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Protein ISGylation: a posttranslational modification with implications for malignant neoplasms
Interferon (IFN)-stimulated gene 15 (ISG15) is a member of the ubiquitin-like (UBL) protein family that can modify specific proteins via a catalytic process called ISGylation. This posttranslational modification can modulate the stability of the ISGylated proteins and protein-protein interactions. S...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Open Exploration Publishing
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10497404/ https://www.ncbi.nlm.nih.gov/pubmed/37711589 http://dx.doi.org/10.37349/etat.2023.00162 |
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author | Tecalco-Cruz, Angeles C. Zepeda-Cervantes, Jesús |
author_facet | Tecalco-Cruz, Angeles C. Zepeda-Cervantes, Jesús |
author_sort | Tecalco-Cruz, Angeles C. |
collection | PubMed |
description | Interferon (IFN)-stimulated gene 15 (ISG15) is a member of the ubiquitin-like (UBL) protein family that can modify specific proteins via a catalytic process called ISGylation. This posttranslational modification can modulate the stability of the ISGylated proteins and protein-protein interactions. Some proteins modified by ISG15 have been identified in malignant neoplasms, suggesting the functional relevance of ISGylation in cancer. This review discusses the ISGylated proteins reported in malignant neoplasms that suggest the potential of ISG15 as a biomarker and therapeutic target in cancer. |
format | Online Article Text |
id | pubmed-10497404 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Open Exploration Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-104974042023-09-14 Protein ISGylation: a posttranslational modification with implications for malignant neoplasms Tecalco-Cruz, Angeles C. Zepeda-Cervantes, Jesús Explor Target Antitumor Ther Review Interferon (IFN)-stimulated gene 15 (ISG15) is a member of the ubiquitin-like (UBL) protein family that can modify specific proteins via a catalytic process called ISGylation. This posttranslational modification can modulate the stability of the ISGylated proteins and protein-protein interactions. Some proteins modified by ISG15 have been identified in malignant neoplasms, suggesting the functional relevance of ISGylation in cancer. This review discusses the ISGylated proteins reported in malignant neoplasms that suggest the potential of ISG15 as a biomarker and therapeutic target in cancer. Open Exploration Publishing 2023 2023-08-31 /pmc/articles/PMC10497404/ /pubmed/37711589 http://dx.doi.org/10.37349/etat.2023.00162 Text en © The Author(s) 2023. https://creativecommons.org/licenses/by/4.0/This is an Open Access article licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, sharing, adaptation, distribution and reproduction in any medium or format, for any purpose, even commercially, as long as 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 Tecalco-Cruz, Angeles C. Zepeda-Cervantes, Jesús Protein ISGylation: a posttranslational modification with implications for malignant neoplasms |
title | Protein ISGylation: a posttranslational modification with implications for malignant neoplasms |
title_full | Protein ISGylation: a posttranslational modification with implications for malignant neoplasms |
title_fullStr | Protein ISGylation: a posttranslational modification with implications for malignant neoplasms |
title_full_unstemmed | Protein ISGylation: a posttranslational modification with implications for malignant neoplasms |
title_short | Protein ISGylation: a posttranslational modification with implications for malignant neoplasms |
title_sort | protein isgylation: a posttranslational modification with implications for malignant neoplasms |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10497404/ https://www.ncbi.nlm.nih.gov/pubmed/37711589 http://dx.doi.org/10.37349/etat.2023.00162 |
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