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PXD068367

PXD068367 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleNitrated products formed on α-synuclein are preferentially incorporated into oligomers but excluded from fibrils: a mechanism for accumulation of neurotoxic species
DescriptionPost-translational modifications (PTMs) such as nitration of Tyr (Y) residues and di-tyrosine (DT) formation are known to impact the aggregation behavior of α-synuclein (α-syn), a protein closely linked to Parkinson’s disease. Using tetranitromethane (TNM) as a model nitrating agent, we systematically investigated the chemical modifications of α-syn and their consequences for aggregation. Mass spectrometry analysis revealed selective nitration of all four Tyr residues, with Y39 and Y125 being most susceptible. DT crosslinks were also observed, primarily involving Y39, but were disfavored at higher TNM concentrations, indicating competition between nitration and crosslinking pathways.
HostingRepositoryPRIDE
AnnounceDate2026-06-19
AnnouncementXMLSubmission_2026-06-19_12:20:05.080.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterLuke Gamon
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationListnitrated L-tyrosine
InstrumenttimsTOF Pro
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-09-15 02:30:58ID requested
12026-06-19 12:20:05announced
Publication List
10.1016/J.BBAPAP.2025.141118;
Keyword List
submitter keyword: tetranitromethane
3-nitrotyrosine
di-tyrosine
crosslinks
fibril formation
Parkinson’s
neurodegeneration
Contact List
Per Hägglund
contact affiliationDepartment of Biomedical Sciences, University of Copenhagen, Denmark
contact emailhagglundperm@gmail.com
lab head
Luke Gamon
contact affiliationThe University of Copenhagen
contact emaillgamon@sund.ku.dk
dataset submitter
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Dataset FTP location
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