Evidence map›Paper›PMID 12011358›Full record

ArticlePlant physiology2002

Glucosylation activity and complex formation of two classes of reversibly glycosylated polypeptides.

Sandra M J Langeveld, Marco Vennik, Marijke Kottenhagen, Ringo Van Wijk, Ankie Buijk, Jan W Kijne, Sylvia de Pater

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Plant physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.5field-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

32 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  3. Transcriptome Analysis of Air Space-Type Variegation Formation inInternational journal of molecular sciences · 2022
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  7. X-ray diffraction analysis and in vitro characterization of the UAM2 protein from Oryza sativa.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Formation of starch in plant cells.Cellular and molecular life sciences : CMLS · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

7 authors at 2 institutions in 1 country.

Sandra M J LangeveldDepartment of Applied Plant Sciences of the Netherlands Organisation for Applied Scientific Research, Center for Phytotechnology, Leiden University, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands. Langeveld@rulbim.leidenuniv.nl
Marco Vennik
Marijke Kottenhagen
Ringo Van Wijk
Ankie Buijk
Jan W Kijne
Sylvia de Pater
Netherlands Organisation for Applied Scientific Research · NLLeiden University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversibly glycosylated polypeptides (RGPs) have been implicated in polysaccharide biosynthesis. In plants, these proteins may function, for example, in cell wall synthesis and/or in synthesis of starch. We have isolated wheat (Triticum aestivum) and rice (Oryza sativa) Rgp cDNA clones to study the function of RGPs. Sequence comparisons showed the existence of two classes of RGP proteins, designated RGP1 and RGP2. Glucosylation activity of RGP1 and RGP2 from wheat and rice was studied. After separate expression of Rgp1 and Rgp2 in Escherichia coli or yeast (Saccharomyces cerevisiae), only RGP1 showed self-glucosylation. In Superose 12 fractions from wheat endosperm extract, a polypeptide with a molecular mass of about 40 kD is glucosylated by UDP-glucose. Transgenic tobacco (Nicotiana tabacum) plants, overexpressing either wheat Rgp1 or Rgp2, were generated. Subsequent glucosylation assays revealed that in RGP1-containing tobacco extracts as well as in RGP2-containing tobacco extracts UDP-glucose is incorporated, indicating that an RGP2-containing complex is active. Gel filtration experiments with wheat endosperm extracts and extracts from transgenic tobacco plants, overexpressing either wheat Rgp1 or Rgp2, showed the presence of RGP1 and RGP2 in high-molecular mass complexes. Yeast two-hybrid studies indicated that RGP1 and RGP2 form homo- and heterodimers. Screening of a cDNA library using the yeast two-hybrid system and purification of the complex by an antibody affinity column did not reveal the presence of other proteins in the RGP complexes. Taken together, these results suggest the presence of active RGP1 and RGP2 homo- and heteromultimers in wheat endosperm.

Indexed as

Amino Acid SequenceCarrier ProteinsCell WallCloning, MolecularDNA, ComplementaryEscherichia coliGene Expression Regulation, PlantGlycoproteinsGlycosylationMolecular Sequence DataNicotianaOryzaPeptidesPlant ProteinsPlants, Genetically ModifiedPolysaccharidesCarrier ProteinsDNA, ComplementaryGlycoproteinsPeptidesPlant ProteinsPolysaccharidesStarch

Identifiers

PMID12011358
PMCPMC155891
OpenAlexW2164825395

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.