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TRIM proteins in blood cancers
Post-translational modification of proteins with ubiquitin plays a central role in regulating numerous cellular processes. E3 ligases determine the specificity of ubiquitination by mediating the transfer of ubiquitin to substrate proteins. The family of tripartite motif (TRIM) proteins make up one o...
| Autores principales: | , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Springer Netherlands
2017
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5842186/ https://www.ncbi.nlm.nih.gov/pubmed/29110249 http://dx.doi.org/10.1007/s12079-017-0423-5 |
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| author | Crawford, Lisa J. Johnston, Cliona K. Irvine, Alexandra E. |
| author_facet | Crawford, Lisa J. Johnston, Cliona K. Irvine, Alexandra E. |
| author_sort | Crawford, Lisa J. |
| collection | PubMed |
| description | Post-translational modification of proteins with ubiquitin plays a central role in regulating numerous cellular processes. E3 ligases determine the specificity of ubiquitination by mediating the transfer of ubiquitin to substrate proteins. The family of tripartite motif (TRIM) proteins make up one of the largest subfamilies of E3 ligases. Accumulating evidence suggests that dysregulation of TRIM proteins is associated with a variety of diseases. In this review we focus on the involvement of TRIM proteins in blood cancers. |
| format | Online Article Text |
| id | pubmed-5842186 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2017 |
| publisher | Springer Netherlands |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-58421862018-03-15 TRIM proteins in blood cancers Crawford, Lisa J. Johnston, Cliona K. Irvine, Alexandra E. J Cell Commun Signal Review Post-translational modification of proteins with ubiquitin plays a central role in regulating numerous cellular processes. E3 ligases determine the specificity of ubiquitination by mediating the transfer of ubiquitin to substrate proteins. The family of tripartite motif (TRIM) proteins make up one of the largest subfamilies of E3 ligases. Accumulating evidence suggests that dysregulation of TRIM proteins is associated with a variety of diseases. In this review we focus on the involvement of TRIM proteins in blood cancers. Springer Netherlands 2017-11-06 2018-03 /pmc/articles/PMC5842186/ /pubmed/29110249 http://dx.doi.org/10.1007/s12079-017-0423-5 Text en © The Author(s) 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
| spellingShingle | Review Crawford, Lisa J. Johnston, Cliona K. Irvine, Alexandra E. TRIM proteins in blood cancers |
| title | TRIM proteins in blood cancers |
| title_full | TRIM proteins in blood cancers |
| title_fullStr | TRIM proteins in blood cancers |
| title_full_unstemmed | TRIM proteins in blood cancers |
| title_short | TRIM proteins in blood cancers |
| title_sort | trim proteins in blood cancers |
| topic | Review |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5842186/ https://www.ncbi.nlm.nih.gov/pubmed/29110249 http://dx.doi.org/10.1007/s12079-017-0423-5 |
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