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Proteolytic protein substrates represent a vast and heterogeneous group of proteins that are subject to enzymatic cleavage by proteases. This term does not refer to a single therapeutic target but rather a functional class of molecules involved in critical biological processes such as the cell cycle, apoptosis, and signal transduction [1, 2]. In many diseases, the aberrant proteolysis of specific substrates—such as the cleavage of amyloid precursor protein in Alzheimer's disease or the degradation of the extracellular matrix in cancer metastasis—drives pathology [3, 4]. While most pharmacological interventions target the proteases themselves (e.g., protease inhibitors), the substrates are the functional recipients of these actions and their cleavage products often serve as vital biomarkers [5]. Because the term encompasses nearly all proteins that can be degraded or processed, it is too broad for specific drug-target classification and typically requires narrowing to a specific protein or pathway.
Modulation of proteolytic processing through the inhibition of proteases or the stabilization of the substrate to prevent enzymatic degradation.
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