Evidence map›Paper›PMID 23797863›Full record

ArticleJournal of the American Society for Mass Spectrometry2013

Analysis of a soluble (UreD:UreF:UreG)2 accessory protein complex and its interactions with Klebsiella aerogenes urease by mass spectrometry.

Mark A Farrugia, Linjie Han, Yueyang Zhong, Jodi L Boer, Brandon T Ruotolo, Robert P Hausinger

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Structural insights into how GTP-dependent conformational changes in a metallochaperone UreG facilitate urease maturation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. The conformational response to Zn(II) and Ni(II) binding of Sporosarcina pasteurii UreG, an intrinsically disordered GTPase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Article
  8. Sumner's legacy: a century of urease crystals and recent structural advances.Critical reviews in biochemistry and molecular biology
    Review
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 2 institutions in 1 country.

Mark A FarrugiaDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
Linjie Han
Yueyang Zhong
Jodi L Boer
Brandon T Ruotolo
Robert P Hausinger
Michigan State University · USUniversity of Michigan–Ann Arbor · US

Funding

Next-generation Mass Spectrometry Technologies for Integrated Structural Proteomics- RenewalR01GM095832 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RUOTOLO, BRANDON T · 2011 to 2024
$5.8M
MECHANISM OF UREASE METALLOCENTER BIOSYNTHESISR01DK045686 · NIDDK · MICHIGAN STATE UNIVERSITY · PI HAUSINGER, ROBERT P · 1994 to 2010
$2.1M
NIDDK NIH HHS DK045686NIDDK NIH HHS R01 DK045686NIGMS NIH HHS GM095832NIGMS NIH HHS R01 GM095832
6 · The paper itself

Abstract

Maturation of the nickel-containing urease of Klebsiella aerogenes is facilitated by the UreD, UreF, and UreG accessory proteins along with the UreE metallo-chaperone. A fusion of the maltose binding protein and UreD (MBP-UreD) was co-isolated with UreF and UreG in a soluble complex possessing a (MBPUreD: UreF:UreG)2 quaternary structure. Within this complex a UreF:UreF interaction was identified by chemical cross-linking of the amino termini of its two UreF protomers, as shown by mass spectrometry of tryptic peptides. A preactivation complex was formed by the interaction of (MBP-UreD:UreF:UreG)2 and urease. Mass spectrometry of intact protein species revealed a pathway for synthesis of the urease pre-activation complex in which individual hetero-trimer units of the (MBP-UreD:UreF:UreG)2 complex bind to urease. Together, these data provide important new insights into the structures of protein complexes associated with urease activation.

Indexed as

Bacterial ProteinsCarrier ProteinsEnterobacter aerogenesEnzyme ActivationModels, MolecularPhosphate-Binding ProteinsProtein Interaction MapsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationUreaseBacterial ProteinsCarrier ProteinsPhosphate-Binding ProteinsUreaseUreD protein, BacteriaUreF protein, bacteriaureG protein, Bacteria

Identifiers

PMID23797863
PMCPMC3788043
OpenAlexW2062420845

What OpenQuestion holds

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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.