Evidence map›Paper›PMID 32327535›Full record

ArticleThe Plant cell2020

Endosidin20 Targets the Cellulose Synthase Catalytic Domain to Inhibit Cellulose Biosynthesis.

Lei Huang, Xiaohui Li, Weiwei Zhang, Nolan Ung, Nana Liu, Xianglin Yin, Yong Li, Robert E Mcewan, Brian Dilkes, Mingji Dai and 4 more

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in The Plant cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. A fungal natural product that inhibits plant cellulose biosynthesis by disrupting cellulose synthase complexes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Frontiers in plant science · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 2 institutions in 2 countries.

Lei HuangDepartment of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0002-4288-2430
Xiaohui LiDepartment of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0002-0012-8018
Weiwei ZhangCenter for Plant Biology, Purdue University, West Lafayette, Indiana 47907 zhang150@purdue.edu.ORCID 0000-0002-4754-6241
Nolan UngDepartment of Botany and Plant Sciences, University of California, Riverside, California 92521.ORCID 0000-0002-1162-2185
Nana LiuDepartment of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0001-9745-8525
Xianglin YinDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0003-4549-0827
Yong LiDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0003-1463-6854
Robert E McewanCenter for Plant Biology, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0002-4520-4643
Brian DilkesCenter for Plant Biology, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0003-2799-954X
Mingji DaiDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0001-7956-6426
Glenn R HicksDepartment of Botany and Plant Sciences, University of California, Riverside, California 92521.ORCID 0000-0002-2502-7782
Natasha V RaikhelDepartment of Botany and Plant Sciences, University of California, Riverside, California 92521.ORCID 0000-0002-9078-8940
Christopher J StaigerDepartment of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907.ORCID 0000-0003-2321-1671
Chunhua ZhangDepartment of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907 zhang150@purdue.edu.ORCID 0000-0003-0985-7185
Purdue University West Lafayette · USUniversity of California, Riverside · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant cellulose is synthesized by rosette-structured cellulose synthase (CESA) complexes (CSCs). Each CSC is composed of multiple subunits of CESAs representing three different isoforms. Individual CESA proteins contain conserved catalytic domains for catalyzing cellulose synthesis, other domains such as plant-conserved sequences, and class-specific regions that are thought to facilitate complex assembly and CSC trafficking. Because of the current lack of atomic-resolution structures for plant CSCs or CESAs, the molecular mechanism through which CESA catalyzes cellulose synthesis and whether its catalytic activity influences efficient CSC transport at the subcellular level remain unknown. Here, by performing chemical genetic analyses, biochemical assays, structural modeling, and molecular docking, we demonstrate that Endosidin20 (ES20) targets the catalytic site of CESA6 in Arabidopsis (

Indexed as

ArabidopsisArabidopsis ProteinsBacterial ProteinsCatalytic DomainCelluloseDose-Response Relationship, DrugEnzyme InhibitorsFluorescence Recovery After PhotobleachingGlucosyltransferasesLuminescent ProteinsMolecular Docking SimulationMutationPlants, Genetically ModifiedProtein ConformationArabidopsis ProteinsBacterial ProteinsCellulosecellulose synthaseEnzyme InhibitorsGlucosyltransferasesLuminescent ProteinsPRC1 protein, Arabidopsisyellow fluorescent protein, Bacteria

Identifiers

PMID32327535
PMCPMC7346566
OpenAlexW3019726833

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.