Evidence map›Paper›PMID 18831539›Full record

ArticleBiochemistry2008

Spin trapping investigation of peroxide- and isoniazid-induced radicals in Mycobacterium tuberculosis catalase-peroxidase.

Kalina Ranguelova, Javier Suarez, Richard S Magliozzo, Ronald P Mason

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Use of DNA microarray chips for the rapid detection ofExperimental and therapeutic medicine · 2017
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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

4 authors at 3 institutions in 1 country.

Kalina RanguelovaLaboratory of Pharmacology, National Institute of Environmental Health Sciences, National Institutes of Health, P.O. Box 12233, MD F0-01, 111 T. W. Alexander Drive, Research Triangle Park, North Carolina 27709, USA. ranguelovak@niehs.nih.gov
Javier Suarez
Richard S Magliozzo
Ronald P Mason
Brooklyn College · USCity University of New York · USThe Graduate Center, CUNY · US

Funding

Protein Derived RadicalsZIAES050139 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MASON, RONALD P · 2009 to 2018
$17.5M
Catalysis of isoniazid action by M tuberculosis KatGR01AI060014 · NIAID · BROOKLYN COLLEGE · PI MAGLIOZZO, RICHARD S · 2005 to 2009
$1.7M
CATALASE-PEROXIDASE CATALYSIS IN ANTIBIOTIC ACTIVATIONR01AI043582 · NIAID · YESHIVA UNIVERSITY · PI MAGLIOZZO, RICHARD S · 1998 to 2002
$603k
Catalysis of Isoniazid action by M. tuberculosis catalase-peroxidaseR56AI060014 · NIAID · BROOKLYN COLLEGE · PI MAGLIOZZO, RICHARD S · 2010 to 2010
$509k
Intramural NIH HHS Z99 ES999999NIAID NIH HHS AI-060014NIAID NIH HHS AI-43582NIAID NIH HHS R01 AI060014NIAID NIH HHS R56 AI060014
6 · The paper itself

Abstract

A new approach, the immuno-spin trapping assay, used a novel rabbit polyclonal anti-DMPO (5,5-dimethyl-1-pyrroline N-oxide) antiserum to detect protein radical-derived DMPO nitrone adducts in the hemoprotein Mycobacterium tuberculosis catalase-peroxidase (KatG). This work demonstrates that the formation of protein nitrone adducts is dependent on the concentrations of tert-BuOOH and DMPO as shown by Western blotting and an enzyme-linked immunosorbent assay (ELISA). We have also detected protein-protein cross-links formed during turnover of Mtb KatG driven by tert-butyl peroxide ( tert-BuOOH) or enzymatic generation of hydrogen peroxide. DMPO inhibits this dimerization due to its ability to trap the amino acid radicals responsible for the cross-linkage. Chemical modifications by tyrosine and tryptophan blockage suggest that tyrosine residues are one site of formation of the dimers. The presence of the tuberculosis drug isoniazid (INH) also prevented cross-linking as a result of its competition for the protein radical. Protein-DMPO nitrone adducts were also generated by a continuous flux of hydrogen peroxide. These findings demonstrated that the protein-based radicals were formed not only during Mtb KatG turnover with alkyl peroxides but also in the presence of hydrogen peroxide. Furthermore, the formation of protein-DMPO nitrone adducts was accelerated in the presence of isoniazid.

Indexed as

Spin TrappingAnimalsAntitubercular AgentsBacterial ProteinsCatalaseCyclic N-OxidesFree RadicalsHydrogen PeroxideIsoniazidMycobacterium tuberculosisNitrogen OxidesOxidantsRabbitsSpin Labels5,5-dimethyl-1-pyrroline-1-oxideAntitubercular AgentsBacterial ProteinsCatalaseCyclic N-OxidesFree RadicalsHydrogen PeroxideIsoniazidkatG protein, Mycobacterium tuberculosisNitrogen OxidesnitronesOxidantsSpin Labels

Identifiers

PMID18831539
PMCPMC2637803
OpenAlexW1991764245

What OpenQuestion holds

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LicenceTDM
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.