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Interestingly, the D box and KEN box of substrates contribute to this activation process.
Similarly, in previous work, we showed that binding of the D box and KEN box of substrates to the activator subunit helps promote catalytic function [ 14].
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When substrates are directly fused to the APC/C core, thus bypassing the need of the D box and the KEN box for the recruitment of substrates to the APC/C, the presence of these degron motifs still increases the ability of the activator to promote ubiquitin transfer [ 14].
Another part of F box proteins recognizes post-translationally modified degradation motifs of substrates, while the F box itself docks the Skp1 components of SCF (Skp, Cullin, F box) E3 ligase complexes.
The SCF complex also contains an adaptor receptor subunit, termed F-box protein, that targets hundreds of substrates through phosphospecific domain interactions (Cenciarelli et al., 1999).
These cycles are presumably necessary to replace F-box proteins which had been ubiquitinated due to the lack of substrates, or to replace F-box proteins which are no more required during developmental processes (Braus et al. 2010).
The three classes of E3 ligases (RING, HECT, U-box) are responsible for the recognition of substrates (Grabbe et al, 2011).
29 30 Phosphorylation of the Thr380 allows cycling E to be recognised by Fbw7, an F box protein substrate of related E3 ubiquitin ligases.
The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets.
SCF complex potentially has a wide network of substrates because of the fact that it can bind with as many as 70 F-box proteins.
Peptides that exhibit a L/H ratio >2 (indicated by the red box) are potential substrates of Mek1.
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