Evidence map›Paper›PMID 19837839›Full record

ArticleApplied and environmental microbiology2009

In vivo display of a multisubunit enzyme complex on biogenic magnetic nanoparticles.

Shoji Ohuchi, Dirk Schüler

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Enzyme Engineering for In Situ Immobilization.Molecules (Basel, Switzerland) · 2016
    Review
  4. Magnetosome biogenesis in magnetotactic bacteria.Nature reviews. Microbiology · 2016
    Review
  5. Review
  6. Article
  7. Article
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  10. Article
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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

2 authors at 2 institutions in 2 countries.

Shoji OhuchiDepartment of Basic Medical Sciences, Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. sohuchi@ims.u-tokyo.ac.jp
Dirk Schüler
Ludwig-Maximilians-Universität München · DEThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Magnetosomes are unique bacterial organelles comprising membrane-enveloped magnetic crystals produced by magnetotactic bacteria. Because of several desirable chemical and physical properties, magnetosomes would be ideal scaffolds on which to display highly complicated biological complexes artificially. As a model experiment for the functional expression of a multisubunit complex on magnetosomes, we examined the display of a chimeric bacterial RNase P enzyme composed of the protein subunit (C5) of Escherichia coli RNase P and the endogenous RNA subunit by expressing a translational fusion of C5 with MamC, a known magnetosome protein, in the magnetotactic bacterium Magnetospirillum gryphiswaldense. As intended, the purified C5 fusion magnetosomes, but not wild-type magnetosomes, showed apparent RNase P activity and the association of a typical bacterial RNase P RNA. Our results demonstrate for the first time that magnetosomes can be employed as scaffolds for the display of multisubunit complexes.

Indexed as

MagnetosomesBacterial ProteinsBase SequenceBiochemistryEscherichia coliMagnetospirillumMolecular Sequence DataMultienzyme ComplexesRecombinant Fusion ProteinsRibonuclease PRNA, BacterialBacterial ProteinsMultienzyme ComplexesRecombinant Fusion ProteinsRibonuclease PRNA, Bacterial

Identifiers

PMID19837839
PMCPMC2794094
OpenAlexW2171101091

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.