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To test whether FKBP12 association disrupts interaction between mTOR and Raptor (Kim et al., 2002), we performed an in vitro assay using purified mTORC1 (Flag-Raptor) and increasing amount of FKBP12-Rapamycin (Fig. 5D).
Also of note is that phosphorylation of Tyr682 also disrupts interaction of APP with Fe65 and other PTB domain proteins [13], [14] and this may be one commonality between APPYG/YG mice and AD brain.
Thus, the G864E mutation disrupts interaction of Fab1p with Vac14p.
Thus, the Cys substitution severely disrupts interaction with GyrB-466.
So, phosphorylation of Ser-55 of vimentin disrupts interaction between VIF and mitochondria.
As expected, the deletion of N-terminus 41 amino acids of CUL3 (CUL3ΔN41) disrupts interaction with KLHL18, and the deletion of N-terminus 65 amino acids within the BTB domain of KLHL18 (KLHL18ΔBTB) disrupts interaction with CUL3 (Fig. 5C).
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It thus appears that 3M urea also disrupts interactions stabilizing the association of the three U snRNAs with C complex.
The not4L35A mutation disrupts interactions between Not4 and its two known E2 ubiquitin-conjugating enzymes, Ubc4 and Ubc5, thus compromising its ubiquitin ligase function [63].
This post-translational modification provides significant negative charges to the acceptor proteins and often disrupts interactions between the acceptor proteins and the DNA.
That rearrangement disrupts interactions between adjacent subunits within the tetrameric IP3R leading to gating of the Ca2+-permeable channel (Seo et al., 2012).
Furthermore, mutation of the BMAL1 TAD disrupts interactions with the CRY1 CC helix and synergistically decreases the level of repression by CRY when assayed with CLOCK PAS-B mutants.
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