Evidence map›Paper›PMID 22791833›Full record

ArticleJournal of experimental botany2012

The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation.

Jan Petersen, Sylvia K Eriksson, Pia Harryson, Steffen Pierog, Thomas Colby, Dorothea Bartels, Horst Röhrig

Open access · greenAbstract read
In one paragraph

Article in Journal of experimental botany, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
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  7. International journal of molecular sciences · 2019
    Article
  8. Article
  9. Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019
    Review
  10. Article
  11. Article
  12. Article
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  16. Article
  17. Drying without senescence in resurrection plants.Frontiers in plant science · 2014
    Review
  18. Review
  19. 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

7 authors at 3 institutions in 2 countries.

Jan PetersenInstitute of Molecular Physiology and Biotechnology of Plants (IMBIO), University of Bonn, Kirschallee 1, 53115 Bonn, Germany.
Sylvia K Eriksson
Pia Harryson
Steffen Pierog
Thomas Colby
Dorothea Bartels
Horst Röhrig
University of Bonn · DEStockholm University · SEMax Planck Institute for Plant Breeding Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The late embryogenesis abundant (LEA)-like protein CDeT11-24 is one of the major desiccation-related phosphoproteins of the resurrection plant Craterostigma plantagineum. In this study, it was shown that CDeT11-24 is mostly intrinsically disordered and protects two different enzymes, citrate synthase and lactate dehydrogenase, against damaging effects caused by desiccation. Lipid-binding assays revealed that CDeT11-24 is able to interact with phosphatidic acid, although electrostatic repulsion was expected due to the overall negative net charge of the protein under the tested physiological conditions. CDeT11-24 carries an N-terminal lysine-rich sequence, which is predicted to form an amphipathic α-helix. Analysis of the truncated CDeT11-24 protein identified this region to be responsible for both activities: enzyme protection and phosphatidic acid interaction. Possible functions of the CDeT11-24 protein are discussed in the context of desiccation tolerance.

Indexed as

Amino Acid MotifsAmino Acid SequenceCitrate (si)-SynthaseCraterostigmaDesiccationEnzyme AssaysL-Lactate DehydrogenaseModels, BiologicalMutagenesis, Site-DirectedPhosphatidic AcidsPlant LeavesPlant ProteinsRecombinant ProteinsSequence AlignmentSignal TransductionWaterCitrate (si)-Synthaselate embryogenesis abundant protein, plantL-Lactate DehydrogenasePhosphatidic AcidsPlant ProteinsRecombinant ProteinsWater

Identifiers

PMID22791833
PMCPMC3428009
OpenAlexW2172172715

What OpenQuestion holds

Textmetadata
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.