Evidence map›Paper›PMID 29690573›Full record

ReviewBiomolecules2018

Protein⁻Phospholipid Interaction Motifs: A Focus on Phosphatidic Acid.

Emeline Tanguy, Nawal Kassas, Nicolas Vitale

Abstract readReview
In one paragraph

Review in Biomolecules, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Nir2 crystal structures reveal a phosphatidic acid-sensing mechanism at ER-PM contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  12. The MIT domain of chitin synthase 1 from the oomyceteBiochemistry and biophysics reports · 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

3 authors.

Emeline TanguyInstitut des Neurosciences Cellulaires et Intégratives, CNRS UPR3212 and Université de Strasbourg, 67000 Strasbourg, France. emeline.tanguy@etu.unistra.fr.
Nawal KassasInstitut des Neurosciences Cellulaires et Intégratives, CNRS UPR3212 and Université de Strasbourg, 67000 Strasbourg, France. Nawal.Kassas@hotmail.com.
Nicolas VitaleInstitut des Neurosciences Cellulaires et Intégratives, CNRS UPR3212 and Université de Strasbourg, 67000 Strasbourg, France. vitalen@inci-cnrs.unistra.fr.ORCID 0000-0002-4752-4907

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular membranes are composed of thousands of different lipids usually maintained within a narrow range of concentrations. In addition to their well-known structural and metabolic roles, signaling functions for many lipids have also emerged over the last two decades. The latter largely depend on the ability of particular classes of lipids to interact specifically with a great variety of proteins and to regulate their localization and activity. Among these lipids, phosphatidic acid (PA) plays a unique role in a large repertoire of cellular activities, most likely in relation to its unique biophysical properties. However, until recently, only incomplete information was available to model the interaction between PA and its protein partners. The development of new liposome-based assays as well as molecular dynamic simulation are now providing novel information. We will review the different factors that have shown to modulate the capacity of PA to interact with specific domains in target proteins.

Indexed as

AnimalsCell MembraneHumansPhosphatidic AcidsPhospholipase DProtein BindingStatic ElectricityPhosphatidic AcidsPhospholipase Dinteraction motiflipid bindingmembranephosphatidic acidphospholipase D

Identifiers

PMID29690573
PMCPMC6022864

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.