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UnknownIdentification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics.
Not available
S-EPMC4288256 | biostudies-literature
UnknownInner membrane YfgM-PpiD heterodimer acts as a functional unit that associates with the SecY/E/G translocon and promotes protein translocation.
Not available
S-EPMC9643414 | biostudies-literature
ProteomicsProteomics study of chaperone network in Escherichia coli
Proteomics study on the periplasmic chaperone network in Escherichia coli
ORGANISM(S): Escherichia coli 
2014-12-12 | PXD000814 | Pride
E. coli  periplasmic chaperone network  yfgm 
UnknownNoncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in Escherichia coli.
Not available
S-EPMC6916481 | biostudies-literature
ProteomicsNon-competitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in E. coli
The SecYEG translocon constitutes the major protein transport channel in bacteria and transfers an enormous variety of different secretory and inner-membrane proteins. The minimal core of the SecYEG translocon consists of three inner-membrane proteins, SecY, SecE, and SecG, which, together with appr...
ORGANISM(S): Escherichia coli 
2019-11-07 | PXD015985 | Pride
Interaction proteomics Yidc Ppid Protein translocation Secyeg translocon Protein cross-linking Protein-protein interaction Quantitative affinity purification mass spectrometry (qap-ms) 
UnknownA trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.
Not available
S-EPMC3522291 | biostudies-literature
ProteomicsThe SecYEG interactome of E. coli: non-competitive binding of PpiD and YidC to the SecYEG translocon
The SecYEG translocon constitutes the major protein transporting channel in bacteria and transports an enormous variety of different secretory and inner membrane proteins. The minimal core of the SecYEG translocon consists of the three inner membrane proteins SecY, SecE and SecG, which together with...
ORGANISM(S): Escherichia coli 
2019-11-07 | PXD015974 | Pride
Yidc Ppid Label-free proteomics Secyeg translocon Protein cross-linking 
UnknownTranslation arrest cancellation of VemP, a secretion monitor in Vibrio, is regulated by multiple cis and trans factors, including SecY.
Not available
S-EPMC11470409 | biostudies-literature
ProteomicsA peptidisc-based AP/MS approach to explore the interactome of the bacterial Sec translocon
We recently presented the peptidisc membrane mimetic for the global reconstitution of membrane proteomes into water-soluble detergent-free particles, termed peptidisc library. We here develop a method that combines the peptidisc library with affinity pulldown and mass spectrometry (AP/MS) to explore...
ORGANISM(S): Escherichia coli (strain K12 / W3110 / ATCC 27325 / DSM 5911) 
2023-03-22 | PXD018866 | Pride
Mass spectrometry Affinity tagging Sec translocon Protein translocation Peptidisc Protein complex analysis Membrane mimetics Membrane protein complexes Protein-protein interactions Affinity purification/mass spectrometry (ap/ms) 
UnknownProfiling the Escherichia coli membrane protein interactome captured in Peptidisc libraries.
Not available
S-EPMC6697469 | biostudies-literature
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