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Bacteria in the gut can modulate the availability and efficacy of therapeutic drugs. Interactions at this level have only recently started to being systematically mapped and the main underlying mechanism proposed is chemical transformation of drugs by microbes (biotransformation). Here, we invest...

2021-07-20 | MTBLS1792 | MetaboLights
We provide a cross-linking/MS workflow that can be applied to complex systems. The software tool MeroX 2.0 can be used to identify cross-linked peptide on a proteome-wide level. We applied the workflow to extracts of Drosophila embryos and identified 5,129 unique cross-linked residue pairs in biolog...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2019-07-09 | PXD012546 | Pride
Cross-linking of BSA with a novel cross-linker. Modification of the cross-linker containing peptides with CuAAC-chemistry to attach a cleavable biotin-derivative. Enrichment with streptavidin-beads.
ORGANISM(S): Bos taurus (Bovine) 
2019-10-14 | PXD015080 | Pride
Epitope mapping studies aim to identify the binding sites of antibody-antigen interactions to enhance the development of vaccines, diagnostics and immunotherapeutic compounds. However, mapping is a laborious process employing time- and resource-consuming M-bM-^@M-^Xwet benchM-bM-^@M-^Y techniques o...
ORGANISM(S): Peromyscus leucopus 
We used a reciprocal cross of Mus musculus and M. domesticus in which F1 males are sterile in one direction and fertile in the other direction, in order to associate expression differences with sterility. Four different crosses were performed. A cross between two strains within each mouse species (M...
ORGANISM(S): Mus musculus musculus x M. m. domesticus 
RNA-protein interactions mediate a vast number of intracellular processes. CLIR-MS (cross-linking of isotope labeled RNA and tandem mass spectrometry) is a mass spectrometric technique that allows the identification of RNA-protein interaction sites at single nucleotide/amino acid resolution in a sin...
ORGANISM(S): Homo sapiens (Human) 
2021-11-04 | PXD024010 | Pride
Using a structural proteomics approach via chemical cross-linking combined with mass spectrometry (XL-MS), we have resolved SCFTIR auxin·AUX/IAA complex overall topology, and established the power of IDRs modulating auxin receptor assemblies.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-05-11 | PXD015285 | Pride
In solution crosslinking mass spectrometry of transcription factors in complex with nucleosomes
ORGANISM(S): Homo sapiens (Human) 
2023-05-23 | PXD033181 | Pride
In this study, the native Sinapis alba plastid-encoded RNA polymerase (PEP) complex was purified and cross-linking MS was used to help in its structure determination.
ORGANISM(S): Sinapis alba 
2024-03-01 | PXD045575 | Pride
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