Evidence map›Paper›PMID 30042487›Full record

ArticleScientific reports2018

Cytological analysis and structural quantification of FtsZ1-2 and FtsZ2-1 network characteristics in Physcomitrella patens.

Bugra Özdemir, Pouyan Asgharzadeh, Annette I Birkhold, Stefanie J Mueller, Oliver Röhrle, Ralf Reski

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

6 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Automatic extraction of actin networks in plants.PLoS computational biology · 2023
    Article
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  4. Article
  5. Review
  6. 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 3 institutions in 1 country.

Bugra ÖzdemirPlant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
Pouyan AsgharzadehInstitute of Applied Mechanics, University of Stuttgart, Pfaffenwaldring 7, 70569, Stuttgart, Germany.
Annette I BirkholdInstitute of Applied Mechanics, University of Stuttgart, Pfaffenwaldring 7, 70569, Stuttgart, Germany.ORCID 0000-0002-6375-4745
Stefanie J MuellerINRES - Chemical Signalling, University of Bonn, Friedrich-Ebert-Allee 144, 53113, Bonn, Germany.ORCID 0000-0003-4061-1175
Oliver RöhrleInstitute of Applied Mechanics, University of Stuttgart, Pfaffenwaldring 7, 70569, Stuttgart, Germany. roehrle@simtech.uni-stuttgart.de.
Ralf ReskiPlant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany. ralf.reski@biologie.uni-freiburg.de.ORCID 0000-0002-5496-6711
University of Stuttgart · DEUniversity of Freiburg · DEUniversity of Bonn · DE

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) TRR 141
6 · The paper itself

Abstract

Although the concept of the cytoskeleton as a cell-shape-determining scaffold is well established, it remains enigmatic how eukaryotic organelles adopt and maintain a specific morphology. The Filamentous Temperature Sensitive Z (FtsZ) protein family, an ancient tubulin, generates complex polymer networks, with striking similarity to the cytoskeleton, in the chloroplasts of the moss Physcomitrella patens. Certain members of this protein family are essential for structural integrity and shaping of chloroplasts, while others are not, illustrating the functional diversity within the FtsZ protein family. Here, we apply a combination of confocal laser scanning microscopy and a self-developed semi-automatic computational image analysis method for the quantitative characterisation and comparison of network morphologies and connectivity features for two selected, functionally dissimilar FtsZ isoforms, FtsZ1-2 and FtsZ2-1. We show that FtsZ1-2 and FtsZ2-1 networks are significantly different for 8 out of 25 structural descriptors. Therefore, our results demonstrate that different FtsZ isoforms are capable of generating polymer networks with distinctive morphological and connectivity features which might be linked to the functional differences between the two isoforms. To our knowledge, this is the first study to employ computational algorithms in the quantitative comparison of different classes of protein networks in living cells.

Indexed as

Protein Interaction MapsAlgorithmsBryopsidaChloroplastsComputational BiologyCytoskeletonGene ExpressionGene Knockout TechniquesGenes, PlantMicroscopy, ConfocalPhenotypePlant ProteinsProtein IsoformsProtoplastsPlant ProteinsProtein Isoforms

Identifiers

PMID30042487
PMCPMC6057934
OpenAlexW2884996791

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.