Evidence map›Paper›PMID 23038274›Full record

ReviewLeukemia2013

SIAH proteins: critical roles in leukemogenesis.

O H Krämer, R H Stauber, G Bug, J Hartkamp, S K Knauer

Abstract readReview
PubMed Publisher
In one paragraph

Review in Leukemia, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.

  1. Pooled it
  2. The deacetylases HDAC1/HDAC2 control JAK2Signal transduction and targeted therapy · 2025
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  6. mMolecular therapy. Nucleic acids · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. PEAK3/C19orf35 pseudokinase, a new NFK3 kinase family member, inhibits CrkII through dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Review
  13. Article
  14. Review
  15. Combination Therapies Targeting HDAC and IKK in Solid Tumors.Trends in pharmacological sciences · 2018
    Review
  16. Article
  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

5 authors at 4 institutions in 1 country.

O H KrämerCenter for Molecular Biomedicine (CMB), Department of Biochemistry, University of Jena, Jena, Germany. Oliver.Kraemer@uni-jena.de
R H Stauber
G Bug
J Hartkamp
S K Knauer
Johannes Gutenberg University Mainz · DERWTH Aachen University · DEUniversity Hospital Frankfurt · DEUniversity of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The delicate balance between the synthesis and the degradation of proteins ensures cellular homeostasis. Proteases act in an irreversible manner and therefore have to be strictly regulated. The ubiquitin-proteasome system (UPS) is a major pathway for the proteolytic degradation of cellular proteins. As dysregulation of the UPS is observed in most cancers including leukemia, the UPS is a valid target for therapeutic intervention strategies. Ubiquitin-ligases selectively bind substrates to target them for poly-ubiquitinylation and proteasomal degradation. Therefore, pharmacological modulation of these proteins could allow a specific level of control. Increasing evidence accumulates that ubiquitin-ligases termed mammalian seven in absentia homologs (SIAHs) are not only critical for the pathogenesis of solid tumors but also for leukemogenesis. However, the relevance and therapeutic potential of SIAH-dependent processes has not been fully elucidated. Here, we summarize functions of SIAH ubiquitin-ligases in leukemias, how they select leukemia-relevant substrates for proteasomal degradation, and how the expression and activity of SIAH1 and SIAH2 can be modulated in vivo. We also discuss that epigenetic drugs belonging to the group of histone deacetylase inhibitors induce SIAH-dependent proteasomal degradation to accelerate the turnover of leukemogenic proteins. In addition, our review highlights potential areas for future research on SIAH proteins.

Indexed as

Animalsfms-Like Tyrosine Kinase 3Gene Expression RegulationHumansLeukemiaMiceMutationNuclear ProteinsSeven in Absentia ProteinsSignal TransductionSubstrate SpecificityTranscription FactorsUbiquitin-Protein LigasesFLT3 protein, humanfms-Like Tyrosine Kinase 3Nuclear ProteinsSeven in Absentia ProteinsTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID23038274
OpenAlexW2075172927

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.