PXD053814

PXD053814 is an original dataset announced via ProteomeXchange.

Title	Discovery of dehydroamino acids and their crosslinks in Alzheimer's Disease
Description	Alzheimer’s disease is characterized by the accumulation of protein aggregates. Dehydroamino acids are rarely observed posttranslational modifications that contain an electrophilic alkene capable of forming protein-protein crosslinks, which may lead to protein aggregation. We used mass spectrometry-based proteomics to discover 412 sites of dehydroamino acid formation in 184 proteins from protein aggregate-enriched human brain samples, an order of magnitude more than observed in the soluble protein fractions. We further report 11 dehydroamino acid-mediated crosslinks, including 3 in the Tau protein that are 10-fold more abundant in Alzheimer’s disease samples compared to age-matched controls. Dehydroamino acids are prevalent modifications in the Alzheimer’s disease brain proteome and give rise to protein crosslinks that may contribute to protein aggregation.
HostingRepository	PRIDE
AnnounceDate	2025-03-06
AnnouncementXML	Submission_2025-03-06_12:28:01.925.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Samuel Markovich
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	dehydroalanine (Cys); dehydroalanine (Ser); dehydrobutyrine (Thr); phosphorylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2024-07-09 18:24:42	ID requested
⏵ 1	2025-03-06 12:28:02	announced

10.1093/braincomms/fcaf019;

submitter keyword: CRMP2,Alzheimer's Disease, Tau, GAPDH, Dehydroamino acids, crosslinks

Lloyd M
contact affiliation	Professor of Chemistry, University of Wisconsin - Madison
contact email	smith@chem.wisc.edu
lab head
Samuel Markovich
contact affiliation	University of Wisconsin-Madison
contact email	smarkovich@wisc.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/2025/03/PXD053814

PRIDE project URI

• PRIDE
  1. PXD053814
     1. Label: PRIDE project
     2. Name: Discovery of dehydroamino acids and their crosslinks in Alzheimer's Disease