Evidence map›Paper›PMID 26438488›Full record

ArticleMolecular biotechnology2015

Molecular Cloning and Biochemical Characterization of the Iron Superoxide Dismutase from the Cyanobacterium Nostoc punctiforme ATCC 29133 and Its Response to Methyl Viologen-Induced Oxidative Stress.

Lakshmipyari Devi Moirangthem, Kalibulla Syed Ibrahim, Rebecca Vanlalsangi, Karin Stensjö, Peter Lindblad, Jyotirmoy Bhattacharya

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Article in Molecular biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Metalloproteins in the Biology of Heterocysts.Life (Basel, Switzerland) · 2019
    Review
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 2 institutions in 2 countries.

Lakshmipyari Devi MoirangthemDepartment of Biotechnology, Mizoram University, PB No. 190, Aizawl, Mizoram, 796004, India.
Kalibulla Syed IbrahimDepartment of Biotechnology, Mizoram University, PB No. 190, Aizawl, Mizoram, 796004, India.
Rebecca VanlalsangiDepartment of Biotechnology, Mizoram University, PB No. 190, Aizawl, Mizoram, 796004, India.
Karin StensjöDepartment of Chemistry- Ångström Laboratory, Science for Life Laboratory, Uppsala University, Box 523, 751 20, Uppsala, Sweden.
Peter LindbladDepartment of Chemistry- Ångström Laboratory, Science for Life Laboratory, Uppsala University, Box 523, 751 20, Uppsala, Sweden.
Jyotirmoy BhattacharyaDepartment of Biotechnology, Mizoram University, PB No. 190, Aizawl, Mizoram, 796004, India. jyotirmoyb@rediffmail.com.
Mizoram University · INScience for Life Laboratory · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Superoxide dismutase (SOD) detoxifies cell-toxic superoxide radicals and constitutes an important component of antioxidant machinery in aerobic organisms, including cyanobacteria. The iron-containing SOD (SodB) is one of the most abundant soluble proteins in the cytosol of the nitrogen-fixing cyanobacterium Nostoc punctiforme ATCC 29133, and therefore, we investigated its biochemical properties and response to oxidative stress. The putative SodB-encoding open reading frame Npun_R6491 was cloned and overexpressed in Escherichia coli as a C-terminally hexahistidine-tagged protein. The purified recombinant protein had a SodB specific activity of 2560 ± 48 U/mg protein at pH 7.8 and was highly thermostable. The presence of a characteristic iron absorption peak at 350 nm, and its sensitivity to H2O2 and azide, confirmed that the SodB is an iron-containing SOD. Transcript level of SodB in nitrogen-fixing cultures of N. punctiforme decreased considerably (threefold) after exposure to an oxidative stress-generating herbicide methyl viologen for 4 h. Furthermore, in-gel SOD activity analysis of such cultures grown at increasing concentrations of methyl viologen also showed a loss of SodB activity. These results suggest that SodB is not the primary scavenger of superoxide radicals induced by methyl viologen in N. punctiforme.

Indexed as

Bacterial ProteinsCloning, MolecularComputational BiologyFree Radical ScavengersHerbicidesHydrogen-Ion ConcentrationNostocOxidative StressParaquatRecombinant ProteinsSuperoxide DismutaseBacterial ProteinsFree Radical ScavengersHerbicidesParaquatRecombinant ProteinsSodB protein, BacteriaSuperoxide DismutaseCyanobacteriaIron superoxide dismutaseMethyl viologenNostoc punctiformeOxidative stressSodB overexpressionSodB transcript

Identifiers

PMID26438488
OpenAlexW1913366217

What OpenQuestion holds

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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.