ArticleAngewandte Chemie (International ed. in English)2020
NMR Spectroscopic Characterization of the C-Mannose Conformation in a Thrombospondin Repeat Using a Selective Labeling Approach.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
10 citing papers in PubMed.
- Is AMOEBA a Good Force Field for Molecular Dynamics Simulations of Carbohydrates?Journal of chemical information and modeling · 2025Review
- A rare peptide scaffold in kineomicins, the glycopeptide antibiotics produced by Actinokineospora auranticolor DSM 44650.Communications chemistry · 2025Article
- Refinement of the Drude Polarizable Force Field for Hexose Monosaccharides: Capturing Ring Conformational Dynamics with Enhanced Accuracy.Journal of chemical theory and computation · 2024Article
- Review
- A unified strategy for the synthesis of aldohexoses by boronate assisted assembly of CHChemical science · 2023Article
- Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase.Nature chemical biology · 2023Article
- Primary Structure of Glycans by NMR Spectroscopy.Chemical reviews · 2023Review
- ProteinMolecules (Basel, Switzerland) · 2021Review
- Yeast- and antibody-based tools for studying tryptophan C-mannosylation.Nature chemical biology · 2021Article
- NMR Spectroscopic Characterization of the C-Mannose Conformation in a Thrombospondin Repeat Using a Selective Labeling Approach.Angewandte Chemie (International ed. in English) · 2020Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR-active nuclei. We report on the incorporation of
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.