Evidence map›Paper›PMID 28407006›Full record

ArticlePloS one2017

Functional and structural characterization of plastidic starch phosphorylase during barley endosperm development.

Jose A Cuesta-Seijo, Christian Ruzanski, Katarzyna Krucewicz, Sebastian Meier, Per Hägglund, Birte Svensson, Monica M Palcic

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Site-Directed Mutations at Phosphorylation Sites inPlants (Basel, Switzerland) · 2023
    Article
  13. Article
  14. Frontiers in plant science · 2023
    Article
  15. Article
  16. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    Review
  17. Review
  18. Review
  19. Review
  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 4 institutions in 2 countries.

Jose A Cuesta-SeijoCarlsberg Research Laboratory, J.C. Jacobsens Gade 4, DK-1799 Copenhagen V, Denmark.ORCID http://orcid.org/0000-0002-3755-9305
Christian RuzanskiCarlsberg Research Laboratory, J.C. Jacobsens Gade 4, DK-1799 Copenhagen V, Denmark.
Katarzyna KrucewiczCarlsberg Research Laboratory, J.C. Jacobsens Gade 4, DK-1799 Copenhagen V, Denmark.
Sebastian MeierCarlsberg Research Laboratory, J.C. Jacobsens Gade 4, DK-1799 Copenhagen V, Denmark.
Per HägglundDTU Department of Biotechnology and Biomedicine, Proteomics Core, Technical University of Denmark, Matematiktorvet, Building 301, DK-2800 Kgs. Lyngby, Denmark.
Birte SvenssonDTU Department of Biotechnology and Biomedicine, Enzyme and Protein Chemistry, Technical University of Denmark, Elektrovej Building 375, DK-2800 Kgs. Lyngby, Denmark.
Monica M PalcicCarlsberg Research Laboratory, J.C. Jacobsens Gade 4, DK-1799 Copenhagen V, Denmark.
Carlsberg Laboratory · DKTechnical University of Denmark · DKNovo Nordisk (Denmark) · DKUniversity of Victoria · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The production of starch is essential for human nutrition and represents a major metabolic flux in the biosphere. The biosynthesis of starch in storage organs like barley endosperm operates via two main pathways using different substrates: starch synthases use ADP-glucose to produce amylose and amylopectin, the two major components of starch, whereas starch phosphorylase (Pho1) uses glucose-1-phosphate (G1P), a precursor for ADP-glucose production, to produce α-1,4 glucans. The significance of the Pho1 pathway in starch biosynthesis has remained unclear. To elucidate the importance of barley Pho1 (HvPho1) for starch biosynthesis in barley endosperm, we analyzed HvPho1 protein production and enzyme activity levels throughout barley endosperm development and characterized structure-function relationships of HvPho1. The molecular mechanisms underlying the initiation of starch granule biosynthesis, that is, the enzymes and substrates involved in the initial transition from simple sugars to polysaccharides, remain unclear. We found that HvPho1 is present as an active protein at the onset of barley endosperm development. Notably, purified recombinant protein can catalyze the de novo production of α-1,4-glucans using HvPho1 from G1P as the sole substrate. The structural properties of HvPho1 provide insights into the low affinity of HvPho1 for large polysaccharides like starch or amylopectin. Our results suggest that HvPho1 may play a role during the initiation of starch biosynthesis in barley.

Indexed as

Catalytic DomainChloroplast ProteinsCrystallography, X-RayEndospermGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGlucosephosphatesHordeumModels, MolecularProtein Structure, SecondaryStarchStarch PhosphorylaseChloroplast Proteinsglucose-1-phosphateGlucosephosphatesStarchStarch Phosphorylase

Identifiers

PMID28407006
PMCPMC5391026
OpenAlexW2605925004

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Registered trials

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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.