Evidence map›Paper›PMID 35000024›Full record

ReviewJournal of plant research2022

Reconsidering the function of the xyloglucan endotransglucosylase/hydrolase family.

Konan Ishida, Ryusuke Yokoyama

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of plant research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
20.4field-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

55 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Functional Analysis of the GH16 Domain-ContainingPlants (Basel, Switzerland) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Xyloglucan Endotransglycosylase/Hydrolase Downregulation IncreasesInternational journal of molecular sciences · 2025
    Article
  13. Article
  14. Article
  15. Identification of novel genomic regions associated with yield-related traits in cowpea (Molecular breeding : new strategies in plant improvement · 2025
    Article
  16. Article
  17. Article
  18. Overexpression ofInternational journal of molecular sciences · 2025
    Article
  19. Article
  20. 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

2 authors at 2 institutions in 2 countries.

Konan IshidaDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1QE, UK.ORCID http://orcid.org/0000-0003-4475-4886
Ryusuke YokoyamaGraduate School of Life Sciences, Tohoku University, Sendai, 980-8578, Japan. ryusuke.yokoyama.d6@tohoku.ac.jp.ORCID http://orcid.org/0000-0003-0326-0433
Tohoku University · JPUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants possess an outer cell layer called the cell wall. This matrix comprises various molecules, such as polysaccharides and proteins, and serves a wide array of physiologically important functions. This structure is not static but rather flexible in response to the environment. One of the factors responsible for this plasticity is the xyloglucan endotransglucosylase/hydrolase (XTH) family, which cleaves and reconnects xyloglucan molecules. Since xyloglucan molecules have been hypothesised to tether cellulose microfibrils forming the main load-bearing network in the primary cell wall, XTHs have been thought to play a central role in cell wall loosening for plant cell expansion. However, multiple lines of recent evidence have questioned this classic model. Nevertheless, reverse genetic analyses have proven the biological importance of XTHs; therefore, a major challenge at present is to reconsider the role of XTHs in planta. Recent advances in analytical techniques have allowed for gathering rich information on the structure of the primary cell wall. Thus, the integration of accumulated knowledge in current XTH studies may offer a turning point for unveiling the precise functions of XTHs. In the present review, we redefine the biological function of the XTH family based on the recent architectural model of the cell wall. We highlight three key findings regarding this enzyme family: (1) XTHs are not strictly required for cell wall loosening during plant cell expansion but play vital roles in response to specific biotic or abiotic stresses; (2) in addition to their transglycosylase activity, the hydrolase activity of XTHs is involved in physiological benefits; and (3) XTHs can recognise a wide range of polysaccharides other than xyloglucans.

Indexed as

Cell WallGlycosyltransferasesHydrolasesPolysaccharidesGlycosyltransferasesHydrolasesPolysaccharidesxyloglucan - xyloglucosyltransferaseCAZyCell wall architectureGH16Hydrolase (XTH)Plant cell wallXyloglucanXyloglucan endotransglucosylase

Identifiers

PMID35000024
OpenAlexW4205472758

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.