Evidence map›Paper›PMID 17130299›Full record

ArticleThe Journal of experimental medicine2006

Deregulated Syk inhibits differentiation and induces growth factor-independent proliferation of pre-B cells.

Thomas Wossning, Sebastian Herzog, Fabian Köhler, Sonja Meixlsperger, Yogesh Kulathu, Gerhard Mittler, Akihiro Abe, Uta Fuchs, Arndt Borkhardt, Hassan Jumaa

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
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  6. Review
  7. Role of spleen tyrosine kinase in liver diseases.World journal of gastroenterology · 2020
    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

10 authors at 4 institutions in 3 countries.

Thomas WossningInstitute of Biology III, Albert-Ludwigs-University of Freiburg, 79104 Freiburg, and Department of Pediatric Hematology and Oncology, Children's Hospital, Munich, Germany.
Sebastian Herzog
Fabian Köhler
Sonja Meixlsperger
Yogesh Kulathu
Gerhard Mittler
Akihiro Abe
Uta Fuchs
Arndt Borkhardt
Hassan Jumaa
University of Freiburg · DELudwig-Maximilians-Universität München · DEMax Planck Institute of Immunobiology and Epigenetics · DENagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nonreceptor protein spleen tyrosine kinase (Syk) is a key mediator of signal transduction in a variety of cell types, including B lymphocytes. We show that deregulated Syk activity allows growth factor-independent proliferation and transforms bone marrow-derived pre-B cells that are then able to induce leukemia in mice. Syk-transformed pre-B cells show a characteristic pattern of tyrosine phosphorylation, increased c-Myc expression, and defective differentiation. Treatment of Syk-transformed pre-B cells with a novel Syk-specific inhibitor (R406) reduces tyrosine phosphorylation and c-Myc expression. In addition, R406 treatment removes the developmental block and allows the differentiation of the Syk-transformed pre-B cells into immature B cells. Because R406 treatment also prevents the proliferation of c-Myc-transformed pre-B cells, our data indicate that endogenous Syk kinase activity may be required for the survival of pre-B cells transformed by other oncogenes. Collectively, our data suggest that Syk is a protooncogene involved in the transformation of lymphocytes, thus making Syk a potential target for the treatment of leukemia.

Indexed as

Adaptor Proteins, Signal TransducingAdoptive TransferAnimalsBenzamidesB-LymphocytesCell DifferentiationCell LineCell ProliferationDNA-Binding ProteinsFusion Proteins, bcr-ablHumansImatinib MesylateIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsLeukemiaMiceAdaptor Proteins, Signal TransducingB cell linker proteinBenzamidesDNA-Binding ProteinsFusion Proteins, bcr-ablImatinib MesylateIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsN4-(2,2-dimethyl-3-oxo-4H-pyrid(1,4)oxazin-6-yl)-5-fluoro-N2-(3,4,5-trimethoxyphenyl)-2,4-pyrimidinediamineOxazinesPhospholipase C gammaPiperazinesProtein Kinase InhibitorsProtein-Tyrosine KinasesProto-Oncogene Proteins c-mycPyridinesPyrimidinesRag2 protein, mouseReceptors, Antigen, B-CellSyk KinaseSYK protein, humanSyk protein, mouse

Identifiers

PMID17130299
PMCPMC2118175
OpenAlexW2097370957

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.