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4. Monitoring of the anti-aggregation activity of the Hsp33 chaperone Hsp33 is the zinc-dependent, redox-regulated chaperone, which binds tightly to unfolding proteins under stress conditions with subsequent release to chaperone “foldases” when non-stress conditions resume (for structure, see Fig. 1). Hsp33 can toggle between reduced and oxidized forms; chaperone activity is activated under oxidizing conditions.9898. U.
Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. J. Biol. Chem. 2019; 294: 2085-2097https://doi.org/10.1074/jbc.REV118.002810 Cote-Hammarlof P.A. Fragata I. Bolon D.N.A. et al. The adaptive potential of the middle domain of yeast Hsp90. Mol. Biol. Evol. 2021; 38: 368-379https://doi.org/10.1093/molbev/msaa211 Kumar L. Planas-Iglesias J. Sarkar S.K. et al. Activity-dependent interdomain dynamics of matrix metalloprotease-1 on fibrin. Sci. Rep.
Results Cardiac CT reduced the need for coronary angiography from 100% to 14% (95% confidence interval 9% to 20%, P<0.001) and was associated with a significantly greater diagnostic yield from coronary angiography: 75% (53% to 90%) v 15% (10% to 22%), P<0.001. Major procedural complications were uncommon (0.3%) and similar across groups. Minor procedural complications were less common in the CT group than in the coronary angiography group: 3.6% (1% to 8%) v 10.5% (6% to 16%), P=0.014.
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