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Lamin A forms polymers at the nuclear lamina with lamin C. While lamin C is produced as mature protein, lamin A is translated as a precursor protein, which undergoes four steps of post-translational modifications, including farnesylation, double endoprotease cleavage and carboxymethylation (Maraldi et al. 2011).
Like other members of the family, myostatin is translated as a precursor protein (MstnPP) that consists of an N-terminal signal sequence, a regulatory propeptide domain (residues 21 266) and a growth factor domain (residues 267 374) which dimerises at the C-terminus via an inter-molecular disulfide bond [5] [7].
Nodal is translated as a precursor form consisting of a signal peptide and pro-domain.
sGP is translated as a precursor (pre-sGP), which is cleaved by furin protease at its C-terminus to yield mature sGP and a secreted cleavage product (Δ-peptide).
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SHH is translated as an inactive precursor 45 kDa protein that is cleaved to generate an active 19 kDa isoform.
The FMDV genome is translated as a single polypeptide precursor that is cleaved into functional proteins predominantly by the highly conserved viral 3C protease, making this enzyme an attractive target for antiviral drugs.
Pol becomes translated as a Gag-Pol precursor polyprotein through a ribosomal frameshift that occurs at a frequency of 5 10% [ 9].
HGF is translated as a single-chain precursor and activated at the site of injury by proteolytic cleavage, resulting in a double-chained active HGF [ 5].
For example, IL-1β is initially translated as a biologically inactive precursor molecule that is subsequently processed into a mature protein associated with IL-1 bioactivity.
TNF-α is present as a homotrimeric protein in which each subunit is initially translated as a 26 kDa transmembrane precursor protein.
TNF is translated as a 26-kDa transmembrane precursor protein (tmTNF) that is proteolytically cleaved to release the soluble and biologically active 17-kDa C-terminal part (soluble TNF; sTNF).
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