Dataset Information

HTPS screen of coagulation proteases at 20C with NaCl, ChCl, LiCl

ABSTRACT: Goal of the experiment is the characterization of proteases activity and specificity upon Na+ binding. Na+ is an allosteric binders that can induce a conformational change of the protease AS to regulate activity and specificity; only proteases with Y and F in position 225 can coordinate a Na+ molecule.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Federico Uliana

LAB HEAD: Ruedi Aebersold

PROVIDER: PXD022959 | Pride | 2021-02-04

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	201026_mvizovisek_001.raw	Raw
	201026_mvizovisek_001_20201028153741.raw	Raw
	201026_mvizovisek_002.raw	Raw
	201026_mvizovisek_003.raw	Raw
	201026_mvizovisek_004.raw	Raw

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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]

PMID: 33727531

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