Evidence map›Paper›PMID 29995887›Full record

ArticlePloS one2018

The phosphoglycerate kinase 1 variants found in carcinoma cells display different catalytic activity and conformational stability compared to the native enzyme.

Annarita Fiorillo, Maria Petrosino, Andrea Ilari, Alessandra Pasquo, Alessandra Cipollone, Maristella Maggi, Roberta Chiaraluce, Valerio Consalvi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 30% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  11. PGK1 : An Essential Player in Modulating Tumor Metabolism.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Article
  13. Analysis and Interpretation of the Impact of Missense Variants in Cancer.International journal of molecular sciences · 2021
    Review
  14. Review
  15. Review
  16. Article
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  18. Review
  19. PGK1-mediated cancer progression and drug resistance.American journal of cancer research · 2019
    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

8 authors at 4 institutions in 1 country.

Annarita FiorilloDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.ORCID 0000-0002-8966-8554
Maria PetrosinoDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Andrea IlariCNR-Institute of Molecular Biology and Pathology, Rome, Italy.ORCID 0000-0002-7754-399X
Alessandra PasquoENEA CR Frascati, Diagnostics and Metrology Laboratory, FSN-TECFIS-DIM, Frascati, Italy.
Alessandra CipolloneDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Maristella MaggiDepartment of Molecular Medicine, Unit of Immunology and General Pathology, University of Pavia, Pavia, Italy.ORCID 0000-0002-9075-8143
Roberta ChiaraluceDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.ORCID 0000-0001-7748-2237
Valerio ConsalviDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza University of Rome, Rome, Italy.
Sapienza University of Rome · ITInstitute of Molecular Biology and Pathology · ITNational Agency for New Technologies, Energy and Sustainable Economic Development · ITUniversity of Pavia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cancer cells are able to survive in difficult conditions, reprogramming their metabolism according to their requirements. Under hypoxic conditions they shift from oxidative phosphorylation to aerobic glycolysis, a behavior known as Warburg effect. In the last years, glycolytic enzymes have been identified as potential targets for alternative anticancer therapies. Recently, phosphoglycerate kinase 1 (PGK1), an ubiquitous enzyme expressed in all somatic cells that catalyzes the seventh step of glycolysis which consists of the reversible phosphotransfer reaction from 1,3-bisphosphoglycerate to ADP, has been discovered to be overexpressed in many cancer types. Moreover, several somatic variants of PGK1 have been identified in tumors. In this study we analyzed the effect of the single nucleotide variants found in cancer tissues on the PGK1 structure and function. Our results clearly show that the variants display a decreased catalytic efficiency and/or thermodynamic stability and an altered local tertiary structure, as shown by the solved X-ray structures. The changes in the catalytic properties and in the stability of the PGK1 variants, mainly due to the local changes evidenced by the X-ray structures, suggest also changes in the functional role of PGK to support the biosynthetic need of the growing and proliferating tumour cells.

Indexed as

Adenosine DiphosphateAmino Acid SequenceBinding SitesCloning, MolecularCrystallography, X-RayEnzyme StabilityEscherichia coliGene ExpressionGenetic VectorsGlyceric AcidsHumansKineticsModels, MolecularMutationNeoplasm ProteinsPhosphoglycerate Kinase3-phosphoglycerateAdenosine DiphosphateGlyceric AcidsNeoplasm ProteinsPGK1 protein, humanPhosphoglycerate KinaseRecombinant Proteins

Identifiers

PMID29995887
PMCPMC6040698
OpenAlexW2861318006

What OpenQuestion holds

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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.