Title : Protein L-isoaspartyl O-methyltransferase inhibits amyloid beta fibrillogenesis in vitro.

Pub. Date : 2011 Jul

PMID : 21812329






4 Functional Relationships(s)
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Protein Name
Organism
1 In this study it was investigated, whether PIMT is able to modulate Abeta fibrillogenesis in vitro by methylation of isoaspartyl residue using purified 5Abeta and PIMT. 5abeta protein-L-isoaspartate (D-aspartate) O-methyltransferase Homo sapiens
2 A Thioflavin-T (Th-T) binding assay conducted after aging Abeta in vitro (37 degrees C, pH 7.4 in PBS) revealed that PIMT inhibited the increase of fluorescence caused by amyloid fibrillogenesis. thioflavin T protein-L-isoaspartate (D-aspartate) O-methyltransferase Homo sapiens
3 A Thioflavin-T (Th-T) binding assay conducted after aging Abeta in vitro (37 degrees C, pH 7.4 in PBS) revealed that PIMT inhibited the increase of fluorescence caused by amyloid fibrillogenesis. thioflavin T protein-L-isoaspartate (D-aspartate) O-methyltransferase Homo sapiens
4 A Thioflavin-T (Th-T) binding assay conducted after aging Abeta in vitro (37 degrees C, pH 7.4 in PBS) revealed that PIMT inhibited the increase of fluorescence caused by amyloid fibrillogenesis. Lead protein-L-isoaspartate (D-aspartate) O-methyltransferase Homo sapiens