ArticleAngewandte Chemie (International ed. in English)2018
Chemoproteomic Profiling of Phosphoaspartate Modifications in Prokaryotes.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Direct energy consumption by inhibitory GABAFrontiers in neuroscience · 2026Article
- Molecular Characterization of the Group A Streptococcus Virulence-Regulatory System FasBCAX.Molecular microbiology · 2025Article
- Single-cell chemoproteomics identifies metastatic activity signatures in breast cancer.Science advances · 2024Article
- Review
- Functionalizing tandem mass tags for streamlining click-based quantitative chemoproteomics.Communications chemistry · 2024Article
- Monitoring host-pathogen interactions using chemical proteomics.RSC chemical biology · 2024Review
- Activity-based protein profiling in microbes and the gut microbiome.Current opinion in chemical biology · 2023Review
- Chemical biology tools for protein labelling: insights into cell-cell communication.The Biochemical journal · 2023Review
- Profiling of the Klebsiella pneumoniae Phosphoproteome under Iron-Limited and Iron-Replete Conditions.Microbiology resource announcements · 2023Article
- Chemoproteomic Approaches for Unraveling Prokaryotic Biology.Israel journal of chemistry · 2023Article
- Discovery of Potent and Selective Inhibitors against Protein-Derived Electrophilic Cofactors.Journal of the American Chemical Society · 2022Article
- A tailored phosphoaspartate probe unravels CprR as a response regulator inChemical science · 2021Article
- Ultrasensitive, multiplexed chemoproteomic profiling with soluble activity-dependent proximity ligation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation at aspartic acid residues represents an abundant and critical post-translational modification (PTM) in prokaryotes. In contrast to most characterized PTMs, such as phosphorylation at serine or threonine, the phosphoaspartate moiety is intrinsically labile, and therefore incompatible with common proteomic profiling methods. Herein, we report a nucleophilic, desthiobiotin-containing hydroxylamine (DBHA) chemical probe that covalently labels modified aspartic acid residues in native proteomes. DBHA treatment coupled with LC-MS/MS analysis enabled detection of known phosphoaspartate modifications, as well as novel aspartic acid sites in the E. coli proteome. Coupled with isotopic labelling, DBHA-dependent proteomic profiling also permitted global quantification of changes in endogenous protein modification status, as demonstrated with the detection of increased E. coli OmpR phosphorylation, but not abundance, in response to changes in osmolarity.
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