Evidence map›Paper›PMID 32204351›Full record

ReviewInternational journal of molecular sciences2020

Common Functions of Disordered Proteins across Evolutionary Distant Organisms.

Arndt Wallmann, Christopher Kesten

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 46 citations in OpenAlex.

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  15. JmjC Family of Histone Demethylases Form Nuclear Condensates.International journal of molecular sciences · 2022
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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.

Arndt WallmannMedical Research Council Toxicology Unit, University of Cambridge, Cambridge CB2 1QR, UK.ORCID 0000-0002-7003-5079
Christopher KestenDepartment of Biology, ETH Zurich, 8092 Zurich, Switzerland.ORCID 0000-0003-0794-2415
ETH Zurich · CHUniversity of Cambridge · GB

Funding

ETH Zürich Foundation SEED-05 19-2Peter and Traudl Engelhorn Stiftung no grant numberRofonda Stiftung Vaduz SEED-05 19-2
6 · The paper itself

Abstract

Intrinsically disordered proteins and regions typically lack a well-defined structure and thus fall outside the scope of the classic sequence-structure-function relationship. Hence, classic sequence- or structure-based bioinformatic approaches are often not well suited to identify homology or predict the function of unknown intrinsically disordered proteins. Here, we give selected examples of intrinsic disorder in plant proteins and present how protein function is shared, altered or distinct in evolutionary distant organisms. Furthermore, we explore how examining the specific role of disorder across different phyla can provide a better understanding of the common features that protein disorder contributes to the respective biological mechanism.

Indexed as

Evolution, MolecularAnimalsGene Expression RegulationHumansIntrinsically Disordered ProteinsPlant ProteinsPlantsProtein ConformationProtein FoldingIntrinsically Disordered Proteinslate embryogenesis abundant protein, plantPlant Proteinsfunctional comparisonintrinsically disordered proteinsplantsprotein function

Identifiers

PMID32204351
PMCPMC7139818
OpenAlexW3011986164

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.