PXD013182

PXD013182 is an original dataset announced via ProteomeXchange.

Title	Proteome Integral Solubility Alteration (PISA): a high-throughput proteomics assay for target deconvolution
Description	Various agents, including drugs as well as non-molecular influences, induce alterations in the physic-chemical properties of proteins in cell lysates, living cells and organisms. These alterations can be probed by applying a stability-modifying factor, such as elevated temperature, to a varying degree. As a second dimension of variation, drug concentration or agent intensity/concentration can be used. A typical example is the thermal stability assay. However, the conventional analysis scheme has a low throughput and high cost. Additionally, since traditional data analysis employs curve fitting, proteins with unusual behavior are frequently ignored. The novel Proteome Integral Stability Alteration (PISA) assay avoids these issues altogether, increasing the analysis throughput by one to two orders of magnitude for unlimited number of factor variation points. The consumption of the compound and biological material decreases by the same factor. As an example, an analogue of a two-dimensional thermal stability assay can be performed in three replicates using a single 10-plex proteome analysis. We envision widespread use of the PISA approach in chemical biology and drug development.
HostingRepository	PRIDE
AnnounceDate	2020-04-01
AnnouncementXML	Submission_2020-04-01_08:10:16.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Massimiliano Gaetani
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; deamidated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2019-03-21 09:20:28	ID requested
⏵ 1	2020-04-01 08:10:18	announced

Gaetani M, Sabatier P, Saei AA, Beusch CM, Yang Z, Lundstr, ö, m SL, Zubarev RA, Proteome Integral Solubility Alteration: A High-Throughput Proteomics Assay for Target Deconvolution. J Proteome Res, 18(11):4027-4037(2019) [pubmed]

submitter keyword: quantitative proteomics, target deconvolution, thermal profiling, protein stability, TMT

Roman A. Zubarev
contact affiliation	Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17 177 Stockholm, Sweden
contact email	roman.zubarev@ki.se
lab head
Massimiliano Gaetani
contact affiliation	Karolinska Institutet
contact email	massimiliano.gaetani@ki.se
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/2020/04/PXD013182

PRIDE project URI

• PRIDE
  1. PXD013182
     1. Label: PRIDE project
     2. Name: Proteome Integral Solubility Alteration (PISA): a high-throughput proteomics assay for target deconvolution