ReviewGlycobiology2014
Structure-function relationships of membrane-associated GT-B glycosyltransferases.
Review in Glycobiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 106 citations in OpenAlex.
- Ngt-1: A glycosyltransferase that confers resistance to three distinct antibiotic classes.The Journal of biological chemistry · 2026Article
- Structural basis for phosphorylation and allosteric regulation of bacterial glycogen phosphorylase by histidine phosphocarrier protein.Nature communications · 2026Article
- Enzymology and Structural Basis of Glycosyltransferases Involved in Saponin C28 Carboxylic AcidJACS Au · 2025Article
- Metabolic engineering ofSynthetic and systems biotechnology · 2025Article
- Computational characterization of the xanthan gum glycosyltransferase GumK.PLoS computational biology · 2025Article
- Pmt4 recognizes two separate acceptor sites to O-mannosylate in the S/T-rich regions of substrate proteins.Nature communications · 2025Article
- Exploring Daptomycin Hypersensitivity inInternational journal of molecular sciences · 2025Article
- Structure and membrane interactions of Arabidopsis thaliana DGD2, a glycosyltransferase in the chloroplast membrane.The Journal of biological chemistry · 2025Article
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- Glycosyltransferases: glycoengineers in human milk oligosaccharide synthesis and manufacturing.Frontiers in molecular biosciences · 2025Review
- Pan-genome analysis of GT64 gene family and expression response to Verticillium wilt in cotton.BMC plant biology · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Cryo-EM analysis ofScience advances · 2024Article
- Specificity determinants revealed by the structure of glycosyltransferase Campylobacter concisus PglA.Protein science : a publication of the Protein Society · 2024Article
- A multi-enzyme machine polymerizes the Haemophilus influenzae type b capsule.Nature chemical biology · 2023Article
- Exopolysaccharide Biosynthesis inInternational journal of molecular sciences · 2023Article
- Characterization of a Glycolipid Synthase Producing α-Galactosylceramide inInternational journal of molecular sciences · 2022Article
- Dilute Bicelles for Glycosyltransferase Studies, Novel Bicelles with Phosphatidylinositol.The journal of physical chemistry. B · 2022Article
- Article
- Proteomic Analysis Reveals Enzymes for β-D-Glucan Formation and Degradation inInternational journal of molecular sciences · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Membrane-associated GT-B glycosyltransferases (GTs) comprise a large family of enzymes that catalyze the transfer of a sugar moiety from nucleotide-sugar donors to a wide range of membrane-associated acceptor substrates, mostly in the form of lipids and proteins. As a consequence, they generate a significant and diverse amount of glycoconjugates in biological membranes, which are particularly important in cell-cell, cell-matrix and host-pathogen recognition events. Membrane-associated GT-B enzymes display two "Rossmann-fold" domains separated by a deep cleft that includes the catalytic center. They associate permanently or temporarily to the phospholipid bilayer by a combination of hydrophobic and electrostatic interactions. They have the remarkable property to access both hydrophobic and hydrophilic substrates that reside within chemically distinct environments catalyzing their enzymatic transformations in an efficient manner. Here, we discuss the considerable progress that has been made in recent years in understanding the molecular mechanism that governs substrate and membrane recognition, and the impact of the conformational transitions undergone by these GTs during the catalytic cycle.
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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.