Evidence map›Paper›PMID 32784707›Full record

ArticleCells2020

Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14.

Nikoletta Murvai, Lajos Kalmar, Bianka Szalaine Agoston, Beata Szabo, Agnes Tantos, Gyorgy Csikos, András Micsonai, József Kardos, Didier Vertommen, Phuong N Nguyen and 7 more

Abstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. A YSK-Type Dehydrin fromInternational journal of molecular sciences · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14.International journal of molecular sciences · 2021
    Article
  9. Article
  10. 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

17 authors.

Nikoletta MurvaiInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Lajos KalmarInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Bianka Szalaine AgostonInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0002-9666-8608
Beata SzaboInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Agnes TantosInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0003-1273-9841
Gyorgy CsikosDepartment of General Zoology, Eötvös Loránd University, 1117 Budapest, Hungary.
András MicsonaiELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, Eötvös Loránd University, 1117 Budapest, Hungary.
József KardosELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, Eötvös Loránd University, 1117 Budapest, Hungary.ORCID 0000-0003-3518-5757
Didier VertommenFaculty of Medicine and de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium.ORCID 0000-0001-7648-8282
Phuong N NguyenStructural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium.
Nevena HristozovaStructural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium.
Andras LangMTA-ELTE Protein Modelling Research Group and Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös L. University, 1117 Budapest, Hungary.
Denes KovacsStructural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium.
Laszlo BudayInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Kyou-Hoon HanGene Editing Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea.
Andras PerczelMTA-ELTE Protein Modelling Research Group and Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös L. University, 1117 Budapest, Hungary.
Peter TompaInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Details of the functional mechanisms of intrinsically disordered proteins (IDPs) in living cells is an area not frequently investigated. Here, we dissect the molecular mechanism of action of an IDP in cells by detailed structural analyses based on an in-cell nuclear magnetic resonance experiment. We show that the ID stress protein (IDSP)

Indexed as

Heat-Shock ResponseArabidopsisArabidopsis ProteinsEscherichia coliIntrinsically Disordered ProteinsMicrobial ViabilityMicroorganisms, Genetically-ModifiedMolecular ChaperonesProtein BindingProtein DomainsProteomeArabidopsis ProteinsERD14 protein, ArabidopsisIntrinsically Disordered ProteinsMolecular ChaperonesProteomecell protectionchaperoneclient proteinin-cell NMRintrinsic structural disorderpre-structured motif

Identifiers

PMID32784707
PMCPMC7465474

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.