HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein,
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

Bacillus subtilis is a well-characterized Gram-positive bacterium and a valuable host for
recombinant protein production because of its efficient secretion ability, high yield, and non …

Heat shock proteins (HSPs) are molecular chaperones with critical roles in the maintenance
of cellular proteostasis. HSPs, which regulate protein folding and refolding, assembly …

Настоящая монография посвящена четырем патогенным для человека вирусам (оспы
коров, оспы обезьян, натуральной оспы и вакцины), принадлежащим к одному роду …

Biological systems have evolved to utilize proteins to accomplish nearly all functional roles
needed to sustain life. A majority of biological functions occur within the crowded …

The application of nitrogen fertilizers in the rice-crab co-culture system may expose juvenile
Eriocheir sinensis to high ammonia concentrations within a short period of time, potentially …

Ammonia-N accumulation in the rice-crab co-culture system may have negative effects on
the health of juvenile Eriocheir sinensis. In this study, physiological, transcriptomic, and …

Protein structure underpins functional roles in all biological processes; therefore, improved
understanding of protein structures is of fundamental importance in nearly all biological and …

Protein misfolding and aggregation are implicated in many neurodegenerative diseases.
One of these diseases is Huntington's, which is caused by increased glutamine-encoding …