Evidence map›Paper›PMID 23592721›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Tertiary model of a plant cellulose synthase.

Latsavongsakda Sethaphong, Candace H Haigler, James D Kubicki, Jochen Zimmer, Dario Bonetta, Seth DeBolt, Yaroslava G Yingling

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
31.9field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 169 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
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  4. Article
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  7. CslA and GlxA fromApplied and environmental microbiology · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. 2-NBDG Uptake inFrontiers in plant science · 2023
    Article
  14. Article
  15. Review
  16. Species-Specific Gene Expansion of theFrontiers in plant science · 2022
    Article
  17. Article
  18. Review
  19. Review
  20. Structure ofProceedings of the National Academy of Sciences of the United States of America · 2021
    Article

20 more citing papers are in PubMed but not listed here.

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

7 authors at 6 institutions in 4 countries.

Latsavongsakda SethaphongDepartment of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Candace H Haigler
James D Kubicki
Jochen Zimmer
Dario Bonetta
Seth DeBolt
Yaroslava G Yingling
Materials Science & Engineering · AUNorth Carolina State University · USPennsylvania State University · USUniversity of Kentucky · USUniversity of Ontario Institute of Technology · CAUniversity of Virginia · US

Funding

Mechanism of Cellulose Synthesis and Transport Across Biological MembranesR01GM101001 · NIGMS · UNIVERSITY OF VIRGINIA · PI ZIMMER, JOCHEN · 2012 to 2021
$3.7M
NIGMS NIH HHS 1R01GM101001NIGMS NIH HHS R01 GM101001
6 · The paper itself

Abstract

A 3D atomistic model of a plant cellulose synthase (CESA) has remained elusive despite over forty years of experimental effort. Here, we report a computationally predicted 3D structure of 506 amino acids of cotton CESA within the cytosolic region. Comparison of the predicted plant CESA structure with the solved structure of a bacterial cellulose-synthesizing protein validates the overall fold of the modeled glycosyltransferase (GT) domain. The coaligned plant and bacterial GT domains share a six-stranded β-sheet, five α-helices, and conserved motifs similar to those required for catalysis in other GT-2 glycosyltransferases. Extending beyond the cross-kingdom similarities related to cellulose polymerization, the predicted structure of cotton CESA reveals that plant-specific modules (plant-conserved region and class-specific region) fold into distinct subdomains on the periphery of the catalytic region. Computational results support the importance of the plant-conserved region and/or class-specific region in CESA oligomerization to form the multimeric cellulose-synthesis complexes that are characteristic of plants. Relatively high sequence conservation between plant CESAs allowed mapping of known mutations and two previously undescribed mutations that perturb cellulose synthesis in Arabidopsis thaliana to their analogous positions in the modeled structure. Most of these mutation sites are near the predicted catalytic region, and the confluence of other mutation sites supports the existence of previously undefined functional nodes within the catalytic core of CESA. Overall, the predicted tertiary structure provides a platform for the biochemical engineering of plant CESAs.

Indexed as

Models, MolecularArabidopsisBacteriaComputational BiologyCytosolGlucosyltransferasesGossypiumMutationPhenotypeProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, Tertiarycellulose synthaseGlucosyltransferases

Identifiers

PMID23592721
PMCPMC3645513
OpenAlexW2046327981

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.