Evidence map›Paper›PMID 28120180›Full record

ArticleInvestigational new drugs2017

A truncated apoptin protein variant selectively kills cancer cells.

Santiago Ruiz-Martínez, Jessica Castro, Maria Vilanova, Marta Bruix, Douglas V Laurents, Marc Ribó, Antoni Benito

Abstract read
PubMed Publisher
In one paragraph

Article in Investigational new drugs, 2017. 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
1.7field-weighted citation impact, top 19% 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, 7 citations in OpenAlex.

  1. Article
  2. The Role of Apoptin in Chicken Anemia Virus Replication.Pathogens (Basel, Switzerland) · 2020
    Review
  3. Review
  4. Apoptosis Triggered by ORF3 Proteins of theFrontiers in cellular and infection microbiology · 2020
    Review
  5. 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

7 authors at 2 institutions in 1 country.

Santiago Ruiz-MartínezLaboratori d'Enginyeria de Proteïnes, Departament de Biologia, Facultat de Ciències, Universitat de Girona and Institut d'Investigació Biomèdica de Girona Josep Trueta (IdIBGi), Girona, Spain.
Jessica CastroLaboratori d'Enginyeria de Proteïnes, Departament de Biologia, Facultat de Ciències, Universitat de Girona and Institut d'Investigació Biomèdica de Girona Josep Trueta (IdIBGi), Girona, Spain.
Maria VilanovaLaboratori d'Enginyeria de Proteïnes, Departament de Biologia, Facultat de Ciències, Universitat de Girona and Institut d'Investigació Biomèdica de Girona Josep Trueta (IdIBGi), Girona, Spain.
Marta BruixInstituto de Química Física "Rocasolano", Consejo Superior de Investigaciones Científicas, Serrano 119, 28006, Madrid, Spain.
Douglas V LaurentsInstituto de Química Física "Rocasolano", Consejo Superior de Investigaciones Científicas, Serrano 119, 28006, Madrid, Spain.
Marc RibóLaboratori d'Enginyeria de Proteïnes, Departament de Biologia, Facultat de Ciències, Universitat de Girona and Institut d'Investigació Biomèdica de Girona Josep Trueta (IdIBGi), Girona, Spain.
Antoni BenitoLaboratori d'Enginyeria de Proteïnes, Departament de Biologia, Facultat de Ciències, Universitat de Girona and Institut d'Investigació Biomèdica de Girona Josep Trueta (IdIBGi), Girona, Spain. antoni.benito@udg.edu.ORCID 0000-0002-9776-1003
Universitat de Girona · ESConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apoptin is a nonstructural protein encoded by one of the three open reading frames of the chicken anemia virus genome. It has attracted a great deal of interest due to its ability to induce apoptosis in multiple transformed and malignant mammalian cell lines without affecting primary and non-transformed cells. However, the use of Apoptin as an anticancer drug is restricted by its strong tendency to aggregate. A number of methods to overcome this problem have been proposed, including transduction techniques to deliver the Apoptin gene into tumor cells, but all such methods have certain drawbacks. Here we describe that a truncated variant of Apoptin, lacking residues 1 to 43, is a soluble, non-aggregating protein that maintains most of the biological properties of wild-type Apoptin when transfected into cells. We show that the cytotoxic effect of this variant is also present when it is added exogenously to cancer cells, but not to normal cells. In addition to the interest this protein has attracted as a promising therapeutic strategy, it is also an excellent model to study the structural properties of Apoptin and how they relate to its mechanism of action.

Indexed as

Antineoplastic AgentsApoptosisCapsid ProteinsCell LineCell Line, TumorDNAEscherichia coliHumansTransfectionAntineoplastic AgentsCapsid ProteinsDNAVP3 protein, Chicken anemia virusAggregationAnticancer drugApoptinProtein engineeringViral protein

Identifiers

PMID28120180
OpenAlexW2581234348

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.