Evidence map›Paper›PMID 21788478›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Iron-containing urease in a pathogenic bacterium.

Eric L Carter, Dale E Tronrud, Scott R Taber, P Andrew Karplus, Robert P Hausinger

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Iron-Containing Ureases.Coordination chemistry reviews · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Emergence of metal selectivity and promiscuity in metalloenzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Review
  11. Review
  12. Article
  13. Structure/function correlations over binuclear non-heme iron active sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Nonredox nickel enzymes.Chemical reviews · 2014
    Review
  19. Nickel-dependent metalloenzymes.Archives of biochemistry and biophysics · 2014
    Review
  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 2 institutions in 1 country.

Eric L CarterDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA.
Dale E Tronrud
Scott R Taber
P Andrew Karplus
Robert P Hausinger
Oregon State University · USMichigan State University · US

Funding

MECHANISM OF UREASE METALLOCENTER BIOSYNTHESISR01DK045686 · NIDDK · MICHIGAN STATE UNIVERSITY · PI HAUSINGER, ROBERT P · 1994 to 2010
$2.1M
Improving Modeling by Learning from Details of High Accuracy Protein StructuresR01GM083136 · NIGMS · OREGON STATE UNIVERSITY · PI KARPLUS, PAUL ANDREW · 2008 to 2015
$1.7M
NIDDK NIH HHS DK04586NIDDK NIH HHS R01 DK045686NIGMS NIH HHS GM083136NIGMS NIH HHS R01 GM083136
6 · The paper itself

Abstract

Helicobacter mustelae, a gastric pathogen of ferrets, synthesizes a distinct iron-dependent urease in addition to its archetypical nickel-containing enzyme. The iron-urease is oxygen-labile, with the inactive protein exhibiting a methemerythrin-like electronic spectrum. Significantly, incubation of the oxidized protein with dithionite under anaerobic conditions leads to restoration of activity and bleaching of the spectrum. Structural analysis of the oxidized species reveals a dinuclear iron metallocenter bridged by a lysine carbamate, closely resembling the traditional nickel-urease active site. Although the iron-urease is less active than the nickel-enzyme, its activity allows H. mustelae to survive the carnivore's low-nickel gastric environment.

Indexed as

AbsorptionCrystallography, X-RayCulture MediaElectronsHelicobacter mustelaeIonsIronKineticsModels, MolecularNickelOxygenSpectrum AnalysisUreaseCulture MediaIonsIronNickelOxygenUrease

Identifiers

PMID21788478
PMCPMC3156221
OpenAlexW2079552045

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.