ArticleNature communications2017
Structural basis for dolichylphosphate mannose biosynthesis.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 45 citations in OpenAlex.
- Real-time monitoring of glycocarrier formation unravels cryptic details in glycosyl transfer.RSC chemical biology · 2026Article
- Crystallographic data for Pyrococcus furiosus dolichylphosphate mannose synthase suggest that the enzyme could flip its glycolipid product.Scientific reports · 2026Article
- Article
- Structural basis of undecaprenyl phosphate glycosylation leading to polymyxin resistance in Gram-negative bacteria.Nature communications · 2025Article
- Mechanistic snapshots of lipid-linked sugar transfer.Nature communications · 2025Article
- GLYCO-BUILD: an enzymatic pipeline for the synthesis of peptides carrying eukaryotic N-glycans.Nature communications · 2025Article
- Convergent evolution of viral-like Borg archaeal extrachromosomal elements and giant eukaryotic viruses.Nature communications · 2025Article
- WrtF fromProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A GDP-mannose-1-phosphate guanylyltransferase as a potential HIGS target against Sclerotinia sclerotiorum.PLoS pathogens · 2025Article
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- Cryo-EM SPR structures of Salmonella typhimurium ArnC; the key enzyme in lipid-A modification conferring polymyxin resistance.Protein science : a publication of the Protein Society · 2025Article
- A Novel MonoallelicKidney international reports · 2024Article
- An improved expression and purification protocol enables the structural characterization of Mnt1, an antifungal target from Candida albicans.Fungal biology and biotechnology · 2024Article
- Molecular mechanisms underlying the structural diversity of rhamnose-rich cell wall polysaccharides in lactococci.The Journal of biological chemistry · 2024Article
- Mannose: A Promising Player in Clinical and Biomedical Applications.Current drug delivery · 2024Review
- Structural and mechanistic studies of the N-glycosylation machinery: from lipid-linked oligosaccharide biosynthesis to glycan transfer.Glycobiology · 2023Review
- Membrane linked RNA glycosylation as new trend to envision epi-transcriptome epoch.Cancer gene therapy · 2023Review
- Discovery and Characterization of Polymyxin-Resistance GenesMicrobiology spectrum · 2023Article
- AepG is a glucuronosyltransferase involved in acidic exopolysaccharide synthesis and contributes to environmental adaptation of Haloarcula hispanica.The Journal of biological chemistry · 2023Article
- Distinct Regions of the Haloferax volcanii Dolichol Phosphate-Mannose Synthase AglD Mediate the Assembly and Subsequent Processing of the Lipid-Linked Mannose.Journal of bacteriology · 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
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein glycosylation is a critical protein modification. In biogenic membranes of eukaryotes and archaea, these reactions require activated mannose in the form of the lipid conjugate dolichylphosphate mannose (Dol-P-Man). The membrane protein dolichylphosphate mannose synthase (DPMS) catalyzes the reaction whereby mannose is transferred from GDP-mannose to the dolichol carrier Dol-P, to yield Dol-P-Man. Failure to produce or utilize Dol-P-Man compromises organism viability, and in humans, several mutations in the human dpm1 gene lead to congenital disorders of glycosylation (CDG). Here, we report three high-resolution crystal structures of archaeal DPMS from Pyrococcus furiosus, in complex with nucleotide, donor, and glycolipid product. The structures offer snapshots along the catalytic cycle, and reveal how lipid binding couples to movements of interface helices, metal binding, and acceptor loop dynamics to control critical events leading to Dol-P-Man synthesis. The structures also rationalize the loss of dolichylphosphate mannose synthase function in dpm1-associated CDG.The generation of glycolipid dolichylphosphate mannose (Dol-P-Man) is a critical step for protein glycosylation and GPI anchor synthesis. Here the authors report the structure of dolichylphosphate mannose synthase in complex with bound nucleotide and donor to provide insight into the mechanism of Dol-P-Man synthesis.
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.