SUMMARY Heat shock protein 90 (Hsp90) participates in proteostasis by facilitating protein
folding, activation, disaggregation, prevention of aggregation, degradation, and protection …

Molecular chaperones are highly conserved across evolution and play a crucial role in
preserving protein homeostasis. The 60 kDa heat shock protein (HSP60), also referred to as …

Tubulin-based microtubule is a core component of flagella axoneme and essential for sperm
motility and male fertility. Structural components of the axoneme have been well explored …

Summary The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential
protein folding machine with a diverse clientele of substrates, including many proteins with β …

Schistosomiasis, caused by Schistosoma spp., is a zoonotic parasitic disease affecting
human health. Rattus norvegicus (rats) are a non-permissive host of Schistosoma, in which …

The integrity and permeability of epithelial and endothelial barriers depend on the formation
of tight junctions, adherens junctions, and a junction-associated cytoskeleton. The …

NO-stimulated guanylyl cyclase (SGC) is a hemoprotein that plays key roles in various
physiological functions. SGC is a typical enzyme-linked receptor that combines the functions …

The CCT/TRiC chaperonin is found in the cytosol of all eukaryotic cells and assists protein
folding in an ATP-dependent manner. The heterozygous double mutation T400P and …

Prefoldins (PFDs) are ubiquitous co-chaperone proteins that originated in archaea during
evolution and are present in all eukaryotes, including yeast, mammals, and plants. Typically …

The microtubule cytoskeleton undergoes major reorganizations during mitosis, process
extension, and ciliogenesis. To achieve these rearrangements, cells must rapidly increase …