Evidence map›Paper›PMID 26960678›Full record

ArticleThe protein journal2016

Unique Characteristics of Recombinant Hybrid Manganese Superoxide Dismutase from Staphylococcus equorum and S. saprophyticus.

Debbie S Retnoningrum, Anis Puji Rahayu, Dina Mulyanti, Astrid Dita, Oliver Valerius, Wangsa T Ismaya

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In one paragraph

Article in The protein journal, 2016. 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
1.3field-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, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The first crystal structure of manganese superoxide dismutase from the genus Staphylococcus.Acta crystallographica. Section F, Structural biology communications · 2018
    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 2 countries.

Debbie S RetnoningrumLaboratory of Pharmaceutical Biotechnology, School of Pharmacy, Bandung Institute of Technology, Jalan Ganesa No. 10, Bandung, 40132, Indonesia. retnoningrum@indo.net.id.
Anis Puji RahayuLaboratory of Pharmaceutical Biotechnology, School of Pharmacy, Bandung Institute of Technology, Jalan Ganesa No. 10, Bandung, 40132, Indonesia.
Dina MulyantiLaboratory of Pharmaceutical Biotechnology, School of Pharmacy, Bandung Institute of Technology, Jalan Ganesa No. 10, Bandung, 40132, Indonesia.
Astrid DitaLaboratory of Pharmaceutical Biotechnology, School of Pharmacy, Bandung Institute of Technology, Jalan Ganesa No. 10, Bandung, 40132, Indonesia.
Oliver ValeriusInstitute for Microbiology and Genetics, Georg-August-University, Grisebachstraße 8, 37077, Göttingen, Germany.
Wangsa T IsmayaDexa Laboratories of Biomolecular Sciences, Kawasan Industri Jababeka II, Jl. Industri Selatan V Blok PP No. 7, Cikarang, 17550, Indonesia.
Bandung Institute of Technology · IDPresident University · IDUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A recombinant hybrid of manganese dependent-superoxide dismutase of Staphylococcus equorum and S. saprophyticus has successfully been overexpressed in Escherichia coli BL21(DE3), purified, and characterized. The recombinant enzyme suffered from degradation and aggregation upon storage at -20 °C, but not at room temperature nor in cold. Chromatographic analysis in a size exclusion column suggested the occurrence of dimeric form, which has been reported to contribute in maintaining the stability of the enzyme. Effect of monovalent (Na(+), K(+)), divalent (Ca(2+), Mg(2+)), multivalent (Mn(2+/4+), Zn(2+/4+)) cations and anions (Cl(-), SO4 (2-)) to the enzyme stability or dimeric state depended on type of cation or anion, its concentration, and pH. However, tremendous effect was observed with 50 mM ZnSO4, in which thermostability of both the dimer and monomer was increased. Similar situation was not observed with MnSO4, and its presence was detrimental at 200 mM. Finally, chelating agent appeared to destabilize the dimer around neutral pH and dissociate it at basic pH. The monomer remained stable upon addition of ethylene diamine tetraacetic acid. Here we reported unique characteristics and stability of manganese dependent-superoxide dismutase from S. equorum/saprophyticus.

Indexed as

Bacterial ProteinsEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationRecombinant Fusion ProteinsSpectrometry, FluorescenceStaphylococcusSuperoxide DismutaseTemperatureBacterial ProteinsRecombinant Fusion ProteinsSuperoxide DismutaseDimerManganese dependent-superoxide dismutaseMonomerRecombinant hybrid proteinStaphylococcus equorumThermal stability

Identifiers

PMID26960678
OpenAlexW2295282658

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.