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ProteomicsOptimized fragmentation improves the identification of peptides cross-linked using MS-cleavable reagents
Cross-linking mass spectrometry (XLMS) is becoming increasingly popular, and current advances are widening the applicability of the technique so that it can be utilized by non-specialist laboratories. Specifically, the use of novel mass spectrometry-cleavable (MS-cleavable) reagents dramatically red...
ORGANISM(S): Bos taurus (Bovine) Cicer arietinum (Chickpea) (Garbanzo) Streptococcus pyogenes serotype M2 Candida albicans (Yeast) Homo sapiens (Human) Oryctolagus cuniculus (Rabbit) Escherichia coli Equus caballus (Horse) 
2019-02-01 | PXD011861 | Pride
Xlms Cross-linking Cleavable cross-linking reagents Dsso Stepped-hcd 
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 
ProteomicsExploring Alternative Cysteine-reactive Chemistry for MS-cleavable Cross-linking Mass Spectrometry
To enable global PPI mapping, we have explored an alternative cysteine labeling chemistry, and thus designed and synthesized a sulfoxide-containing MS-cleavable haloacetamide-based cross-linker, DiBromoAcetamide SulfOxide (DBrASO). In combination with a newly developed SEC-HpHt fractionation method,...
ORGANISM(S): Homo sapiens (Human) 
2023-07-20 | PXD037443 | Pride
Cysteine Proteomics Cross-linking mass spectrometry 
ProteomicsDSSBU: novel cross-linker tested on bovine serum albumin and human hemoglobin
Protein cross-linking has assumed an irreplaceable role in structural proteomics. Recently, significant efforts have been made to develop novel MS-cleavable reagents. These cross-linkers enhance the reliability of cross-link identification. Presently, only water-insoluble MS-cleavable cross-linkers ...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2025-05-07 | PXD055284 | Pride
Dssbu Hemoglobin Xl-ms Ms-cleavable cross-linker Bsa 
UnknownEnabling Photoactivated Cross-Linking Mass Spectrometric Analysis of Protein Complexes by Novel MS-Cleavable Cross-Linkers.
Not available
S-EPMC8214149 | biostudies-literature
UnknownTrioxane-based MS-cleavable cross-linking mass spectrometry for profiling multimeric interactions of cellular networks.
Not available
S-EPMC12215968 | biostudies-literature
ProteomicsNHS Carbamate Cross-Linkers Provide Complementary XL-MS Restraints via Preferential N-Terminal Targeting
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 ms Cross-linking ms Dsso carbamate Nhs carbamate cross-linkers N-terminal reactivity Xl-ms Cross-linking mass spectrometry Ms-cleavable cross-linkers 
ProteomicsAn integrative structural biology approach to identify the binding mode of a nanobody towards the pea Ascorbate Peroxidase
The optimization of diagnostic devices such as biosensors often requires understanding the molecular details of the interaction between capture and target biomolecules. This can be experimentally obtained by cryo-electron microscopy, the preferred method for the analysis of large protein complexes, ...
ORGANISM(S): Populus nigra x Populus x canadensis 
2026-03-10 | PXD070481 | Pride
Nanobodies  ascorbate peroxidase  hydrogen-deuterium exchange coupled to mass spectrometry  integrative structural biology  protein cross-linking 
UnknownECL 3.0: a sensitive peptide identification tool for cross-linking mass spectrometry data analysis.
Not available
S-EPMC10510197 | biostudies-literature
UnknownDevelopment of a Novel Sulfoxide-Containing MS-Cleavable Homobifunctional Cysteine-Reactive Cross-Linker for Studying Protein-Protein Interactions.
Not available
S-EPMC6037416 | biostudies-literature
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