Abstract Background Heat shock factors (Hsfs) and proteins (Hsps) belong to an essential group of molecular regulators involved in controlling cellular processes under normal stress conditions. The role Hsfs Hsps is well known model plant species diverse While plants are vital components the signal transduction response maintain homeostasis, function as chaperones helping folding damaged newly ...

Both prokaryotes and eukaryotes tolerate different stress conditions (e.g., metabolic, environmental and pathophysiological stress) by up-regulating the expression of heat shock proteins (HSPs). These proteins are divided into six main families such as Hsp100, Hsp90, Hsp70, Hsp60, Hsp40 and small heat shock proteins (sHsps) based on their molecular weights (MW) and sequence homology [1, 2]. Amo...

Heat shock proteins (Hsps) are known to associate with estrogen receptors (ER) and regulate ER-mediated cell proliferation. Historically, the studies in this area have focused on Hsp90. However, some critical aspects of the Hsp-ERα interactions remain unclear. For example, we do not know which Hsps are the major or minor ERα interactants and whether or not different Hsp isoforms associate equal...

According to The American Heritage College Dictionary,1 a chaperone is “a guide or companion whose purpose is to ensure propriety or restrict activity.” The term “molecular chaperone” is applied to proteins that control the proper folding of nascent polypeptides into the correct 3D structure (ensure propriety) or maintain polypeptides in an inactive state (restrict activity) until they have bee...

This paper presents a robust approach to solve Hoist Scheduling Problems (HSPs) based on an integration of Constraint Logic Programming (CLP) and Mixed Integer Programming (MIP). By contrast with previous dedicated models and algorithms for solving classes of HSPs, we deene only one model and run diierent solvers. The robust approach is achieved by using a CLP formalism. We show that our models...

Heat shock proteins (Hsps) are believed to primarily protect and maintain cell viability under stressful conditions such as those occurring during thermal and oxidative challenges chiefly by refolding and stabilizing proteins. Hsps are found throughout the various tissues of the eye where they are thought to confer protection from disease states such as cataract, glaucoma, and cancer. This mini...

Heat shock proteins belong to a group of molecular chaperones responsible for the regulation of many intracellular processes. HSPs play a pivotal role in the survival of cells under stressful conditions. Overexpression of these proteins have been found in both healthy and a great number of cancer cells. HSPs may be involved in numerous carcinogenic and chemoresistant processes. Due to that fact...

The dynamic responses of honeycomb sandwich panels (HSPs) subjected to in-plane projectile impact were studied by means of explicit nonlinear finite element simulations using LS-DYNA. The HSPs consisted of two identical aluminum alloy face-sheets and an aluminum honeycomb core featuring three types of unit cell configurations (regular, rectangular-shaped, and reentrant hexagons). The ballistic ...

Many different external and intrinsic apoptotic stimuli induce the accumulation in the cells of a set of proteins known as stress or heat shock proteins (HSPs). HSPs are conserved proteins present in both prokaryotes and eukaryotes. These proteins play an essential role as molecular chaperones by assisting the correct folding of nascent and stress-accumulated misfolded proteins, and by preventi...

During stress conditions, such as infection, the synthesis of heat shock proteins (HSPs) in microorganisms is upregulated. Since a high degree of homology exists within each HSP family, we postulated that exposure to microorganisms could prime the immune system for evolutionarily diverse HSPs. We tested this hypothesis by priming mice with three microorganisms, namely, Mycobacterium bovis BCG, ...