Evidence map›Paper›PMID 25210595›Full record

ReviewComputational and structural biotechnology journal2014

Structure and function of nucleotide sugar transporters: Current progress.

Barbara Hadley, Andrea Maggioni, Angel Ashikov, Christopher J Day, Thomas Haselhorst, Joe Tiralongo

Open access · goldAbstract readReview
In one paragraph

Review in Computational and structural biotechnology journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

63 citing papers in PubMed, 98 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Medicinal Value ofInternational journal of molecular sciences · 2026
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  8. The Ubiquitous Wilt-Inducing PathogenPathogens (Basel, Switzerland) · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Mucin Glycans: A Target for Cancer Therapy.Molecules (Basel, Switzerland) · 2023
    Review
  14. The CmSphere · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

3 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 3 countries.

Barbara HadleyInstitute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
Andrea MaggioniInstitute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
Angel AshikovInstitut für Zelluläre Chemie, Zentrum Biochemie, Medizinische Hochschule Hannover, Carl-Neuberg Strasse 1, 30625 Hannover, Germany ; Laboratory of Genetic, Endocrine and Metabolic Diseases, Department of Neurology, Radboud University Medical Center, Geert Grooteplein Zuid 10 (route 830), Nijmegen, The Netherlands.
Christopher J DayInstitute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
Thomas HaselhorstInstitute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
Joe TiralongoInstitute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.
Griffith University · AURadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteomes of eukaryotes, bacteria and archaea are highly diverse due, in part, to the complex post-translational modification of protein glycosylation. The diversity of glycosylation in eukaryotes is reliant on nucleotide sugar transporters to translocate specific nucleotide sugars that are synthesised in the cytosol and nucleus, into the endoplasmic reticulum and Golgi apparatus where glycosylation reactions occur. Thirty years of research utilising multidisciplinary approaches has contributed to our current understanding of NST function and structure. In this review, the structure and function, with reference to various disease states, of several NSTs including the UDP-galactose, UDP-N-acetylglucosamine, UDP-N-acetylgalactosamine, GDP-fucose, UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose and CMP-sialic acid transporters will be described. Little is known regarding the exact structure of NSTs due to difficulties associated with crystallising membrane proteins. To date, no three-dimensional structure of any NST has been elucidated. What is known is based on computer predictions, mutagenesis experiments, epitope-tagging studies, in-vitro assays and phylogenetic analysis. In this regard the best-characterised NST to date is the CMP-sialic acid transporter (CST). Therefore in this review we will provide the current state-of-play with respect to the structure-function relationship of the (CST). In particular we have summarised work performed by a number groups detailing the affect of various mutations on CST transport activity, efficiency, and substrate specificity.

Indexed as

CMP-sialic acid transporterEndoplasmic reticulumGolgi apparatusNucleotide sugar transportersSTD NMR spectroscopy

Identifiers

PMID25210595
PMCPMC4151994
OpenAlexW2153209603

What OpenQuestion holds

Textmetadata
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.