Proteomics study of chaperone network in Escherichia coli
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Escherichia Coli
SUBMITTER: 
Gianluca Maddalo
LAB HEAD: Albert J.R. Heck
PROVIDER: PXD000814 | Pride | 2014-12-12
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Data_DSurADyfgM.xlsx | Xlsx | |||
| Data_DskpDyfgM.xlsx | Xlsx | |||
| Data_DyfgM.xlsx | Xlsx | |||
| ON-OFF_DskpDyfgM.xlsx | Xlsx | |||
| ON-OFF_DsurADyfgM.xlsx | Xlsx |
Items per page: 5 1 - 5 of 150 |
Publications
Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics.
Götzke Hansjörg H Muheim Claudio C Altelaar A F Maarten AF Heck Albert J R AJ Maddalo Gianluca G Daley Daniel O DO
Molecular & cellular proteomics : MCP 20141117 1
How proteins are trafficked, folded, and assembled into functional units in the cell envelope of Gram-negative bacteria is of significant interest. A number of chaperones have been identified, however, the molecular roles of these chaperones are often enigmatic because it has been challenging to assign substrates. Recently we discovered a novel periplasmic chaperone, called YfgM, which associates with PpiD and the SecYEG translocon and operates in a network that contains Skp and SurA. The aim of ...[more]
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