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Emerging role of misfolded proteins in human cancer

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Almost all the genetic aberrations or environmental carcinogens linked to human cancer can induce qualitative changes in protein conformation, ultimately leading to formation of proteins with misfolded conformation. Despite this apparent link of oncogenic aberrations to the production of misfolded proteins, ...

Almost all the genetic aberrations or environmental carcinogens linked to human cancer can induce qualitative changes in protein conformation, ultimately leading to formation of proteins with misfolded conformation. Despite this apparent link of oncogenic aberrations to the production of misfolded proteins, evidence suggesting a fundamental role of misfolded proteins in human cancer has emerged just recently. Due to the highly transitional nature of the misfolded state, a misfolded protein can acquire pleotropic function and trigger malignant transformation through a variety of unique mechanisms. Apart from the simple “loss of normal function” effect due to destabilization of native state, a misfolded protein can acquire pleotropic function through the destabilization of its misfolded state and can promote malignant growth and transformation through the activation of variety of oncogenic pathways such as unfolded protein response (UPR), autophagy and metabolic reprograming. In this way, a single misfolded protein can alter the conformation and function of many cellular proteins and derail multiple regulatory pathways. However, due to the highly transitional state of the misfolded conformation, a misfolded protein also offers the best possible avenue for effective therapeutic intervention.

The aim of this Research Topic is to generate novel insights and unique hypothesis based on the oncogenic misfolded proteins and their cellular consequences such as ER stress, UPR, autophagy and metabolic reprogramming; and apply these insights into the design and development of misfolded protein based novel molecular targeted therapeutic approaches for cancer. We welcome contributions from scientists working on oncogenic aberrations that could produce misfolded proteins, oncogenic signalling linked to aberrant post-translational modifications and cellular protein quality control mechanism such as unfolded protein response (UPR), autophagy and metabolic reprogramming.


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