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Cross-linking mass spectrometry (XL-MS) has become a valuable tool for investigating the structural morphology and plasticity of proteins. Traditional cross-linkers contain two N-hydroxy succinimide (NHS) esters that mainly react with lysine residues. In this work, we optimized the in-solution react...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2026-03-30 | PXD069252 | Pride
Crosslinking mass spectrometry (XL-MS) is emerging as a unique method at the crossroads of structural and cellular biology, uniquely capable of identifying protein-protein interactions with residue-level resolution and on the proteome-wide scale. With the development of crosslinkers that can form li...
ORGANISM(S): Escherichia coli 
2023-12-07 | PXD036884 | Pride
Crosslinking mass spectrometry (XL-MS) is emerging as a method at the crossroads of structural and cellular biology, uniquely capable of identifying protein-protein interactions with residue-level resolution and on the proteome-wide scale. With the development of crosslinkers that can form linkages ...
ORGANISM(S): Escherichia coli 
2023-06-27 | PXD041148 | Pride
The diazirine photoreactive group has been widely used for photo-labeling and photo-cross-linking (PXL) of proteins. Yet, due to the mechanistic complexity of diazirine photo-reaction, site-specific and quantitative analysis of protein PXL data remains challenging. Herein, we have built an in-line p...
ORGANISM(S): Bos taurus (Bovine) 
2024-06-22 | PXD048452 | Pride
We used a state of the art proteomics workflow, based upon nano-UPLC-MS\MS and advanced database searching to identify oxidative modifications to functional residues of hemoglobin subunit beta . Progressive accumulation of oxidized residues in stored erythrocytes and selective removal in vesicles wa...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-10-04 | MSV000080222 | MassIVE
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