IndraLab

Statements


MME binds F3. 7 / 7
| 7

sparser
"However, since TF is not an essential protein [ xref ], it is likely that only a fraction of emerging nascent polypeptides interact with TF."

sparser
"At the ribosome, TF interacts physically with nascent polypeptides as they emerge from the polypeptide exit tunnel where, it is suggested, hydrophobic segments preferentially contact TF to facilitate folding ( xref ; xref ; xref ; xref )."

sparser
"Moreover, heat shock and TF overproduction affected GroEL binding to other denatured polypeptides in distinct ways; only TF promoted binding to certain polypeptides, whereas only phosphorylation increased binding to others."

sparser
"Second, TF associates with the ribosome to sequester and protect polypeptides just as they emerge from the peptide exit tunnel [ xref ] and this association is crucial for its in vivo function [ xref ]."

sparser
"TF chaperone action is thought to require association with the ribosome at the polypeptide exit tunnel and is attributed to TF interactions with emergent nascent polypeptides ( xref ; xref ; xref ; xref ; xref ; xref ; xref )."

sparser
"Factor III was associated with EPN suppression, whereas the number of experienced traumatic events was not a significant predictor."

sparser
"Studies of the Escherichia coli chaperone Trigger Factor (TF) reveal that, while TF can interact with many polypeptides, β-barrel outer membrane proteins are the most prominent substrates."