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ProteomicsImproved peptide backbone fragmentation is the primary advantage of MS-cleavable crosslinkers
Proteome-wide crosslinking mass spectrometry studies have coincided with the advent of MS-cleavable crosslinkers that can reveal the individual masses of the two crosslinked peptides. However, recently such studies have also been published with non-cleavable crosslinkers suggesting that MS-cleavabil...
ORGANISM(S): Mus musculus (Mouse) Escherichia coli Drosophila melanogaster (Fruit fly) 
2022-06-24 | PXD032821 | Pride
Lc-msms Dsbu Ms-cleavable crosslinker Dsso Crosslinking Clms 
ProteomicsIdentification of MS-Cleavable and Non-Cleavable Chemically Crosslinked Peptides with MetaMorpheus
The present work describes a novel search program for the detection of both MS-cleavable and non-cleavable crosslinked peptides and it is the first software program reported with both capacities. The search strategy has been implemented in the computer program MetaMorpheus, which has a user-friendly...
ORGANISM(S): Escherichia coli 
2018-07-16 | PXD009000 | Pride
Proteomics Ms-cleavable chemical crosslink Protein-protein interactions Ion index 
UnknownImproved Peptide Backbone Fragmentation Is the Primary Advantage of MS-Cleavable Crosslinkers.
Not available
S-EPMC9178559 | biostudies-literature
ProteomicsLight-induced orthogonal fragmentation of crosslinked peptides
Crosslinking mass spectrometry provides pivotal information on the structure and interaction of proteins. MS-cleavable crosslinkers are regarded as a cornerstone for the analysis of complex mixtures. Yet they fragment under similar conditions as peptides, leading to mixed fragmentation spectra of th...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2023-08-28 | PXD040267 | Pride
Clms Cleavable crosslinker Crosslinking Uvpd 
ProteomicsImproving identification of in-organello protein-protein interactions using an affinity-enrichable, isotopically-coded, and mass spectrometry-cleavable chemical crosslinker
An experimental and computational approach for identification of protein-protein interactions by in-vivo chemical crosslinking and mass spectrometry (CLMS) has been developed that takes advantage of the specific characteristics of cyanurbiotindipropionylsuccinimide (CBDPS), an affinity-tagged isotop...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-03-17 | PXD017066 | Pride
Cross-linking Yeast Mitochondria 
ProteomicsImproving identification of in-organello protein-protein interactions using an affinity-enrichable, isotopically-coded, and mass spectrometry-cleavable chemical crosslinker
An experimental and computational approach for identification of protein-protein interactions by in-vivo chemical crosslinking and mass spectrometry (CLMS) has been developed that takes advantage of the specific characteristics of cyanurbiotindipropionylsuccinimide (CBDPS), an affinity-tagged isotop...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-03-17 | PXD014055 | Pride
Cross-linking Yeast Mitochondria 
UnknownDeveloping a new cleavable crosslinker reagent for in-cell crosslinking.
Not available
S-EPMC12185727 | biostudies-literature
ProteomicsDeciphering the interaction between TopBP1 and GINS using crosslinking mass spectrometry
Recombinant TopBP1 and GINS were cross linked using the MS non-cleavable crosslinker BS3. Crosslinked proteins were then subsequently either digested directly using the SP3 strategy or first seperated on SDS-PAGE and then in-gel digested. cross-linked peptides were identified by LC-MS. The informati...
ORGANISM(S): Homo sapiens (Human) 
2024-05-24 | PXD040156 | Pride
Cross linking Gins Topbp1 Bs3 
UnknownAll-in-One Pseudo-MS3 Method for the Analysis of Gas-Phase Cleavable Protein Crosslinking Reactions.
Not available
S-EPMC11250984 | biostudies-literature
ProteomicsProteome-wide non-cleavable crosslink identification with MS Annika 3.0 reveals the structure of the C. elegans Box C/D complex
The field of crosslinking mass spectrometry has seen substantial advancements over the past decades, enabling the structural analysis of proteins and protein-complexes and serving as a powerful tool in protein-protein interaction studies. However, data analysis of large non-cleavable crosslink studi...
ORGANISM(S): Caenorhabditis elegans 
2024-12-19 | PXD055488 | Pride
Non-cleavable C. elegans Crosslinker Dsg Crosslink Crosslinking 
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