> top > projects > sentences > docs > PubMed:31028175 > annotations
sentences Home  

PubMed:31028175 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-128 Sentence denotes Loss of the p53 transactivation domain results in high amyloid aggregation of the Δ40p53 isoform in endometrial carcinoma cells.
T2 129-274 Sentence denotes Dysfunctional p53 formation and activity can result from aberrant expression and subcellular localization of distinct p53 isoforms or aggregates.
T3 275-424 Sentence denotes Endometrial carcinoma (EC) is a cancer type in which p53 status is correlated with prognosis, and TP53 mutations are a frequent genetic modification.
T4 425-644 Sentence denotes Here we aimed to evaluate the expression patterns of different p53 isoforms and their contributions to the formation and subcellular localization of p53 amyloid aggregates in both EC and endometrial nontumor cell lines.
T5 645-872 Sentence denotes We found that full-length (fl) p53 and a truncated p53 isoform, Δ40p53, resulting from alternative splicing of exon 2 or alternative initiation of translation at ATG-40, are the predominantly expressed p53 variants in EC cells.
T6 873-945 Sentence denotes However, Δ40p53 was the major p53 isoform in endometrial nontumor cells.
T7 946-1151 Sentence denotes Immunofluorescence assays revealed that Δ40p53 is mainly localized to cytoplasmic punctate structures of EC cells, resembling solid-phase structures similar to those found in neurodegenerative pathologies.
T8 1152-1412 Sentence denotes Using light-scattering kinetics, CD, and transmission EM, we noted that the p53 N-terminal transactivation domain significantly reduces aggregation of the WT p53 DNA-binding domain, confirming the higher aggregation tendency of Δ40p53, which lacks this domain.
T9 1413-1518 Sentence denotes This is the first report of cytoplasmic Δ40p53 in EC cells being a major component of amyloid aggregates.
T10 1519-1748 Sentence denotes The differential aggregation properties of p53 isoforms in EC cells may open up new avenues in the development of therapeutic strategies that preferentially target specific p53 isoforms to prevent p53 amyloid aggregate formation.