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GP96 is a major endoplasmic reticulum (ER)-resident heat shock protein and a paralog of HSP90. It functions as an ATP-dependent molecular chaperone, playing essential roles in protein folding, quality control, and cellular homeostasis. It is induced by the accumulation of misfolded proteins in the ER. GP96 is also involved in immune system modulation, particularly in antigen presentation and dendritic cell activation, bridging innate and adaptive immunity. It plays a pro-oncogenic role, especially in liver cancer.
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