Evidence map›Paper›PMID 28443615›Full record

ArticleScientific reports2017

The plant cell-wall enzyme AtXTH3 catalyses covalent cross-linking between cellulose and cello-oligosaccharide.

Naoki Shinohara, Naoki Sunagawa, Satoru Tamura, Ryusuke Yokoyama, Minoru Ueda, Kiyohiko Igarashi, Kazuhiko Nishitani

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
17.7field-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

36 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. AtGAP1 Promotes the Resistance toInternational journal of molecular sciences · 2022
    Article
  8. Building an extensible cell wall.Plant physiology · 2022
    Article
  9. Review
  10. Review
  11. Review
  12. The Xyloglucan Endotransglucosylase/Hydrolase GeneInternational journal of molecular sciences · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

7 authors at 2 institutions in 1 country.

Naoki ShinoharaPlant Cell Wall Biology Laboratory, Graduate School of Life Sciences, Tohoku University, Aoba-Ku, Sendai, 980-8578, Japan.
Naoki SunagawaDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-Ku, Tokyo, 113-8657, Japan.
Satoru TamuraLaboratory of Organic Chemistry, Department of Chemistry, Graduate School of Science, Tohoku University, Aoba-Ku, Sendai 980-8578, Japan.
Ryusuke YokoyamaPlant Cell Wall Biology Laboratory, Graduate School of Life Sciences, Tohoku University, Aoba-Ku, Sendai, 980-8578, Japan.
Minoru UedaLaboratory of Organic Chemistry, Department of Chemistry, Graduate School of Science, Tohoku University, Aoba-Ku, Sendai 980-8578, Japan.
Kiyohiko IgarashiDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-Ku, Tokyo, 113-8657, Japan.
Kazuhiko NishitaniPlant Cell Wall Biology Laboratory, Graduate School of Life Sciences, Tohoku University, Aoba-Ku, Sendai, 980-8578, Japan.
Tohoku University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellulose is an economically important material, but routes of its industrial processing have not been fully explored. The plant cell wall - the major source of cellulose - harbours enzymes of the xyloglucan endotransglucosylase/hydrolase (XTH) family. This class of enzymes is unique in that it is capable of elongating polysaccharide chains without the requirement for activated nucleotide sugars (e.g., UDP-glucose) and in seamlessly splitting and reconnecting chains of xyloglucan, a naturally occurring soluble analogue of cellulose. Here, we show that a recombinant version of AtXTH3, a thus far uncharacterized member of the Arabidopsis XTH family, catalysed the transglycosylation between cellulose and cello-oligosaccharide, between cellulose and xyloglucan-oligosaccharide, and between xyloglucan and xyloglucan-oligosaccharide, with the highest reaction rate observed for the latter reaction. In addition, this enzyme formed cellulose-like insoluble material from a soluble cello-oligosaccharide in the absence of additional substrates. This newly found activity (designated "cellulose endotransglucosylase," or CET) can potentially be involved in the formation of covalent linkages between cellulose microfibrils in the plant cell wall. It can also comprise a new route of industrial cellulose functionalization.

Indexed as

ArabidopsisArabidopsis ProteinsBiocatalysisCelluloseCell WallCross-Linking ReagentsGlycosylationGlycosyltransferasesHydrogen-Ion ConcentrationKineticsOligosaccharidesPlant CellsSubstrate SpecificityTemperatureArabidopsis ProteinsCelluloseCross-Linking ReagentsGlycosyltransferasesOligosaccharidesXTH3 protein, Arabidopsis

Identifiers

PMID28443615
PMCPMC5405413
OpenAlexW2608527701

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.