Evidence map›Paper›PMID 30985278›Full record

ArticleeLife2019

Structural basis for mammalian nucleotide sugar transport.

Shivani Ahuja, Matthew R Whorton

Abstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. The oncogene SLC35F2 is a high-specificity transporter for the micronutrients queuine and queuosine.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Polysialic Acid in the Immune System.Frontiers in immunology · 2021
    Review
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.

Shivani AhujaVollum Institute, Oregon Health & Science University, Portland, United States.ORCID 0000-0002-0123-711X
Matthew R WhortonVollum Institute, Oregon Health & Science University, Portland, United States.ORCID 0000-0002-9915-7467

Funding

Supplement to Structure and function of nucleotide sugar transporters.R01GM130909 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI BACONGUIS, ISABELLE RHYSSA JOE EDURIA · 2019 to 2023
$1.6M
Asymmetric flow FFF and Composition Gradient/Light Scattering SystemS10RR023748 · NCRR · YALE UNIVERSITY · PI FOLTA-STOGNIEW, EWA JOANNA · 2007 to 2007
$271k
NCRR NIH HHS S10 RR023748NIGMS NIH HHS R01 GM130909NIH HHS R01GM130909
6 · The paper itself

Abstract

Nucleotide-sugar transporters (NSTs) are critical components of the cellular glycosylation machinery. They transport nucleotide-sugar conjugates into the Golgi lumen, where they are used for the glycosylation of proteins and lipids, and they then subsequently transport the nucleotide monophosphate byproduct back to the cytoplasm. Dysregulation of human NSTs causes several debilitating diseases, and NSTs are virulence factors for many pathogens. Here we present the first crystal structures of a mammalian NST, the mouse CMP-sialic acid transporter (mCST), in complex with its physiological substrates CMP and CMP-sialic acid. Detailed visualization of extensive protein-substrate interactions explains the mechanisms governing substrate selectivity. Further structural analysis of mCST's unique lumen-facing partially-occluded conformation, coupled with the characterization of substrate-induced quenching of mCST's intrinsic tryptophan fluorescence, reveals the concerted conformational transitions that occur during substrate transport. These results provide a framework for understanding the effects of disease-causing mutations and the mechanisms of this diverse family of transporters.

Indexed as

AnimalsBiological TransportCrystallography, X-RayCytidine MonophosphateCytidine Monophosphate N-Acetylneuraminic AcidMiceProtein BindingProtein ConformationCytidine MonophosphateCytidine Monophosphate N-Acetylneuraminic AcidglycobiologyGolgihumanmolecular biophysicsmousenucleotide sugarsialic acidstructural biologytransporter

Identifiers

PMID30985278
PMCPMC6508934

What OpenQuestion holds

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Registered trials

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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.