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We examined additional cat-4 mutants with missense mutations altering different highly conserved amino acids; these mutants showed a range of phenotypes.
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We analyze the fate of four different types of mutations altering the parental-care phenotypes.
Two were intronic mutations with unknown function, leaving a total of 48 mutations altering the TP53 protein in 39 different patients (28.9%).
For instance, mutations altering a particular residue of MreB confer a range of different cell widths in E. coli (our unpublished observations).
Point mutations altering V774 and G779 have been previously documented to result in amino acid substitutions different than those found in this study.
Gelbart et al. (1976) found XDH activity in ry / ry mutants to be 2.5% of wild-type levels, likely the result of weak activity of hybrid multimers, since XDH functions as a homodimer and these mutations alter residues in different domains of the polypeptide (Gelbart et al. 1976; Hille 1996).
Crucially, by demonstrating that different point mutations alter the regulation of some but not other processes, we have proven that the pleiotropy observed in sgol2 Δ/Δ oocytes is not due to knock on effects (secondary or even tertiary pathology) of eliminating a single function.
Different disease-causing mutations alter the Nav1.4 channel function through distinct mechanisms.
Reconstruction allowed us to examine how different combinations of mutations alter the dynamics of the polarization module.
This dynamic and energetic model of PrPC conformational perturbation corroborates these experimental observations: mutations alter the properties of the native state to different extents so that unfolding can take different pathways, giving rise to different conformations of partially unfolded states and/or populating different intermediates as found in the folding kinetics studies [23].
Mutations alter an organism's genotype and occasionally this causes different phenotypes to appear.
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