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PXD042587

PXD042587 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleIn situ observation of chaperonin function in protein folding
DescriptionThe GroEL/GroES chaperonin mediates protein folding in bacteria in an ATP-dependent process. Studies in vitro show that the GroEL double-ring and the lid-shaped GroES transiently encapsulate unfolded protein for folding unimpaired by aggregation. To clarify critical aspects of this mechanism, we used cryo-electron tomography in situ to visualize and quantify functional GroEL:ES complexes in their intact cellular environment. Mass spectrometry was used to estimate stoichiometries of GroEL, GroES, cellular ribosome content and substrates.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_06:47:37.554.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterRoman Körner
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListmonohydroxylated residue
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-05-31 10:58:17ID requested
12024-06-27 01:34:10announced
22024-10-22 06:47:37announced2024-10-22: Updated project metadata.
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: Chaperonin, ATPase, CHAPERONE, heat shock, Folding cage, proteostasis
Contact List
F. Ulrich Hartl
contact affiliationMax-Planck Institute of Biochemistry, Department of Cellular Biochemistry
contact emailuhartl@biochem.mpg.de
lab head
Roman Körner
contact affiliationMax-Planck Institute of Biochemistry, Department of Cellular Biochemistry
contact emailrkoerner@biochem.mpg.de
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
Repository Record List
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