ArticleThe Journal of biological chemistry2013
Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 48 citations in OpenAlex.
- Revealing the Structure of Sheer N-Acetylglucosamine, an Essential Chemical Scaffold in Glycobiology.The journal of physical chemistry letters · 2024Article
- Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Divergent Enzymatic Assembly of a Comprehensive 64-Membered IgG N-Glycan Library for Functional Glycomics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- Innovative Metrics for Reporting and Comparing the Glycan Structural Profile in Biotherapeutics.Molecules (Basel, Switzerland) · 2023Article
- A Data Set of Ion Mobility Collision Cross Sections and Liquid Chromatography Retention Times from 71 Pyridylaminated N-Linked Oligosaccharides.Journal of the American Society for Mass Spectrometry · 2022Article
- Profiling the Bisecting N-acetylglucosamine Modification in Amniotic Membrane via Mass Spectrometry.Genomics, proteomics & bioinformatics · 2022Article
- Systematic synthesis of bisectedChemical science · 2022Article
- The aryl hydrocarbon receptor instructs the immunomodulatory profile of a subset of Clec4a4Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Resources and Methods for Engineering "Designer" Glycan-Binding Proteins.Molecules (Basel, Switzerland) · 2021Review
- Simplifying Glycan Profiling through a High-Throughput Micropermethylation Strategy.SLAS technology · 2020Article
- Structural insight into the recognition of pathogen-derived phosphoglycolipids by C-type lectin receptor DCAR.The Journal of biological chemistry · 2020Article
- The Essential Functions and Detection of Bisecting GlcNAc in Cell Biology.Frontiers in chemistry · 2020Review
- N-glycome inheritance from cells to extracellular vesicles in B16 melanomas.FEBS letters · 2019Article
- Chemoenzymatic synthesis of glycopeptides bearing rare N-glycan sequences with or without bisecting GlcNAc.Chemical science · 2018Article
- Structures of N-Glycans ofMolecular & cellular proteomics : MCP · 2018Article
- Targeting DEC-205Molecular medicine (Cambridge, Mass.) · 2018Article
- The glycomic effect of N-acetylglucosaminyltransferase III overexpression in metastatic melanoma cells. GnT-III modifies highly branched N-glycans.Glycoconjugate journal · 2018Article
- Mechanism of pathogen recognition by human dectin-2.The Journal of biological chemistry · 2017Article
- Binding Sites for Acylated Trehalose Analogs of Glycolipid Ligands on an Extended Carbohydrate Recognition Domain of the Macrophage Receptor Mincle.The Journal of biological chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dendritic cell inhibitory receptor 2 (DCIR2) is a C-type lectin expressed on classical dendritic cells. We recently identified the unique ligand specificity of mouse DCIR2 (mDCIR2) toward biantennary complex-type glycans containing bisecting N-acetylglucosamine (GlcNAc). Here, we report the crystal structures of the mDCIR2 carbohydrate recognition domain in unliganded form as well as in complex with an agalactosylated complex-type N-glycan unit carrying a bisecting GlcNAc residue. Bisecting GlcNAc and the α1-3 branch of the biantennary oligosaccharide asymmetrically interact with canonical and non-canonical mDCIR2 residues. Ligand-protein interactions occur directly through mDCIR2-characteristic amino acid residues as well as via a calcium ion and water molecule. Our structural and biochemical data elucidate for the first time the unique binding mode of mDCIR2 for bisecting GlcNAc-containing glycans, a mode that contrasts sharply with that of other immune C-type lectin receptors such as DC-SIGN.
Indexed as
Identifiers
What OpenQuestion holds
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.