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RNA binding protein may function also as a ssDNA binding protein.
Our previous studies have shown that α-Tocopherol-associated protein (TAP), a vitamin E binding protein, may function as a tumor suppressor-like factor in breast carcinogenesis.
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Chromatin binding proteins may function as histone-modifying enzymes related to certain activator or repressor recruitment modifications.
We further suggest that this RNA-binding protein may function to translationally-regulate or interact with key factors required to guide the germ cells through development, from stage to stage, and is required for the post-migratory pluripotent germ cells to begin reprogramming and switch from mitotic to meiotic divisions (Figure 9A 9D).
Thus, these GTP-binding proteins may function in protein import into chloroplasts.
Plastidic mRNA binding proteins often function in association with other proteins; in fact, the rbcL mRNA-based affinity purification of several proteins along with RLSB provides evidence that this protein may function as part of a larger protein complex.
Conserved residues in alignments of NifH-like sequences with NifH sequences show that 4Fe-4S iron sulfur cluster-ligating cysteines and the P-loop/MgATP binding motif are invariant, suggesting that these proteins may function analogously to dinitrogenase reductase.
Potentially any cysteinyl-tRNA binding protein may aid in this protective function.
Dynein heavy chain 9 and kinesin-like calmodulin binding protein may be related to flagellar functions as well as cell division [ 46, 47].
The cognate ligand for CD40, CD154 (CD40 ligand, CD40L, gp39, TRAP) does not bind other TNFR although it can interact with the soluble complement inhibitor C4b binding protein which may function as a competitive inhibitor of CD40 activation [8].
These binding proteins may perform functions extracellularly (e.g. in plasma) or transport these agents; to the nucleus to interact with nuclear receptors (principally PPARs and retinoic acid receptors 16) or for interaction with metabolic enzymes.
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