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Cullin 3 as a novel target in diverse pathologies()
Recent evidence suggests that the malfunctioning disposal system of cell protein called ubiquitin–proteasome system (UPS) plays an important role in the development of disorders, including cancer and neurodegenerative diseases. Accumulating evidence suggests that the abnormal regulation of the E3 ub...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3757711/ https://www.ncbi.nlm.nih.gov/pubmed/24024173 http://dx.doi.org/10.1016/j.redox.2013.07.003 |
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author | Andérica-Romero, Ana Cristina González-Herrera, Irma Gabriela Santamaría, Abel Pedraza-Chaverri, José |
author_facet | Andérica-Romero, Ana Cristina González-Herrera, Irma Gabriela Santamaría, Abel Pedraza-Chaverri, José |
author_sort | Andérica-Romero, Ana Cristina |
collection | PubMed |
description | Recent evidence suggests that the malfunctioning disposal system of cell protein called ubiquitin–proteasome system (UPS) plays an important role in the development of disorders, including cancer and neurodegenerative diseases. Accumulating evidence suggests that the abnormal regulation of the E3 ubiquitin ligases, essential components of the UPS, contributes to uncontrolled proliferation, genomic instability and cancer, since these ligases and their substrates are involved in the regulation of cell cycle progression, gene transcription, signal transduction, DNA replication and others. Through selective degradation of specific substrates, E3 ligases regulate different biological processes. Cullins are a family of proteins that confer substrate specificity to multimeric complex of E3 ligases acting as scaffold proteins. So far, seven members of the cullin family of proteins have been identified. Interestingly, the data generated by several groups indicate that cullin 3 (Cul3) has begun to emerge as a protein involved in the etiopathology of multiple diseases. In this paper we examine the latest advances in basic research on the biology of Cul3 and how it could help to direct drug discovery efforts on this target. |
format | Online Article Text |
id | pubmed-3757711 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-37577112013-09-10 Cullin 3 as a novel target in diverse pathologies() Andérica-Romero, Ana Cristina González-Herrera, Irma Gabriela Santamaría, Abel Pedraza-Chaverri, José Redox Biol Mini Review Recent evidence suggests that the malfunctioning disposal system of cell protein called ubiquitin–proteasome system (UPS) plays an important role in the development of disorders, including cancer and neurodegenerative diseases. Accumulating evidence suggests that the abnormal regulation of the E3 ubiquitin ligases, essential components of the UPS, contributes to uncontrolled proliferation, genomic instability and cancer, since these ligases and their substrates are involved in the regulation of cell cycle progression, gene transcription, signal transduction, DNA replication and others. Through selective degradation of specific substrates, E3 ligases regulate different biological processes. Cullins are a family of proteins that confer substrate specificity to multimeric complex of E3 ligases acting as scaffold proteins. So far, seven members of the cullin family of proteins have been identified. Interestingly, the data generated by several groups indicate that cullin 3 (Cul3) has begun to emerge as a protein involved in the etiopathology of multiple diseases. In this paper we examine the latest advances in basic research on the biology of Cul3 and how it could help to direct drug discovery efforts on this target. Elsevier 2013-07-16 /pmc/articles/PMC3757711/ /pubmed/24024173 http://dx.doi.org/10.1016/j.redox.2013.07.003 Text en © 2013 The Authors http://creativecommons.org/licenses/BY-license/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Mini Review Andérica-Romero, Ana Cristina González-Herrera, Irma Gabriela Santamaría, Abel Pedraza-Chaverri, José Cullin 3 as a novel target in diverse pathologies() |
title | Cullin 3 as a novel target in diverse pathologies() |
title_full | Cullin 3 as a novel target in diverse pathologies() |
title_fullStr | Cullin 3 as a novel target in diverse pathologies() |
title_full_unstemmed | Cullin 3 as a novel target in diverse pathologies() |
title_short | Cullin 3 as a novel target in diverse pathologies() |
title_sort | cullin 3 as a novel target in diverse pathologies() |
topic | Mini Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3757711/ https://www.ncbi.nlm.nih.gov/pubmed/24024173 http://dx.doi.org/10.1016/j.redox.2013.07.003 |
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