Evidence map›Paper›PMID 32878987›Full record

ArticleThe Journal of biological chemistry2020

Dissecting the structural and functional roles of a putative metal entry site in encapsulated ferritins.

Cecilia Piergentili, Jennifer Ross, Didi He, Kelly J Gallagher, Will A Stanley, Laurène Adam, C Logan Mackay, Arnaud Baslé, Kevin J Waldron, David J Clarke and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.6field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Structure and heterogeneity of a highly cargo-loaded encapsulin shell.bioRxiv : the preprint server for biology · 2023
    Article
  4. Article
  5. Encapsulins.Annual review of biochemistry · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. 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

11 authors at 2 institutions in 1 country.

Cecilia PiergentiliSchool of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
Jennifer RossEaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland.
Didi HeInstitute of Quantitative Biology, Biochemistry and Biotechnology, School of Biological Sciences, The University of Edinburgh, Edinburgh, Scotland.
Kelly J GallagherEaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland.
Will A StanleySchool of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
Laurène AdamSchool of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
C Logan MackayEaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland.
Arnaud BasléBiosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom.
Kevin J WaldronBiosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom.
David J ClarkeEaStCHEM School of Chemistry, University of Edinburgh, Edinburgh, Scotland. Electronic address: Dave.clarke@ed.ac.uk.
Jon Marles-WrightSchool of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, United Kingdom. Electronic address: Jon.marles-wright1@ncl.ac.uk.
Newcastle University · GBUniversity of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M010996/1Biotechnology and Biological Sciences Research Council BB/N005570/1Biotechnology and Biological Sciences Research Council BB/R013942/1Biotechnology and Biological Sciences Research Council BB/R013993/1Wellcome TrustWellcome Trust 098375/Z/12/Z
6 · The paper itself

Abstract

Encapsulated ferritins belong to the universally distributed ferritin superfamily, whose members function as iron detoxification and storage systems. Encapsulated ferritins have a distinct annular structure and must associate with an encapsulin nanocage to form a competent iron store that is capable of holding significantly more iron than classical ferritins. The catalytic mechanism of iron oxidation in the ferritin family is still an open question because of the differences in organization of the ferroxidase catalytic site and neighboring secondary metal-binding sites. We have previously identified a putative metal-binding site on the inner surface of the

Indexed as

Bacterial ProteinsCatalytic DomainCeruloplasminCrystallography, X-RayIronMetalsMutagenesis, Site-DirectedOxidation-ReductionProtein ConformationRecombinant ProteinsRhodospirillum rubrumZincBacterial ProteinsCeruloplasminIronMetalsRecombinant ProteinsZinccrystal structureencapsulated ferritinencapsulinferritinferroxidaseironiron metabolismmass spectrometry (MS)native mass spectrometryX-ray crystallography

Identifiers

PMID32878987
PMCPMC7667983
OpenAlexW3081726774

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.