AbstractMolecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the ‘J domains’ of these ‘cochaperones’ activate substrate binding by Hsp70 molecules
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...
AbstractMolecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding...
AbstractThe discovery of a new co-chaperone, Hip, that interacts with Hsp70 underscores the complexi...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
The 70kDa members of the heat shock protein family (eg. Hsp70) function as molecular chaperones by ...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...
The Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificit...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...
AbstractMolecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding...
AbstractThe discovery of a new co-chaperone, Hip, that interacts with Hsp70 underscores the complexi...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
The 70kDa members of the heat shock protein family (eg. Hsp70) function as molecular chaperones by ...
Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...
The Hsp40/Hsp70 chaperone families combine versatile folding capacity with high substrate specificit...
Heat shock protein 40s (Hsp40s) and heat shock protein 70s (Hsp70s) form chaperone partnerships that...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation throu...