Evidence map›Paper›PMID 23842869›Full record

ReviewTopics in current chemistry2015

UDP-GlcNAc 2-Epimerase/ManNAc Kinase (GNE): A Master Regulator of Sialic Acid Synthesis.

Stephan Hinderlich, Wenke Weidemann, Tal Yardeni, Rüdiger Horstkorte, Marjan Huizing

Open access · greenAbstract readReview
In one paragraph

Review in Topics in current chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
9.3field-weighted citation impact, top 2% 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

66 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Review
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  7. Journal of neuromuscular diseases · 2026
    Article
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  13. [Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2025
    Review
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  15. Article
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  19. RecessiveGenes · 2024
    Article
  20. Article

6 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

5 authors at 4 institutions in 4 countries.

Stephan HinderlichDepartment of Life Sciences and Technology, Beuth Hochschule für Technik Berlin, University of Applied Sciences, Berlin, Germany, hinderlich@beuth-hochschule.de.
Wenke Weidemann
Tal Yardeni
Rüdiger Horstkorte
Marjan Huizing
Luther University · KRBerliner Hochschule für Technik · DENational Human Genome Research Institute · USNational Institutes of Health · US

Funding

Cell Biology of Metabolic DisordersZIAHG200322 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI GAHL, WILLIAM · 2009 to 2014
$3.1M
Intramural NIH HHS ZIA HG200322NHGRI NIH HHS ZIA HG200322-09
6 · The paper itself

Abstract

UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is the key enzyme of sialic acid biosynthesis in vertebrates. It catalyzes the first two steps of the cytosolic formation of CMP-N-acetylneuraminic acid from UDP-N-acetylglucosamine. In this review we give an overview of structure, biochemistry, and genetics of the bifunctional enzyme and its complex regulation. Furthermore, we will focus on diseases related to UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase.

Indexed as

Genes, RegulatorAnimalsCytidine Monophosphate N-Acetylneuraminic AcidDisease Models, AnimalDistal MyopathiesGene Expression RegulationHumansMiceMice, TransgenicMultienzyme ComplexesMutationProtein Structure, QuaternarySialic Acid Storage DiseaseUridine Diphosphate N-AcetylglucosamineCytidine Monophosphate N-Acetylneuraminic AcidMultienzyme ComplexesUDP-N-acetylglucosamine 2-epimerase - N-acetylmannosamine kinaseUridine Diphosphate N-Acetylglucosamine

Identifiers

PMID23842869
PMCPMC4161665
OpenAlexW98195085

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.