ArticleJournal of the American Chemical Society2012
Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
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.
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Who cites it
36 citing papers in PubMed, 73 citations in OpenAlex.
- Advances in protein glycosylation and its role in tissue repair and regeneration.Glycoconjugate journal · 2023Review
- Changes of IgGFrontiers in immunology · 2022Article
- Insights into substrate recognition and specificity for IgG by Endoglycosidase S2.PLoS computational biology · 2021Article
- Antibody mediated activation of natural killer cells in malaria exposed pregnant women.Scientific reports · 2021Article
- Glycine additive facilitates site-specific glycosylation profiling of biopharmaceuticals by ion-pairing hydrophilic interaction chromatography mass spectrometry.Analytical and bioanalytical chemistry · 2021Article
- Global view of human protein glycosylation pathways and functions.Nature reviews. Molecular cell biology · 2020Review
- Aglycosylated antibody-producing mice for aglycosylated antibody-lectin coupled immunoassay for the quantification of tumor markers (ALIQUAT).Communications biology · 2020Article
- Fc-Engineered Antibodies with Enhanced Fc-Effector Function for the Treatment of B-Cell Malignancies.Cancers · 2020Review
- A synopsis of recent developments defining how N-glycosylation impacts immunoglobulin G structure and function.Glycobiology · 2020Review
- Comparing different domains of analysis for the characterisation of N-glycans on monoclonal antibodies.Journal of pharmaceutical analysis · 2020Article
- Mechanistic reconstruction of glycoprotein secretion through monitoring of intracellular N-glycan processing.Science advances · 2019Article
- Oligosaccharide Synthesis and Translational Innovation.Journal of the American Chemical Society · 2019Review
- Structural analysis of glycoproteins: building N-linked glycans with Coot.Acta crystallographica. Section D, Structural biology · 2018Article
- Structural characterization of the Man5 glycoform of human IgG3 Fc.Molecular immunology · 2017Article
- Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans.Scientific reports · 2016Article
- Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies.Biochimica et biophysica acta · 2016Review
- Stabilizing the CH2 Domain of an Antibody by Engineering in an Enhanced Aromatic Sequon.ACS chemical biology · 2016Article
- Site-Specific N-Glycosylation of Recombinant Pentameric and Hexameric Human IgM.Journal of the American Society for Mass Spectrometry · 2016Article
- A Novel Platform for the Potentiation of Therapeutic Antibodies Based on Antigen-Dependent Formation of IgG Hexamers at the Cell Surface.PLoS biology · 2016Article
- Fc glycans of therapeutic antibodies as critical quality attributes.Glycobiology · 2015Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Human IgG Fc glycosylation modulates immunological effector functions such as antibody-dependent cellular cytotoxicity and phagocytosis. Engineering of Fc glycans therefore enables fine-tuning of the therapeutic properties of monoclonal antibodies. The N-linked glycans of Fc are typically complex-type, forming a network of noncovalent interactions along the protein surface of the Cγ2 domain. Here, we manipulate the mammalian glycan-processing pathway to trap IgG1 Fc at sequential stages of maturation, from oligomannose- to hybrid- to complex-type glycans, and show that the Fc is structurally stabilized following the transition of glycans from their hybrid- to complex-type state. X-ray crystallographic analysis of this hybrid-type intermediate reveals that N-linked glycans undergo conformational changes upon maturation, including a flip within the trimannosyl core. Our crystal structure of this intermediate reveals a molecular basis for antibody biogenesis and provides a template for the structure-guided engineering of the protein-glycan interface of therapeutic antibodies.
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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.