Evidence map›Paper›PMID 29109147›Full record

ArticleThe Journal of biological chemistry2017

Structural and dynamical characterization of the pH-dependence of the pectin methylesterase-pectin methylesterase inhibitor complex.

Fabien Sénéchal, Olivier Habrylo, Ludivine Hocq, Jean-Marc Domon, Paulo Marcelo, Valérie Lefebvre, Jérôme Pelloux, Davide Mercadante

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Genome-Wide Analyses and Expression Profiling ofPlants (Basel, Switzerland) · 2025
    Article
  4. Article
  5. Article
  6. Auxin as an architect of the pectin matrix.Journal of experimental botany · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. 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

8 authors at 3 institutions in 2 countries.

Fabien SénéchalFrom the EA3900-BIOPI Biologie des Plantes et Innovation SFR Condorcet FR CNRS 3417, Université de Picardie, 80039 Amiens, France.
Olivier HabryloFrom the EA3900-BIOPI Biologie des Plantes et Innovation SFR Condorcet FR CNRS 3417, Université de Picardie, 80039 Amiens, France.
Ludivine HocqFrom the EA3900-BIOPI Biologie des Plantes et Innovation SFR Condorcet FR CNRS 3417, Université de Picardie, 80039 Amiens, France.
Jean-Marc DomonFrom the EA3900-BIOPI Biologie des Plantes et Innovation SFR Condorcet FR CNRS 3417, Université de Picardie, 80039 Amiens, France.
Paulo Marcelothe Plateforme ICAP, Centre Universitaire de Recherche en Santé, Université de Picardie Jules Verne, 80054 Amiens, France.
Valérie LefebvreFrom the EA3900-BIOPI Biologie des Plantes et Innovation SFR Condorcet FR CNRS 3417, Université de Picardie, 80039 Amiens, France.
Jérôme PellouxFrom the EA3900-BIOPI Biologie des Plantes et Innovation SFR Condorcet FR CNRS 3417, Université de Picardie, 80039 Amiens, France, jerome.pelloux@u-picardie.fr.
Davide Mercadantethe Heidelberg Institute for Theoretical Studies, Heidelberg-HITS, 16920 Heidelberg, Germany, and d.mercadante@bioc.uzh.ch.
Biologie des Plantes et Innovation · FRHeidelberg University · DEUniversité de Picardie Jules Verne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pectin methylesterases (PMEs) catalyze the demethylesterification of pectin, one of the main polysaccharides in the plant cell wall, and are of critical importance in plant development. PME activity generates highly negatively charged pectin and mutates the physiochemical properties of the plant cell wall such that remodeling of the plant cell can occur. PMEs are therefore tightly regulated by proteinaceous inhibitors (PMEIs), some of which become active upon changes in cellular pH. Nevertheless, a detailed picture of how this pH-dependent inhibition of PME occurs at the molecular level is missing. Herein, using an interdisciplinary approach that included homology modeling, MD simulations, and biophysical and biochemical characterizations, we investigated the molecular basis of PME3 inhibition by PMEI7 in

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCarboxylic Ester HydrolasesCell MembraneCell WallGene Expression Regulation, PlantHydrogen-Ion ConcentrationPectinsPlant ProteinsProtein Interaction Domains and MotifsArabidopsis ProteinsCarboxylic Ester Hydrolasespectinesterasepectin methylesterase 3, ArabidopsisPectinsPlant ProteinsPME17 protein, Arabidopsismolecular dynamicsmolecular modelingpH regulationplant biochemistryplant cell wallplant physiologyprotein–protein interaction

Identifiers

PMID29109147
PMCPMC5766959
OpenAlexW2767545044

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.