SHSPs
Small Heat Shock Protein
Alpha Crystallin
Chaperone Protein
Redox
Prion
Amyloid
Extremophile
Alphaproteobacteria
Endosymbiont
Immortal Cell Line
Nanobacteria
Hydrozoa

https://en.m.wikipedia.org/wiki/Endothelial_dysfunction

https://en.m.wikipedia.org/wiki/Endothelium

https://en.m.wikipedia.org/wiki/Superoxide

https://en.m.wikipedia.org/wiki/Hydroxyl_radical

https://en.m.wikipedia.org/wiki/Paraquat

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Structure of the α-crystallin domain from the Redox-sensitive Chaperone, HSPB1

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4589510/

The principal heat-shock proteins that have chaperone activity (that is, they protect newly made proteins from misfolding) belong to five conserved classes: HSP100, HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs).

The Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium Chloride

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3591616/

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alphaproteobacteria mimics biological function, and hide in cell nucleolus, bone marrow & brain, misfolding proteins.