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ProteomicsCotranslational activity of the GroEL chaperonin
Various proteins in the cell begin to fold during synthesis at the ribosome, many with the assistance of molecular chaperones. While the cotranslational activity of ribosome-associated chaperones and Hsp70 is frequently studied, the role of Hsp60 chaperonins during protein synthesis remains poorly u...
ORGANISM(S): Escherichia coli 
2025-10-14 | PXD054376 | Pride
Groel Hdx-ms Rnc 
ProteomicsCotranslational activity of the GroEL chaperonin
Various proteins in the cell begin to fold during synthesis at the ribosome, many with the assistance of molecular chaperones. While the cotranslational activity of ribosome-associated chaperones and Hsp70 is frequently studied, the role of Hsp60 chaperonins during protein synthesis remains poorly u...
ORGANISM(S): Escherichia coli 
2025-10-14 | PXD054379 | Pride
Groel Xl-ms Rnc 
ProteomicsGroEL interaction and folding of MetF studied by hydrogen/deuterium exchange – mass spectrometry
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in E. coli by transiently encapsulating non-native substrate in a nano-cage formed by the GroEL ring cavity and the lid-shaped GroES. We analyzed the spontaneous and chaperonin-assisted folding of the essen...
ORGANISM(S): Escherichia coli 
2020-03-05 | PXD016666 | Pride
Groel Chaperone Folding Metf Hydrogen/deuterium exchange Chaperonin 
ProteomicsGroEL-proteotypbing-based stable isotope probing of Thauera aromatica K172, Pseudomonas putida KT2440, and Escherichia coli BL21(DE3)
This dataset has been used to establish GroEL-SIP, coupling a targeted proteotyping approach for assessing bacterial community compositions using the taxonomic marker protein GroEL with stable isotope probing to link the identified taxa to substrate assimilation. This dataset contains raw data of fo...
ORGANISM(S): Thauera aromatica K172 Escherichia coli BL21(DE3) Pseudomonas putida KT2440 Bacteria 
2024-10-17 | PXD048255 | Pride
Protein-sip Stable isotope probing Groel-proteotyping 
ProteomicsPure and mixed crude extracts of Thauera aromatica K172 and Pseudomonas putida KT2440 for benchmarking GroEL-proteotyping
This dataset has been used to establish GroEL-proteotyping, a targeted proteotyping approach for assessing bacterial community compositions using the taxonomic marker protein GroEL. This dataset contains raw data of two experiments: 1. Pure cultures of T. aromatica (sample names: TA, TB, TC) and P. ...
ORGANISM(S): Thauera aromatica K172 Pseudomonas putida KT2440 
2023-10-27 | PXD046460 | Pride
Shotgun proteomics Taxonomic profiling Chaperon Sds-page Proteotyping Chaperonin Metaproteomics 
ProteomicsCotranslational activity of the GroEL chaperonin
Various proteins in the cell begin to fold during synthesis at the ribosome, many with the assistance of molecular chaperones. While the cotranslational activity of ribosome-associated chaperones and Hsp70 is frequently studied, the role of Hsp60 chaperonins during protein synthesis remains poorly u...
ORGANISM(S): Escherichia coli 
2025-10-14 | PXD054251 | Pride
Groel Rnc Ibaq 
ProteomicsProteome dysregulation induced by degrader peptides targeting GroEL chaperone in Escherichia coli
Inducible degradation presents an attractive alternative for modulating protein levels in bacteria without genome editing or RNA interference. In this work we constructed a series of plasmids encoding degrader peptides which bring together an essential GroEL chaperone and activated ClpXP protease to...
ORGANISM(S): Escherichia coli 
2025-06-24 | PXD045730 | Pride
Targeted protein degradation Groel Peptide Degrader Proteostasis 
UnknownCreating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.
Not available
S-EPMC5575113 | biostudies-literature
UnknownProbing open conformation of GroEL rings by cross-linking reveals single and double open ring structures of GroEL in ADP and ATP.
Not available
S-EPMC2755691 | biostudies-literature
UnknownDifferentiation of rickettsiae by groEL gene analysis.
Not available
S-EPMC165385 | biostudies-literature
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