ArticleNature chemical biology2015
Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
43 citing papers in PubMed, 72 citations in OpenAlex.
- ER quality control of Crumbs2 and Notch proteins by GXYLT1-dependent xylosyl elongation of O-glucose glycans.The Journal of biological chemistry · 2026Article
- Systematic Quantification of Protein O-GlcNAcylation Reveals Common and Cell-Type-Specific Responses to N-Glycosylation Inhibition in Human Cells.Analytical chemistry · 2026Article
- Structural basis of EGF-repeat O-glucosylation by the protein O-glucosyltransferase POGLUT2.The Journal of biological chemistry · 2026Article
- Mechanism of 3-The Journal of organic chemistry · 2025Article
- Article
- Crystal structure of the fungal mannosyltransferase Och1 reveals active site primed for N-glycan binding.PloS one · 2025Article
- Enhancer-driven gene regulatory networks inference from single-cell RNA-seq and ATAC-seq data.Briefings in bioinformatics · 2024Article
- 1-L Transcription of SARS-CoV-2 Spike Protein S1 Subunit.International journal of molecular sciences · 2024Article
- Glycosyltransferase 8 domain-containing protein 1 (GLT8D1) is a UDP-dependent galactosyltransferase.Scientific reports · 2023Article
- Molecular mechanism of decision-making in glycosaminoglycan biosynthesis.Nature communications · 2023Article
- Structural basis for heparan sulfate co-polymerase action by the EXT1-2 complex.Nature chemical biology · 2023Article
- Roles of Notch Signaling in the Tumor Microenvironment.International journal of molecular sciences · 2022Review
- Significant Roles of NotchMolecules (Basel, Switzerland) · 2022Review
- Enzymatic activity of glycosyltransferase GLT8D1 promotes human glioblastoma cell migration.iScience · 2022Article
- Generation of Properly Folded Epidermal Growth Factor-Like (EGF) Repeats and Glycosyltransferases Enables In Vitro O-Glycosylation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Structural and mechanistic investigations of protein S-glycosyltransferases.Cell chemical biology · 2021Article
- Current Views on the Roles ofBiomolecules · 2021Review
- Multifaceted regulation of Notch signaling by glycosylation.Glycobiology · 2021Review
- Recent Progress in Structural Studies on the GT-C Superfamily of Protein Glycosyltransferases.Sub-cellular biochemistry · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
A major question remaining in glycobiology is how a glycosyltransferase (GT) that retains the anomeric linkage of a sugar catalyzes the reaction. Xyloside α-1,3-xylosyltransferase (XXYLT1) is a retaining GT that regulates Notch receptor activation by adding xylose to the Notch extracellular domain. Here, using natural acceptor and donor substrates and active Mus musculus XXYLT1, we report a series of crystallographic snapshots along the reaction, including an unprecedented natural and competent Michaelis reaction complex for retaining enzymes. These structures strongly support the SNi-like reaction as the retaining mechanism for XXYLT1. Unexpectedly, the epidermal growth factor-like repeat acceptor substrate undergoes a large conformational change upon binding to the active site, providing a structural basis for substrate specificity. Our improved understanding of this retaining enzyme will accelerate the design of retaining GT inhibitors that can modulate Notch activity in pathological situations in which Notch dysregulation is known to cause cancer or developmental disorders.
Indexed as
Identifiers
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.