PXD019913

PXD019913 is an original dataset announced via ProteomeXchange.

Title	Stochiometric Quantification of the Thiol Redox Proteome Reveals Subcellular Compartmentalization and Susceptibility to Oxidative Perturbations
Description	Posttranslational modifications of protein cysteine thiols play a significant role in redox regulation and the pathogenesis of human diseases. However, the cellular redox landscape in terms of quantitative, site-specific occupancies of thiol modifications at the proteome level, especially under physiological conditions, is still largely uncharacterized. Herein, we report the site occupancies of both S-glutathionylation (SSG) and total reversible thiol oxidation (total oxidation) in RAW 264.7 macrophage cells under basal conditions. The occupancies of thiol modifications for ~4,000 cysteine sites were quantified, which revealed a mean site occupancy of 4.0% for SSG and 11.9% for total oxidation, respectively. Correlations between site occupancies and structural features such as pKa, relative residue surface accessibility, and hydrophobicity were observed. Proteome-wide site occupancy analysis also revealed a strong subcellular compartmentalization in thiol redox status, where the average occupancies of SSG and total oxidation in distinct compartments correlate well with the redox potentials of respective organelles.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:10:45.592.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD019913
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Matthew Monroe
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	Nethylmaleimide; Oxidation
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2020-06-19 16:47:30	ID requested
1	2020-08-13 04:21:55	announced
⏵ 2	2024-10-22 05:10:46	announced	2024-10-22: Updated project metadata.

10.1016/j.redox.2020.101649;

Duan J, Zhang T, Gaffrey MJ, Weitz KK, Moore RJ, Li X, Xian M, Thrall BD, Qian WJ, Stochiometric quantification of the thiol redox proteome of macrophages reveals subcellular compartmentalization and susceptibility to oxidative perturbations. Redox Biol, 36():101649(2020) [pubmed]

10.6019/PXD019913;

submitter keyword: site-occupancy, macrophage, resin-assisted enrichment, redox proteomics, S-glutathionylation, stoichiometry, redox modification,Protein thiols

Wei-Jun Qian
contact affiliation	Pacific Northwest National Laboratory, USA
contact email	Weijun.Qian@pnnl.gov
lab head
Matthew Monroe
contact affiliation	Pacific Northwest National Laboratory
contact email	matthew.monroe@pnnl.gov
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/08/PXD019913

PRIDE project URI

• PRIDE
  1. PXD019913
     1. Label: PRIDE project
     2. Name: Stochiometric Quantification of the Thiol Redox Proteome Reveals Subcellular Compartmentalization and Susceptibility to Oxidative Perturbations