Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochondria. Folding occurs at the surface of hsp60 in an ATP-mediated reaction, followed by release of the bound polypeptides. We propose that hsp60 catalyses protein folding
To maintain healthy mitochondrial enzyme content and function, mitochondria possess a complex protei...
Unfolding and import of preproteins into mitochondria are facilitated by a molecular motor in which ...
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and d...
Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochondr...
AbstractI propose that a molecular chaperone hsp60 binds to and dissociates from the unfolded polype...
Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed ...
Protein folding in the cell requires ATP-driven chaperone machines such as the conserved Hsp70 and H...
Proteins are essential elements that are responsible for a variety of cellular activities within org...
Hsp70s are highly conserved ATPase molecular chaperones mediating the correct folding of de novo syn...
The E. coli GroEL/GroES chaperonin complex acts as a folding cage by producing a bullet-like asymmet...
Proteins are essential elements that are responsible for a variety of cellular activities within org...
This review is focused on the mechanisms by which ATP bind-ing and hydrolysis drive chaperone machin...
This review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machine...
The human mitochondrial chaperonin is a macromolecular machine that catalyzes the proper folding and...
In the large class of molecules that maintain protein homeostasis, called molecular chaperones, chap...
To maintain healthy mitochondrial enzyme content and function, mitochondria possess a complex protei...
Unfolding and import of preproteins into mitochondria are facilitated by a molecular motor in which ...
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and d...
Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochondr...
AbstractI propose that a molecular chaperone hsp60 binds to and dissociates from the unfolded polype...
Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed ...
Protein folding in the cell requires ATP-driven chaperone machines such as the conserved Hsp70 and H...
Proteins are essential elements that are responsible for a variety of cellular activities within org...
Hsp70s are highly conserved ATPase molecular chaperones mediating the correct folding of de novo syn...
The E. coli GroEL/GroES chaperonin complex acts as a folding cage by producing a bullet-like asymmet...
Proteins are essential elements that are responsible for a variety of cellular activities within org...
This review is focused on the mechanisms by which ATP bind-ing and hydrolysis drive chaperone machin...
This review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machine...
The human mitochondrial chaperonin is a macromolecular machine that catalyzes the proper folding and...
In the large class of molecules that maintain protein homeostasis, called molecular chaperones, chap...
To maintain healthy mitochondrial enzyme content and function, mitochondria possess a complex protei...
Unfolding and import of preproteins into mitochondria are facilitated by a molecular motor in which ...
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and d...