Evidence map›Paper›PMID 25860585›Full record

ArticleScientific reports2015

A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.

Jana Indra Führing, Johannes Thomas Cramer, Julia Schneider, Petra Baruch, Rita Gerardy-Schahn, Roman Fedorov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

32 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  5. The post-reactive structures ofMicrobiology spectrum · 2025
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  6. Uridine as a hub in cancer metabolism and RNA biology.Experimental & molecular medicine · 2025
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  9. Review
  10. Article
  11. Article
  12. Article
  13. Exploring Redox Modulation of Plant UDP-Glucose Pyrophosphorylase.International journal of molecular sciences · 2023
    Article
  14. Review
  15. Filament Negative RegulatorJournal of fungi (Basel, Switzerland) · 2022
    Article
  16. Article
  17. UDP-glucose pyrophosphorylase 2, a regulator of glycogen synthesis and glycosylation, is critical for pancreatic cancer growth.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Review
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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

6 authors at 1 institution in 1 country.

Jana Indra FühringInstitute for Cellular Chemistry, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
Johannes Thomas CramerInstitute for Cellular Chemistry, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
Julia SchneiderInstitute for Cellular Chemistry, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
Petra BaruchResearch Division for Structural Analysis, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
Rita Gerardy-SchahnInstitute for Cellular Chemistry, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
Roman Fedorov1] Research Division for Structural Analysis, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany [2] Institute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany.
Medizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In mammals, UDP-glucose pyrophosphorylase (UGP) is the only enzyme capable of activating glucose-1-phosphate (Glc-1-P) to UDP-glucose (UDP-Glc), a metabolite located at the intersection of virtually all metabolic pathways in the mammalian cell. Despite the essential role of its product, the molecular basis of UGP function is poorly understood. Here we report the crystal structure of human UGP in complex with its product UDP-Glc. Beyond providing first insight into the active site architecture, we describe the substrate binding mode and intermolecular interactions in the octameric enzyme that are crucial to its activity. Importantly, the quaternary mechanism identified for human UGP in this study may be common for oligomeric sugar-activating nucleotidyltransferases. Elucidating such mechanisms is essential for understanding nucleotide sugar metabolism and opens the perspective for the development of drugs that specifically inhibit simpler organized nucleotidyltransferases in pathogens.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsCatalytic DomainGlucoseHumansMetabolic Networks and PathwaysModels, MolecularMolecular ConformationMolecular Sequence DataMutationProtein BindingProtein StabilityProtein SubunitsStructure-Activity RelationshipSubstrate SpecificityGlucoseProtein SubunitsUridine Diphosphate GlucoseUTP-Glucose-1-Phosphate Uridylyltransferase

Identifiers

PMID25860585
PMCPMC5381698
OpenAlexW2092367174

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.