PXD037380

PXD037380 is an original dataset announced via ProteomeXchange.

Title	Evaluation of peptide pulldown coupled to mass spectrometry approaches for investigation of motif-based protein-protein interactions
Description	Eight different, SLiM-containing peptides were tested for pulldowns immobilized on magnetic beads, and the same sequences were used for PRISMA experiments. Double repeat of peptides were also used for higher local concentration of the motifs.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:58:50.895.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Eszter Kassa
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; deaminated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-10-13 14:53:09	ID requested
1	2023-03-07 07:21:37	announced
⏵ 2	2023-11-14 08:58:51	announced	2023-11-14: Updated project metadata.

Dataset with its publication pending

submitter keyword: AP-MS, PRISMA, pulldown, SLiM,protein-protein interaction

Ylva Ivarsson
contact affiliation	Uppsala University, Chemistry-BMC
contact email	ylva.ivarsson@kemi.uu.se
lab head
Eszter Kassa
contact affiliation	Uppsala University
contact email	eszter.kassa@kemi.uu.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/2023/03/PXD037380

PRIDE project URI

• PRIDE
  1. PXD037380
     1. Label: PRIDE project
     2. Name: Evaluation of peptide pulldown coupled to mass spectrometry approaches for investigation of motif-based protein-protein interactions