Evidence map›Paper›PMID 20304929›Full record

ArticleThe Journal of biological chemistry2010

Dominant negative mutations affect oligomerization of human pyruvate kinase M2 isozyme and promote cellular growth and polyploidy.

Vibhor Gupta, Ponnusamy Kalaiarasan, Mohammad Faheem, Nishant Singh, Mohammad Askandar Iqbal, Rameshwar N K Bamezai

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

  1. Trial
  2. Alkaptonuria.Nature reviews. Disease primers · 2024
    Review
  3. Article
  4. Article
  5. Alkaptonuria: Current Perspectives.The application of clinical genetics · 2020
    Review
  6. Review
  7. Article
  8. Deubiquitinases and cancer: A snapshot.Critical reviews in oncology/hematology · 2016
    Review
  9. Article
  10. Article
  11. Pyruvate kinase M2 at a glance.Journal of cell science · 2015
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Human pyruvate kinase M2: a multifunctional protein.Protein science : a publication of the Protein Society · 2010
    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

6 authors at 1 institution in 1 country.

Vibhor GuptaNational Centre of Applied Human Genetics, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.
Ponnusamy Kalaiarasan
Mohammad Faheem
Nishant Singh
Mohammad Askandar Iqbal
Rameshwar N K Bamezai
Jawaharlal Nehru University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study was designed to understand the mechanism and functional implication of the two heterozygous mutations (H391Y and K422R) of human pyruvate kinase M2 isozyme (PKM(2)) observed earlier in a Bloom syndrome background. The co-expression of homotetrameric wild type and mutant PKM(2) in the cellular milieu resulting in the interaction between the two at the monomer level was substantiated further by in vitro experiments. The cross-monomer interaction significantly altered the oligomeric state of PKM(2) by favoring dimerization and heterotetramerization. In silico study provided an added support in showing that hetero-oligomerization was energetically favorable. The hetero-oligomeric populations of PKM(2) showed altered activity and affinity, and their expression resulted in an increased growth rate of Escherichia coli as well as mammalian cells, along with an increased rate of polyploidy. These features are known to be essential to tumor progression. This study provides insight in understanding the modulated role of large oligomeric multifunctional proteins such as PKM(2) by affecting cellular behavior, which is an essential observation to understand tumor sustenance and progression and to design therapeutic intervention in future.

Indexed as

Genes, DominantMutationAnimalsCell ProliferationDisease ProgressionEscherichia coliFlow CytometryGlutathione TransferaseHeLa CellsHumansIsoenzymesKineticsPolyploidyPyruvate KinaseTwo-Hybrid System TechniquesGlutathione TransferaseIsoenzymesPyruvate Kinase

Identifiers

PMID20304929
PMCPMC2878009
OpenAlexW2003494696

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.