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ProteomicsUtilising crosslinking MS to explore protein structure and interactions
In this study, we performed proteome-wide crosslinking mass spectrometry (XLMS) on human HEK293 intact organelles and examined the combined utility of these crosslinks with AlphaFold.
ORGANISM(S): Homo sapiens (Human) 
2023-04-24 | PXD035844 | Pride
Xlms Crosslinking ms Alphafold Crosslinking 
ProteomicsCross-linking mass spectrometry uncovers interactions between high-density lipoproteins and the SARS-CoV-2 spike glycoprotein
Multiple studies to date have shown that high-density lipoprotein (HDL) levels are reduced in patients with coronavirus disease 2019 (COVID-19), and that the extent of this reduction is associated with poor clinical outcomes. While lipoproteins are known to play a key role during the lifecycle of he...
ORGANISM(S): Homo sapiens (Human) 
2023-07-20 | PXD042625 | Pride
Hdl Spike Xlms. cov 
UnknownCross-linking mass spectrometry reveals structural insights of the glutamine synthetase from Leishmania braziliensis.
Not available
S-EPMC8752055 | biostudies-literature
ProteomicsCross-linking mass spectrometry uncovers interactions between high-density lipoproteins and the SARS-CoV-2 spike glycoprotein
Multiple studies to date have shown that high-density lipoprotein (HDL) levels are reduced in patients with coronavirus disease 2019 (COVID-19), and that the extent of this reduction is associated with poor clinical outcomes. While lipoproteins are known to play a key role during the lifecycle of he...
ORGANISM(S): Homo sapiens (Human) 
2023-07-20 | PXD036640 | Pride
Xlms Covid Spike Sars-cov-2 Hdl 
ProteomicsCharacterizing protein conformers by cross-linking mass spectrometry and pattern recognition
Motivation: Chemical cross-linking coupled to mass spectrometry (XLMS) emerged as a powerful technique for studying protein structures and large-scale protein-protein interactions. Nonetheless, XLMS lacks software tailored toward dealing with multiple conformers; this scenario can lead to high-quali...
ORGANISM(S): Homo sapiens (Human) 
2025-01-03 | PXD022443 | Pride
Hsp90 Cross-link Quantification 
UnknownCombination of deep XLMS with deep learning reveals an ordered rearrangement and assembly of a major protein component of the vaccinia virion.
Not available
S-EPMC10653903 | biostudies-literature
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 
ProteomicsComprehensive identification of crosslinked peptides from methyltransferase Hmt1 and its substrate Npl3: use of multiple crosslinkers, mass spectrometry approaches and software platforms
Chemical-Crosslinking Mass Spectrometry (XLMS) using MS-cleavable crosslinkers is fast becoming an established technique in the study of protein-protein interactions for both small and large scale samples. With the increased uptake of XLMS as a technique, different combinations of crosslinker types,...
ORGANISM(S): Escherichia coli Saccharomyces cerevisiae (Baker's yeast) 
2018-07-20 | PXD008348 | Pride
Crosslinking-mass spectrometry Ms-cleavable linkers 
UnknownMembrane Interactions of α-Synuclein Revealed by Multiscale Molecular Dynamics Simulations, Markov State Models, and NMR.
Not available
S-EPMC8006134 | biostudies-literature
ProteomicsCrosslinking/mass spectrometry analysis of Human Separase-Scc1-fusion and cohesin SMC1/SMC3 complexes
In this study, we employed the photoactivatable crosslinker (sulfo-SDA) to investigate protein-protein interaction between human Separase-Scc1 fusion protein and SMC1/SMC3 cohesin subunits complex in the presence of DNA.
ORGANISM(S): Homo sapiens (Human) 
2025-08-28 | PXD061667 | Pride
Sulfo-sda Smc1 Smc3 Scc1 Separase Xlms 
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