Evidence map›Paper›PMID 24819161›Full record

ArticlePloS one2014

Bacterial magnetosome biomineralization--a novel platform to study molecular mechanisms of human CDF-related Type-II diabetes.

Natalie Zeytuni, René Uebe, Michal Maes, Geula Davidov, Michal Baram, Oliver Raschdorf, Assaf Friedler, Yifat Miller, Dirk Schüler, Raz Zarivach

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. 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
1.3field-weighted citation impact, top 21% 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, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Magnetosome biogenesis in magnetotactic bacteria.Nature reviews. Microbiology · 2016
    Review
  11. Article
  12. Review
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 3 institutions in 2 countries.

Natalie ZeytuniDepartment of Life Sciences, Ben Gurion University of the Negev, Beer-Sheva, Israel; The National Institute for Biotechnology in the Negev, Ben Gurion University of the Negev, Beer-Sheva, Israel.
René UebeLudwig Maximillian University of Munich, Dept. Biology I, Martinsried, Germany.
Michal MaesInstitute of Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem, Israel.
Geula DavidovDepartment of Life Sciences, Ben Gurion University of the Negev, Beer-Sheva, Israel; The National Institute for Biotechnology in the Negev, Ben Gurion University of the Negev, Beer-Sheva, Israel.
Michal BaramDepartment of Chemistry, Ben Gurion University of the Negev, Beer-Sheva, Israel; Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Oliver RaschdorfLudwig Maximillian University of Munich, Dept. Biology I, Martinsried, Germany.
Assaf FriedlerInstitute of Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem, Israel.
Yifat MillerDepartment of Chemistry, Ben Gurion University of the Negev, Beer-Sheva, Israel; Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Dirk SchülerLudwig Maximillian University of Munich, Dept. Biology I, Martinsried, Germany.
Raz ZarivachDepartment of Life Sciences, Ben Gurion University of the Negev, Beer-Sheva, Israel; The National Institute for Biotechnology in the Negev, Ben Gurion University of the Negev, Beer-Sheva, Israel.
Ben-Gurion University of the Negev · ILLudwig-Maximilians-Universität München · DEHebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cation diffusion facilitators (CDF) are part of a highly conserved protein family that maintains cellular divalent cation homeostasis in all organisms. CDFs were found to be involved in numerous human health conditions, such as Type-II diabetes and neurodegenerative diseases. In this work, we established the magnetite biomineralizing alphaproteobacterium Magnetospirillum gryphiswaldense as an effective model system to study CDF-related Type-II diabetes. Here, we introduced two ZnT-8 Type-II diabetes-related mutations into the M. gryphiswaldense MamM protein, a magnetosome-associated CDF transporter essential for magnetite biomineralization within magnetosome vesicles. The mutations' effects on magnetite biomineralization and iron transport within magnetosome vesicles were tested in vivo. Additionally, by combining several in vitro and in silico methodologies we provide new mechanistic insights for ZnT-8 polymorphism at position 325, located at a crucial dimerization site important for CDF regulation and activation. Overall, by following differentiated, easily measurable, magnetism-related phenotypes we can utilize magnetotactic bacteria for future research of CDF-related human diseases.

Indexed as

AllelesAmino Acid SequenceBacterial ProteinsCation Transport ProteinsDiabetes Mellitus, Type 2Ferrosoferric OxideHumansMagnetosomesMagnetospirillumMineralsModels, MolecularMolecular Sequence DataMutationProtein MultimerizationProtein StabilityProtein Structure, QuaternaryBacterial ProteinsCation Transport ProteinsFerrosoferric OxideMineralsZinc

Identifiers

PMID24819161
PMCPMC4018254
OpenAlexW2072640177

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.