Evidence map›Paper›PMID 33260399›Full record

ReviewMolecules (Basel, Switzerland)2020

Plant Xyloglucan Xyloglucosyl Transferases and the Cell Wall Structure: Subtle but Significant.

Barbora Stratilová, Stanislav Kozmon, Eva Stratilová, Maria Hrmova

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
7.4field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
  7. Review
  8. Article
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  14. Review
  15. Plant direct · 2023
    Article
  16. BREVIPEDICELLUS Positively Regulates Salt-Stress Tolerance inInternational journal of molecular sciences · 2023
    Article
  17. Review
  18. 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

4 authors at 2 institutions in 3 countries.

Barbora StratilováInstitute of Chemistry, Centre for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538 Bratislava, Slovakia.ORCID 0000-0001-6123-9857
Stanislav KozmonInstitute of Chemistry, Centre for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538 Bratislava, Slovakia.ORCID 0000-0002-0946-3453
Eva StratilováInstitute of Chemistry, Centre for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538 Bratislava, Slovakia.ORCID 0000-0002-8753-9820
Maria HrmovaSchool of Life Science, Huaiyin Normal University, Huai'an 223300, China.ORCID 0000-0002-3545-0605
Institute of Chemistry of the Slovak Academy of Sciences · SKHuaiyin Normal University · CN

Funding

Australian Research Council DP120100900VEGA 2/0137/20
6 · The paper itself

Abstract

Plant xyloglucan xyloglucosyl transferases or xyloglucan endo-transglycosylases (XET; EC 2.4.1.207) catalogued in the glycoside hydrolase family 16 constitute cell wall-modifying enzymes that play a fundamental role in the cell wall expansion and re-modelling. Over the past thirty years, it has been established that XET enzymes catalyse homo-transglycosylation reactions with xyloglucan (XG)-derived substrates and hetero-transglycosylation reactions with neutral and charged donor and acceptor substrates other than XG-derived. This broad specificity in XET isoforms is credited to a high degree of structural and catalytic plasticity that has evolved ubiquitously in algal, moss, fern, basic Angiosperm, monocot, and eudicot enzymes. These XET isoforms constitute gene families that are differentially expressed in tissues in time- and space-dependent manners during plant growth and development, and in response to biotic and abiotic stresses. Here, we discuss the current state of knowledge of broad specific plant XET enzymes and how their inherently carbohydrate-based transglycosylation reactions tightly link with structural diversity that underlies the complexity of plant cell walls and their mechanics. Based on this knowledge, we conclude that multi- or poly-specific XET enzymes are widespread in plants to allow for modifications of the cell wall structure in muro, a feature that implements the multifaceted roles in plant cells.

Indexed as

BiocatalysisCell WallGlycosylationGlycosyltransferasesPlantsSubstrate SpecificityGlycosyltransferasesxyloglucan - xyloglucosyltransferaseenzyme structure and functionGH16 familyhomo- and hetero-transglycosylation reactionsmolecular modelling and simulationsplant cell walls loosening and re-modelling

Identifiers

PMID33260399
PMCPMC7729885
OpenAlexW3107298451

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.