Add to ORKGHsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Heat shock protein 70 (Hsp70) is a molecular chaperone that plays a central role in cellular protein...
Molecular chaperones bind to misfolded proteins (“clients”) to protect them from aggregation and pro...
Protein homeostasis (proteostasis) is an essential pillar for correct cellular function. Impairments...
Heat shock protein 70 (HSP70) chaperones play a central role in protein quality control and are cruc...
Heat shock protein 70 (Hsp70) is a molecular chaperone and central regulator of protein homeostasis ...
The Hsp70 family protein members are involved in many diverse processes that are essential for cell ...
Background. Chaperones and their co-factors are components of a cellular network; they collaborate t...
International audienceHeat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conse...
Hsp70 molecular chaperones protect proteins from aggregation, assist in their native structure forma...
Heat shock protein 70 (Hsp70) is a molecular chaperone that plays critical roles in protein homeosta...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts...
AbstractMolecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding...
The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protection from str...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Heat shock protein 70 (Hsp70) is a molecular chaperone that plays a central role in cellular protein...
Molecular chaperones bind to misfolded proteins (“clients”) to protect them from aggregation and pro...
Protein homeostasis (proteostasis) is an essential pillar for correct cellular function. Impairments...
Heat shock protein 70 (HSP70) chaperones play a central role in protein quality control and are cruc...
Heat shock protein 70 (Hsp70) is a molecular chaperone and central regulator of protein homeostasis ...
The Hsp70 family protein members are involved in many diverse processes that are essential for cell ...
Background. Chaperones and their co-factors are components of a cellular network; they collaborate t...
International audienceHeat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conse...
Hsp70 molecular chaperones protect proteins from aggregation, assist in their native structure forma...
Heat shock protein 70 (Hsp70) is a molecular chaperone that plays critical roles in protein homeosta...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts...
AbstractMolecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding...
The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protection from str...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Heat shock protein 70 (Hsp70) is a molecular chaperone that plays a central role in cellular protein...
Molecular chaperones bind to misfolded proteins (“clients”) to protect them from aggregation and pro...