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ProteomicsAnalysis of protein-DNA interactions in chromatin by UV induced cross-linking and mass spectrometry
Protein–DNA interactions are key to the functionality and stability of the genome. Identification and mapping of protein–DNA interaction interfaces and sites is crucial for understanding DNA-dependent processes. Here, we present a workflow that allows mass spectrometric (MS) identification of protei...
ORGANISM(S): Homo sapiens (Human) Xenopus laevis (African clawed frog) 
2020-10-20 | PXD020290 | Pride
Mass spectrometry Protein-dna interactions Uv-cross-linking 
ProteomicsStructural requirements for photo-induced RNA-protein cross-linking
Cross-linking of isotope-labelled RNA coupled with mass spectrometry (CLIR-MS) was used to study the UV cross-linking behavior of in vitro reconstituted FOX1 RRM in complex with its cognate RNA sequence, the Fox binding element (FBE), (U)GCAUGU. The FBE heptanucleotide was subsequently mutated, and ...
ORGANISM(S): Homo sapiens (Human) 
2022-06-09 | PXD031381 | Pride
Uv cross-linking  mbnl1  fox1  ptbp1  sf3a1  u1  u2  cross-linking  xl-ms  structural proteomics  protein-rna  rna-protein  protein-rna complex  rna-protein complex  clir-ms 
ProteomicsStructural insights into protein-RNA interactions within biomolecular condensates using UV cross-linking and mass spectrometry
UV-light-induced protein-RNA cross-linking followed by MS analysis was used to identify the interaction sites between protein and RNA in different phase-separated and non-phase separated states of complexes involving the following proteins: PTBP1, FUS, and SARS-CoV-2 nucleocapsid protein.
ORGANISM(S): Homo sapiens (Human) Severe acute respiratory syndrome coronavirus 2 
2024-03-06 | PXD046267 | Pride
Protein-rna cross-linking Uv cross-linking Protein-rna complexes Biomolecular condensates Liquid-liquid phase separation 
ProteomicsSingle Nucleotide Resolution RNA-Protein Cross-Linking/MS: Simple Extension of the CLIR-MS Workflow
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
Protein rna cross-linking clir-ms uv xl 
ProteomicsCharacterizing the dynamic oligomerization of Hsp90β using photo-cross-linking
Cross-linking mass spectrometry (XL-MS) is a powerful tool for probing protein structures. While conventional chemical cross-linkers react with specific residues with defined chemistry, photo-cross-linkers, despite their superior reactivity, have been hindered by incomplete mechanistic understanding...
ORGANISM(S): Homo sapiens (Human) 
2026-04-09 | PXD072009 | Pride
Hsp90 Cleavable cross-linkers Diazirine Photo-cross-linking 
ProteomicsDon’t Waste Time – Ensure Success in Your Cross-Linking Mass Spectrometry Experiments Before You Begin.
Cross-linking mass spectrometry (XL-MS) is becoming a more popular tool for researchers to turn towards for studying proteins and their complexes of interest especially in complex samples such as lysates or whole-cells. Studying a targeted proteins in a complex mixture can be difficult as data on ot...
ORGANISM(S): Neisseria meningitidis serogroup C (strain 8013) Bacteria 
2024-02-07 | PXD045792 | Pride
Cross-linking Mass spectrometry Protein abundance Ibaq 
ProteomicsSensitive detection and structural characterisation of UV-induced cross-links in protein-ribonucleic acid complexes using stable isotope labelling and mass spectrometry
The recently introduced cross-linking of isotope-labelled RNA coupled with mass spectrometry (CLIR-MS) technique enables protein-RNA cross-links to be used as precisely localized distance restraints in de novo structural modelling, but little is known about the structural characteristics of UV-induc...
ORGANISM(S): Homo sapiens (Human) 
2023-09-06 | PXD029930 | Pride
Uv cross-linking  mbnl1  fox1  ptbp1  sf3a1  u1  u2  cross-linking  xl-ms  structural proteomics  protein-rna  rna-protein  protein-rna complex  rna-protein complex  clir-ms 
ProteomicsRNxQuest: an extension to the xQuest pipeline enabling analysis of protein-RNA cross-linking/mass spectrometry data
The recently introduced cross-linking of isotope-labelled RNA coupled with mass spectrometry (CLIR-MS) technique enables protein-RNA cross-links to be used as precisely localized distance restraints in de novo structural modelling. The novel data type requires a bespoke data analysis approach. The n...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2023-09-06 | PXD039754 | Pride
Uv cross-linking  mbnl1  fox1  ptbp1  bsa  cross-linking  xl-ms  structural proteomics  protein-rna  rna-protein  protein-rna complex  rna-protein complex  clir-ms 
ProteomicsEnabling Photoactivated Cross-linking Mass Spectrometric Analysis of Protein Complexes by Novel MS-cleavable Cross-linkers
Cross-linking mass spectrometry (XL-MS) is a powerful tool for studying protein-protein interactions and elucidating architectures of protein complexes. While residue-specific XL-MS studies have been very successful, accessibility of interaction regions non-targetable by specific chemistries remain ...
ORGANISM(S): Bos taurus (Bovine) Saccharomyces cerevisiae (Baker's yeast) 
2021-05-07 | PXD022690 | Pride
26s proteasome Photocross-linking Sdaso Bsa 
ProteomicsA complimentary benzophenone cross-linking/mass spectrometry photochemistry
We introduce a complimentary, heterobifunctional, photoactivatable, benzophenone containing cross-linker and show its successful application to cross-linking/mass spectrometry, by increasing data density, when used alongside a previously developed diazirine-based heterobifunctional cross-linker.
ORGANISM(S): Homo sapiens (Human) 
2017-04-26 | PXD004920 | Pride
Cross-linking/mass spectrometry  high-density data  complimentary chemistry  protein chemistry  human serum albumin 
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