IndraLab

Statements

CFTR binds OTUB1. 5 / 5
| 2 3
reach
"While the highest intensity signals corresponded to unmodified OTUB1 and the ΔF508-harboring CFTR nucleotide-binding domain used in this experiment, potentially indicating low levels of target engagement under these experimental conditions, we observed significant CFTR-OTUB1 complex formation with NJH-2-057 treatment, but not with DMSO vehicle or EN523 treatment (Figure 3h–3i)."
35210618
sparser
"Having identified NJH-2-057 as a DUBTAC that was capable of stabilizing mutant CFTR in cells, we next sought to confirm the formation of a ternary complex between CFTR, NJH-2-057, and OTUB1 in vitro using recombinant protein and native mass spectrometry (MS)-based approaches ( xref – xref )."
35210618
sparser
"While the highest intensity signals corresponded to unmodified OTUB1 and the ΔF508-harboring CFTR nucleotide-binding domain used in this experiment, potentially indicating low levels of target engagement under these experimental conditions, we observed significant CFTR-OTUB1 complex formation with NJH-2-057 treatment, but not with DMSO vehicle or EN523 treatment ( xref – xref )."
35210618
sparser
"Nonetheless, given that this OTUB1-CFTR complex was only observed with DUBTAC treatment but not with DMSO or EN523 treatment, our data strongly suggests that the DUBTAC enables ternary complex formation."
35210618
reach
"Nonetheless, given that this OTUB1-CFTR complex was only observed with DUBTAC treatment but not with DMSO or EN523 treatment, our data strongly suggests that the DUBTAC enables ternary complex formation."
35210618