Evidence map›Paper›PMID 19232721›Full record

ArticleLeukemia research2009

Molecular targeting of MLL-rearranged leukemia cell lines with the synthetic peptide PFWT synergistically enhances the cytotoxic effect of established chemotherapeutic agents.

Cecily A Bennett, Amanda C Winters, Nisha N Barretto, Charles S Hemenway

Open access · greenAbstract read
In one paragraph

Article in Leukemia research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Binding cavities and druggability of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2015
    Article
  2. An AF9/ENL-targted peptide with therapeutic potential in mixed lineage leukemias.Journal of experimental therapeutics & oncology · 2014
    Article
  3. Article
  4. Article
  5. 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

4 authors at 2 institutions in 1 country.

Cecily A BennettDepartment of Epidemiology, Tulane University, New Orleans, LA 70112, United States.
Amanda C Winters
Nisha N Barretto
Charles S Hemenway
Loyola University Chicago · USTulane University · US

Funding

UNCOVERING THE MECHANISMS OF OSTEOSARCOMA METASTASIS SUPPRESSION BY MTBPP20RR020152 · NCRR · TULANE UNIVERSITY OF LOUISIANA · PI YOU, ZONGBING · 2004 to 2011
$17.0M
Targeted therapy for 11q23 acute leukemias.R01CA098459 · NCI · TULANE UNIVERSITY OF LOUISIANA · PI HEMENWAY, CHARLES STANLEY · 2004 to 2012
$1.5M
NCI NIH HHS CA 098459NCI NIH HHS R01 CA098459NCRR NIH HHS P20 RR020152NCRR NIH HHS RR 020152
6 · The paper itself

Abstract

MLL leukemias are characterized cytogenetically by reciprocal translocations of the MLL gene at 11q23 and clinically by unfavorable outcomes. Evidence indicating that MLL leukemias are resistant to apoptosis encourages the identification of agents that induce cell death by other mechanisms. The AF4-mimetic peptide PFWT induces necrosis in the t(4;11) leukemia cell line, MV4-11. Treatment of MV4-11 cells with PFWT in combination with four chemotherapeutic compounds results in sequence-dependent synergy, induction of both apoptotic and necrotic cell death, and inhibition of MV4-11 clonogenicity. Therefore, PFWT holds promise as a therapy for MLL leukemias that augments the effects of several clinically available chemotherapeutic agents.

Indexed as

Gene RearrangementAntimetabolites, AntineoplasticAntineoplastic Agents, PhytogenicApoptosisBlotting, WesternCell CycleCell ProliferationChromosomes, Human, Pair 11Chromosomes, Human, Pair 4Chromosomes, Human, Pair 9Colony-Forming Units AssayCytarabineDNA-Binding ProteinsDrug SynergismEtoposideHistone-Lysine N-MethyltransferaseAFF1 protein, humanAntimetabolites, AntineoplasticAntineoplastic Agents, PhytogenicCytarabineDNA-Binding ProteinsEtoposideHistone-Lysine N-MethyltransferaseKMT2A protein, humanMyeloid-Lymphoid Leukemia ProteinNuclear ProteinsPeptide FragmentsTranscriptional Elongation Factors

Identifiers

PMID19232721
PMCPMC2710145
OpenAlexW2035711319

What OpenQuestion holds

Textmetadata
LicenceTDM
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.