ArticleNature communications2018
Structure and mechanism of cancer-associated N-acetylglucosaminyltransferase-V.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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
54 citing papers in PubMed, 114 citations in OpenAlex.
- Highly branched complex-type N-glycans on integrin β1 in extracellular vesicles enhance the binding of sEVs to laminin on recipient cells.The Journal of biological chemistry · 2026Article
- Enzymatic basis of branching and extension of O-Man glycans for keratan sulfate biosynthesis.The Journal of biological chemistry · 2026Article
- Circulating Testican-2 and MGT5A are Markers of Membranous Nephropathy.Kidney international reports · 2026Article
- Charting the immune terrain: a novel risk model for thyroid cancer prognosis.Frontiers in genetics · 2026Article
- Article
- Evolutionary analyses of the animal glycosyltransferase family 54 reveals two β1,4-N-acetylglucosaminyltransferase families.iScience · 2025Article
- Hans Paulsen: Contributions to the Investigations of Glycoprotein Biosynthesis.Molecules (Basel, Switzerland) · 2025Review
- Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma.Scientific reports · 2025Article
- The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025Review
- N-acetylglucosaminyltransferase V attenuates myocardial infarction by mediating the insulin-like growth factor 1 receptor signaling pathway.Journal of translational internal medicine · 2025Article
- Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025Review
- Crystal structure of the fungal mannosyltransferase Och1 reveals active site primed for N-glycan binding.PloS one · 2025Article
- Glycosylation in Cancer.Handbook of experimental pharmacology · 2025Review
- N-Acetylated Monosaccharides and Derived Glycan Structures Occurring in N- and O-Glycans During Prostate Cancer Development.Cancers · 2024Review
- A Bioorthogonal Precision Tool for HumanJournal of the American Chemical Society · 2024Article
- Regulation of intracellular activity of N-glycan branching enzymes in mammals.The Journal of biological chemistry · 2024Review
- The Association between UrineBiomedicines · 2024Article
- Association ofmedRxiv : the preprint server for health sciences · 2023Article
- Aberrant N-glycosylation in cancer: MGAT5 and β1,6-GlcNAc branched N-glycans as critical regulators of tumor development and progression.Cellular oncology (Dordrecht, Netherlands) · 2023Review
- Abnormal glycosylation in glioma: related changes in biology, biomarkers and targeted therapy.Biomarker research · 2023Review
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 4 institutions in 2 countries.
Funding
Abstract
N-acetylglucosaminyltransferase-V (GnT-V) alters the structure of specific N-glycans by modifying α1-6-linked mannose with a β1-6-linked N-acetylglucosamine branch. β1-6 branch formation on cell surface receptors accelerates cancer metastasis, making GnT-V a promising target for drug development. However, the molecular basis of GnT-V's catalytic mechanism and substrate specificity are not fully understood. Here, we report crystal structures of human GnT-V luminal domain with a substrate analog. GnT-V luminal domain is composed of a GT-B fold and two accessary domains. Interestingly, two aromatic rings sandwich the α1-6 branch of the acceptor N-glycan and restrain the global conformation, partly explaining the fine branch specificity of GnT-V. In addition, interaction of the substrate N-glycoprotein with GnT-V likely contributes to protein-selective and site-specific glycan modification. In summary, the acceptor-GnT-V complex structure suggests a catalytic mechanism, explains the previously observed inhibition of GnT-V by branching enzyme GnT-III, and provides a basis for the rational design of drugs targeting N-glycan branching.
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.