Study demonstrates 'tunability' of a molecular chaperone

For decades, molecular biologists studying a class of molecular chaperones known as heat shock proteins (Hsp70s) have relied on the Hsp70s found in bacteria as the model system. Now one of the world's experts on the molecule ...

Cellular stress defense

Small heat-shock proteins (sHSPs) are molecular chaperones that bind to unfolded proteins to prevent protein aggregation and defend against cellular stress. Mutations in human sHSPs are associated with inherited diseases ...

Maximum precision in protein synthesis

Researchers from the Center for Molecular Biology of Heidelberg University (ZMBH) and the German Cancer Research Center (DKFZ) have investigated the mode of action of a molecular chaperone vital to protein synthesis. Together ...

Molecular assembly line brings muscles into shape

Scientists at the Research Institute of Molecular Pathology (IMP) in Vienna, Austria and at the University of Cologne, Germany have discovered the molecular basis underlying the patterned folding and assembly of muscle proteins. ...

Biochemists trap a chaperone machine in action

Molecular chaperones have emerged as exciting new potential drug targets, because scientists want to learn how to stop cancer cells, for example, from using chaperones to enable their uncontrolled growth. Now a team of biochemists ...

Chaperone protein subverts removal of glaucoma-causing protein

The chaperone protein Grp94 can interfere with the clearance of another protein known to cause the glaucoma when mutated, a new study led by researchers at the University of South Florida has found. Using a cell model, the ...

New insights to the function of molecular chaperones

(Phys.org)—Heidelberg molecular biologists have gained new insights into the function of so-called molecular chaperones in protein synthesis. The team headed by Dr. Günter Kramer and Prof. Dr. Bernd Bukau of the DKFZ-ZMBH ...

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