Evidence map›Paper›PMID 26381917›Full record

ReviewRedox biology2015

Redox control of protein degradation.

Marta Pajares, Natalia Jiménez-Moreno, Irundika H K Dias, Bilge Debelec, Milica Vucetic, Kari E Fladmark, Huveyda Basaga, Samo Ribaric, Irina Milisav, Antonio Cuadrado

Open access · goldAbstract readReview
In one paragraph

Review in Redox biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 168 citations in OpenAlex.

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  16. Diabetic Retinopathy-A Review.Current diabetes reviews · 2025
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51 more citing papers are in PubMed but not listed here.

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

10 authors at 8 institutions in 6 countries.

Marta PajaresInstituto de Investigaciones Biomédicas Alberto Sols (CSIC-UAM), 28029 Madrid, Spain; Instituto de Investigación Sanitaria La Paz (IdiPAZ), 28029 Madrid, Spain; Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas (CIBERNED), ISCIII, Spain.
Natalia Jiménez-MorenoInstituto de Investigaciones Biomédicas Alberto Sols (CSIC-UAM), 28029 Madrid, Spain; Instituto de Investigación Sanitaria La Paz (IdiPAZ), 28029 Madrid, Spain; Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas (CIBERNED), ISCIII, Spain.
Irundika H K DiasAston Research Centre for Healthy Ageing, Life and Health Sciences and, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
Bilge DebelecDepartment of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, 35100 Bornova, Izmir, Turkey.
Milica VuceticDepartment of Physiology, Institute for Biological Research "Sinisa Stankovic", University of Belgrade, 11060 Belgrade, Serbia.
Kari E FladmarkDepartment of Molecular Biology, University of Bergen, Bergen N-5020, Norway.
Huveyda BasagaMolecular Biology Genetics and Bioengineering Preogram, Sabanci University, 34956 Tuzla, Istanbul, Turkey.
Samo RibaricUniversity of Ljubljana, Faculty of Medicine, Inst. of Pathophysiology, Zaloska 4, SI-1000 Ljubljana, Slovenia.
Irina MilisavUniversity of Ljubljana, Faculty of Medicine, Inst. of Pathophysiology, Zaloska 4, SI-1000 Ljubljana, Slovenia; Laboratory of Oxidative Stress Research, Faculty of Health Sciences, Zdravstvena pot 5, SI-1000 Ljubljana, Slovenia.
Antonio CuadradoInstituto de Investigaciones Biomédicas Alberto Sols (CSIC-UAM), 28029 Madrid, Spain; Instituto de Investigación Sanitaria La Paz (IdiPAZ), 28029 Madrid, Spain; Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas (CIBERNED), ISCIII, Spain. Electronic address: antonio.cuadrado@uam.es.
Instituto de Salud Carlos III · ESUniversity of Ljubljana · SIAston University · GBBiomedical Research Networking Center on Neurodegenerative Diseases · ESEge University · TRSabancı Üniversitesi · TRUniversity of Belgrade · RSUniversity of Bergen · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular proteolysis is critical to maintain timely degradation of altered proteins including oxidized proteins. This review attempts to summarize the most relevant findings about oxidant protein modification, as well as the impact of reactive oxygen species on the proteolytic systems that regulate cell response to an oxidant environment: the ubiquitin-proteasome system (UPS), autophagy and the unfolded protein response (UPR). In the presence of an oxidant environment, these systems are critical to ensure proteostasis and cell survival. An example of altered degradation of oxidized proteins in pathology is provided for neurodegenerative diseases. Future work will determine if protein oxidation is a valid target to combat proteinopathies.

Indexed as

Protein Processing, Post-TranslationalAlzheimer DiseaseAutophagyHumansNerve Tissue ProteinsOxidation-ReductionParkinson DiseasePrion DiseasesProteasome Endopeptidase ComplexProteolysisReactive Oxygen SpeciesUbiquitinUbiquitinationUnfolded Protein ResponseNerve Tissue ProteinsProteasome Endopeptidase ComplexReactive Oxygen SpeciesUbiquitinAutophagyProteasomeProtein oxidationProteolysisUnfolded protein response

Identifiers

PMID26381917
PMCPMC4576413
OpenAlexW1778688476

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.