Controlled proteolysis underlies a vast diversity of protective and regulatory processes that
are of key importance to cell fate. The unique molecular architecture of the widely conserved …

The HtrA family refers to a group of related oligomeric serine proteases that combine a
trypsin-like protease domain with at least one PDZ interaction domain. Mammals encode …

Alteration of mitochondria-associated membranes (MAMs) has been proposed to contribute
to the pathogenesis of Alzheimer's disease (AD). We studied herein the subcellular …

Brains of patients affected by Alzheimer's disease (AD) contain large deposits of aggregated
amyloid β-protein (Aβ). Only a small fraction of the amyloid precursor protein (APP) gives …

Alzheimer disease (AD) is a devastating neurodegenerative disease with no cure. The
pathogenesis of AD is believed to be driven primarily by amyloid-β (Aβ), the principal …

Endoplasmic reticulum-associated degradation (ERAD) is a system by which proteins
accumulated in the endoplasmic reticulum (ER) are retrotranslocated to the cytosol and …

The HtrA proteases degrade damaged proteins and thus control the quality of proteins and
protect cells against the consequences of various stresses; they also recognize specific …

Protein quality control is vital for all living cells and sophisticated molecular mechanisms
have evolved to prevent the excessive accumulation of unfolded proteins. High-temperature …

The human HtrA family of serine proteases consists of four members: HtrA1, HtrA2, HtrA3
and HtrA4. Although prokaryotic HtrA proteins are well characterized in their dual roles as …

• Introduction‐Chaperones: the basics‐Hsp90, Hsp70 and CHIP‐Substrate processing‐
Client degradation versus folding‐Chaperone expression‐Small Hsps• Chaperone …