ArticleChemical science2017
Synthesis of rhamnosylated arginine glycopeptides and determination of the glycosidic linkage in bacterial elongation factor P.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 31 citations in OpenAlex.
- Constant trouble with prolines-navigating a global translation dilemma.Nucleic acids research · 2026Review
- Evidence of Gas Phase Glucosyl Transfer and Glycation in the CID/HCD-Spectra of S-Glucosylated Peptides.International journal of molecular sciences · 2024Article
- CRISPRi-Mediated Silencing ofJournal of proteome research · 2023Article
- Arginine ADP-Ribosylation: Chemical Synthesis of Post-Translationally Modified Ubiquitin Proteins.Journal of the American Chemical Society · 2022Article
- Convergent Palladium-Catalyzed Stereospecific Arginine Glycosylation Using Glycals.Organic letters · 2021Article
- A β-hairpin epitope as novel structural requirement for protein arginine rhamnosylation.Chemical science · 2020Article
- Bacteria-Catalyzed Arginine Glycosylation in Pathogens and Host.Frontiers in cellular and infection microbiology · 2020Review
- Complex Structure ofJournal of bacteriology · 2019Article
- The bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD).The Journal of biological chemistry · 2017Article
- Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.mBio · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
A new class of N-linked protein glycosylation - arginine rhamnosylation - has recently been discovered as a critical modification for the function of bacterial elongation factor P (EF-P). Herein, we describe the synthesis of suitably protected α- and β-rhamnosylated arginine amino acid "cassettes" that can be directly installed into rhamnosylated peptides. Preparation of a proteolytic fragment of
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Registered trials
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