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It is possible that site-specific phosphorylations of FipA by two different kinases regulate interaction with different substrates.
Another intriguing possibility is that subtle structural differences between CYP isoforms may regulate interaction with CPR and cytochrome b5.
FIH-mediated HIFα hydroxylation is important to regulate interaction with the transcriptional coactivator p300, a function that is impaired under low oxygen levels [ 254].
To more systematically test the possibility that meA and meB splice inserts in LAR-RPTPs regulate interaction with SALM3, we performed cell-based binding assays in the reverse orientation.
We suggest the different conformations might regulate interaction with other factors: the A-subdomain might be stabilized against the OB-fold during one cell cycle stage, masking an interaction surface that becomes exposed by a conformational switch.
While the three tyrosine motifs in the N-terminal part of SH2B1, which regulate interaction with the insulin receptor [ 42], are not directly affected by this exchange, it is possible that altered protein folding due to an non-conservative amino acid exchange in a highly conserved position prevents their phosphorylation.
Similar(54)
Specific phosphorylated residues may thus promote or inhibit interactions between proteins or protein domains, or regulate interactions with small molecule substrates or ligands (40, 41 ).
First, protein kinases adopt similar inactive DFG-out conformation and use similar amino acid types to regulate interactions with type-II inhibitors.
Viewed in this context, the docking of the Sac3 PCI domain onto the Med31/Med7N submodule could locally alter Mediator conformation and thereby regulate interactions with Pol II.
2) We agree that the idea that the different A-domain conformations might regulate interactions with other factors or control helicase function is intriguing, however, this concept is not tested.
For example, NPxY motif tyrosine phosphorylation by Src family kinases (SFK) may positively or negatively regulate interactions with phosphotyrosine-binding (PTB) domain-containing proteins [e.g., talin and Dok1].
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