Evidence map›Paper›PMID 29203664›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation.

Man Hon Yuen, Yu Hang Fong, Yap Shing Nim, Pak Ho Lau, Kam-Bo Wong

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. New Directions inInfection and drug resistance · 2025
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  7. Implications of lncRNAs inFrontiers in cellular and infection microbiology · 2024
    Review
  8. iScience · 2023
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021
    Review
  16. Nickel and GTP ModulateBiomolecules · 2020
    Article
  17. Structure, function, and biosynthesis of nickel-dependent enzymes.Protein science : a publication of the Protein Society · 2020
    Review
  18. Article
  19. Bimodal Nickel-Binding Site onInorganic chemistry · 2019
    Article
  20. Article
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.

Man Hon YuenSchool of Life Sciences, Centre for Protein Science and Crystallography, Partner State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong, China.
Yu Hang FongSchool of Life Sciences, Centre for Protein Science and Crystallography, Partner State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong, China.
Yap Shing NimSchool of Life Sciences, Centre for Protein Science and Crystallography, Partner State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong, China.
Pak Ho LauSchool of Life Sciences, Centre for Protein Science and Crystallography, Partner State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong, China.
Kam-Bo WongSchool of Life Sciences, Centre for Protein Science and Crystallography, Partner State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong, China kbwong@cuhk.edu.hk.
Chinese University of Hong Kong · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of metallochaperones to allosterically regulate the binding/release of metal ions and to switch protein-binding partners along the metal delivery pathway is essential to the metallation of the metalloenzymes. Urease, catalyzing the hydrolysis of urea into ammonia and carbon dioxide, contains two nickel ions bound by a carbamylated lysine in its active site. Delivery of nickel ions for urease maturation is dependent on GTP hydrolysis and is assisted by four urease accessory proteins UreE, UreF, UreG, and UreH(UreD). Here, we determined the crystal structure of the UreG dimer from

Indexed as

Protein ConformationAmino Acid SequenceBacterial ProteinsCarrier ProteinsEnzyme ActivationGuanosine TriphosphateMetallochaperonesModels, BiologicalModels, MolecularMutationNickelPhosphate-Binding ProteinsProtein BindingProtein MultimerizationStructure-Activity RelationshipUreaseBacterial ProteinsCarrier ProteinsGuanosine TriphosphateMetallochaperonesNickelPhosphate-Binding ProteinsUreaseureG protein, BacteriaG proteinHelicobacter pylorimetallochaperonesnickelurease maturation

Identifiers

PMID29203664
PMCPMC5754787
OpenAlexW2771320172

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.