Evidence map›Paper›PMID 22085337›Full record

ArticleBiochemistry2011

Escherichia coli SlyD, more than a Ni(II) reservoir.

Harini Kaluarachchi, Jei Wei Zhang, Deborah B Zamble

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure, function, and biosynthesis of nickel-dependent enzymes.Protein science : a publication of the Protein Society · 2020
    Review
  6. Article
  7. Co(II) and Ni(II) binding of theThe Journal of biological chemistry · 2018
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

3 authors.

Harini KaluarachchiDepartment of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6.
Jei Wei Zhang
Deborah B Zamble

Funding

CIHR 77644
6 · The paper itself

Abstract

SlyD interacts with HypB and contributes to nickel insertion during [NiFe]-hydrogenase biogenesis. Herein, we provide evidence of SlyD acting as a nickel storage determinant in Escherichia coli and show that this Ni(II) can be mobilized to HypB in vitro even under competitive conditions. Furthermore, SlyD enhances the GTPase activity of HypB, and acceleration of release of Ni(II) from HypB is more pronounced when HypB is GDP-bound. The data support a model in which a HypB-SlyD complex establishes communication between GTP hydrolysis and nickel delivery and provide insight into the role of the HypB-SlyD complex during [NiFe]-hydrogenase biosynthesis.

Indexed as

ApoproteinsBinding SitesBiocatalysisCarrier ProteinsChelating AgentsEscherichia coliEscherichia coli ProteinsGTP-Binding ProteinsGuanosine DiphosphateGuanosine TriphosphateHydrogenaseKineticsModels, ChemicalMutant ProteinsNickelPeptide FragmentsApoproteinsCarrier ProteinsChelating AgentsEscherichia coli ProteinsGTP-Binding ProteinsGuanosine DiphosphateGuanosine TriphosphateHydrogenaseHypB protein, E coliMutant ProteinsNickelnickel-iron hydrogenasePeptide FragmentsPeptidylprolyl IsomeraseRecombinant ProteinsSlyD protein, E coli

Identifiers

PMID22085337
PMCPMC3253374

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.