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HECT E3s and human disease
In a simplified view, members of the HECT E3 family have a modular structure consisting of the C-terminal HECT domain, which is catalytically involved in the attachment of ubiquitin to substrate proteins, and N-terminal extensions of variable length and sequence that mediate the substrate specificit...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2007
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106370/ https://www.ncbi.nlm.nih.gov/pubmed/18047743 http://dx.doi.org/10.1186/1471-2091-8-S1-S6 |
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author | Scheffner, Martin Staub, Olivier |
author_facet | Scheffner, Martin Staub, Olivier |
author_sort | Scheffner, Martin |
collection | PubMed |
description | In a simplified view, members of the HECT E3 family have a modular structure consisting of the C-terminal HECT domain, which is catalytically involved in the attachment of ubiquitin to substrate proteins, and N-terminal extensions of variable length and sequence that mediate the substrate specificity of the respective HECT E3. Although the physiologically relevant substrates of most HECT E3s have remained elusive, it is becoming increasingly clear that HECT E3s play an important role in sporadic and hereditary human diseases including cancer, cardiovascular (Liddle's syndrome) and neurological (Angelman syndrome) disorders, and/or in disease-relevant processes including bone homeostasis, immune response and retroviral budding. Thus, molecular approaches to target the activity of distinct HECT E3s, regulators thereof, and/or of HECT E3 substrates could prove valuable in the treatment of the respective diseases. Publication history: Republished from Current BioData's Targeted Proteins database (TPdb; ). |
format | Text |
id | pubmed-2106370 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-21063702007-12-05 HECT E3s and human disease Scheffner, Martin Staub, Olivier BMC Biochem Review In a simplified view, members of the HECT E3 family have a modular structure consisting of the C-terminal HECT domain, which is catalytically involved in the attachment of ubiquitin to substrate proteins, and N-terminal extensions of variable length and sequence that mediate the substrate specificity of the respective HECT E3. Although the physiologically relevant substrates of most HECT E3s have remained elusive, it is becoming increasingly clear that HECT E3s play an important role in sporadic and hereditary human diseases including cancer, cardiovascular (Liddle's syndrome) and neurological (Angelman syndrome) disorders, and/or in disease-relevant processes including bone homeostasis, immune response and retroviral budding. Thus, molecular approaches to target the activity of distinct HECT E3s, regulators thereof, and/or of HECT E3 substrates could prove valuable in the treatment of the respective diseases. Publication history: Republished from Current BioData's Targeted Proteins database (TPdb; ). BioMed Central 2007-11-22 /pmc/articles/PMC2106370/ /pubmed/18047743 http://dx.doi.org/10.1186/1471-2091-8-S1-S6 Text en Copyright © 2007 Scheffner and Staub; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Scheffner, Martin Staub, Olivier HECT E3s and human disease |
title | HECT E3s and human disease |
title_full | HECT E3s and human disease |
title_fullStr | HECT E3s and human disease |
title_full_unstemmed | HECT E3s and human disease |
title_short | HECT E3s and human disease |
title_sort | hect e3s and human disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106370/ https://www.ncbi.nlm.nih.gov/pubmed/18047743 http://dx.doi.org/10.1186/1471-2091-8-S1-S6 |
work_keys_str_mv | AT scheffnermartin hecte3sandhumandisease AT staubolivier hecte3sandhumandisease |