17 research outputs found
Tensile deformation behavior of coarse-grained Ti-55 titanium alloy with different hydrogen additions
The Modification of Electrochemical Properties of Pd by its Alloying with Ru, Rh, and Pt: the Study of Ternary Systems
Tet2-mediated epigenetic drive for astrocyte differentiation from embryonic neural stem cells
Theoretical Investigation of the Mechanical and Thermodynamic Properties of the Layered Yttrium Diborocarbides
`The HSP70 chaperone machinery:J proteins as drivers of functional specificity
Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in a myriad of biological processes, modulating polypeptide folding, degradation and translocation across membranes, and protein-protein interactions. This multitude of roles is not easily reconciled with the universality of the activity of HSP70s in ATP-dependent client protein-binding and release cycles. Much of the functional diversity of the HSP70s is driven by a diverse class of cofactors: J proteins. Often, multiple J proteins function with a single HSP70. Some target HSP70 activity to clients at precise locations in cells and others bind client proteins directly, thereby delivering specific clients to HSP70 and directly determining their fate