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The neck domain (735 889), following the motor core, contains 6 IQ motifs believed to bind myosin light chain binding, probably calmodulin [ 58].
Recently, calmodulin-related proteins have been identified that specifically bind to a certain myosin, e.g. a light chain binding to Toxoplasma gondii Myo14A [TgMLC-1, [ 16]], or the light chain binding to Accanthamoeba castellanii Myo1C [AcMICLC, [ 17]].
Seibenhener, M. L. et al. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation.
This can be attributed to the enhancement of chain binding by the polar interactions and suppression of chain-slippage.
We have investigated the effects of chemical alkylation of microsomal membranes on nascent chain binding and translocation.
To determine if additional, Sec61p independent, stages of the ribosome binding reaction could be identified, ribosome/nascent chain binding was assayed as a function of RM concentration.
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GRP78, also referred to as BiP (immunoglobulin heavy-chain binding protein), resides primarily in the ER, binds to calcium and serves as an ER stress signaling regulator [ 5].
There is, therefore, no indication of a specific side-chain binding site in this enzyme.
A cellular mRNA, encoding the immunoglobulin heavy-chain binding protein, can be translated in poliovirus-infected cells at a time when cap-dependent translation of host cell mRNAs is inhibited.
Translation of the mRNA encoding the immunoglobulin heavy-chain binding protein (BiP) is enhanced in poliovirus-infected cells at a time when translation of host cell mRNAs is inhibited.
Our results suggest strong evolutionary selection for quaternary structure in cofactor-binding MBS homomers, whereas neutral processes are more important in complexes with single-chain binding sites.
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