Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

Mass spectrometry is a central technology in the life sciences, providing our most
comprehensive account of the molecular inventory of the cell. In parallel with developments …

Small heat shock proteins (sHSPs) are present in all kingdoms of life and play fundamental
roles in cell biology. sHSPs are key components of the cellular protein quality control …

Crystallins are the predominant structural proteins in the lens that are evolutionarily related
to stress proteins. They were first discovered outside the vertebrate eye lens by Bhat and …

Heat shock proteins (HSP) are a subset of the molecular chaperones, best known for their
rapid and abundant induction by stress. HSP genes are activated at the transcriptional level …

Malignant gliomas are the most common and deadly type of central nervous system tumors.
Despite some advances in treatment, the mean survival time remains only about 1.25 years …

The primary function of the eye lens is to focus light on the retina. The major proteins in the
lens—α, β, and γ-crystallins—are constantly subjected to age-related changes such as …

Over the past two decades, mass spectrometry (MS) has emerged as a bone fide approach
for structural biology. MS can inform on all levels of protein organization, and enables …

Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone
proteins that play a critical role in mitigating and preventing protein aggregation under stress …

The fact that ions of macromolecular complexes produced by electrospray ionization can be
maintained intact in a mass spectrometer has stimulated exciting new lines of research. In …