Post translational modifications (PTMs) of a protein significantly impact on its structure and function which may have distinct ramifications in the biology of health and disease. Protein methylation may contribute to tumor suppressor activity, whereas histone acetylation can finely tune the genes response. Phosphorylation and SUMOylating of a protein may either enhance or mitigate their activity and play a role in their sub-compartmentalization within cell. Ubiquitination of proteins on the other hand though majorly drives their degradation, it may also impact their functionality. Abnormal status of any of these PTMs is frequently involved in cancer. Therefore, an integrative and deeper understanding of PTMs and their association with cancer pathology is important for therapeutical application for better treatment outcomes.
A precise characterization of PTMs is important for the understanding of protein regulatory mechanisms and their role in disease. However, experimental studies focusing on such PTMs of key oncogenic factors are very limited. The aim of this Research Topic is to provide a deeper insight into basic, translational, and clinical research of protein modifications.
Original Research Articles and Review Articles are invited which deal with experimental evidence and depict the roles of PTMs in context of proteins oncogenicity or tumor suppressor activity.
Topics covered in this issue include, but are not limited to:
- Effect of PTMs on functional transition of onco/regulatory proteins
- New identified PTMs of onco/regulatory proteins
- Upstream molecular mechanisms responsible for PTMs
- Identification of new downstream effectors of modified proteins
- Novel therapeutic strategies targeting PTMs for cancer treatment
Please note: manuscripts consisting solely of bioinformatics or computational analysis of public genomic or transcriptomic databases which are not accompanied by validation (independent cohort or biological validation in vitro or in vivo) are out of scope for this section and will not be accepted as part of this Research Topic.
Post translational modifications (PTMs) of a protein significantly impact on its structure and function which may have distinct ramifications in the biology of health and disease. Protein methylation may contribute to tumor suppressor activity, whereas histone acetylation can finely tune the genes response. Phosphorylation and SUMOylating of a protein may either enhance or mitigate their activity and play a role in their sub-compartmentalization within cell. Ubiquitination of proteins on the other hand though majorly drives their degradation, it may also impact their functionality. Abnormal status of any of these PTMs is frequently involved in cancer. Therefore, an integrative and deeper understanding of PTMs and their association with cancer pathology is important for therapeutical application for better treatment outcomes.
A precise characterization of PTMs is important for the understanding of protein regulatory mechanisms and their role in disease. However, experimental studies focusing on such PTMs of key oncogenic factors are very limited. The aim of this Research Topic is to provide a deeper insight into basic, translational, and clinical research of protein modifications.
Original Research Articles and Review Articles are invited which deal with experimental evidence and depict the roles of PTMs in context of proteins oncogenicity or tumor suppressor activity.
Topics covered in this issue include, but are not limited to:
- Effect of PTMs on functional transition of onco/regulatory proteins
- New identified PTMs of onco/regulatory proteins
- Upstream molecular mechanisms responsible for PTMs
- Identification of new downstream effectors of modified proteins
- Novel therapeutic strategies targeting PTMs for cancer treatment
Please note: manuscripts consisting solely of bioinformatics or computational analysis of public genomic or transcriptomic databases which are not accompanied by validation (independent cohort or biological validation in vitro or in vivo) are out of scope for this section and will not be accepted as part of this Research Topic.