Evidence map›Paper›PMID 24349308›Full record

ArticlePloS one2013

TALE-PvuII fusion proteins--novel tools for gene targeting.

Mert Yanik, Jamal Alzubi, Thomas Lahaye, Toni Cathomen, Alfred Pingoud, Wolfgang Wende

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. 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

6 authors at 3 institutions in 1 country.

Mert YanikInstitute for Biochemistry, Justus-Liebig-University Giessen, Giessen, Germany.
Jamal AlzubiInstitute for Cell and Gene Therapy, University Medical Center Freiburg, Freiburg, Germany ; Center for Chronic Immunodeficiency, University Medical Center Freiburg, Freiburg, Germany.
Thomas LahayeZMBP - General Genetics, University of Tuebingen, Tuebingen, Germany.
Toni CathomenInstitute for Cell and Gene Therapy, University Medical Center Freiburg, Freiburg, Germany ; Center for Chronic Immunodeficiency, University Medical Center Freiburg, Freiburg, Germany.
Alfred PingoudInstitute for Biochemistry, Justus-Liebig-University Giessen, Giessen, Germany.
Wolfgang WendeInstitute for Biochemistry, Justus-Liebig-University Giessen, Giessen, Germany.
University of Giessen · DEUniversity Medical Center Freiburg · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Zinc finger nucleases (ZFNs) consist of zinc fingers as DNA-binding module and the non-specific DNA-cleavage domain of the restriction endonuclease FokI as DNA-cleavage module. This architecture is also used by TALE nucleases (TALENs), in which the DNA-binding modules of the ZFNs have been replaced by DNA-binding domains based on transcription activator like effector (TALE) proteins. Both TALENs and ZFNs are programmable nucleases which rely on the dimerization of FokI to induce double-strand DNA cleavage at the target site after recognition of the target DNA by the respective DNA-binding module. TALENs seem to have an advantage over ZFNs, as the assembly of TALE proteins is easier than that of ZFNs. Here, we present evidence that variant TALENs can be produced by replacing the catalytic domain of FokI with the restriction endonuclease PvuII. These fusion proteins recognize only the composite recognition site consisting of the target site of the TALE protein and the PvuII recognition sequence (addressed site), but not isolated TALE or PvuII recognition sites (unaddressed sites), even at high excess of protein over DNA and long incubation times. In vitro, their preference for an addressed over an unaddressed site is > 34,000-fold. Moreover, TALE-PvuII fusion proteins are active in cellula with minimal cytotoxicity.

Indexed as

Binding SitesCell LineDNA-Binding ProteinsDNA CleavageDNA-Cytosine MethylasesGene TargetingHomeodomain ProteinsHumansModels, MolecularProtein ConformationProtein MultimerizationRecombinant Fusion ProteinsSubstrate SpecificityDNA-Binding ProteinsDNA-Cytosine MethylasesDNA modification methylase PvuIIHomeodomain ProteinsRecombinant Fusion Proteins

Identifiers

PMID24349308
PMCPMC3857828
OpenAlexW2098634358

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.