Evidence map›Paper›PMID 26045557›Full record

ArticleThe Journal of biological chemistry2015

Engineering a Nickase on the Homing Endonuclease I-DmoI Scaffold.

Rafael Molina, María José Marcaida, Pilar Redondo, Marco Marenchino, Phillippe Duchateau, Marco D'Abramo, Guillermo Montoya, Jesús Prieto

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Applications of Alternative Nucleases in the Age of CRISPR/Cas9.International journal of molecular sciences · 2017
    Review
  4. 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

8 authors at 3 institutions in 3 countries.

Rafael MolinaFrom the Macromolecular Crystallography Group and.
María José MarcaidaFrom the Macromolecular Crystallography Group and.
Pilar RedondoFrom the Macromolecular Crystallography Group and.
Marco MarenchinoNMR Unit, Structural Biology and Biocomputing Program, Spanish National Cancer Research Center (CNIO), c/Melchor Fernández Almagro 3, 28029 Madrid, Spain.
Phillippe DuchateauCELLECTIS S.A., 8 Rue de la Croix Jarry, 75013 Paris, France.
Marco D'AbramoDepartment of Chemistry, University of Rome "La Sapienza," Piazzale Aldo Moro 5, 00185, Rome, Italy, and.
Guillermo MontoyaFrom the Macromolecular Crystallography Group and Novo Nordisk Foundation Center for Protein Research, Protein Structure and Function Program, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark guillermo.montoya@cpr.ku.dk.
Jesús PrietoFrom the Macromolecular Crystallography Group and jprieto@cnio.es.
Centro de Investigación del Cáncer · ESSpanish National Cancer Research Centre · ESSapienza University of Rome · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homing endonucleases are useful tools for genome modification because of their capability to recognize and cleave specifically large DNA targets. These endonucleases generate a DNA double strand break that can be repaired by the DNA damage response machinery. The break can be repaired by homologous recombination, an error-free mechanism, or by non-homologous end joining, a process susceptible to introducing errors in the repaired sequence. The type of DNA cleavage might alter the balance between these two alternatives. The use of "nickases" producing a specific single strand break instead of a double strand break could be an approach to reduce the toxicity associated with non-homologous end joining by promoting the use of homologous recombination to repair the cleavage of a single DNA break. Taking advantage of the sequential DNA cleavage mechanism of I-DmoI LAGLIDADG homing endonuclease, we have developed a new variant that is able to cut preferentially the coding DNA strand, generating a nicked DNA target. Our structural and biochemical analysis shows that by decoupling the action of the catalytic residues acting on each strand we can inhibit one of them while keeping the other functional.

Indexed as

Gene TargetingProtein EngineeringAmino Acid MotifsCatalytic DomainCircular DichroismCrystallography, X-RayDeoxyribonuclease IDeoxyribonucleases, Type I Site-SpecificDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA End-Joining RepairHomologous RecombinationMolecular Dynamics SimulationDeoxyribonuclease IDeoxyribonucleases, Type I Site-SpecificDNA-Binding Proteinsendodeoxyribonuclease I-Dmo Igene targetinggeneticsnucleasesprotein-DNA interactionprotein engineeringprotein-nucleic acid interactionx-ray crystallography

Identifiers

PMID26045557
PMCPMC4513113
OpenAlexW2211382893

What OpenQuestion holds

Textmetadata
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.