Evidence map›Paper›PMID 31133698›Full record

ArticleNature structural & molecular biology2019

Structural basis for the delivery of activated sialic acid into Golgi for sialyation.

Emmanuel Nji, Ashutosh Gulati, Abdul Aziz Qureshi, Mathieu Coincon, David Drew

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
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  8. 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
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  9. Article
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  11. Review
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  15. Mucin Glycans: A Target for Cancer Therapy.Molecules (Basel, Switzerland) · 2023
    Review
  16. Review
  17. 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

5 authors at 1 institution in 1 country.

Emmanuel Nji *Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-6991-1046
Ashutosh Gulati *Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-0960-994X
Abdul Aziz Qureshi *Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Mathieu CoinconDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-3928-7155
David DrewDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. ddrew@dbb.su.se.ORCID http://orcid.org/0000-0001-8866-6349
Stockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The decoration of secretory glycoproteins and glycolipids with sialic acid is critical to many physiological and pathological processes. Sialyation is dependent on a continuous supply of sialic acid into Golgi organelles in the form of CMP-sialic acid. Translocation of CMP-sialic acid into Golgi is carried out by the CMP-sialic acid transporter (CST). Mutations in human CST are linked to glycosylation disorders, and CST is important for glycopathway engineering, as it is critical for sialyation efficiency of therapeutic glycoproteins. The mechanism of how CMP-sialic acid is recognized and translocated across Golgi membranes in exchange for CMP is poorly understood. Here we have determined the crystal structure of a Zea mays CST in complex with CMP. We conclude that the specificity of CST for CMP-sialic acid is established by the recognition of the nucleotide CMP to such an extent that they are mechanistically capable of both passive and coupled antiporter activity.

Indexed as

Binding SitesCrystallography, X-RayCytidine Monophosphate N-Acetylneuraminic AcidGolgi ApparatusHumansModels, MolecularN-Acetylneuraminic AcidNucleotide Transport ProteinsPlant ProteinsProtein ConformationProtein MultimerizationZea maysCytidine Monophosphate N-Acetylneuraminic AcidN-Acetylneuraminic AcidNucleotide Transport ProteinsPlant Proteins

Identifiers

PMID31133698
OpenAlexW2921827279

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.