How chaperonins orchestrate the successful folding of even the most elaborate of proteins is a question of central importance. In two recent studies in Cell by Joachimiak et al. and Freund et al.; a new class of TRiC substrate is identified, and how the chaperonin exploits its different subunits to extend its substrate repertoire and direct productive folding is revealed
The TCP-1 ring complex (TRiC) is a multi-subunit group II chaperonin that assists nascent or misfold...
The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein acti...
The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar ...
How chaperonins orchestrate the successful folding of even the most elaborate of proteins is a quest...
Folding within the crowded cellular milieu often requires assistance from molecular chaperones that ...
Cellular health is dependent on the proper folding of proteins and dysregulation of this pathway can...
AbstractEfficient de novo folding of actins and tubulins requires two molecular chaperones, the chap...
The eukaryotic chaperonin, TRiC/CCT (TRiC, TCP-1 ring complex; CCT, chaperonin containing TCP-1), us...
The integrity of a cell’s proteome depends on correct folding of polypeptides by chaperonins. The ch...
SummaryThe eukaryotic chaperonin TRiC (also called CCT) is the obligate chaperone for many essential...
AbstractRecent work has shown that the eukaryotic chaperonin CCT/TRiC facilitates folding of WD-repe...
The TRiC chaperonin belongs to the group II chaperonin that is ubiquitously expressed in the cytosol...
In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a protein foldin...
Recent work has shown that the eukaryotic chaperonin CCT/TRiC facilitates folding of WD-repeat prote...
AbstractChaperonins use ATPase cycling to promote conformational changes leading to protein folding....
The TCP-1 ring complex (TRiC) is a multi-subunit group II chaperonin that assists nascent or misfold...
The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein acti...
The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar ...
How chaperonins orchestrate the successful folding of even the most elaborate of proteins is a quest...
Folding within the crowded cellular milieu often requires assistance from molecular chaperones that ...
Cellular health is dependent on the proper folding of proteins and dysregulation of this pathway can...
AbstractEfficient de novo folding of actins and tubulins requires two molecular chaperones, the chap...
The eukaryotic chaperonin, TRiC/CCT (TRiC, TCP-1 ring complex; CCT, chaperonin containing TCP-1), us...
The integrity of a cell’s proteome depends on correct folding of polypeptides by chaperonins. The ch...
SummaryThe eukaryotic chaperonin TRiC (also called CCT) is the obligate chaperone for many essential...
AbstractRecent work has shown that the eukaryotic chaperonin CCT/TRiC facilitates folding of WD-repe...
The TRiC chaperonin belongs to the group II chaperonin that is ubiquitously expressed in the cytosol...
In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a protein foldin...
Recent work has shown that the eukaryotic chaperonin CCT/TRiC facilitates folding of WD-repeat prote...
AbstractChaperonins use ATPase cycling to promote conformational changes leading to protein folding....
The TCP-1 ring complex (TRiC) is a multi-subunit group II chaperonin that assists nascent or misfold...
The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein acti...
The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex with eight distinct but similar ...