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Articles by Duong T. Bui
Glycolipid recognition and binding by Siglec-6 hinges on interactions with the cell membrane - Communications Biology
Abstract Sialic acid-binding immunoglobulin-type lectins (Siglecs) regulate immune response through interactions with sialylated glycans on glycoproteins and glycolipids. Human Siglecs count 14 unique proteins and in all of those the recognition and binding of the sialic acid on the glycan target involves a conserved, or canonical, Arg residue.
Production of human cathepsins using Expi293™ mammalian cell expression system for off‐target activity of cysteine protease inhibitor screening
1 INTRODUCTION Cathepsins are a family of proteases that are abundantly found in the lysosomes with diverse functions in the cell, ranging from antigen presentation in the immune response to maintaining cellular homeostasis (Brix et al., 2008; Roberts, 2005; Turk et al., 2000). Their dysregulation has been implicated in a range of pathological states (Reiser et al., 2010).
Quantifying Protein-Glycan Interactions Using Native Mass Spectrometry
ACE2 angiotensin-converting enzyme 2 CaR catch-and-release CBM carbohydrate-binding module CD charge detection CID collision-induced dissociation COIN concentration independent CRD carbohydrate recognition domain CRM charge residue model CTB5 cholera toxin B subunit homopentamer CUPRA competitive universal proxy receptor assay ESI electrospray ionization FAC-MS frontal affinity chromatography coupled to MS GBP glycan binding protein GL glycolipid GSL glycosphingolipid IS internal standard ITC...
A Kinetic Trapping Approach for Facile Access to 3FaxNeu5Ac and a Photo-Cross-Linkable Sialyltransferase Probe
Sialic acid (Neu5Ac, 1) is a nine-carbon α-keto acid monosaccharide that caps cellular glycoconjugates on mammalian cells. (1) Addition of Neu5Ac to the underlying glycan is catalyzed by a family of enzymes called sialyltransferases (STs), (2) which use cytidine monophosphate sialic acid (CMP-Neu5Ac, 2) as their Leloir donor, to transfer 1 to a specific hydroxyl group on a glycan acceptor (Figure S1a).
Chemoenzymatic synthesis of genetically-encoded multivalent liquid N-glycan arrays - Nature Communications
Abstract Cellular glycosylation is characterized by chemical complexity and heterogeneity, which is challenging to reproduce synthetically. Here we show chemoenzymatic synthesis on phage to produce a genetically-encoded liquid glycan array (LiGA) of complex type N-glycans. Implementing the approach involved by ligating an azide-containing sialylglycosyl-asparagine to phage functionalized with 50–1000 copies of dibenzocyclooctyne.
Native Mass Spectrometry Quantitation of α2-3-Linked N-Acetylneuraminic Acid Content of Prostate-Specific Antigen: An Accurate Liquid Biopsy for Clinically Significant Prostate Cancer
Application of the prostate-specific antigen (PSA) test, which measures PSA levels in blood, is standard in prostate cancer (PCa) screening. However, because PSA levels may be elevated for reasons other than PCa, it leads to high rates of misdiagnosis and overtreatment.
Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa - Nature Communications
Abstract Synthase-dependent secretion systems are a conserved mechanism for producing exopolysaccharides in Gram-negative bacteria. Although widely studied, it is not well understood how these systems are organized to coordinate polymer biosynthesis, modification, and export across both membranes and the peptidoglycan.
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