ArticleACS chemical biology2012
Deciphering structural elements of mucin glycoprotein recognition.
Article in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 58 citations in OpenAlex.
- Divergent synthesis of amino acid-linked O-GalNAc glycan core structures.Nature protocols · 2025Review
- Serum antibody screening using glycan arrays.Chemical Society reviews · 2024Review
- Identification of the glycopeptide epitope recognized by a protectiveInfection and immunity · 2023Article
- Targeting altered glycosylation in secreted tumor glycoproteins for broad cancer detection.Glycobiology · 2023Article
- Review
- MUC1 Glycopeptide Vaccine Modified with a GalNAc Glycocluster Targets the Macrophage Galactose C-type Lectin on Dendritic Cells to Elicit an Improved Humoral Response.Journal of the American Chemical Society · 2023Article
- Synthesis and biomedical applications of mucin mimic materials.Advanced drug delivery reviews · 2022Review
- Identification and characterization of circulating immune complexes in IgA nephropathy.Science advances · 2022Article
- Contrasting the conformational effects of α-O-GalNAc and α-O-Man glycan protein modifications and their impact on the mucin-like region of alpha-dystroglycan.Glycobiology · 2021Article
- The Biological Synthesis and the Function of Mucin 2 in Pseudomyxoma Peritonei.Cancer management and research · 2021Review
- Potential of Anti-MUC1 Antibodies as a Targeted Therapy for Gastrointestinal Cancers.Vaccines · 2020Review
- Identification of Tn antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies.Glycobiology · 2020Article
- Nucleocytoplasmic O-glycosylation in protists.Current opinion in structural biology · 2019Review
- Identification of a secondary binding site in human macrophage galactose-type lectin by microarray studies: Implications for the molecular recognition of its ligands.The Journal of biological chemistry · 2019Article
- Differential expression of Cosmc, T-synthase and mucins in Tn-positive colorectal cancers.BMC cancer · 2018Article
- Generation of Novel Anti-MUC1 Monoclonal Antibodies with Designed Carbohydrate Specificities Using MUC1 Glycopeptide Library.ACS omega · 2017Article
- Optimization of the Small Glycan Presentation for Binding a Tumor-Associated Antibody: Application to the Construction of an Ultrasensitive Glycan Biosensor.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- Compatible topologies and parameters for NMR structure determination of carbohydrates by simulated annealing.PloS one · 2017Article
- Perspectives on Anti-Glycan Antibodies Gleaned from Development of a Community Resource Database.ACS chemical biology · 2016Review
- Engineered CAR T Cells Targeting the Cancer-Associated Tn-Glycoform of the Membrane Mucin MUC1 Control Adenocarcinoma.Immunity · 2016Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
Mucin glycoproteins present a complex structural landscape arising from the multiplicity of glycosylation patterns afforded by their numerous serine and threonine glycosylation sites, often in clusters, and with variations in respective glycans. To explore the structural complexities in such glycoconjugates, we used NMR to systematically analyze the conformational effects of glycosylation density within a cluster of sites. This allows correlation with molecular recognition through analysis of interactions between these and other glycopeptides, with antibodies, lectins, and sera, using a glycopeptide microarray. Selective antibody interactions with discrete conformational elements, reflecting aspects of the peptide and disposition of GalNAc residues, are observed. Our results help bridge the gap between conformational properties and molecular recognition of these molecules, with implications for their physiological roles. Features of the native mucin motifs impact their relative immunogenicity and are accurately encoded in the antibody binding site, with the conformational integrity being preserved in isolated glycopeptides, as reflected in the antibody binding profile to array components.
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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.