CRYAB is a member of the small heat shock protein family, first discovered in the lens of the
eye, and involved in various diseases, such as eye and heart diseases and even cancers …

Heat shock proteins (HSPs) are a large molecular chaperone family classified by their
molecular weights, including HSP27, HSP40, HSP60, HSP70, HSP90, and HSP110. HSPs …

The tumour suppressor p53 (encoded by TP53) protects the genome against cellular stress
and is frequently mutated in cancer. Mutant p53 acquires gain-of-function oncogenic …

Breast cancer (BC) cell lines are useful experimental models to understand cancer biology.
Yet, their relevance to modelling cancer remains unclear. To better understand the tumour …

Life-saving renal replacement therapy by peritoneal dialysis (PD) is limited in use and
duration by progressive impairment of peritoneal membrane integrity and homeostasis …

Heterogeneity in small heat shock proteins (sHsps) spans multiple spatiotemporal regimes—
from fast fluctuations of part of the protein, to conformational variability of tertiary structure …

The mechanisms that maintain genome stability are critical for preventing tumor progression.
In the past decades, many strategies were developed for cancer treatment to disrupt the …

Proper protein folding relies on the assistance of molecular chaperones post-translation.
Dysfunctions in chaperones can cause diseases associated with protein misfolding …

Background Bladder cancer is a common malignancy characterized by a high recurrence
rate and the development of drug resistance. Frequent mutations and gene expression …

Abstract Alpha B-crystallin (CRYAB, HSPB5) is a protein that was first discovered in the lens
of the eye. It is a member of the small heat-shock protein family (sHsps). CRYAB functions …