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UnknownMaXLinker: Proteome-wide Cross-link Identifications with High Specificity and Sensitivity.
Not available
S-EPMC7050104 | biostudies-literature
ProteomicsRetention time as an extra dimension for proteome-wide cross-link identification
Chemical crosslinking methods have not been successfully applied to protein-protein interaction discovery mainly due to the computation complexity (O (n2)) issue. In a previous report, we proposed a decision tree searching strategy which can reduce complexity by orders of magnitude. In this study, w...
ORGANISM(S): Bos taurus (Bovine) Escherichia coli 
2021-07-29 | PXD024253 | Pride
Xl-ms Chemical crosslinking Proteome-wide cross-link identification Retention time 
UnknownOptimized fragmentation schemes and data analysis strategies for proteome-wide cross-link identification.
Not available
S-EPMC5454533 | biostudies-literature
UnknownTwo-Dimensional Fractionation Method for Proteome-Wide Cross-Linking Mass Spectrometry Analysis.
Not available
S-EPMC9056026 | biostudies-literature
ProteomicsRetention time as an extra dimension for proteome-wide cross-link identification
Chemical crosslinking methods have not been successfully applied to protein-protein interaction discovery mainly due to the computation complexity (O (n2)) issue. In a previous report, we proposed a decision tree searching strategy which can reduce complexity by orders of magnitude. In this study, w...
ORGANISM(S): Escherichia Coli 
2021-08-06 | PXD027831 |
ProteomicsA simplified in vivo cross-linking mass spectrometry strategy for proteome-wide studies.
Chemical cross-linking (XL) coupled to mass spectrometry (MS) has become a powerful approach to probe the structure of protein assemblies. Although most of the applications concerned purified complexes, latest developments focus on large-scale in vivo studies. Pushing in this direction, we describe ...
ORGANISM(S): Neisseria meningitidis Bacteria 
2021-02-25 | PXD021553 | Pride
Click-chemistry Mass spectrometry Structural biology In vivo biochemistry Cross-linking 
UnknownIdentification of MS-Cleavable and Noncleavable Chemically Cross-Linked Peptides with MetaMorpheus.
Not available
S-EPMC6501566 | biostudies-literature
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 
ProteomicsAn Optimized Miniaturized Filter Aided Sample Preparation Method for Sensitive Cross-linking Mass Spectrometry Analysis of Microscale Samples
Cross-linking mass spectrometry (XL-MS) is a powerful tool for elucidating protein structures and protein-protein interactions (PPIs) at the global scale. However, sensitive XL-MS analysis of mass-limited samples remains challenging, due to serious sample loss during sample preparation of the low-ab...
ORGANISM(S): Homo sapiens (Human) 
2025-01-03 | PXD051322 | Pride
Cross-linking mass spectrometry Microscale samples 
UnknownRedesigning error control in cross-linking mass spectrometry enables more robust and sensitive protein-protein interaction studies.
Not available
S-EPMC11696718 | biostudies-literature
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