Evidence map›Paper›PMID 19487290›Full record

ArticleCancer research2009

Targeting LMO2 with a peptide aptamer establishes a necessary function in overt T-cell neoplasia.

Alex Appert, Chang-Hoon Nam, Natividad Lobato, Eva Priego, Ricardo Nunez Miguel, Tom Blundell, Lesley Drynan, Helen Sewell, Tomoyuki Tanaka, Terence Rabbitts

Open access · bronzeAbstract readValidation Study
In one paragraph

Article in Cancer research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. LIM-domain-only proteins in cancer.Nature reviews. Cancer · 2013
    Review
  9. Solution structure of a tethered Lmo2(LIM2) /Ldb1(LID) complex.Protein science : a publication of the Protein Society · 2012
    Article
  10. Article
  11. Article
  12. Article
  13. Purification, crystallization and preliminary X-ray analysis of a fusion of the LIM domains of LMO2 and the LID domain of Ldb1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  14. Article
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 6 institutions in 3 countries.

Alex AppertMedical Research Council Laboratory of Molecular Biology, University of Cambridge, Addenbrooke's Hospital, Cambridge, United Kingdom.
Chang-Hoon Nam
Natividad Lobato
Eva Priego
Ricardo Nunez Miguel
Tom Blundell
Lesley Drynan
Helen Sewell
Tomoyuki Tanaka
Terence Rabbitts
Medical Research Council · GBUniversity of Cambridge · GBAddenbrooke's Hospital · GBInstituto de Química Médica · ESSt James's University Hospital · GBUniversity of Leeds · GB

Funding

Medical Research Council G0600914Medical Research Council MC_U105178807
6 · The paper itself

Abstract

LMO2 is a transcription regulator involved in human T-cell leukemia, including some occurring in X-SCID gene therapy trials, and in B-cell lymphomas and prostate cancer. LMO2 functions in transcription complexes via protein-protein interactions involving two LIM domains and causes a preleukemic T-cell development blockade followed by clonal tumors. Therefore, LMO2 is necessary but not sufficient for overt neoplasias, which must undergo additional mutations before frank malignancy. An open question is the importance of LMO2 in tumor development as opposed to sustaining cancer. We have addressed this using a peptide aptamer that binds to the second LIM domain of the LMO2 protein and disrupts its function. This specificity is mediated by a conserved Cys-Cys motif, which is similar to the zinc-binding LIM domains. The peptide inhibits Lmo2 function in a mouse T-cell tumor transplantation assay by preventing Lmo2-dependent T-cell neoplasia. Lmo2 is, therefore, required for sustained T-cell tumor growth, in addition to its preleukemic effect. Interference with LMO2 complexes is a strategy for controlling LMO2-mediated cancers, and the finger structure of LMO2 is an explicit focus for drug development.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsAptamers, PeptideCHO CellsCricetinaeCricetulusDNA-Binding ProteinsDrug Delivery SystemsHumansLIM Domain ProteinsMetalloproteinsMiceMice, TransgenicModels, MolecularMolecular Sequence DataAdaptor Proteins, Signal TransducingAptamers, PeptideDNA-Binding ProteinsLIM Domain ProteinsLmo2 protein, mouseMetalloproteins

Identifiers

PMID19487290
PMCPMC2690635
OpenAlexW2159735448

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.