Evidence map›Paper›PMID 28527238›Full record

ArticleeLife2017

A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases.

Niels Bradshaw, Vladimir M Levdikov, Christina M Zimanyi, Rachelle Gaudet, Anthony J Wilkinson, Richard Losick

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. SpoIIE drives asymmetric cell division inbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Gallium Resistance inApplied microbiology (Basel, Switzerland) · 2025
    Article
  7. Article
  8. Article
  9. Cell division machinery drives cell-specific gene activation during differentiation inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

6 authors at 2 institutions in 2 countries.

Niels BradshawDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-6845-4717
Vladimir M LevdikovStructural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.
Christina M ZimanyiDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-6782-507X
Rachelle GaudetDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-9177-054X
Anthony J WilkinsonStructural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.ORCID 0000-0003-4577-9479
Richard LosickDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-5130-6582
Harvard University · USUniversity of York · GB

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Role of RNA Polymerase in Bacterial DifferentionR01GM018568 · NIGMS · HARVARD UNIVERSITY · PI LOSICK, RICHARD MARC · 1985 to 2018
$11.5M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM018568
6 · The paper itself

Abstract

PP2C phosphatases control biological processes including stress responses, development, and cell division in all kingdoms of life. Diverse regulatory domains adapt PP2C phosphatases to specific functions, but how these domains control phosphatase activity was unknown. We present structures representing active and inactive states of the PP2C phosphatase SpoIIE from

Indexed as

Allosteric RegulationBacillus subtilisBacterial ProteinsCatalytic DomainCrystallography, X-RayModels, MolecularPeptide HydrolasesProtein ConformationBacterial ProteinsPeptide Hydrolasesspore-specific proteins, BacillusallosterybiochemistryB. subtiliscell fateinfectious diseasemicrobiologymolecular evolutionproteasomeprotein phosphatase

Identifiers

PMID28527238
PMCPMC5468089
OpenAlexW2615561589

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.