Sort   by:  
 Page size 
ProteomicsA Collision-induced Dissociation Cleavable Isobaric Tag for Peptide Fragment Ion-based Quantification in Proteomics
Fragment ion-based proteome quantification methods quantify peptides based on unique peptide fragment ions avoiding the issue of ratio distortion that is commonly observed for reporter ion-based quantification approaches. Herein, we present a novel approach that relies on a collision-induced dissoci...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-08-17 | PXD018790 | Pride
Isotopic labelling Proteomics Cid cleavable tag Fragment ion-based quantification Isobaric labelling 
ProteomicsEvaluation and Optimization of Chemically-Cleavable Linkers for Quantitative Mapping of Small Molecule-Protein Interactomes
Numerous reagents have been developed to enable chemical proteomic analysis of small molecule-protein interactomes. However, the performance of these reagents has not been systematically evaluated and compared. Herein, we report our efforts to conduct a parallel assessment of two widely-used chemica...
ORGANISM(S): Homo sapiens (Human) 
2019-08-21 | PXD014066 | Pride
Azobenzene Dacomitinib Tmt Cleavable biotin linker Dialkoxydiphenylsilane 
ProteomicsEnabling Photoactivated Cross-linking Mass Spectrometric Analysis of Protein Complexes by Novel MS-cleavable Cross-linkers
Cross-linking mass spectrometry (XL-MS) is a powerful tool for studying protein-protein interactions and elucidating architectures of protein complexes. While residue-specific XL-MS studies have been very successful, accessibility of interaction regions non-targetable by specific chemistries remain ...
ORGANISM(S): Bos taurus (Bovine) Saccharomyces cerevisiae (Baker's yeast) 
2021-05-07 | PXD022690 | Pride
26s proteasome Photocross-linking Sdaso Bsa 
ProteomicsTrioxane-based MS-cleavable Cross-linking Mass Spectrometry for Profiling Multimeric Interactions of Cellular Networks
Here, we present a novel trioxane-based MS-cleavable homotrifunctional cross-linker TSTO, which can target three proximal lysine residues simultaneously. Owing to its unique structure and MS-cleavability, TSTO enables fast and unambiguous identification of cross-linked peptides using LC-MSn analysis...
ORGANISM(S): Homo sapiens (Human) 
2025-05-30 | PXD054551 | Pride
Tsto Xl-ms Cross-linking mass spectrometry 
ProteomicsTrioxane-based MS-cleavable Cross-linking Mass Spectrometry for Profiling Multimeric Interactions of Cellular Networks
Here, we present a novel trioxane-based MS-cleavable homotrifunctional cross-linker TSTO, which can target three proximal lysine residues simultaneously. Owing to its unique structure and MS-cleavability, TSTO enables fast and unambiguous identification of cross-linked peptides using LC-MSn analysis...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-30 | PXD063825 | Pride
Tsto Xl-ms Lc-msn 
ProteomicsDeveloping In Vivo Cross-linking Mass Spectrometry (XL-MS) to Decipher Protein Interaction Landscapes at the Proteome Scale
We have developed a new and robust in vivo cross-linking mass spectrometry (XL-MS) that utilizes a multifunctional MS-cleavable cross-linker to enable the efficient capture, enrichment, and identification of in vivo cross-linked peptides at the whole proteome scale.
ORGANISM(S): Homo sapiens (Human) 
2021-07-30 | PXD012788 | Pride
Human Lc-ms Cross-linking mass spec Ms-cleavable Click chemistry Enrichable Proteome wide 
ProteomicsLens Disulfide crosslink - Evidence of highly conserved β-crystallin disulfidome that can be mimicked by in vitro oxidation in age-related human cataract and glutathione depleted LEGSKO mouse lens
Low glutathione levels are associated with crystallin oxidation in age-related nuclear cataract (ARNC). To understand the role of cysteine residue oxidation, we used the novel approach of comparing human cataracts with glutathione-depleted LEGSKO mouse lenses for intra- vs. intermolecular disulfide ...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2015-10-16 | PXD002658 | Pride
Cataract Lens Disulfide bond 
ProteomicsIntegrative Structural Characterization of the Human Canonical and Non-canonical Cop9 Signalosome Complexes
The COP9 signalosome (CSN) is an evolutionarily conserved protein complex that functions as a deneddylase to inactivate Cullin-RING E3 ligases for controlling protein ubiquitination. CSN possesses structural flexibility that is important for its activation upon binding to a diverse array of CRLs. Th...
ORGANISM(S): Homo sapiens (Human) 
2020-02-04 | PXD014673 | Pride
Mass spectrometry Sulfoxided based cross-linkers Cross-linking Intergrative modeling platform (imp) Ms-cleavable Cop9 signalosme 
Sort   by:  
 Page size