Abstract Protein aggregates are spatially organized and regulated in cells to prevent deleterious effects of proteostatic stress. Misfolding of proteins in the ER result in aggregate formation, but ...

Healthy cells are constantly breaking down proteins and building up new ones with the help of enzymes aptly named unfoldases, because they unravel proteins tagged for destruction or recycling. Now, a ...

In addition, mutations in lens α-crystallins have been associated with congenital cataracts (Sun et al., 2017; Berry et al., 2020). Thus, through their complementary roles in preventing protein damage ...

Conclusion We are the first to explore rabbit lens protein stability changes with ageing using biophysical methods under physiological conditions, and this study can conclude that the structural ...

Founded in 2014, ViewPoint discovered and developed alpha-crystallin aggregation inhibitors as investigational non-surgical treatments to correct protein misfolding in the lens.

Humans express 10 ATP-independent protein chaperones called small heat-shock proteins (sHSPs). The highly abundant sHSP chaperone present in eye lens, α-crystallin, delays lens protein aggregation and ...

The technology is not perfect. But it can predict the shape of a protein with an accuracy that rivals physical experiments about 63 percent of the time, according to independent benchmark tests.

Cataract is one of the most prevalent protein aggregation disorders and the leading cause of vision loss worldwide. As the eye lens lacks cellular or protein turnover, efficient mechanisms have ...

FIGURE 1. Relative functional activity of αAG98R and αA-WT proteins. The chaperone activity of αAG98R and αA-WT protein was compared at 60 min assay point and tested against— (A), EDTA-induced ...

There is currently no definitive test for early detection of neurodegeneration which is linked with protein aggregation. Finding methods capable of detecting intermediate states of protein aggregates, ...