The unfolded protein response (UPR) is an evolutionarily conserved mechanism that
activates both proapoptotic and survival pathways to allow eukaryotic cells to adapt to …

Abstract Glucose-regulated protein 78 (GRP78)/BiP is a multifunctional protein which plays
a major role in endoplasmic reticulum (ER) protein processing, protein quality control …

Due to inadequate vascularization and rapid growth, tumor cells experience hypoxia and
receive reduced amounts of nutrients including both amino acids and glucose. Inadequate …

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 …

Poor chemosensitivity and the development of chemoresistance remain major obstacles to
successful chemotherapy of malignant gliomas. GRP78 is a key regulator of the unfolded …

In response to cell stress, cancer cells often activate the endoplasmic reticulum (EnR) stress
sensor, the unfolded protein response (UPR). Little was known about the potential role in …

Increased protein translation in cells and various factors in the tumor microenvironment can
induce endoplasmic reticulum (ER) stress, which initiates the unfolded protein response …

GRP78, also referred to as BiP, is a central regulator of endoplasmic reticulum (ER) function
due to its roles in protein folding and assembly, targeting misfolded protein for degradation …

GRP78/BiP is a major endoplasmic reticulum (ER) chaperone protein critical for protein
quality control of the ER, as well as controlling the activation of the ER-transmembrane …

Cancer cells adapt to chronic stress in the tumor microenvironment by inducing the
expression of GRP78/BiP, a major endoplasmic reticulum chaperone with Ca2+-binding and …