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UnknownAn enhanced protein crosslink identification strategy using CID-cleavable chemical crosslinkers and LC/MS(n) analysis.
Not available
S-EPMC3426502 | biostudies-literature
UnknownCrosslink: An R Package for Network Visualization of Grouped Nodes.
Not available
S-EPMC8322777 | biostudies-literature
ProteomicsProteome-wide non-cleavable crosslink identification with MS Annika 3.0 reveals the structure of the C. elegans Box C/D complex
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): Caenorhabditis elegans 
2024-12-19 | PXD055488 | Pride
Non-cleavable C. elegans Crosslinker Dsg Crosslink Crosslinking 
UnknownHigh Sensitivity Crosslink Detection Coupled With Integrative Structure Modeling in the Mass Spec Studio.
Not available
S-EPMC5013318 | biostudies-literature
ProteomicsDual role of PCNA-monoubiquitination in facilitating Fanconi Anemia-mediated interstrand crosslink repair
The Fanconi Anemia (FA) repair pathway governs the repair of highly genotoxic DNA interstrand crosslinks (ICLs) with the assistance of translesion synthesis (TLS), that is facilitated by site-specific monoubiquitination of PCNA (PCNA-Ub) at lysine 164 (K164). Mutation at this residue (K164R) renders...
ORGANISM(S): Mus musculus (Mouse) 
2024-08-09 | PXD035337 | Pride
Lc-msms Rime Interstrand crosslink repair Mouse Dna damage tolerance Mismatch repair Fanconi anemia Pcna ubiquitination 
ProteomicsMetalloprotease SPRTN/DVC1 Orchestrates Replication-Coupled DNA-Protein Crosslink Removal
Cytotoxicity of DNA-protein crosslinks (DPCs) is ascribed largely to their ability to block the progression of DNA replication fork. DPCs are frequently occurring in cells, either as a consequence of metabolism or exogenous agents. The mechanism of DPCs removal is not completely understood. Here, we...
ORGANISM(S): Homo sapiens (Human) 
2016-10-06 | PXD004154 | Pride
Dna-protein crosslink 
ProteomicsANR DeepProt : A structural analysis of heated Ovalbumin by crosslink proteomics
In the present study, we mobilized the latest methodologies in tandem mass spectrometry and cross-link proteomics to decipher the heat-induced structural changes of OVA in the presence or absence of sugar. Our objective was to better understand how these structural changes could lead to a modulation...
ORGANISM(S): Gallus gallus (Chicken) 
2023-04-13 | PXD030366 | Pride
Glycation Ova Crosslink proteomics Aggregation 
ProteomicsThe ubiquitin-like modifier FAT10 interferes with SUMO activation
In this study, the proteins SumoE1 and Fat10 or Fat10-AV mutant were crosslinked using the crosslinking reagent H12/D12 BS3 in order to determine specific interaction sites of Fat10 and SumoE1. Furthermore, quantitative chemical crosslinking coupled to mass spectrometry (q-XL-MS) was used to compare...
ORGANISM(S): Homo sapiens (Human) 
2019-10-08 | PXD012592 | Pride
Fat10 Q-xl-ms Xl-ms Sumoe1 
UnknownA Dominant Mutation in Human RAD51 Reveals Its Function in DNA Interstrand Crosslink Repair Independent of Homologous Recombination.
Not available
S-EPMC4529964 | biostudies-literature
ProteomicsCooperation of the NEIL3 and Fanconi Anemia/BRCA Pathways in Interstrand Crosslink Repair
The NEIL3 DNA glycosylase is a base excision repair enzyme that excises bulky base lesions from DNA. Although NEIL3 has been shown to unhook interstrand crosslinks (ICL) in Xenopus extracts, how NEIL3 participants in ICL repair in human cells and its corporation with the canonical Fanconi anemia (FA...
ORGANISM(S): Homo sapiens (Human) 
2020-01-20 | PXD016256 | Pride
Neil3 Psoralen interstrand crosslink Fanconi anemia 
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