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Prediction of SNPs that cause a destabilization of the protein structure was made using CUPSAT (Parthiban et al. 2006).
For instance, lipophilic or surface-active lipophilic compounds may cause a destabilization of the eye tear film leading to epithelial damage of the conjunctiva (Wolkoff et al. 2003).
Alternatively, artemisinic acid could directly cause a destabilization (e.g. increased porosity) of the yeast cell wall, leading to decreased plasma membrane stability.
Hence, a decrease in the levels of these polycations might cause a destabilization of important cell structures, leading to alterations in cell integrity and inducing cell death.
MMP-9 and gelatinase activity have been shown to cause a destabilization of advanced plaques in mouse models, and in humans MMP-9 is a biomarker for risk of acute coronary events (Gough et al. 2006; Hlatky et al. 2007).
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Acetylation of H3K64 may cause a slight destabilization of nucleosomes at NaCl concentrations greater than 0.35 M. The localization of H3K64ac during spermatogenesis was also examined.
For example, mutation I48A in the Hordeum vulgare chymotrypsin (UniProtKB/Swiss-Prot ID: ICI2_HORVU) (The_UniProt_Consortium, 2010) was shown by Jackson et al. (1993) to cause a major destabilization of the protein.
Moreover, comparably to the 2′-SCF3 pyrimidinucleosidesdes, the purine counterparts were also found to cause a significant thermodynamic destabilization when located in double helical regions.
Interestingly, substitutions of the C122 and C164 with Ser residues caused a different destabilization.
Substitution of these residues inevitably causes a structural destabilization of the LRR domain.
For example, H2A. Zextends the H2A/H2B acidic patch and causes a subtle destabilization of the H2A/H2B interface with H3/H4.
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