IndraLab

Statements

F3 binds MME. 11 / 11
| 11
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 )."
19737520
sparser
"However, since TF is not an essential protein [ xref ], it is likely that only a fraction of emerging nascent polypeptides interact with TF."
21538896
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."
8999853
sparser
"Protease protection appears to depend on a hydrophobic interaction of TF with nascent polypeptides."
16359675
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."
22153074
sparser
"Therefore, both TF 2 dimers and TF monomers can interact with polypeptides."
27626893
sparser
"Studies of the Escherichia coli chaperone trigger factor (TF) reveal that, though TF can interact with many polypeptides, β-barrel outer-membrane proteins are the most prominent substrates."
22153074
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 ]."
20920237
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 )."
19737520
sparser
"Upon deleting dnaK or dnaJ , the population increase of TF bound to the free ribosomal subunits can be rationalized by the possibility that TF takes over DnaK’s role as a complement in facilitating ribosome assembly ( xref , xref ), while the population increase of the polypeptide-bound TF can be rationalized by the interruption of the pathway in which TF-polypeptide complexes interact with DnaK/DnaJ to transfer the unfolded polypeptides to complete folding ( xref )."
27626893
sparser
"Factor III was associated with EPN suppression, whereas the number of experienced traumatic events was not a significant predictor."
30807662