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PubMed:28584052 JSONTXT 61 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-106 Sentence denotes Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability.
T2 107-248 Sentence denotes N-Acetylglucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential and dynamic post-translational modification.
T3 249-423 Sentence denotes The O-GlcNAc modification is present on numerous nuclear and cytosolic proteins and has been implicated in essential cellular functions such as signaling and gene expression.
T4 424-549 Sentence denotes Accordingly, altered levels of protein O-GlcNAcylation have been associated with developmental defects and neurodegeneration.
T5 550-636 Sentence denotes However, mutations in the OGT gene have not yet been functionally confirmed in humans.
T6 637-868 Sentence denotes Here, we report on two hemizygous mutations in OGT in individuals with X-linked intellectual disability (XLID) and dysmorphic features: one missense mutation (p.Arg284Pro) and one mutation leading to a splicing defect (c.463-6T>G).
T7 869-976 Sentence denotes Both mutations reside in the tetratricopeptide repeats of OGT that are essential for substrate recognition.
T8 977-1172 Sentence denotes We observed slightly reduced levels of OGT protein and reduced levels of its opposing enzyme O-GlcNAcase in both patient-derived fibroblasts, but global O-GlcNAc levels appeared to be unaffected.
T9 1173-1293 Sentence denotes Our data suggest that mutant cells attempt to maintain global O-GlcNAcylation by down-regulating O-GlcNAcase expression.
T10 1294-1464 Sentence denotes We also found that the c.463-6T>G mutation leads to aberrant mRNA splicing, but no stable truncated protein was detected in the corresponding patient-derived fibroblasts.
T11 1465-1758 Sentence denotes Recombinant OGT bearing the p.Arg284Pro mutation was prone to unfolding and exhibited reduced glycosylation activity against a complex array of glycosylation substrates and proteolytic processing of the transcription factor host cell factor 1, which is also encoded by an XLID-associated gene.
T12 1759-1913 Sentence denotes We conclude that defects in O-GlcNAc homeostasis and host cell factor 1 proteolysis may play roles in mediation of XLID in individuals with OGT mutations.