Heat shock proteins (Hsps) are conserved molecules whose main role is to facilitate folding
of other proteins. Most Hsps are generally stress-inducible as they play a particularly …

Heat shock proteins (HSPs) play cytoprotective activities under pathological conditions
through the initiation of protein folding, repair, refolding of misfolded peptides, and possible …

The phosphatidylinositol 3-kinase (PI3K)/AKT/mammalian target of the rapamycin (mTOR)
signalling pathway is hyperactivated or altered in many cancer types and regulates a broad …

Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

Achieving sufficient coverage of regulatory phosphorylation sites by mass spectrometry (MS)-
based phosphoproteomics for signaling pathway reconstitution is challenging, especially …

Cells can respond to stress in various ways ranging from the activation of survival pathways
to the initiation of cell death that eventually eliminates damaged cells. Whether cells mount a …

Akt/PKB is a serine/threonine protein kinase that functions as a critical regulator of cell
survival and proliferation. Akt/PKB family comprises three highly homologous members …

Liver ischemia/reperfusion injury has been extensively studied during the last decades and
has been implicated in the pathophysiology of many clinical entities following hepatic …

Protein phosphorylation and dephosphorylation play a major role in intracellular signal
transduction activated by extracellular stimuli. Protein kinase B (PKB/Akt) is a central player …

Heat shock proteins (Hsps) are a family of highly homologous chaperone proteins that are
induced in response to environmental, physical and chemical stresses and that limit the …