AbstractA number of molecular chaperones have been found to interact with nascent polypeptides attached to ribosomes, allowing these protein-synthesis machines to play a key part in protein folding and targeting
De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperone...
Ribosome-associated chaperone Trigger Factor (TF) initi-ates folding of newly synthesized proteins i...
AbstractNewly synthesized proteins often require the assistance of molecular chaperones to efficient...
AbstractA number of molecular chaperones have been found to interact with nascent polypeptides attac...
AbstractThe physiological roles of the molecular chaperones trigger factor and DnaK in de novo prote...
In all organisms, the ribosome synthesizes and folds full length polypeptide chains into active thre...
A central dogma in biology is the conversion of genetic information into active proteins. The biosyn...
Newly synthesized proteins leave the ribosome through a narrow tunnel in the large subunit. During o...
How nascent polypeptides emerging from ribosomes fold into functional structures is poorly understoo...
Upon their synthesis by ribosomes, proteins have to fold into unique three-dimensional structures to...
Trigger factor is a 48-kDa cytosolic chaperone protein found in all eubacteria. It has been shown to...
In prokaryotes, the ribosome-associated Trigger Factor is the first chaperone newly synthesized poly...
AbstractChaperones and foldases are two groups of accessory proteins which assist maturation of nasc...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperone...
Ribosome-associated chaperone Trigger Factor (TF) initi-ates folding of newly synthesized proteins i...
AbstractNewly synthesized proteins often require the assistance of molecular chaperones to efficient...
AbstractA number of molecular chaperones have been found to interact with nascent polypeptides attac...
AbstractThe physiological roles of the molecular chaperones trigger factor and DnaK in de novo prote...
In all organisms, the ribosome synthesizes and folds full length polypeptide chains into active thre...
A central dogma in biology is the conversion of genetic information into active proteins. The biosyn...
Newly synthesized proteins leave the ribosome through a narrow tunnel in the large subunit. During o...
How nascent polypeptides emerging from ribosomes fold into functional structures is poorly understoo...
Upon their synthesis by ribosomes, proteins have to fold into unique three-dimensional structures to...
Trigger factor is a 48-kDa cytosolic chaperone protein found in all eubacteria. It has been shown to...
In prokaryotes, the ribosome-associated Trigger Factor is the first chaperone newly synthesized poly...
AbstractChaperones and foldases are two groups of accessory proteins which assist maturation of nasc...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones...
De novo protein folding is delicate and error-prone and requires the guidance of molecular chaperone...
Ribosome-associated chaperone Trigger Factor (TF) initi-ates folding of newly synthesized proteins i...
AbstractNewly synthesized proteins often require the assistance of molecular chaperones to efficient...
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