Sort   by:  
 Page size 
ProteomicsA synthetic crosslinked peptide library for benchmarking crosslinking mass spectrometry search engines
We have created a synthetic crosslinked peptide library to benchmark crosslinking mass spectrometry search engines. The unique benefit of the library is knowing which identified crosslinks are true and which are false. The data collected from mass spectrometry measurements of the peptide library wer...
ORGANISM(S): Streptococcus pyogenes ABC020006030 
2020-07-28 | PXD014337 | Pride
Crosslinking mass spectrometry peptide library 
ProteomicsMapping protein-DNA interactions by UV femtosecond laser crosslinking and mass spectrometry analysis
Transcription factors (TFs) regulate target genes by specific interaction with DNA sequences. Detecting and understanding these interactions on molecular level is of fundamental interest in both biological and clinical context. Crosslinking mass spectrometry is a powerful tool to assist structure pr...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) Sus scrofa domesticus (domestic pig) 
2020-06-22 | PXD014898 | Pride
Femtosecond laser Uv Transcription factor Protein-dna crosslinking Mass spectrometry 
ProteomicsIn Situ Structural Restraints from Crosslinking Mass Spectrometry in Human Mitochondria
The field of structural biology is increasingly focusing on studying proteins in situ, i.e. in a larger biological context. Crosslinking mass spectrometry is contributing to this effort, typically through the use of MS-cleavable crosslinkers. Here, we apply the popular non-cleavable crosslinker disu...
ORGANISM(S): Homo sapiens (Human) 
2019-12-03 | PXD014675 | Pride
Crosslinking mass spectrometry Human mitochondria In situ large-scale structural biology Non-cleavable dss crosslinker Comparative modelling 
UnknownEvaluation of Cleavable Crosslinking for Characterization of Proteoform Structural Differences by Top-Down Mass Spectrometry.
Not available
S-EPMC12798706 | biostudies-literature
ProteomicsQuantitative photo-crosslinking mass spectrometry reveals protein structure response to environmental changes
Conformational changes of protein structures depend on their chemical and physical environment. Studying conformational changes depending on environmental parameters is notoriously difficult as many methods of structural biology are affected by parameters like temperature or pH. To make such conform...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2019-07-01 | PXD012939 | Pride
Data-independent acquisition Structural dynamics Human serum albumin Dia-qclms Quantitation Xi Cytochrome c Spectronaut Label-free Mass spectrometry Photo-crosslinking Cross-linking Sda 
ProteomicsHistone interaction landscapes visualized by crosslinking mass spectrometry in intact cell nuclei
Cells organize their actions partly through tightly controlled protein-protein interactions – collectively termed the interactome. Here we use crosslinking mass spectrometry (XL-MS) to chart the interactome of intact human nuclei. We overall identified ~8700 crosslinks, of which 2/3 represent links ...
ORGANISM(S): Homo sapiens (Human) 
2018-07-23 | PXD007513 | Pride
Crosslinking mass spectrometry Histone interaction network – ptm interplay Nuclear interactome Histone variant specific interactions Nuclear protein-protein interactions 
ProteomicsCrosslinking mass spectrometry analysis of 𝛾TuRC complex
The 𝛾-tubulin ring complex (𝛾TuRC) is the major microtubule nucleator in cells. The mechanism of its regulation is not understood. To understand the molecular basis of microtubule nucleation, we investigate the structure of 𝛾TuRC using crosslinking mass spectrometry.
ORGANISM(S): Homo sapiens (Human) 
2021-01-27 | PXD018106 | Pride
Integrative structural analysis Crosslinking mass spectrometry 𝛾turc complex 
UnknownHistone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
Not available
S-EPMC6166682 | biostudies-literature
ProteomicsMapping the Toxoplasma gondii cytosolic interactome by crosslinking mass spectrometry and machine learning
Protein–protein interactions (PPIs) are fundamental to cellular processes and pathogen biology, yet remain undercharacterized in the human parasite Toxoplasma gondii. Here, we apply crosslinking mass spectrometry (XL-MS) to map the cytosolic interactome of T. gondii tachyzoites at proteome scale. Us...
ORGANISM(S): Toxoplasma gondii type I 
2025-07-26 | PXD062479 | Pride
Machine learning Cytosol Protein–protein interactions Dense granule proteins Crosslinking mass spectrometry Interactome Dsbso Host-pathogen interactions Structural mapping Toxoplasma gondii Lightgbm Parasite proteomics Ribosome Proteasome 
ProteomicsEvaluation of cleavable crosslinking for characterization of proteoform structural differences by top-down mass spectrometry
Cleavable crosslinking has traditionally been employed in bottom-up mass spectrometry to elucidate protein structure and protein-protein interactions through identification of peptides bearing characteristic mass adducts. Here, we demonstrate the application of cleavable crosslinking in top-down mas...
ORGANISM(S): Homo Sapiens (human) Equus Caballus 
2026-01-17 | PXD073175 | JPOST Repository
Sort   by:  
 Page size