Evidence map›Paper›PMID 26312997›Full record

ArticlePloS one2015

Intermediate Tyrosyl Radical and Amyloid Structure in Peroxide-Activated Cytoglobin.

Juliana C Ferreira, Marcelo F Marcondes, Marcelo Y Icimoto, Thyago H S Cardoso, Aryane Tofanello, Felipe S Pessoto, Erica G A Miranda, Tatiana Prieto, Otaciro R Nascimento, Vitor Oliveira and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Peroxidase activity of rice (Oryza sativa) hemoglobin: distinct role of tyrosines 112 and 151.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
  2. Article
  3. 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

11 authors at 3 institutions in 1 country.

Juliana C FerreiraDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, Brazil.
Marcelo F MarcondesDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, Brazil.
Marcelo Y IcimotoDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, Brazil.
Thyago H S CardosoDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, Brazil.
Aryane TofanelloLaboratório de Nanoestruturas para Biologia e Materiais Avançados, Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, Brazil.
Felipe S PessotoLaboratório de Nanoestruturas para Biologia e Materiais Avançados, Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, Brazil.
Erica G A MirandaLaboratório de Nanoestruturas para Biologia e Materiais Avançados, Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, Brazil.
Tatiana PrietoGrupo de Biofísica Molecular "Sérgio Mascarenhas," Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, Brazil; Laboratório de Nanoestruturas para Biologia e Materiais Avançados, Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, Brazil.
Otaciro R NascimentoGrupo de Biofísica Molecular "Sérgio Mascarenhas," Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, Brazil.
Vitor OliveiraDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, Brazil.
Iseli L NantesDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, Brazil; Laboratório de Nanoestruturas para Biologia e Materiais Avançados, Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, Brazil.
Universidade Federal de São Paulo · BRUniversidade Federal do ABC · BRUniversidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We characterized the peroxidase mechanism of recombinant rat brain cytoglobin (Cygb) challenged by hydrogen peroxide, tert-butylhydroperoxide and by cumene hydroperoxide. The peroxidase mechanism of Cygb is similar to that of myoglobin. Cygb challenged by hydrogen peroxide is converted to a Fe4+ oxoferryl π cation, which is converted to Fe4+ oxoferryl and tyrosyl radical detected by direct continuous wave-electron paramagnetic resonance and by 3,5-dibromo-4-nitrosobenzene sulfonate spin trapping. When organic peroxides are used as substrates at initial reaction times, and given an excess of peroxide present, the EPR signals of the corresponding peroxyl radicals precede those of the direct tyrosyl radical. This result is consistent with the use of peroxide as a reducing agent for the recycling of Cygb high-valence species. Furthermore, we found that the Cygb oxidation by peroxides leads to the formation of amyloid fibrils. This result suggests that Cygb possibly participates in the development of degenerative diseases; our findings also support the possible biological role of Cygb related to peroxidase activity.

Indexed as

AmyloidAnimalsBenzenesulfonatesCytoglobinElectron Spin Resonance SpectroscopyGlobinsHydrogen PeroxideIronNitroso CompoundsOxidation-ReductionPeroxidaseRats3,5-dibromo-4-nitrosobenzenesulfonateAmyloidBenzenesulfonatesCygb protein, ratCytoglobinGlobinsHydrogen PeroxideIronNitroso CompoundsPeroxidase

Identifiers

PMID26312997
PMCPMC4552303
OpenAlexW1681117623

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.