human segregation and mouse embryonic expression inform disease context. The authors lacked patient cells for the proposed cellular mechanism. The complete freshly fetched normal-cache main text was read; complete tables, figure captions/images and supplements were not inspected. A live PMC challenge page was not counted as article access. |
| PMID:22158438 | Publisher PDF; pp. 2–4, Results and Figures 1–3; p. 8, Methods, Plasmid constructs, Transfection and cell staining, and Enzyme activity assay | The actual nine-page publisher PDF was recovered independently despite a subscription preview in the browser. Fly Eogt expressed in S2 cells transfers radiolabeled GlcNAc to folded EGF20 after affinity purification. Figure 2 tests donor and acceptor specificity. Figure 3c–f tests GFP-KDEL colocalization and secretion after deleting RNEL or adding a C-terminal tag. Relevant text, Methods, full Figure 2–3 captions and page images were read. These are fly localization/catalysis experiments. Supplementary material was not read. |
| PMID:22310717 | Publisher; abstract only | The official mouse Q8BYW9 record and current QuickGO IDA assertions cite this source for catalytic activity and protein O-linked glycosylation. The abstract identifies mouse Eogt1, reports folded-EGF substrate specificity and describes further galactosylation of EOGT-generated O-GlcNAc. Full Methods and figures were not recovered; the Elsevier API response contained metadata only. Specific original assay details are not independently verified. Human catalytic activity is separately established by PMID:23671640. |
| PMID:25488668 | Original article; Experimental Procedures, all paragraphs; Results associated with Figures 1–2 and 5–8; Discussion | Complete cached Methods, Results and Discussion were read. CHO-expressed purified mouse EOGT transfers radiolabeled GlcNAc to fly EGF20; kinetic constants belong to mouse enzyme. Results/Figure 1B reports mouse EOGT ER localization, whereas Figure 1C reports the glycosylation-product signal overlapping calnexin. Mutant studies use mouse EOGT, including human-equivalent W207S/R377Q and a truncation mimic. These are not human enzyme or natural splice-product assays. Complete figure captions, pixels, primer-table entries and supplements were not independently read. |
The current normal cache for PMID:22158438 remains abstract-only even though its publisher PDF was independently read. The review YAML now records this recovered-original access under reference_review; it does not mark this accessible original unavailable. External access does not alter the immutable cached source.
Database snapshots were captured on 2026-10-24. Original evidence remains source- and preparation-specific. No additional process assertion is inferred from disease association, fly rescue, or discussion hypotheses.
Fresh QuickGO term responses and the OLS term record, retrieved on 2026-10-24, both identify GO:7770074 as an active biological-process term, protein O-linked glycosylation via N-acetylglucosamine. OLS records creation on 2026-05-07 and links ontology issue 32044. The term is a current direct is_a child of GO:0006493. Its numeric range does not make it invalid.
The saved official responses make this check inspectable without network access. The current GO:0006493 descendants were also checked: other direct process children distinguish the initiating sugar (mannose, fucose, glucose, galactose, xylose, arabinose or GalNAc), rather than providing a generic serine-only or threonine-only alternative. GO:7770074 remains the relevant GlcNAc-specific comparator, but its definition excludes extension into an oligosaccharide. The accepted parent therefore covers the initiating EOGT step while allowing the later glycan extension reported in the mammalian source; it does not assign that extension reaction to EOGT.
The single core combines the accepted catalytic reaction, ER-lumen location and protein O-linked glycosylation process. Direct human activity is established for the canonical 527-residue protein; inherited ER localization is corroborated by fly and mouse originals. No claim is made that every shorter human product has the same activity or location.