Development of CBAP-BPyne, a probe for γ-secretase and presenilinase Journal Article

   


Authors: Gestsik, N.; Ballard, T. E.; Am Ende, C. W.; Johnson, D. S.; Li, Y. M.
Article Title: Development of CBAP-BPyne, a probe for γ-secretase and presenilinase
Abstract: γ-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 γ-secretase and PSase activities. To probe γ-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. © 2014 The Royal Society of Chemistry.
Journal Title: MedChemComm
Volume: 5
Issue: 3
ISSN: 2040-2503
Publisher: Royal Society of Chemistry  
Date Published: 2014-01-01
Start Page: 338
End Page: 341
Language: English
DOI: 10.1039/c3md00281k
PROVIDER: scopus
PMCID: PMC4048150
PUBMED: 24914408
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-84895079393&partnerID=40&md5=ad35cde6d62b2e41b27acd006949fc07
Notes: Export Date: 2 April 2014 -- CODEN: MCCEA -- Source: Scopus
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MSK Authors
  1. Yueming Li
    132 Li
  2. Natalya Gestsik
    8 Gestsik
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