ReviewCellular and molecular life sciences : CMLS2018
Crystal structures of eukaryote glycosyltransferases reveal biologically relevant enzyme homooligomers.
Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Human Proteoglycan Linkage Region Glycosyltransferases are Dimeric and Show Unexpected Specificities.Angewandte Chemie (International ed. in English) · 2026Article
- Revealing Amur tiger family pedigrees based on age identification using fecal microbiome and kinship analysis.Frontiers in microbiology · 2025Article
- Mutations in Glycosyltransferases and Glycosidases: Implications for Associated Diseases.Biomolecules · 2024Article
- The underlying mechanisms of arenaviral entry through matriglycan.Frontiers in molecular biosciences · 2024Review
- Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023Review
- The structure of EXTL3 helps to explain the different roles of bi-domain exostosins in heparan sulfate synthesis.Nature communications · 2022Article
- Article
- Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes.Frontiers in plant science · 2021Article
- Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features.Computational and structural biotechnology journal · 2020Review
- Assembly of B4GALT1/ST6GAL1 heteromers in the Golgi membranes involves lateral interactions via highly charged surface domains.The Journal of biological chemistry · 2019Article
- N-acetylglucosaminyltransferases and nucleotide sugar transporters form multi-enzyme-multi-transporter assemblies in golgi membranes in vivo.Cellular and molecular life sciences : CMLS · 2019Article
- Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V.Nature communications · 2018Article
- Article
- TheFood technology and biotechnologyArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Glycosyltransferases (GTases) transfer sugar moieties to proteins, lipids or existing glycan or polysaccharide molecules. GTases form an important group of enzymes in the Golgi, where the synthesis and modification of glycoproteins and glycolipids take place. Golgi GTases are almost invariably type II integral membrane proteins, with the C-terminal globular catalytic domain residing in the Golgi lumen. The enzymes themselves are divided into 103 families based on their sequence homology. There is an abundance of published crystal structures of GTase catalytic domains deposited in the Protein Data Bank (PDB). All of these represent either of the two main characteristic structural folds, GT-A or GT-B, or present a variation thereof. Since GTases can function as homomeric or heteromeric complexes in vivo, we have summarized the structural features of the dimerization interfaces in crystal structures of GTases, as well as considered the biochemical data available for these enzymes. For this review, we have considered all 898 GTase crystal structures in the Protein Data Bank and highlight the dimer formation characteristics of various GTases based on 24 selected structures.
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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.