Evidence map›Paper›PMID 29143814›Full record

ArticleNature2017

Structural basis of nucleotide sugar transport across the Golgi membrane.

Joanne L Parker, Simon Newstead

Abstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.5field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

58 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
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  11. MprF fromScience advances · 2025
    Article
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  14. Article
  15. Article
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  17. The NMR studies of CMP inhibition of polysialylation.Journal of enzyme inhibition and medicinal chemistry · 2023
    Article
  18. Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Joanne L Parker1Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Simon Newstead1Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
University of Oxford · GB

Funding

Wellcome TrustWellcome Trust 102890/Z/13/AWellcome Trust 102890/Z/13/Z
6 · The paper itself

Abstract

Glycosylation is a fundamental cellular process that, in eukaryotes, occurs in the lumen of both the Golgi apparatus and the endoplasmic reticulum. Nucleotide sugar transporters (NSTs) are an essential component of the glycosylation pathway, providing the diverse range of substrates required for the glycosyltransferases. NSTs are linked to several developmental and immune disorders in humans, and in pathogenic microbes they have an important role in virulence. How NSTs recognize and transport activated monosaccharides, however, is currently unclear. Here we present the crystal structure of an NST, the GDP-mannose transporter Vrg4, in both the substrate-free and the bound states. A hitherto unobserved requirement of short-chain lipids in activating the transporter supports a model for regulation within the highly dynamic membranes of the Golgi apparatus. Our results provide a structural basis for understanding nucleotide sugar recognition, and provide insights into the transport and regulatory mechanism of this family of intracellular transporters.

Indexed as

Biological TransportCrystallography, X-RayGlycosylationGolgi ApparatusMembrane Transport ProteinsMonosaccharidesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipSubstrate SpecificityMembrane Transport ProteinsMonosaccharidesSaccharomyces cerevisiae ProteinsVRG4 protein, S cerevisiae

Identifiers

PMID29143814
PMCPMC5701743
OpenAlexW2768448654

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.