Sort   by:  
 Page size 
UnknownAccurate and Automated High-Coverage Identification of Chemically Cross-Linked Peptides with MaxLynx.
Not available
S-EPMC8792900 | biostudies-literature
ProteomicsOriginal TIMS-TOF pro BSA data sets for MaxLynx, a novel computational proteomics workflow for XL-MS integrated into the MaxQuant environment.
Cross-linking combined with mass spectrometry (XL-MS) provides a wealth of information about the 3D structure of proteins and their interactions. We introduce MaxLynx, a novel computational proteomics workflow for XL-MS integrated into the MaxQuant environment and here we have tested the performance...
ORGANISM(S): Bos taurus (Bovine) 
2022-01-11 | PXD027161 | Pride
Cross-linking 
ProteomicsReanalysis of publicly available medium size protein complex data set with MaxLynx
Reanalysis of the publicly available medium size protein complex data set by Kokic and co-workers, Nat Commun. 2019 (PXD013947)
ORGANISM(S): Homo sapiens (Human) 
2022-01-11 | PXD030578 | Pride
Maxquant Cross-linking Maxlynx 
ProteomicsReanalysis of a proteome-wide level study with MaxLynx
Reanalysis of the publicly available proteome-wide level dataset with DSBU from Goetze et al., Anal Chem. 2019 (PXD012546).
ORGANISM(S): Homo sapiens (Human) 
2022-01-11 | PXD027188 | Pride
Maxquant Cross-linking Maxlynx 
ProteomicsReanalysis of a synthetic cross-linked peptide library with MaxLynx
Reanalysis of a synthetic crosslinked peptide library datasets with DSS (non-cleavable), DSSO and DSBU (MS-cleavable) cross linkers from Beveridge et al., Nat. Commun., 2020 (PXD014337)
ORGANISM(S): Streptococcus pyogenes ABC020006030 
2022-01-11 | PXD027159 | Pride
Crosslinking 
ProteomicsAE-MS to profile SLO-human plasma protein interactome landscape; HDX-MS and XL-MS to study protein interaction and dynamics of PLG-SLO
Group A Streptococcus is known to exploit the human fibrinolysis system, particularly by targeting the plasminogen/plasmin pathway through redundant pathomechanisms. In this study, we began with affinity-enrichment mass spectrometry to map the interaction landscape between streptolysin O and human p...
ORGANISM(S): Homo sapiens (Human) Streptococcus pyogenes MGAS315 
2024-10-17 | PXD051261 | Pride
Ae-ms Human Streptolysin o Streptococcus pyogenes Xl-ms Hdx-ms Plasminogen Lc-ms/ms 
ProteomicsComparison of MS Annika 3.0 against other crosslink search engines
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): Streptoccous pyogenes Escherichia coli 
2024-12-19 | PXD055512 | Pride
Non-cleavable Dss Adh Crosslinker Crosslinking 
ProteomicsMimicked synthetic ribosomal protein complex for benchmarking cross-linking mass spectrometry workflows
The field of cross-linking mass spectrometry has matured to a frequently used tool for the investiga-tion of protein structures as well as interactome studies up to a system wide level. The growing com-munity generated a broad spectrum of applications, linker types, acquisition strategies and specia...
ORGANISM(S): Escherichia coli 
2022-05-24 | PXD029252 | Pride
Mass spectrometry Ribosome Fdr Crosslinking 
ProteomicsEpitope and paratope mapping of a SUMO-remnant antibody using cross-linking mass spectrometry and molecular docking
The small ubiquitin-like modifier (SUMO) is an important post-translational modification that regulates the function of various proteins essential for DNA damage repair, genome integrity and cell homeostasis. To identify protein SUMOylation effectively, an enrichment step is necessary, often require...
ORGANISM(S): Oryctolagus cuniculus (Rabbit) 
2025-02-19 | PXD055077 | Pride
Antibody Cross-linking Mass spectrometry Molecular docking Paratope mapping Sumo 
ProteomicsEpitope and paratope mapping of a SUMO-remnant antibody using cross-linking mass spectrometry and molecular docking
The small ubiquitin-like modifier (SUMO) is an important post-translational modification that regulates the function of various proteins essential for DNA damage repair, genome integrity and cell homeostasis. To identify protein SUMOylation effectively, an enrichment step is necessary, often require...
ORGANISM(S): Oryctolagus sp. 'Rabbit_OD' 
2025-02-19 | PXD055085 | Pride
Antibody Cross-linking Mass spectrometry Molecular docking Paratope mapping Sumo 
Sort   by:  
 Page size