The accumulation of unfolded or misfolded proteins within the endoplasmic reticulum (ER),
due to genetic determinants and extrinsic environmental factors, leads to endoplasmic …

A growing body of evidence supports the beneficial effects of the ketone bodies (KBs),
acetoacetate and β-hydroxybutyrate (BHB), on diverse physiological processes and …

Aging is a major risk factor to develop neurodegenerative diseases and is associated with
decreased buffering capacity of the proteostasis network. We investigated the significance of …

Abstract Background Maintaining homeostasis of Ca2+ stores in the endoplasmic reticulum
(ER) is crucial for proper Ca2+ signaling and key cellular functions. Although Ca2+ …

The proteasome plays key roles in synaptic plasticity and memory by regulating protein
turnover, quality control, and elimination of oxidized/misfolded proteins. Here, we investigate …

Cells rely on the endoplasmic reticulum (ER) to fold and assemble newly synthesized
transmembrane and secretory proteins—essential for cellular structure–function and for both …

Oxidative stress, hyperactivation of compensatory mechanisms (unfolded protein response,
UPR; nuclear factor erythroid 2-related factor 2, Nrf2) and the stimulation of maladaptive …

Aging trajectories vary among individuals, characterized by progressive functional decline,
often leading to disease states. One of the central hallmarks of aging is the deterioration of …

This preface introduces the Journal of Neurochemistry Special Issue on Brain Proteostasis.
Adequate control of protein homeostasis, or proteostasis, has been at the center stage of …

RTP801/REDD1 is a stress-responsive protein overexpressed in neurodegenerative
diseases such as Alzheimer's disease (AD) that contributes to cognitive deficits and …