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ProteomicsIntact mass spectrometry analysis of covalent binding between purified recombinant human FGFR2 V564F protein and small-molecule compound LC-F2-1 incubated at a molar ratio of 1:2 or 1:5 at room temperature via Agilent 6230 time-of-flight LC/MS system for the characterization of their covalent binding products in protein-drug interaction studies
This dataset corresponds to an intact mass spectrometry study focusing on the covalent binding interaction between purified FGFR2 V564F protein and compound LC-F2-1. The purified FGFR2 V564F was adjusted to 28 μM, then incubated with LC-F2-1 at molar ratios of 1:2 or 1:5 for 4 hours at room temperat...
ORGANISM(S): Homo sapiens (Human) 
2026-09-14 | PXD073416 | Pride
Covalent binding Lc-ms Lc-f2-1 Fgfr2 v564f 
ProteomicsScreening for covalent SUMOylation and noncovalent SUMO interactions with SIM-binding groove SUMO mutants
Small ubiquitin-like modifier (SUMO) proteins affect protein function through both covalent modification of target proteins and noncovalent protein-protein interactions. The best characterized mode of SUMO interaction involves binding of a SUMO-interaction motif (SIM) to a conserved binding groove i...
ORGANISM(S): Homo sapiens (Human) 
2025-04-03 | PXD050651 | Pride
Sumo Protein interactions Sim 
ProteomicsProtein Targets of Acetaminophen Covalent Binding in Rat and Mouse Liver Studied by LC-MS/MS
Acetaminophen (N-acetyl-p-aminophenol; APAP) is a mild analgesic and antipyretic used commonly worldwide. Although APAP is considered a safe and effective over-the-counter medication, it is also the leading cause of drug-induced acute liver failure. Its hepatotoxicity has been linked to the covalent...
ORGANISM(S): Mus musculus (Mouse) Rattus norvegicus (Rat) 
2022-02-17 | PXD027674 | Pride
Covalent binding Reactive metabolite Napqi Acetaminophen Rat Liver Mouse 
TranscriptomicsQuantitative modeling of transcription factor binding specificities using DNA shape
Accurate predictions of the DNA binding specificities of transcription factors (TFs) are necessary for understanding gene regulatory mechanisms. Traditionally, predictive models are built based on nucleotide sequence features. Here, we employed three- dimensional DNA shape information obtained on a ...
ORGANISM(S): Homo sapiens 
2014-11-04 | E-GEOD-59845 | biostudies-arrayexpress
ProteomicsStructural and mechanistic analysis of covalent ligands targeting the RNA-binding protein NONO
RNA-binding proteins (RBPs) play important roles in mRNA transcription, processing, and translation. Chemical tools are lacking for RBPs, which has hindered efforts to perturb and understand RBP function in cells. We recently reported a chloroacetamide compound (R)-SKBG-1 that covalently binds the ...
ORGANISM(S): Homo sapiens (Human) 
2026-02-23 | PXD064685 | Pride
Proteomics Chemical biology Rbps Rna-binding protein 
OtherInsights into RNA biology from an atlas of mammalian mRNA-binding proteins.
Data from ProteomeXchange, PXD ID: PXD002880. Experiment: KS_A4_3, file: folder summary. Published as part of Cell. 2012 Jun 8;149(6):1393-406 . From the Abstract: {{i}} RNA-binding proteins (RBPs) determine RNA fate from synthesis to decay. Employing two complementary protocols for covalent UV cro...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM11210041750 | GPMDB
Resource Reanalysis 
ProteomicsCovalent allosteric inhibition of AARS1 lactyltransferase
Alanyl-tRNA synthetase 1 (AARS1) was recently identified as a lactyltransferase responsible for protein lactylation, a modification associated with epigenetic regulation and metabolic adaptation. AARS1 catalyzes lysine lactylation via an ATP- and lactate- dependent, but lactyl-CoA-independent mechan...
ORGANISM(S): Homo sapiens (Human) 
2026-07-29 | PXD076410 | Pride
Lactyltransferase Covalent ligand Aars1 
ProteomicsIdentification of the covalent binding site of Ibrutinib and 5Z-7-Oxozeaenol to ZAK
The goal of this experiment was to identify the reaction site of Ibrutinib and 5Z-7-Oxozeaenol to ZAK by determination of mass shifts according to a covalent modification by the inhibitors using mass spectrometry.
ORGANISM(S): Homo sapiens (Human) 
2017-10-13 | PXD007752 | Pride
Ibrutinib 5z-7-oxozeaenol Cys150 Recombinant zak Cys22 Covalent modification 
GenomicsEngineering covalent small molecule–RNA complexes in living cells
Engineering covalent small molecule–RNA complexes in living cells
PRJNA1133002 | ENA
GenomicsDevelopment of potent and selective KDM5 covalent inhibitors
Development of potent and selective KDM5 covalent inhibitors
PRJNA486160 | ENA
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