Evidence map›Paper›PMID 24816797›Full record

ArticlePloS one2014

Association of nuclear-localized Nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.

Gina Shaw-Hallgren, Katarzyna Chmielarska Masoumi, Reihaneh Zarrizi, Ulf Hellman, Per Karlsson, Khalil Helou, Ramin Massoumi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Atypical MAPKs in cancer.The FEBS journal · 2025
    Review
  2. Therapeutic Targeting of Nemo-like Kinase in Primary and Acquired Endocrine-resistant Breast Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2021
    Article
  3. Review
  4. Nemo-Like Kinase in Development and Diseases: Insights from Mouse Studies.International journal of molecular sciences · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The emerging role of Nemo-like kinase (NLK) in the regulation of cancers.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Review
  11. Article
  12. 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

7 authors at 3 institutions in 1 country.

Gina Shaw-HallgrenTranslational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
Katarzyna Chmielarska MasoumiTranslational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
Reihaneh ZarriziTranslational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
Ulf HellmanLudwig Institute for Cancer Research, Uppsala, Sweden.
Per KarlssonInstitute of Clinical Sciences, Department of Oncology, University of Gothenburg, Gothenburg, Sweden.
Khalil HelouInstitute of Clinical Sciences, Department of Oncology, University of Gothenburg, Gothenburg, Sweden.
Ramin MassoumiTranslational Cancer Research, Molecular Tumor Pathology, Department of Laboratory Medicine, Lund University, Lund, Sweden.
Lund University · SEUniversity of Gothenburg · SELudwig Cancer Research · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nemo-like kinase (NLK), a proline-directed serine/threonine kinase regulated by phosphorylation, can be localized in the cytosol or in the nucleus. Whether the localization of NLK can affect cell survival or cell apoptosis is yet to be disclosed. In the present study we found that NLK was mainly localized in the nuclei of breast cancer cells, in contrast to a cytosolic localization in non-cancerous breast epithelial cells. The nuclear localization of NLK was mediated through direct interaction with Heat shock protein 27 (HSP27) which further protected cancer cells from apoptosis. The present study provides evidence of a novel mechanism by which HSP27 recognizes NLK in the breast cancer cells and prevents NLK-mediated cell apoptosis.

Indexed as

Antineoplastic Agents, PhytogenicApoptosisBlotting, WesternBreast NeoplasmsCell LineCell Line, TumorCell NucleusCytoplasmDown-RegulationEtoposideFemaleHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHumansImmunohistochemistryIntracellular Signaling Peptides and ProteinsAntineoplastic Agents, PhytogenicEtoposideHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanIntracellular Signaling Peptides and ProteinsMolecular ChaperonesNLK protein, humanProtein Serine-Threonine KinasesTumor Necrosis Factor-alpha

Identifiers

PMID24816797
PMCPMC4015990
OpenAlexW2032845032

What OpenQuestion holds

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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.