Post-translational modifications (PTMs) are well-known covalent and reversible processing events catalyzed by the opposing responsible enzymes. For instance, protein acetylation and phosphorylation are reversible posttranslational modifications catalyzed by protein acetyltransferases/deacetylases and kinases/phosphatases, respectively. PTMs functionally affect many aspects of modified proteins by governing their folding, stability, localization, and binding with other proteins. Therefore, aberrancy in PTMs or the enzymes responsible for PTMs will cause diverse human diseases, including cancer, immune diseases, diabetes, aging, and inflammatory diseases. Thus, the enzymes regulating the PTMs have successfully attracted huge attention to be pharmacological targets for diseases therapies.
Given the predominant roles of PTMs in tumorigenesis, we will welcome investigators to contribute Original Research and Review articles. That will stimulate the continuing efforts to understand the potential mechanism of PTMs affecting the development of cancer as well as immunotherapy. Notably, we will mainly focus on studying or summarizing how the PTMs, including but not limited to phosphorylation, ubiquitination, methylation, and acetylation, confer to the development of cancer, as well as how to develop strategies to target the process of PTMs for benefiting the cancer immunotherapy.
We welcome the submission of manuscripts, related, but not limited to, the following sub-topics:
• Novel PTMs in tumorigenesis, and cancer immunotherapy
• PTMs induced protein functional and structural alteration in cancer immunotherapy
• Methodological developments especially for the high throughput approach in the PTMs field during tumorigenesis
• Proteins involved in PTMs signaling: writers, erasers, and readers
• PTMs and drug resistance in cancer immunity
• PTMs and metabolic homeostasis in cancer immunity
• Strategies for targeting PTMs and related proteins for cancer immunotherapy
Post-translational modifications (PTMs) are well-known covalent and reversible processing events catalyzed by the opposing responsible enzymes. For instance, protein acetylation and phosphorylation are reversible posttranslational modifications catalyzed by protein acetyltransferases/deacetylases and kinases/phosphatases, respectively. PTMs functionally affect many aspects of modified proteins by governing their folding, stability, localization, and binding with other proteins. Therefore, aberrancy in PTMs or the enzymes responsible for PTMs will cause diverse human diseases, including cancer, immune diseases, diabetes, aging, and inflammatory diseases. Thus, the enzymes regulating the PTMs have successfully attracted huge attention to be pharmacological targets for diseases therapies.
Given the predominant roles of PTMs in tumorigenesis, we will welcome investigators to contribute Original Research and Review articles. That will stimulate the continuing efforts to understand the potential mechanism of PTMs affecting the development of cancer as well as immunotherapy. Notably, we will mainly focus on studying or summarizing how the PTMs, including but not limited to phosphorylation, ubiquitination, methylation, and acetylation, confer to the development of cancer, as well as how to develop strategies to target the process of PTMs for benefiting the cancer immunotherapy.
We welcome the submission of manuscripts, related, but not limited to, the following sub-topics:
• Novel PTMs in tumorigenesis, and cancer immunotherapy
• PTMs induced protein functional and structural alteration in cancer immunotherapy
• Methodological developments especially for the high throughput approach in the PTMs field during tumorigenesis
• Proteins involved in PTMs signaling: writers, erasers, and readers
• PTMs and drug resistance in cancer immunity
• PTMs and metabolic homeostasis in cancer immunity
• Strategies for targeting PTMs and related proteins for cancer immunotherapy