29 research outputs found
LPS alters pattern of sickness behavior but does not affect glutathione level in aged male rats
Effects of material and test parameters on the wear behavior of particulate filled composites Part 1: SiC-epoxy and 13; Gr-epoxy composites
Studies were carried out on a (RT) cure epoxy (LY556xFE;HY951) composite system13; comprising of silicon carbide (SiC) and graphite (Gr) particulates. Results showed that13; the wear resistance and coefficient of friction of both the composites increased with sliding13; distance and contact load (contact pressure) for the range of filler contents (5x2013;40% wt) considered.13; The Gr-composite exhibited its distinct (superior) tribological feature compared to the13; SiC-composite. A wear endurance index has been identified from the experimental data, to serve13; as a parameter to assess the long term wear life (residual wear life) of these composites
High molecular weight hyaluronic acid: a two-pronged protectant against infection of the urogenital tract?
Modeling of Cold Metal Transfer Spot Welding of AA6061-T6 Aluminum Alloy and Galvanized Mild Steel
A novel allosteric means of inhibiting heat shock 70 proteins
The highly conserved heat shock 70 proteins (HSP70) play an integral role in the chaperone network where ATP-driven cycles of protein folding are carefully controlled. HSP70 dysregulation has been implicated in numerous diseases including cancer and neurodegeneration, however, elucidating the precise role of HSP70 in the cellular context using genetic tools are hampered by the redundancy and intricate regulation of the chaperone network. Through yeast chemogenomic profiling we identified a novel natural product, novolactone, with a unique means of altering HSP70 activity. The compound does not compete with ATP or HSP40, but allosterically inhibits HSP70 ATPase activity through a selective covalent interaction. Co-crystalization with novolactone reveals a novel binding pocket that is conserved between HSP70 and HSC70, and treatment of mammalian cells leads to degradation of HSP90 client proteins. Thus, this small molecule is a valuable tool to explore the cellular requirements for the heat shock 70 chaperones in a disease context