PXD002635-1

PXD002635 is an original dataset announced via ProteomeXchange.

Title	Evaluation of of kinase acitivity profiling using chemical proteomics
Description	Evaluation of kinase binding to immobilized inhibitors upon kinase activation. Comparison of cheomproteomic binding changes to phosphoproteomic activation profiles.
HostingRepository	PRIDE
AnnounceDate	2016-01-04
AnnouncementXML	Submission_2016-01-04_12:05:44.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Benjamin Ruprecht
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue
Instrument	Q Exactive; LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2015-07-30 00:05:17	ID requested
⏵ 1	2016-01-04 12:05:47	announced
2	2024-10-22 04:05:01	announced	2024-10-22: Updated project metadata.

Ruprecht B, Zecha J, Heinzlmeir S, M, é, dard G, Lemeer S, Kuster B, Evaluation of Kinase Activity Profiling Using Chemical Proteomics. ACS Chem Biol, 10(12):2743-52(2015) [pubmed]

curator keyword: Biological, Technical

submitter keyword: Phosphoprotoemics, Chemical Proteomics, Mass Spectrometry, Kinase, Activity

Bernhard Kuster
contact affiliation	Chair of Proteomics and Bioanalytics Technical University of Munich
contact email	kuster@tum.de
lab head
Benjamin Ruprecht
contact affiliation	TUM
contact email	Benjamin.Ruprecht@tum.de
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/2016/01/PXD002635

PRIDE project URI

• PRIDE
  1. PXD002635
     1. Label: PRIDE project
     2. Name: Evaluation of of kinase acitivity profiling using chemical proteomics