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Here we report mutations of key catalytic residues within CDTa and their effect on CDT cytotoxicity.
The mutations of key residues significantly alter the folding by distorting the cooperative interactions, which can result in the misfolding or aggregation; nonetheless, the rational design by mutations can be beneficial to protein folding.
Mutations of key residues involved in Greek-key motiformationon in γD have been associated with more severe cataracts than those occurred at the loops, termini or surfaces of β/γ-crystallins (Vendra et al., 2013).
Continuous proliferation of cells in serum-free medium could be attributed to mutations of key genes (e.g., K-Ras).
Surprisingly, we found that the amphipathic helix also plays important roles in septin spiral formation and axial budding, since mutations of key hydrophobic residues in the amphipathic helix in Bud3p-M19 (841–1220) and Bud3p-N/M6 abolished their ability to form septin spiral formation and to restore axial budding, respectively (Fig. 5D, Fig.7A).
Mutations of key hydrophobic residues within the endogenous 1-8-14 1-8-14 1-8-14he peptides.
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Mutation of key coiled-coil residues destroys looping and causes a loss of Ter condensation in vivo.
Notably, mutation of key residues inside the mCAR ligand-binding pocket entirely eliminated the stimulatory effect of TCPOBOP, as well as the inhibitory effect of androstanes, without affecting the constitutive activity of CAR (Tzameli et al., 2000).
Single-mutation of key HyPRE catalytic cysteine abrogates enzymatic activity supporting the presence of two reaction centers per homodimer.
In gut, the mutation of key tumor suppressor molecules in the Wnt signaling pathway leads to amplification of stem/progenitor compartments, followed by the appearance of differentiated adenomas and tumors [6], [7], [8].
This effect does not reflect a loss of SH3 domain function since mutation of key WW residues in the SH3 domain that are needed for SH3 domain binding did not interfere with binding between SKAP-55 and RasGRP1 (data not shown).
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