Targeting ubiquitin signaling for cancer immunotherapy

Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The development and clinical application of immune checkpoint inhibitors represent one of the most extraordinary accomplishments in cancer immunotherapy. In a...

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Published inSignal transduction and targeted therapy Vol. 6; no. 1; pp. 16 - 15
Main Authors Zhou, Xiaofei, Sun, Shao-Cong
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 13.01.2021
Nature Publishing Group
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Abstract Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The development and clinical application of immune checkpoint inhibitors represent one of the most extraordinary accomplishments in cancer immunotherapy. In addition, considerable progress is being made in understanding the mechanism of antitumor immunity and characterizing novel targets for developing additional therapeutic approaches. One active area of investigation is protein ubiquitination, a post-translational mechanism of protein modification that regulates the function of diverse immune cells in antitumor immunity. Accumulating studies suggest that E3 ubiquitin ligases and deubiquitinases form a family of potential targets to be exploited for enhancing antitumor immunity in cancer immunotherapy.
AbstractList Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The development and clinical application of immune checkpoint inhibitors represent one of the most extraordinary accomplishments in cancer immunotherapy. In addition, considerable progress is being made in understanding the mechanism of antitumor immunity and characterizing novel targets for developing additional therapeutic approaches. One active area of investigation is protein ubiquitination, a post-translational mechanism of protein modification that regulates the function of diverse immune cells in antitumor immunity. Accumulating studies suggest that E3 ubiquitin ligases and deubiquitinases form a family of potential targets to be exploited for enhancing antitumor immunity in cancer immunotherapy.
Abstract Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The development and clinical application of immune checkpoint inhibitors represent one of the most extraordinary accomplishments in cancer immunotherapy. In addition, considerable progress is being made in understanding the mechanism of antitumor immunity and characterizing novel targets for developing additional therapeutic approaches. One active area of investigation is protein ubiquitination, a post-translational mechanism of protein modification that regulates the function of diverse immune cells in antitumor immunity. Accumulating studies suggest that E3 ubiquitin ligases and deubiquitinases form a family of potential targets to be exploited for enhancing antitumor immunity in cancer immunotherapy.
Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The development and clinical application of immune checkpoint inhibitors represent one of the most extraordinary accomplishments in cancer immunotherapy. In addition, considerable progress is being made in understanding the mechanism of antitumor immunity and characterizing novel targets for developing additional therapeutic approaches. One active area of investigation is protein ubiquitination, a post-translational mechanism of protein modification that regulates the function of diverse immune cells in antitumor immunity. Accumulating studies suggest that E3 ubiquitin ligases and deubiquitinases form a family of potential targets to be exploited for enhancing antitumor immunity in cancer immunotherapy.Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The development and clinical application of immune checkpoint inhibitors represent one of the most extraordinary accomplishments in cancer immunotherapy. In addition, considerable progress is being made in understanding the mechanism of antitumor immunity and characterizing novel targets for developing additional therapeutic approaches. One active area of investigation is protein ubiquitination, a post-translational mechanism of protein modification that regulates the function of diverse immune cells in antitumor immunity. Accumulating studies suggest that E3 ubiquitin ligases and deubiquitinases form a family of potential targets to be exploited for enhancing antitumor immunity in cancer immunotherapy.
ArticleNumber 16
Author Sun, Shao-Cong
Zhou, Xiaofei
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  year: 2021
  text: 2021-01-13
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PublicationTitle Signal transduction and targeted therapy
PublicationTitleAbbrev Sig Transduct Target Ther
PublicationTitleAlternate Signal Transduct Target Ther
PublicationYear 2021
Publisher Nature Publishing Group UK
Nature Publishing Group
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Snippet Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The development...
Abstract Cancer immunotherapy has become an attractive approach of cancer treatment with tremendous success in treating various advanced malignancies. The...
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SubjectTerms 631/250/251
631/250/580
Cancer
Cancer Research
Cell Biology
Deubiquitinating Enzymes - immunology
Humans
Immune Checkpoint Inhibitors - therapeutic use
Immunotherapy
Internal Medicine
Medicine
Medicine & Public Health
Neoplasm Proteins - immunology
Neoplasms - immunology
Neoplasms - therapy
Oncology
Pathology
Review
Review Article
Ubiquitin - immunology
Ubiquitin-Protein Ligases - immunology
Ubiquitination - immunology
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Title Targeting ubiquitin signaling for cancer immunotherapy
URI https://link.springer.com/article/10.1038/s41392-020-00421-2
https://www.ncbi.nlm.nih.gov/pubmed/33436547
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https://pubmed.ncbi.nlm.nih.gov/PMC7804490
https://doaj.org/article/d9592e3b2b9f482e870503d222a2096c
Volume 6
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