Cancer progression is characterized by rapidly proliferating cancer cells that are in need of
increased protein synthesis. Therefore, enhanced endoplasmic reticulum (ER) activity is …

During carcinogenesis, almost all the biological processes are modified in one way or
another. Among these biological processes affected, anomalies in protein synthesis are …

Recent studies have shown that 3-Deazaneplanocin A (DZNep), a histone
methyltransferase inhibitor, disrupts polycomb-repressive complex 2 (PRC2), and …

The unfolded protein response (UPR) is an evolutionarily conserved mechanism to allow
cells to adapt to stress targeting the endoplasmic reticulum (ER). Induction of ER chaperone …

PML-RARα oncoprotein is a fusion protein of promyelocytic leukemia (PML) and the retinoic
acid receptor-α (RARα) and causes acute promyelocytic leukemias (APL). A hallmark of all …

In protein folding and secretion disorders, activation of endoplasmic reticulum (ER) stress
signaling (ERSS) protects cells, alleviating stress that would otherwise trigger apoptosis …

Tumor necrosis factor alpha (TNF-α) plays a role in apoptosis and proliferation in multiple
types of cells, and defects in TNF-α-induced apoptosis are associated with various …

Endoplasmic reticulum (ER) malfunction, leading to ER stress, can be a consequence of
genome instability and hypoxic tissue environments. Cancer cells survive by acquiring or …

Changes in the expression of the protein disulfide isomerase genes PDIA3and PDIA6may
increase endoplasmic reticulum stress, leading to cellular instability and neoplasia. We …

RFP2, a gene frequently lost in various malignancies, encodes a protein with RING finger, B-
box, and coiled-coil domains that belongs to the RBCC/TRIM family of proteins. Here we …