Evidence map›Paper›PMID 27253887›Full record

ArticlePloS one2016

Recombinant L-Asparaginase from Zymomonas mobilis: A Potential New Antileukemic Agent Produced in Escherichia coli.

Karen Einsfeldt, Isis Cavalcante Baptista, Juliana Christina Castanheira Vicente Pereira, Isabele Campos Costa-Amaral, Elaine Sobral da Costa, Maria Cecília Menks Ribeiro, Marcelo Gerardin Poirot Land, Tito Lívio Moitinho Alves, Ariane Leites Larentis, Rodrigo Volcan Almeida

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 7% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Recombinant l-Asparaginase II fromIndian journal of microbiology · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Karen EinsfeldtPrograma de Engenharia Química, COPPE, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Isis Cavalcante BaptistaPrograma de Engenharia Química, COPPE, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Juliana Christina Castanheira Vicente PereiraPrograma de Engenharia Química, COPPE, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Isabele Campos Costa-AmaralPrograma de Saúde Pública e Meio Ambiente, Escola Nacional de Saúde Pública Sergio Arouca (ENSP), Centro de Estudos da Saúde do Trabalhador e Ecologia Humana (CESTEH), Fundação Oswaldo Cruz (FIOCRUZ), Rio de Janeiro, Rio de Janeiro, Brazil.
Elaine Sobral da CostaPrograma de Pós-Graduação em Clínica Médica, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Maria Cecília Menks RibeiroPrograma de Pós-Graduação em Clínica Médica, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Marcelo Gerardin Poirot LandPrograma de Pós-Graduação em Clínica Médica, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Tito Lívio Moitinho AlvesPrograma de Engenharia Química, COPPE, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Ariane Leites LarentisPrograma de Saúde Pública e Meio Ambiente, Escola Nacional de Saúde Pública Sergio Arouca (ENSP), Centro de Estudos da Saúde do Trabalhador e Ecologia Humana (CESTEH), Fundação Oswaldo Cruz (FIOCRUZ), Rio de Janeiro, Rio de Janeiro, Brazil.
Rodrigo Volcan AlmeidaPrograma de Pós-Graduação em Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro (UFRJ), Rio de Janeiro, Brazil.
Universidade Federal do Rio de Janeiro · BREscola Nacional de Saúde Pública · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-asparaginase is an enzyme used as a chemotherapeutic agent, mainly for treating acute lymphoblastic leukemia. In this study, the gene of L-asparaginase from Zymomonas mobilis was cloned in pET vectors, fused to a histidine tag, and had its codons optimized. The L-asparaginase was expressed extracellularly and intracellularly (cytoplasmically) in Escherichia coli in far larger quantities than obtained from the microorganism of origin, and sufficient for initial cytotoxicity tests on leukemic cells. The in silico analysis of the protein from Z. mobilis indicated the presence of a signal peptide in the sequence, as well as high identity to other sequences of L-asparaginases with antileukemic activity. The protein was expressed in a bioreactor with a complex culture medium, yielding 0.13 IU/mL extracellular L-asparaginase and 3.6 IU/mL intracellular L-asparaginase after 4 h of induction with IPTG. The cytotoxicity results suggest that recombinant L-asparaginase from Z. mobilis expressed extracellularly in E.coli has a cytotoxic and cytostatic effect on leukemic cells.

Indexed as

Antineoplastic AgentsApoptosisAsparaginaseBase SequenceBioreactorsCell CycleCell Line, TumorCell Nucleus ShapeCell ProliferationCell SurvivalChildChild, PreschoolCloning, MolecularComputer SimulationEscherichia coliFemaleAntineoplastic AgentsAsparaginaseRecombinant Proteins

Identifiers

PMID27253887
PMCPMC4890785
OpenAlexW2409136364

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.