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Biochemical Tools for Tracking Proteolysis

期刊

JOURNAL OF PROTEOME RESEARCH
卷 20, 期 12, 页码 5264-5279

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.1c00289

关键词

proteases; protease inhibitor; N-terminomics; proteomics; LC-MS/MS; HPP; MEROPS; neXtProt

资金

  1. Alberta Innovates Summer Studentships
  2. NSERC [RGPIN-2018-05881, DGECR-201900112, 416380250]
  3. Alberta Innovates AICE concepts [202102341]
  4. Canadian Institutes of Health Research [449589]

向作者/读者索取更多资源

Proteases play a crucial role in regulating cellular processes and targeting them has led to effective therapies, despite limited knowledge about their substrates. Inhibiting proteases could be a key strategy for developing new drugs in the future.
All living organisms depend on tightly regulated cellular networks to control biological functions. Proteolysis is an important irreversible post-translational modification that regulates most, if not all, cellular processes. Proteases are a large family of enzymes that perform hydrolysis of protein substrates, leading to protein activation or degradation. The 473 known and 90 putative human proteases are divided into 5 main mechanistic groups: metalloproteases, serine proteases, cysteine proteases, threonine proteases, and aspartic acid proteases. Proteases are fundamental to all biological systems, and when dysregulated they profoundly influence disease progression. Inhibiting proteases has led to effective therapies for viral infections, cardiovascular disorders, and blood coagulation just to name a few. Between 5 and 10% of all pharmaceutical targets are proteases, despite limited knowledge about their biological roles. More than 50% of all human proteases have no known substrates. We present here a comprehensive list of all current known human proteases. We also present current and novel biochemical tools to characterize protease functions in vitro, in vivo, and ex vivo. These tools make it achievable to define both beneficial and detrimental activities of proteases in health and disease.

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