Evidence map›Paper›PMID 28738898›Full record

ArticleBMC biology2017

Silicanin-1 is a conserved diatom membrane protein involved in silica biomineralization.

Alexander Kotzsch, Philip Gröger, Damian Pawolski, Paul H H Bomans, Nico A J M Sommerdijk, Michael Schlierf, Nils Kröger

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Review
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  5. Review
  6. Biomineral-Based Composite Materials in Regenerative Medicine.International journal of molecular sciences · 2024
    Review
  7. Nanoengineered Silica-Based Biomaterials for Regenerative Medicine.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. The molecular basis for pore pattern morphogenesis in diatom silica.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. 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

7 authors at 2 institutions in 2 countries.

Alexander KotzschB CUBE Center for Molecular Bioengineering, CMCB, TU Dresden, Arnoldstrasse 18, 01307, Dresden, Germany.
Philip GrögerB CUBE Center for Molecular Bioengineering, CMCB, TU Dresden, Arnoldstrasse 18, 01307, Dresden, Germany.
Damian PawolskiB CUBE Center for Molecular Bioengineering, CMCB, TU Dresden, Arnoldstrasse 18, 01307, Dresden, Germany.
Paul H H BomansDepartment of Chemical Engineering and Chemistry, Laboratory of Materials and Interface Chemistry & Center of Multiscale Electron Microscopy, P.O. Box 513, 5600 MB, Eindhoven, The Netherlands.
Nico A J M SommerdijkDepartment of Chemical Engineering and Chemistry, Laboratory of Materials and Interface Chemistry & Center of Multiscale Electron Microscopy, P.O. Box 513, 5600 MB, Eindhoven, The Netherlands.
Michael SchlierfB CUBE Center for Molecular Bioengineering, CMCB, TU Dresden, Arnoldstrasse 18, 01307, Dresden, Germany.
Nils KrögerB CUBE Center for Molecular Bioengineering, CMCB, TU Dresden, Arnoldstrasse 18, 01307, Dresden, Germany. nils.kroeger@tu-dresden.de.ORCID 0000-0002-8115-4129
Center for Systems Biology Dresden · DEEindhoven University of Technology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBiological mineral formation (biomineralization) proceeds in specialized compartments often bounded by a lipid bilayer membrane. Currently, the role of membranes in biomineralization is hardly understood.

resultsInvestigating biomineralization of SiO

conclusionsSin1 is the first identified SDV transmembrane protein, and is highly conserved throughout the diatom realm, which suggests a fundamental role in the biomineralization of diatom silica. Through interaction with long-chain polyamines, Sin1 could serve as a molecular link by which the SDV membrane exerts control on the assembly of biosilica-forming organic matrices in the SDV lumen.

Indexed as

DiatomsMembrane ProteinsRNA, AlgalSilicon DioxideMembrane ProteinsRNA, AlgalSilicon DioxideBiomineralization vesiclesCryo-TEMDiatom biosilicaExocytosisProtein self-assemblySilica formation activityTime-lapse confocal fluorescence microscopyTransmembrane proteinVesicle biogenesis

Identifiers

PMID28738898
PMCPMC5525289
OpenAlexW2737089463

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.