Evidence map›Paper›PMID 24748166›Full record

ArticlePloS one2014

Acetobixan, an inhibitor of cellulose synthesis identified by microbial bioprospecting.

Ye Xia, Lei Lei, Chad Brabham, Jozsef Stork, James Strickland, Adam Ladak, Ying Gu, Ian Wallace, Seth DeBolt

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

12 citing papers in PubMed, 19 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
    Article
  2. Article
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
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  10. Article
  11. Plant chemical biology: are we meeting the promise?Frontiers in plant science · 2014
    Article
  12. Review
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

9 authors at 5 institutions in 1 country.

Ye XiaDepartment of Horticulture, University of Kentucky, Lexington, Kentucky, United States of America.
Lei LeiDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, State College, Pennsylvania, United States of America.
Chad BrabhamDepartment of Horticulture, University of Kentucky, Lexington, Kentucky, United States of America.
Jozsef StorkDepartment of Horticulture, University of Kentucky, Lexington, Kentucky, United States of America.
James StricklandUnited State Department of Agriculture Forage-Animal Production Research Unit, University of Kentucky Campus, USDA-ARS, Lexington, Kentucky, United States of America.
Adam LadakWaters Waters Corporation, Milford, Massachusetts, United States of America.
Ying GuDepartment of Biochemistry and Molecular Biology, Pennsylvania State University, State College, Pennsylvania, United States of America.
Ian WallaceDepartment of Biochemistry and Molecular Biology, University of Nevada, Reno, Nevada, United States of America.
Seth DeBoltDepartment of Horticulture, University of Kentucky, Lexington, Kentucky, United States of America.
University of Kentucky · USPennsylvania State University · USUnited States Department of State · USUniversity of Nevada, Reno · USWaters (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, cellulose biosynthesis is an essential process for anisotropic growth and therefore is an ideal target for inhibition. Based on the documented utility of small-molecule inhibitors to dissect complex cellular processes we identified a cellulose biosynthesis inhibitor (CBI), named acetobixan, by bio-prospecting among compounds secreted by endophytic microorganisms. Acetobixan was identified using a drug-gene interaction screen to sift through hundreds of endophytic microbial secretions for one that caused synergistic reduction in root expansion of the leaky AtcesA6prc1-1 mutant. We then mined this microbial secretion for compounds that were differentially abundant compared with Bacilli that failed to mimic CBI action to isolate a lead pharmacophore. Analogs of this lead compound were screened for CBI activity, and the most potent analog was named acetobixan. In living Arabidopsis cells visualized by confocal microscopy, acetobixan treatment caused CESA particles localized at the plasma membrane (PM) to rapidly re-localize to cytoplasmic vesicles. Acetobixan inhibited 14C-Glc uptake into crystalline cellulose. Moreover, cortical microtubule dynamics were not disrupted by acetobixan, suggesting specific activity towards cellulose synthesis. Previous CBI resistant mutants such as ixr1-2, ixr2-1 or aegeus were not cross resistant to acetobixan indicating that acetobixan targets a different aspect of cellulose biosynthesis.

Indexed as

MicrobiologyAcetamidesBase SequenceCelluloseChromatography, LiquidDNA PrimersMass SpectrometryMicroscopy, ConfocalRNA, Ribosomal, 16SAcetamidesCelluloseDNA PrimersN-(2-methoxybenzyl)-2-(phenylthio)acetamideRNA, Ribosomal, 16S

Identifiers

PMID24748166
PMCPMC3991599
OpenAlexW2129926470

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.