Your English writing platform
Discover LudwigExact(4)
Seminal paper presenting an alternative model for IRE-1 activation through direct binding of unfolded proteins.
Gln105 of Ire1α, which forms hydrogen bond to adjacent residues, prevents direct binding of unfolded proteins.
From this observation, it was proposed that the direct binding of unfolded proteins to Ire1 lumenal domain is sufficient to activate the UPR in yeast.
Ire1 is activated by either direct binding of unfolded proteins, or from the release of the molecular chaperone BiP from the lumenal domain of Ire1.
Similar(56)
Interestingly, a study attempted to reconcile the involvement of BiP in UPR activation with direct binding of unfolded protein to luminal domains (Pincus et al., 2010).
A second mechanism driving activation of these sensor proteins may also involve binding of unfolded protein domains to a peptide-binding groove in both IRE1 and PERK, and possibly ATF6 [ 17].
This structure allows BiP to cycle between ATP and ADP exchange, coupled to the binding and release of unfolded proteins [ 3].
The encoded protein has a chaperone-like activity, binding the mature portion of unfolded proteins and aiding their import into mitochondria (Chewawiwat et al., 1999).
Next, HscA386 and HscA395 were subjected to heat denaturation in the presence of a dye (SYPRO orange) that fluoresces (excitation at 492 nm and emission at 610 nm) upon binding to hydrophobic patches of unfolded proteins.
Thus, defects in the BiP ATP/ADP exchange cycle that result in altered substrate binding or release cause accumulation of unfolded proteins and ER stress (2, 4).
In fact, ATP binding to the ATPases by itself supports the rapid degradation of unfolded proteins.
Write better and faster with AI suggestions while staying true to your unique style.
Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com