Journal
MEDCHEMCOMM
Volume 5, Issue 3, Pages 338-341Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3md00281k
Keywords
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Funding
- NIH [R01-AG026660, R01-NS076117]
- Alzheimer Association [IIRG-08-90824]
- Commonwealth Foundation for Cancer Research
- Experimental Therapeutics Center of MSKCC
- William Randolph Hearst Fund in Experimental Therapeutics
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gamma-Secretase undergoes endoproteolysis of its catalytic subunit, presenilin (PS), to form PS N-terminal and C-terminal fragments (PS-NTF/CTF), which generate the active site. PS endoproteolysis, catalyzed by presenilinase (PSase), remains poorly understood and requires novel chemical approaches for its mechanistic study. CBAP is a dual inhibitor that suppresses both gamma-secretase and PSase activities. To probe gamma-secretase and PSase activity in cells, we have synthesized the clickable photoaffinity probe CBAP-BPyne. We found that CBAP-BPyne specifically labels PS1-NTF and signal peptide peptidase (SPP). CBAP-BPyne is a valuable tool to directly study the mechanism of endoproteolysis.
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