Evidence map›Paper›PMID 25061812›Full record

ArticlePloS one2014

Silencer of death domains controls cell death through tumour necrosis factor-receptor 1 and caspase-10 in acute lymphoblastic leukemia.

Adam Cisterne, Rana Baraz, Naveed I Khan, Robert Welschinger, Jordan Basnett, Carina Fung, Helen Rizos, Kenneth F Bradstock, Linda J Bendall

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 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

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  5. Matteucinol combined with temozolomide inhibits glioblastoma proliferation, invasion, and progression: an in vitro, in silico, and in vivo study.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2022
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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

9 authors at 2 institutions in 1 country.

Adam CisterneCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
Rana BarazCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
Naveed I KhanCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
Robert WelschingerCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
Jordan BasnettCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
Carina FungCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
Helen RizosCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
Kenneth F BradstockBlood and Marrow Transplant Service, Department of Haematology, Westmead Hospital, Sydney, New South Wales, Australia.
Linda J BendallCentre for Cancer Research, Westmead Millennium Institute, University of Sydney, Sydney, New South Wales, Australia.
The University of Sydney · AUWestmead Hospital · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Resistance to apoptosis remains a significant problem in drug resistance and treatment failure in malignant disease. NO-aspirin is a novel drug that has efficacy against a number of solid tumours, and can inhibit Wnt signaling, and although we have shown Wnt signaling to be important for acute lymphoblastic leukemia (ALL) cell proliferation and survival inhibition of Wnt signaling does not appear to be involved in the induction of ALL cell death. Treatment of B lineage ALL cell lines and patient ALL cells with NO-aspirin induced rapid apoptotic cell death mediated via the extrinsic death pathway. Apoptosis was dependent on caspase-10 in association with the formation of the death-inducing signaling complex (DISC) incorporating pro-caspase-10 and tumor necrosis factor receptor 1 (TNF-R1). There was no measurable increase in TNF-R1 or TNF-α in response to NO-aspirin, suggesting that the process was ligand-independent. Consistent with this, expression of silencer of death domain (SODD) was reduced following NO-aspirin exposure and lentiviral mediated shRNA knockdown of SODD suppressed expansion of transduced cells confirming the importance of SODD for ALL cell survival. Considering that SODD and caspase-10 are frequently over-expressed in ALL, interfering with these proteins may provide a new strategy for the treatment of this and potentially other cancers.

Indexed as

ApoptosisAdaptor Proteins, Signal TransducingCaspase 10Cells, CulturedDeath Domain Receptor Signaling Adaptor ProteinsGene SilencingHumansJurkat CellsPrecursor Cell Lymphoblastic Leukemia-LymphomaAdaptor Proteins, Signal TransducingBAG4 protein, humanCaspase 10Death Domain Receptor Signaling Adaptor Proteins

Identifiers

PMID25061812
PMCPMC4111576
OpenAlexW1999578065

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.