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The disease-causing mutations decrease the mechanical stability of the glomerular basement membrane (GBM).
"Loss-of-function" mutations decrease the cell surface localization of ferroportin, thereby reducing its ability to export iron.
RPS19 mutations decrease the proliferation of progenitor cells; however, terminal erythrocyte differentiation remains normal, with little sign of apoptosis.
Alternatively, "unpreferred" mutations decrease the frequency of major codons by changing a major codon to a minor one.
These data indicate that the Qp site mutations decrease the efficacy of MitoVES-induced ROS generation and that the induced cell death depends on CII-derived ROS.
These mutations decrease the protein's affinity towards nucleotides, leading to an exchange in favor of cytosolic GTP, of which there is a ten-fold higher level than GDP.
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Mutations decreased the hydrolysis activity of the enzyme and caused various modulations in its transglycosylation properties.
This tendency offers an explanation for the observation that mutations decreasing the hydrophobic character of the MPER in many cases result in conformational changes that increase the affinity of this region for the 2F5 antibody.
All mutations decreased the viral replicative capacity including mutations in residues G359 and K390.
In this regard, mutations decreasing the pH of HA conformational change and, therefore, stabilizing the HA of H5 HPAIVs might be a prerequisite for their efficient spread in humans via a large droplet mechanism infecting the upper respiratory tract (nose).
It appeared that all four single mutations decreased the stability of the protein (Fig. 2).
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