Identification C3 cleavage sites by alpha-Thrombin
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Elite
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Federico Uliana
LAB HEAD: Ruedi Aebersold
PROVIDER: PXD022971 | Pride | 2021-02-04
REPOSITORIES: Pride
Publications
Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen.
Uliana Federico F Vizovišek Matej M Acquasaliente Laura L Ciuffa Rodolfo R Fossati Andrea A Frommelt Fabian F Goetze Sandra S Wollscheid Bernd B Gstaiger Matthias M De Filippis Vincenzo V Auf dem Keller Ulrich U Aebersold Ruedi R
Nature communications 20210316 1
Proteases are among the largest protein families and critical regulators of biochemical processes like apoptosis and blood coagulation. Knowledge of proteases has been expanded by the development of proteomic approaches, however, technology for multiplexed screening of proteases within native environments is currently lacking behind. Here we introduce a simple method to profile protease activity based on isolation of protease products from native lysates using a 96FASP filter, their analysis in ...[more]
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