Add to ORKGIn this issue of Molecular Cell, Sahasrabudhe et al. (2017) present a dramatically renovated functional cycle for the molecular chaperone Hsp90, which stimulates re-thinking of the mechanism of this vital protein folding machine
International audienceThe Ninth International Conference on the Hsp90 Chaperone Machine concluded in...
AbstractHsp90, the most abundant cellular protein, has been implicated in numerous physiological and...
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the...
In this issue of Molecular Cell, Sahasrabudhe et al. (2017) present a dramatically renovated functio...
The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Desp...
AbstractHsp90 is a dimeric molecular chaperone required for the activation and stabilization of nume...
Molecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein fo...
AbstractThe heat shock protein Hsp90 is a molecular chaperone which assists the refolding of misfold...
SummaryA comprehensive understanding of the cellular functions of the Hsp90 molecular chaperone has ...
Molecular chaperones have evolved to support the general stability and maintenance of the cellular p...
AbstractCellular environments are highly complex and contain a copious variety of proteins that must...
The Hsp90 chaperone is responsible for the activation and maturation of an eclectic set of proteins....
AbstractMembers of the Hsp90 molecular chaperone family are found in the cytosol, ER, mitochondria a...
Deciphering functional mechanisms of the Hsp90 chaperone machinery is an important objective in canc...
Protein folding quality control in cells requires the activity of a class of proteins known as molec...
International audienceThe Ninth International Conference on the Hsp90 Chaperone Machine concluded in...
AbstractHsp90, the most abundant cellular protein, has been implicated in numerous physiological and...
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the...
In this issue of Molecular Cell, Sahasrabudhe et al. (2017) present a dramatically renovated functio...
The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Desp...
AbstractHsp90 is a dimeric molecular chaperone required for the activation and stabilization of nume...
Molecular chaperones are vital proteins that maintain protein homeostasis by assisting in protein fo...
AbstractThe heat shock protein Hsp90 is a molecular chaperone which assists the refolding of misfold...
SummaryA comprehensive understanding of the cellular functions of the Hsp90 molecular chaperone has ...
Molecular chaperones have evolved to support the general stability and maintenance of the cellular p...
AbstractCellular environments are highly complex and contain a copious variety of proteins that must...
The Hsp90 chaperone is responsible for the activation and maturation of an eclectic set of proteins....
AbstractMembers of the Hsp90 molecular chaperone family are found in the cytosol, ER, mitochondria a...
Deciphering functional mechanisms of the Hsp90 chaperone machinery is an important objective in canc...
Protein folding quality control in cells requires the activity of a class of proteins known as molec...
International audienceThe Ninth International Conference on the Hsp90 Chaperone Machine concluded in...
AbstractHsp90, the most abundant cellular protein, has been implicated in numerous physiological and...
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the...