Evidence map›Paper›PMID 22970728›Full record

ArticleBMC plant biology2012

Protein disorder in plants: a view from the chloroplast.

Inmaculada Yruela, Bruno Contreras-Moreira

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

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  8. Pervasive convergent evolution and extreme phenotypes define chaperone requirements of protein homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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  13. Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017
    Review
  14. Article
  15. Article
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  19. Protein intrinsic disorder in plants.Frontiers in plant science · 2013
    Review
  20. 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

2 authors at 2 institutions in 1 country.

Inmaculada YruelaEstación Experimental de Aula Dei, Consejo Superior de Investigaciones Científicas, Avda, Montañana, 1005, Zaragoza 50059, Spain. yruela@eead.csic.es
Bruno Contreras-Moreira
Estación Experimental de Aula Dei · ESUniversidad de Zaragoza · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe intrinsically unstructured state of some proteins, observed in all living organisms, is essential for basic cellular functions. In this field the available information from plants is limited but it has been reached a point where these proteins can be comprehensively classified on the basis of disorder, function and evolution.

resultsOur analysis of plant genomes confirms that nuclear-encoded proteins follow the same trend than other multi-cellular eukaryotes; however, chloroplast- and mitochondria- encoded proteins conserve the patterns of Archaea and Bacteria, in agreement with their phylogenetic origin. Based on current knowledge about gene transference from the chloroplast to the nucleus, we report a strong correlation between the rate of disorder of transferred and nuclear-encoded proteins, even for polypeptides that play functional roles back in the chloroplast. We further investigate this trend by reviewing the set of chloroplast ribosomal proteins, one of the most representative transferred gene clusters, finding that the ribosomal large subunit, assembled from a majority of nuclear-encoded proteins, is clearly more unstructured than the small one, which integrates mostly plastid-encoded proteins.

conclusionsOur observations suggest that the evolutionary dynamics of the plant nucleus adds disordered segments to genes alike, regardless of their origin, with the notable exception of proteins currently encoded in both genomes, probably due to functional constraints.

Indexed as

Genome, PlantAmino Acid SequenceCell NucleusChloroplast ProteinsChloroplastsComputational BiologyEvolution, MolecularMitochondriaMitochondrial ProteinsNuclear ProteinsPhylogenyPlant ProteinsPlantsProtein TransportRibosomal ProteinsChloroplast ProteinsMitochondrial ProteinsNuclear ProteinsPlant ProteinsRibosomal Proteins

Identifiers

PMID22970728
PMCPMC3460767
OpenAlexW2046875882

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.