Evidence map›Paper›PMID 32512867›Full record

ArticleCancers2020

The Progression of Acute Myeloid Leukemia from First Diagnosis to Chemoresistant Relapse: A Comparison of Proteomic and Phosphoproteomic Profiles.

Elise Aasebø, Frode S Berven, Randi Hovland, Stein Ove Døskeland, Øystein Bruserud, Frode Selheim, Maria Hernandez-Valladares

Open access · goldAbstract read
In one paragraph

Article in Cancers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Mitochondrial Ribosomal Proteins and Cancer.Medicina (Kaunas, Lithuania) · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Combination Therapies Targeting Apoptosis in Paediatric AML:International journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

7 authors at 2 institutions in 1 country.

Elise AasebøDepartment of Clinical Science, University of Bergen, 5021 Bergen, Norway.ORCID 0000-0002-6939-8059
Frode S BervenThe Department of Biomedicine, The Proteomics Unit at the University of Bergen (PROBE), University of Bergen, 5009 Bergen, Norway.
Randi HovlandDepartment for Medical Genetics, Haukeland University Hospital, 5021 Bergen, Norway.
Stein Ove DøskelandThe Department of Biomedicine, University of Bergen, 5009 Bergen, Norway.
Øystein BruserudDepartment of Clinical Science, University of Bergen, 5021 Bergen, Norway.
Frode SelheimThe Department of Biomedicine, The Proteomics Unit at the University of Bergen (PROBE), University of Bergen, 5009 Bergen, Norway.
Maria Hernandez-ValladaresDepartment of Clinical Science, University of Bergen, 5021 Bergen, Norway.ORCID 0000-0001-9347-7841
University of Bergen · NOHaukeland University Hospital · NO

Funding

Kreftforeningen 100933
6 · The paper itself

Abstract

Acute myeloid leukemia (AML) is an aggressive hematological malignancy. Nearly 50% of the patients who receive the most intensive treatment develop chemoresistant leukemia relapse. Although the leukemogenic events leading to relapse seem to differ between patients (i.e., regrowth from a clone detected at first diagnosis, progression from the original leukemic or preleukemic stem cells), a common characteristic of relapsed AML is increased chemoresistance. The aim of the present study was to investigate at the proteomic level whether leukemic cells from relapsed patients present overlapping molecular mechanisms that contribute to this chemoresistance. We used liquid chromatography-tandem mass spectrometry (LC-MS/MS) to compare the proteomic and phosphoproteomic profiles of AML cells derived from seven patients at the time of first diagnosis and at first relapse. At the time of first relapse, AML cells were characterized by increased levels of proteins important for various mitochondrial functions, such as mitochondrial ribosomal subunit proteins (MRPL21, MRPS37) and proteins for RNA processing (DHX37, RNA helicase; RPP40, ribonuclease P component), DNA repair (ERCC3, DNA repair factor IIH helicase; GTF2F1, general transcription factor), and cyclin-dependent kinase (CDK) activity. The levels of several cytoskeletal proteins (MYH14/MYL6/MYL12A, myosin chains; VCL, vinculin) as well as of proteins involved in vesicular trafficking/secretion and cell adhesion (ITGAX, integrin alpha-X; CD36, platelet glycoprotein 4; SLC2A3, solute carrier family 2) were decreased in relapsed cells. Our study introduces new targetable proteins that might direct therapeutic strategies to decrease chemoresistance in relapsed AML.

Indexed as

acute myeloid leukemiaCDKdegranulationkinasemarkersmass spectrometryminimal residual diseasemitochondriapatient relapsephosphoproteomeproteomesecretion

Identifiers

PMID32512867
PMCPMC7352627
OpenAlexW3033501199

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.