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The clustering of major protein groups is indicated by the color code used in Figure 2. In many cases proteins are either down- (green) or up-regulated (red).
Adherence to all three models is observed in nature, and in many cases, proteins from hyperthermophiles utilize various combinations of these mechanisms [ 50- 55].
However, in many cases proteins with multispecificity are also capable of enzymatically modifying the proteins with which they interact [ 5- 9, 11].
In many cases, proteins that were reported to be a target for a specific PKMT were not present on the array, including, p53 [ 16], DNMT1 [ 21] and TAF10 [ 22], which have all reported to be methylated by SETD7.
Consequently, in many cases proteins that are very similar based on sequence are not necessarily associated with the same set of GO terms, and this can greatly reduce the effectiveness of the mapping.
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Noteworthy, in many cases protein protection was achieved by similarly charged polyelectrolyte, and the higher level of protection by polycation was achieved at lower pH despite the weakening of the Coulomb attraction.
In many cases, protein quality control systems are induced or activated during conditions of proteotoxic stress.
Proteins may evolve through the recruitment and modification of discrete domains, and in many cases, protein action can be dissected at the domain level.
By attaching ubiquitin molecules to their substrates, E3 ligases have direct control over the functions and, in many cases, protein turnover of these substrates.
In many cases protein function is maintained against occurring disadvantageous mutations by purifying selection resulting in high conservation of such sites or domains (ω < 1).
While commonly referred to as exome sequencing, because in many cases protein coding regions have been enriched, in fact any portion of the genome can be chosen for target enrichment [ 6, 7].
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