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More specifically, the mutation or modification of these proteins may trap them in highly unstructured or partially-folded states with a large portion of hydrophobic side chains exposed/accessible to bulk solvent.

Instead, our data fit best with a model in which any mutation or modification that increases flexibility in the 90 93 loop enables C4F6 reactivity.

Overall, these data suggest that while mutation or modification of Y1065 does not alter the overall stability of the protein, the presence of a negative charge at Y1065 can slightly alter helix bundle packing interactions.

As shown in Figure 2A, far-UV spectra for Y1065 variants and pY-Vt were similar to WT Vt, indicating that mutation or modification of Y1065 does not significantly alter the overall α-helical signature of Vt.

In this model, we propose that prolonged checkpoint arrest will lead to adaptation through "inactivation" of the yeast Rfa1 N-terminus (DBD-F; similar to that of the rfa1 -t11 mutation) or modification of the yeast Rfa2 N-terminus.

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Mutations or modifications in disease-specific proteins can cause misfolding and consequently formation of aggregates.

A large number of mutations or modifications have suggested the key role of the six outermost base-pairs for binding of IN to virus DNA [1], [12].

Mutations or modifications of the copy number in CYCLIN B, GRAPES, and MEI-41 led to a lack of cell cycle lengthening from cycles 10 13, and modifications in the copy number of CDC25string resulted in an absence of cycle 14 lengthening [50], which is what we observed in our dcr-2 embryos at 29°C.

Inherited stable changes in cell functioning that cannot be explained as the result of mutations or modifications in the DNA sequence are considered as epigenetic (Bird, 2007).

Schizosaccharomyces pombe strains with the following mutations or modifications have been described: nda3-KM311 [ 32], mad1+-GFP≪kanR, mad2+-GFP≪kanR, mad3+-GFP≪kanR, plo1+-mCherry, ark1+-GFP [ 7], bub1+-GFP≪kanR [ 33], bub3+-GFP≪kanR [ 10], mad1Δ::ura4+ [ 34], bub1Δ::ura4+ [ 35].

In both these cases, the molecular lesion that causes the ASIC2 trafficking defect is unknown – in glioma it might be oncogenic mutations or modifications, whereas, in vascular smooth muscle cells, the truncated form could be involved.

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