Evidence map›Paper›PMID 29540834›Full record

ReviewOncogene2018

Controlling the master-upstream regulation of the tumor suppressor LKB1.

Lars Kullmann, Michael P Krahn

Abstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 2 pooled it
5.8field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 2 syntheses or guidelines pooled it, 70 citations in OpenAlex.

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  11. Endocannabinoid biosynthetic enzymes regulate pain response via LKB1-AMPK signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

2 authors at 1 institution in 1 country.

Lars KullmannInternal Medicine D, University Hospital of Münster, Domagkstr. 3a, 48149, Münster, Germany.
Michael P KrahnInternal Medicine D, University Hospital of Münster, Domagkstr. 3a, 48149, Münster, Germany. Michael.Krahn@ukmuenster.de.
University Hospital Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tumor suppressor LKB1 is an essential serine/threonine kinase, which regulates various cellular processes such as cell metabolism, cell proliferation, cell polarity, and cell migration. Germline mutations in the STK11 gene (encoding LKB1) are the cause of the Peutz-Jeghers syndrome, which is characterized by benign polyps in the intestine and a higher risk for the patients to develop intestinal and extraintestinal tumors. Moreover, mutations and misregulation of LKB1 have been reported to occur in most types of tumors and are among the most common aberrations in lung cancer. LKB1 activates several downstream kinases of the AMPK family by direct phosphorylation in the T-loop. In particular the activation of AMPK upon energetic stress has been intensively analyzed in various diseases, including cancer to induce a metabolic switch from anabolism towards catabolism to regulate energy homeostasis and cell survival. In contrast, the regulation of LKB1 itself has long been only poorly understood. Only in the last years, several proteins and posttranslational modifications of LKB1 have been analyzed to control its localization, activity and recognition of substrates. Here, we summarize the current knowledge about the upstream regulation of LKB1, which is important for the understanding of the pathogenesis of many types of tumors.

Indexed as

Genes, Tumor SuppressorAllyl CompoundsAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesBiphenyl CompoundsCalcium-Binding ProteinsGene Expression Regulation, NeoplasticHumansLignansLung NeoplasmsLysosomesMutationPeutz-Jeghers SyndromePhenolsPhosphorylationProtein Serine-Threonine KinasesAllyl CompoundsAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesBiphenyl CompoundsCAB39 protein, humanCalcium-Binding ProteinshonokiolLignansPhenolsProtein Serine-Threonine KinasesSTK11 protein, human

Identifiers

PMID29540834
OpenAlexW2791774324

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.