Evidence map›Paper›PMID 35006475›Full record

ReviewPlant molecular biology2022

Structure, function, and evolution of plant ADP-glucose pyrophosphorylase.

Carlos M Figueroa, Matías D Asencion Diez, Miguel A Ballicora, Alberto A Iglesias

Open access · hybridAbstract readReview
PubMed Publisher
In one paragraph

Review in Plant molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

31 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Genome-Wide Analysis of AGPase IdentifiesInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. A Suite of Pea (International journal of molecular sciences · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The activation ofPlant direct · 2024
    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 2 countries.

Carlos M Figueroa *Instituto de Agrobiotecnología del Litoral, Universidad Nacional del Litoral, Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Bioquímica y Ciencias Biológicas, Santa Fe, Argentina.ORCID http://orcid.org/0000-0003-4047-0480
Matías D Asencion Diez *Instituto de Agrobiotecnología del Litoral, Universidad Nacional del Litoral, Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Bioquímica y Ciencias Biológicas, Santa Fe, Argentina.ORCID http://orcid.org/0000-0001-6495-387X
Miguel A BallicoraDepartment of Chemistry and Biochemistry, Loyola University Chicago, Chicago, IL, USA. mballic@luc.edu.ORCID http://orcid.org/0000-0002-5324-0724
Alberto A IglesiasInstituto de Agrobiotecnología del Litoral, Universidad Nacional del Litoral, Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Bioquímica y Ciencias Biológicas, Santa Fe, Argentina. iglesias@fbcb.unl.edu.ar.ORCID http://orcid.org/0000-0001-9729-7338
Consejo Nacional de Investigaciones Científicas y Técnicas · ARLoyola University Chicago · US

Funding

agencia nacional de promoción científica y tecnológica PICT-2017-1515agencia nacional de promoción científica y tecnológica PICT-2018-00698agencia nacional de promoción científica y tecnológica PICT-2018-00865agencia nacional de promoción científica y tecnológica PICT-2018-00929conicet PUE-2016-0040max-planck-gesellschaft Partner Group for Plant Biochemistrynational science foundation MCB 1616851universidad nacional del litoral CAI+D 2020
6 · The paper itself

Abstract

key messageThis review outlines research performed in the last two decades on the structural, kinetic, regulatory and evolutionary aspects of ADP-glucose pyrophosphorylase, the regulatory enzyme for starch biosynthesis. ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the first committed step in the pathway of glycogen and starch synthesis in bacteria and plants, respectively. Plant ADP-Glc PPase is a heterotetramer allosterically regulated by metabolites and post-translational modifications. In this review, we focus on the three-dimensional structure of the plant enzyme, the amino acids that bind the regulatory molecules, and the regions involved in transmitting the allosteric signal to the catalytic site. We provide a model for the evolution of the small and large subunits, which produce heterotetramers with distinct catalytic and regulatory properties. Additionally, we review the various post-translational modifications observed in ADP-Glc PPases from different species and tissues. Finally, we discuss the subcellular localization of the enzyme found in grain endosperm from grasses, such as maize and rice. Overall, this work brings together research performed in the last two decades to better understand the multiple mechanisms involved in the regulation of ADP-Glc PPase. The rational modification of this enzyme could improve the yield and resilience of economically important crops, which is particularly important in the current scenario of climate change and food shortage.

Indexed as

Evolution, MolecularAllosteric RegulationGlucose-1-Phosphate AdenylyltransferaseModels, MolecularPlantsProtein ConformationStarchGlucose-1-Phosphate AdenylyltransferaseStarchAllosteric regulationEnzyme evolutionNucleotide-sugar synthesisPost-translational regulationRedox regulationSubfunctionalization

Identifiers

PMID35006475
OpenAlexW4205287354

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.