Evidence map›Paper›PMID 32509571›Full record

ReviewFrontiers in oncology2020

Adenylate Kinase and Metabolic Signaling in Cancer Cells.

Aleksandr Klepinin, Song Zhang, Ljudmila Klepinina, Egle Rebane-Klemm, Andre Terzic, Tuuli Kaambre, Petras Dzeja

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in oncology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
7.9field-weighted citation impact, top 1% 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

47 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
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  5. Review
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  7. Review
  8. Article
  9. Energy Metabolism Profiling of Human Colorectal Tumours.Journal of cellular and molecular medicine · 2025
    Article
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  11. The Study of the Protection Mechanism of Calycosin-7-Molecules (Basel, Switzerland) · 2025
    Article
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  15. Review
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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 2 institutions in 2 countries.

Aleksandr KlepininLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia.
Song ZhangDepartment of Cardiovascular Medicine, Mayo Clinic, Rochester, MN, United States.
Ljudmila KlepininaLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia.
Egle Rebane-KlemmLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia.
Andre TerzicDepartment of Cardiovascular Medicine, Mayo Clinic, Rochester, MN, United States.
Tuuli KaambreLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia.
Petras DzejaDepartment of Cardiovascular Medicine, Mayo Clinic, Rochester, MN, United States.
National Institute of Chemical Physics and Biophysics · EEMayo Clinic in Arizona · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A hallmark of cancer cells is the ability to rewire their bioenergetics and metabolic signaling circuits to fuel their uncontrolled proliferation and metastasis. Adenylate kinase (AK) is the critical enzyme in the metabolic monitoring of cellular adenine nucleotide homeostasis. It also directs AK→ AMP→ AMPK signaling controlling cell cycle and proliferation, and ATP energy transfer from mitochondria to distribute energy among cellular processes. The significance of AK isoform network in the regulation of a variety of cellular processes, which include cell differentiation and motility, is rapidly growing. Adenylate kinase 2 (AK2) isoform, localized in intermembrane and intra-cristae space, is vital for mitochondria nucleotide exchange and ATP export. AK2 deficiency disrupts cell energetics, causes severe human diseases, and is embryonically lethal in mice, signifying the importance of catalyzed phosphotransfer in cellular energetics. Suppression of AK phosphotransfer and AMP generation in cancer cells and consequently signaling through AMPK could be an important factor in the initiation of cancerous transformation, unleashing uncontrolled cell cycle and growth. Evidence also builds up that shift in AK isoforms is used later by cancer cells for rewiring energy metabolism to support their high proliferation activity and tumor progression. As cell motility is an energy-consuming process, positioning of AK isoforms to increased energy consumption sites could be an essential factor to incline cancer cells to metastases. In this review, we summarize recent advances in studies of the significance of AK isoforms involved in cancer cell metabolism, metabolic signaling, metastatic potential, and a therapeutic target.

Indexed as

adenylate kinasecancerenergy metabolismmitochondriaphosphotransfer

Identifiers

PMID32509571
PMCPMC7248387
OpenAlexW3016350142

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.