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These factors have unique requirements for associated binding partners, and are involved in different functions.
In this conformation, SFKs are free to engage intermolecular binding partners and are highly susceptible to phosphorylating and dephosphorylating enzymes.
Sem1 family proteins are natively disordered in the absence of binding partners, and are the only stoichiometric proteasome subunits listed in DisProt (DP00617).
Clock and cycle function as binding partners and are required for 24-hour transcriptional cycling of the core-circadian clock [ 14].
As a result proteasomal proteolysis serves to eliminate obsolete proteins which compete with functional proteins for binding partners and are prone to associate with irreversible and toxic protein aggregates (Goldberg, 2003).
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PGC-1α has multiple binding partners and is thereby able to simultaneously induce transcription of a broad set of genes, most of which are involved in energy metabolism and redox handling, including Prx3 and Trx2 [ 23, 24].
The intrinsically disordered nature of ribosomal proteins is highly conserved in different domains of life, indicating that the lack of rigid structure and the resulting capabilities of the ribosomal proteins to interact with various binding partners and be involved in the wide spectrum of the moonlighting activities represent strong evolutionary advantage.
STAR-domain proteins form contacts with different protein-binding partners and are themselves controlled by translational modifications (e.g., Resnick et al. 1997; Di Fruscio et al. 1999; Clifford et al. 2000; Stoss et al. 2001; Côté et al. 2003; Selenko et al. 2003; Zhang et al. 2003; Robard et al. 2006; Huot et al. 2009; Nir et al. 2012).
Therefore, the formation of the α-helix in BMPR-IA's β4β5-loop seems to depend on the nature of the binding partner and is thus not "imprinted" during complex formation with a protein binding partner.
These proteins form well-defined structures when they bind to other proteins, for example, BRCA2 and TREX-2, but the structure is determined by the binding partner and is different in each complex.
C3G (Crk SH 3-domain-binding guanine-nucleotide releasing factor) was isolated in a screen for Crk SH3N-binding partners and was the first protein identified that bound to the SH3 domain of Crk [ 114, 115].
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