Ontology highlight
ABSTRACT:
ORGANISM(S): Escherichia Coli
SUBMITTER: Hideki Taguchi
PROVIDER: PXD033134 | JPOST Repository | Mon Jun 27 00:00:00 BST 2022
REPOSITORIES: jPOST
Action | DRS | |||
---|---|---|---|---|
MG1655_Ara_S1.wiff | Wiff | |||
MG1655_Ara_S1.wiff.scan | Wiff | |||
MG1655_Ara_S3.wiff | Wiff | |||
MG1655_Ara_S3.wiff.scan | Wiff | |||
MG1655_Glc_S1.wiff | Wiff |
Items per page: 1 - 5 of 20 |
Molecules (Basel, Switzerland) 20220611 12
The <i>Escherichia coli</i> chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in <i>E. coli</i> are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these substrates, when overexpressed, tend to form aggregates, whereas the GroE substrates expressed at low or endogenous levels are degraded, probably due to misfolded states. However, the protease(s) involved in the degradation process ...[more]