Correction to "Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes"

The maximum likelihood/s A weighted 2F obs @F calc electron density map (gray) is contoured at 1.0 sigma. D) Structure of raIDUA complexed with a fragment of ABP 3, illustrating

(a) Probe 5 only labels GBA1, while 6 labels GBA1 and GLB1, and 8 only shows non-specific labelling of proteins in gel, although pull-down analysis shows enrichment of GLB1 and

Speci fic binding in C2C12 cell culture was further assessed by pre-incubation with the MG132, and reduced LWA300 signal fluorescence was found for β5, β1, and β2 subunits (Figure

View Journal | View Issue.. This journal is © The Royal Society of Chemistry 2017 Chem. 1b): BODIPY-ABP 3, which permits the detection of the enzyme in complex proteome samples

Specialty section: This article was submitted to Protein Folding, Misfolding and Degradation, a section of the journal Frontiers in Molecular Biosciences Received: 31 January

Enzyme specificity can be readily charac- terized using competitive ABP labeling strategies, which measure the susceptibility of ABP labeled enzymes to inhibition by substrates

The a-Glucosidase Probes Label a Distinct Subproteome To test the labeling by the new probes, Arabidopsis leaf extracts were labeled with JJB382 and JJB70, which differ in

The maximum likelihood/s A weighted 2F obs F calc electron density map (gray) is contoured at 1.0 sigma. D) Structure of raIDUA complexed with a fragment of ABP 3, illustrating