Misfolding, aggregation, and aberrant accumulation of proteins are central components in
the progression of neurodegenerative disease. Cellular molecular chaperone systems …

The family of the human small Heat Shock Proteins (HSPBs) consists of ten members of
chaperones (HSPB1-HSPB10), characterized by a low molecular weight and capable of …

Small heat shock proteins are ubiquitously expressed chaperones, yet mutations in some of
them cause tissue-specific diseases. Here, we will discuss how small heat shock proteins …

Protein homeostasis (proteostasis) is essential for maintaining the functionality of the
proteome. The disruption of proteostasis, due to genetic mutations or an age-related decline …

Alzheimer's disease (AD), the most common neurodegenerative disorder, is characterized
by neurofibrillary tangles, synaptic impairments, and loss of neurons. Oligomers of β …

A plethora of studies indicate the important role of cAMP and cGMP cascades in neuronal
plasticity and memory function. As a result, altered cyclic nucleotide signaling has been …

A major hallmark of Alzheimer's disease is the misfolding and aggregation of the amyloid-β
peptide (Aβ). While early research pointed towards large fibrillar-and plaque-like aggregates …

Small heat shock proteins (sHsps) are a group of proteins with molecular mass between 12
and 43 kDa. Currently, 11 members of this family have been classified, namely HspB1 to …

The review discusses the role of small heat shock proteins (sHsps) in human
neurodegenerative disorders, such as Charcot-Marie-Tooth disease (CMT), Parkinson's and …

Previous research has indicated that variation in the proteome profile of longissimus
lumborum (LL) and psoas major (PM) post-rigor influences meat quality attributes such as …