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Most likely, intracellular acidosis develops and affects a number of intracellular mechanisms involved in calcium handling and contraction; for example, a deactivation of contractile proteins including impaired calcium binding to troponin C, impaired interaction of the troponin-tropomyosin complex, and impaired actin-myosin interactions [ 8, 32, 33].
Our results indicated that the G174A substitution impaired interaction of the β clamp with the α catalytic subunit of pol III.
Conversely, addition of GTPγS that stabilizes/favors a GTP-bound form of Arf proteins markedly impaired interaction (Figure 6).
The aggregated ReLPS, due to its compact nature and to the steric obstacle caused by the saccharide portion, has an impaired interaction with the peptide.
Indeed, impaired interaction of IRF-3 with the coactivator CREB binding protein (CBP) in neonatal blood cells exposed to LPS was associated with impaired expression of IFNβ, IFN-inducible genes (such as CXCL10) and bioactive IL-12p70 [13]. IL-12p70 [13]
In vinculin-ΔEx20, the basic ladder and a part of the basic collar but not the C-terminus are missing, suggesting impaired interaction of vinculin-ΔEx20 with acidic phospholipids.
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Moreover, impaired interactions between mother(s) and children have been associated with long-term impairments in children's cognitive and emotional development [ 14].
Indeed, deletion of the putative pilin adhesin in GBS resulted in a mutant strain expressing pili composed of the major subunit only, which showed impaired interactions with human BMEC [28].
For other proteins, interactions or impaired interactions with chaperones, intracellular or extracellular matrixes, other proteins, small molecules and other endogenous factors can induce conformational changes and increase propensity to misfold.
We recognize that these mutations might also exhibit impaired interactions with other integrin binding proteins, and therefore we generated a number of mutants to reveal a general picture of the functional role of skelemin integrin interactions.
We demonstrate that the addition of a negative charge significantly impairs interaction with and activation by its cognate guanine exchange factor (GEF), Rabin8.
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