Mechanism of cleavage of alpha-synuclein by the 20S proteasome and modulation of its degradation by the RedOx state of the N-terminal methionines

Author:

Alvarez-Castelao Beatriz,Goethals Marc,Vandekerckhove Joël,Castaño José G.

Funder

MINECO

Comunidad de Madrid

CIBERNED

Fund for Scientific Research-Flanders (Belgium)

Ghent University

European Union Interaction Proteome

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference63 articles.

1. Synphilin-1 inhibits alpha-synuclein degradation by the proteasome;Alvarez-Castelao;Cell. Mol. Life Sci.,2011

2. Thioredoxin Txnl1/TRP32 is a redox active co-factor of the 26S proteasome;Andersen;J. Biol. Chem.,2009

3. Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex;Arribas;J. Biol. Chem.,1994

4. Kinetic studies of the differential effect of detergents on the peptidase activities of the multicatalytic proteinase from rat liver;Arribas;J. Biol. Chem.,1990

5. Site-specific methionine oxidation initiates calmodulin degradation by the 20S proteasome;Balog;Biochemistry,2009

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