Evidence map›Paper›PMID 32079172›Full record

ReviewMolecules (Basel, Switzerland)2020

Modeling to Understand Plant Protein Structure-Function Relationships-Implications for Seed Storage Proteins.

Faiza Rasheed, Joel Markgren, Mikael Hedenqvist, Eva Johansson

Abstract 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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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.

  1. MultilevelCurrent research in structural biology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The development of a silage-based biorefinery to deliver the maximum nutritional benefit for human consumption from UK grasslands.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors.

Faiza RasheedDepartment of Plant Breeding, The Swedish University of Agricultural Sciences, Box 101, SE-230 53 Alnarp, Sweden.
Joel MarkgrenDepartment of Plant Breeding, The Swedish University of Agricultural Sciences, Box 101, SE-230 53 Alnarp, Sweden.
Mikael HedenqvistKTH Royal Institute of Technology, School of Chemical Science and Engineering, Fibre and Polymer Technology, SE-100 44 Stockholm, Sweden.
Eva JohanssonDepartment of Plant Breeding, The Swedish University of Agricultural Sciences, Box 101, SE-230 53 Alnarp, Sweden.

Funding

the Swedish Research Council 2013-05991
6 · The paper itself

Abstract

Proteins are among the most important molecules on Earth. Their structure and aggregation behavior are key to their functionality in living organisms and in protein-rich products. Innovations, such as increased computer size and power, together with novel simulation tools have improved our understanding of protein structure-function relationships. This review focuses on various proteins present in plants and modeling tools that can be applied to better understand protein structures and their relationship to functionality, with particular emphasis on plant storage proteins. Modeling of plant proteins is increasing, but less than 9% of deposits in the Research Collaboratory for Structural Bioinformatics Protein Data Bank come from plant proteins. Although, similar tools are applied as in other proteins, modeling of plant proteins is lagging behind and innovative methods are rarely used. Molecular dynamics and molecular docking are commonly used to evaluate differences in forms or mutants, and the impact on functionality. Modeling tools have also been used to describe the photosynthetic machinery and its electron transfer reactions. Storage proteins, especially in large and intrinsically disordered prolamins and glutelins, have been significantly less well-described using modeling. These proteins aggregate during processing and form large polymers that correlate with functionality. The resulting structure-function relationships are important for processed storage proteins, so modeling and simulation studies, using up-to-date models, algorithms, and computer tools are essential for obtaining a better understanding of these relationships.

Indexed as

Models, MolecularFoodIndustrySeed Storage ProteinsStructure-Activity RelationshipSeed Storage Proteinsalbuminglobulinglutelinmolecular dynamics simulationmonte carlo simulationprolamin

Identifiers

PMID32079172
PMCPMC7071054

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.