Evidence map›Paper›PMID 34201246›Full record

ArticleInternational journal of molecular sciences2021

Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14.

Nikoletta Murvai, Lajos Kalmar, Beata Szabo, Eva Schad, András Micsonai, József Kardos, László Buday, Kyou-Hoon Han, Peter Tompa, Agnes Tantos

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Foods (Basel, Switzerland) · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022
    Review
  8. Article
  9. 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

10 authors.

Nikoletta MurvaiResearch Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.
Lajos KalmarResearch Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.
Beata SzaboResearch Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.
Eva SchadResearch Centre for Natural Sciences, Institute of Enzymology, 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 0000-0002-2135-2932
László BudayResearch Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.
Kyou-Hoon HanBiomedical Translational Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Korea.
Peter TompaResearch Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.ORCID 0000-0001-8042-9939
Agnes TantosResearch Centre for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary.

Funding

Hungarian Academy of Sciences Bolyai János ScholarshipHungarian Academy of Sciences Lendület GrantKorea Research Council of Fundamental Science and Technology 2010-88343National Research Council of Science and Technology NTM2231712National Research, Development and Innovation Office, Hungary K120391National Research, Development and Innovation Office, Hungary K124670National Research, Development and Innovation Office, Hungary K125340National Research, Development and Innovation Office, Hungary K131702National Research, Development and Innovation Office, Hungary KH125597National Research, Development and Innovation Office, Hungary PD135510Research Foundation Flanders G.0029.12SOLEIL Synchrotron, France 20171582SOLEIL Synchrotron, France 20180805SOLEIL Synchrotron, France 20181890
6 · The paper itself

Abstract

Disordered plant chaperones play key roles in helping plants survive in harsh conditions, and they are indispensable for seeds to remain viable. Aside from well-known and thoroughly characterized globular chaperone proteins, there are a number of intrinsically disordered proteins (IDPs) that can also serve as highly effective protecting agents in the cells. One of the largest groups of disordered chaperones is the group of dehydrins, proteins that are expressed at high levels under different abiotic stress conditions, such as drought, high temperature, or osmotic stress. Dehydrins are characterized by the presence of different conserved sequence motifs that also serve as the basis for their categorization. Despite their accepted importance, the exact role and relevance of the conserved regions have not yet been formally addressed. Here, we explored the involvement of each conserved segment in the protective function of the intrinsically disordered stress protein (IDSP)

Indexed as

Stress, PhysiologicalArabidopsisArabidopsis ProteinsIntrinsically Disordered ProteinsMolecular ChaperonesOsmotic PressurePlant ProteinsArabidopsis ProteinsERD14 protein, ArabidopsisIntrinsically Disordered ProteinsMolecular ChaperonesPlant ProteinsCD spectroscopydehydrinearly response to dehydrationheat stressintrinsic structural disorderLEA proteinplant chaperonestructure-function relationship

Identifiers

PMID34201246
PMCPMC8230022

What OpenQuestion holds

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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.