PXD000860

PXD000860 is an original dataset announced via ProteomeXchange.

Title	SILAC-Based Strategy for Proteome-Wide Analysis of Protein-Ligand Binding Interactions (Part 2/2)
Description	A quantitative mass spectrometry-based proteomics method for the large-scale thermodynamic analysis of protein-ligand binding interactions. The methodology utilizes a chemical modification strategy termed, Stability of Proteins from Rates of Oxidation (SPROX), in combination with a Stable Isotope Labeling with Amino Acids in Cell Culture (SILAC) approach to compare the equilibrium folding/unfolding properties of proteins in the absence and presence of target ligands. The method, which is general with respect to ligand, measures the ligand-induced changes in protein stability associated with protein-ligand binding. The methodology is demonstrated in a proof-of-principle study in which the well-characterized protein-drug interaction between cyclosporine A and cyclophilin A is analyzed in the context of a yeast cell lysate. The method is also utilized for the global analysis of adenosine triphosphate (ATP) binding to proteins in the yeast proteome using the non-hydrolyzable ATP analogue, adenylyl imidodiphosphate (AMP-PNP), and the proteins in a yeast cell lysate.
HostingRepository	PRIDE
AnnounceDate	2014-10-23
AnnouncementXML	Submission_2014-10-23_03:08:38.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jagat Adhikari
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	deamidated residue; monohydroxylated residue; iodoacetamide derivatized residue; 6x(13)C labeled residue; methylthiolated residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2014-03-27 04:48:26	ID requested
1	2014-07-31 07:50:07	announced
⏵ 2	2014-10-23 03:08:39	announced	Updated project metadata.

Tran DT, Adhikari J, Fitzgerald MC, StableIsotope Labeling with Amino Acids in Cell Culture (SILAC)-based strategy for proteome-wide thermodynamic analysis of protein-ligand binding interactions. Mol Cell Proteomics, 13(7):1800-13(2014) [pubmed]

curator keyword: Biological

submitter keyword: ATP, Cyclosporine A, Shot-gun proteomics,Yeast

Michael C. Fitzgerald
contact affiliation	Chemistry Department, Duke University
contact email	michael.c.fitzgerald@duke.edu
lab head
Jagat Adhikari
contact affiliation	Duke University
contact email	ja117@duke.edu
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/2014/07/PXD000860

PRIDE project URI

• PRIDE
  1. PXD000860
     1. Label: PRIDE project
     2. Name: SILAC-Based Strategy for Proteome-Wide Analysis of Protein-Ligand Binding Interactions (Part 2/2)