Fast Profiling of Protease Specificity reveals similar substrate specificities for cathepsins K, L and S
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Blood Cell, Blood
SUBMITTER: 
Emmy Van Quickelberghe
LAB HEAD: Kris Gevaert
PROVIDER: PXD001536 | Pride | 2015-02-10
REPOSITORIES: Pride
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Fast profiling of protease specificity reveals similar substrate specificities for cathepsins K, L and S.
Vizovišek Matej M Vidmar Robert R Van Quickelberghe Emmy E Impens Francis F Andjelković Uroš U Sobotič Barbara B Stoka Veronika V Gevaert Kris K Turk Boris B Fonović Marko M
Proteomics 20150309 14
Proteases are important effectors of numerous physiological and pathological processes. Reliable determination of a protease's specificity is crucial to understand protease function and to develop activity-based probes and inhibitors. During the last decade, various proteomic approaches for profiling protease substrate specificities were reported. Although most of these approaches can identify up to thousands of substrate cleavage events in a single experiment, they are often time consuming and ...[more]
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