Heat shock proteins (HSPs) encompass both extrinsic chaperones and stress proteins.
These proteins, with molecular weights ranging from 14 to 120 kDa, are conserved across …

Heat shock proteins (Hsps) are robustly induced by diverse stressors that denature proteins.
In addition to stress resistance, Hsps are involved in the folding of nascent proteins, plant …

Climate change is predicted to change the distribution and abundance of species, yet
underlying physiological mechanisms are complex and methods for detecting populations at …

The largemouth bass is an important freshwater fish in China. As global climate changes,
mass mortality in largemouth bass due to extremely low/high temperatures has aroused …

Despite the threat of climate change, the physiological mechanisms responsible for reduced
performance at high temperatures remain unclear for most species. Elevated but sublethal …

The frequency of extreme thermal events in temperate freshwater systems is expected to
increase alongside global surface temperature. The Miramichi River, located in eastern …

The retention of a nucleus in the mature state of fish red blood cells (RBCs) and the ability to
easily collect and manipulate blood in nonterminal experiments make blood an ideal tissue …

Heat shock proteins (HSPs) are highly conserved, cytoprotective proteins, the best know
function of which is to facilitate the proper folding of nascent proteins. Environmental …

Highly evolutionary conserved heat shock proteins (HSPs) act as molecular chaperones in
regulation of cellular homeostasis and promoting survival. Generally they are induced by a …

When faced with limited resources, juvenile salmonid fish form dominance hierarchies that
result in social stress for socially subordinate individuals. Social stress, in turn, can have …