Evidence map›Paper›PMID 28166209›Full record

ArticleNature chemical biology2017

A tight tunable range for Ni(II) sensing and buffering in cells.

Andrew W Foster, Rafael Pernil, Carl J Patterson, Andrew J P Scott, Lars-Olof Pålsson, Robert Pal, Ian Cummins, Peter T Chivers, Ehmke Pohl, Nigel J Robinson

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
11.2field-weighted citation impact, top 2% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Compatibility of intracellular binding: Evolutionary design principles for metal sensors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Protein metalation in biology.Current opinion in chemical biology · 2022
    Review
  13. Article
  14. Direct Detection of the Labile Nickel Pool inJournal of the American Chemical Society · 2021
    Article
  15. Article
  16. The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021
    Review
  17. Review
  18. Article
  19. 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

10 authors at 1 institution in 1 country.

Andrew W Foster *Department of Biosciences, Durham University, DH1 3LE, UK.
Rafael Pernil *Department of Biosciences, Durham University, DH1 3LE, UK.
Carl J PattersonDepartment of Biosciences, Durham University, DH1 3LE, UK.
Andrew J P ScottDepartment of Biosciences, Durham University, DH1 3LE, UK.
Lars-Olof PålssonDepartment of Chemistry, Durham University, DH1 3LE, UK.
Robert PalDepartment of Chemistry, Durham University, DH1 3LE, UK.
Ian CumminsDepartment of Biosciences, Durham University, DH1 3LE, UK.
Peter T ChiversDepartment of Biosciences, Durham University, DH1 3LE, UK.
Ehmke PohlDepartment of Biosciences, Durham University, DH1 3LE, UK.
Nigel J RobinsonDepartment of Biosciences, Durham University, DH1 3LE, UK.
Durham University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H006052/2Biotechnology and Biological Sciences Research Council BB/K00817X/1Biotechnology and Biological Sciences Research Council BB/L009226/1Biotechnology and Biological Sciences Research Council BB/L013711/1
6 · The paper itself

Abstract

The metal affinities of metal-sensing transcriptional regulators co-vary with cellular metal concentrations over more than 12 orders of magnitude. To understand the cause of this relationship, we determined the structure of the Ni(II) sensor InrS and then created cyanobacteria (Synechocystis PCC 6803) in which transcription of genes encoding a Ni(II) exporter and a Ni(II) importer were controlled by InrS variants with weaker Ni(II) affinities. Variant strains were sensitive to elevated nickel and contained more nickel, but the increase was small compared with the change in Ni(II) affinity. All of the variant sensors retained the allosteric mechanism that inhibits DNA binding following metal binding, but a response to nickel in vivo was observed only when the sensitivity was set to respond in a relatively narrow (less than two orders of magnitude) range of nickel concentrations. Thus, the Ni(II) affinity of InrS is attuned to cellular metal concentrations rather than the converse.

Indexed as

BuffersModels, MolecularNickelRepressor ProteinsSynechocystisBuffersNickelRepressor Proteins

Identifiers

PMID28166209
PMCPMC5365139
OpenAlexW2587553267

What OpenQuestion holds

Textmetadata
LicenceTDM
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.