Evidence map›Paper›PMID 30195939›Full record

ArticleBiophysical journal2018

Folding and Lipid Composition Determine Membrane Interaction of the Disordered Protein COR15A.

Carlos Navarro-Retamal, Anne Bremer, Helgi I Ingólfsson, Jans Alzate-Morales, Julio Caballero, Anja Thalhammer, Wendy González, Dirk K Hincha

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

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  13. Similar Yet Different-Structural and Functional Diversity amongInternational journal of molecular sciences · 2020
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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

8 authors at 4 institutions in 3 countries.

Carlos Navarro-RetamalCenter for Bioinformatics and Molecular Simulations, Universidad de Talca, Casilla, Talca, Chile.
Anne BremerMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam, Germany.
Helgi I IngólfssonGroningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, AG Groningen, The Netherlands.
Jans Alzate-MoralesCenter for Bioinformatics and Molecular Simulations, Universidad de Talca, Casilla, Talca, Chile.
Julio CaballeroCenter for Bioinformatics and Molecular Simulations, Universidad de Talca, Casilla, Talca, Chile.
Anja ThalhammerPhysikalische Biochemie, Universität Potsdam, Potsdam, Germany.
Wendy GonzálezCenter for Bioinformatics and Molecular Simulations, Universidad de Talca, Casilla, Talca, Chile; Millennium Nucleus of Ion Channels-Associated Diseases (MiNICAD), Universidad de Talca, Casilla, Talca, Chile.
Dirk K HinchaMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam, Germany. Electronic address: hincha@mpimp-golm.mpg.de.
University of Talca · CLMax Planck Institute of Molecular Plant Physiology · DEUniversity of Groningen · NLUniversity of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants from temperate climates, such as the model plant Arabidopsis thaliana, are challenged with seasonal low temperatures that lead to increased freezing tolerance in fall in a process termed cold acclimation. Among other adaptations, this involves the accumulation of cold-regulated (COR) proteins, such as the intrinsically disordered chloroplast-localized protein COR15A. Together with its close homolog COR15B, it stabilizes chloroplast membranes during freezing. COR15A folds into amphipathic α-helices in the presence of high concentrations of low-molecular-mass crowders or upon dehydration. Under these conditions, the (partially) folded protein binds peripherally to membranes. In our study, we have used coarse-grained molecular dynamics simulations to elucidate the details of COR15A-membrane binding and its effects on membrane structure and dynamics. Simulation results indicate that at least partial folding of COR15A and the presence of highly unsaturated galactolipids in the membranes are necessary for efficient membrane binding. The bound protein is stabilized on the membrane by interactions of charged and polar amino acids with galactolipid headgroups and by interactions of hydrophobic amino acids with the upper part of the fatty acyl chains. Experimentally, the presence of liposomes made from a mixture of lipids mimicking chloroplast membranes induces additional folding in COR15A under conditions of partial dehydration, in agreement with the simulation results.

Indexed as

Protein FoldingArabidopsisArabidopsis ProteinsCell MembraneGlycolipidsLipid BilayersMolecular Dynamics SimulationProtein BindingProtein ConformationArabidopsis ProteinsCOR15 protein, ArabidopsisGlycolipidsLipid Bilayers

Identifiers

PMID30195939
PMCPMC6139882
OpenAlexW2887932614

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.