Elastase-like Activity Is Dominant to Chymotrypsin-like Activity in 20S Proteasome’s β5 Catalytic Subunit-Reference-Cited by-同舟云学术

Elastase-like Activity Is Dominant to Chymotrypsin-like Activity in 20S Proteasome’s β5 Catalytic Subunit

Published:2016-05-02 Issue:7 Volume:11 Page:1800-1804
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Bensinger Dennis¹,Neumann Theresa¹,Scholz Christoph¹,Voss Constantin¹,Knorr Sabine²,Kuckelkorn Ulrike³,Hamacher Kay²,Kloetzel Peter-Michael³,Schmidt Boris¹

Affiliation:

1. Clemens Schöpf Institute for Organic Chemistry & Biochemistry, Technische Universität Darmstadt, Alarich Weiss Str. 4-8, 64287 Darmstadt, Germany

2. Computational Biology & Simulation, Technische Universität Darmstadt, Schnittspahnstr. 10, 64287 Darmstadt, Germany

3. Institute of Biochemistry CCM, Charité Universitätsmedizin Berlin, Charitéplatz 1/Virchowweg 6, 10117 Berlin, Germany

Funder

Deutsche Forschungsgemeinschaft

Hans und Ilse Breuer Stiftung

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.6b00023

Reference22 articles.

1. ATP-dependent degradation of ubiquitin-protein conjugates.

2. 20S Proteasome and Its Inhibitors: Crystallographic Knowledge for Drug Development

3. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome

4. Carfilzomib

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1. Cell‐Based Optimization of Covalent Reversible Ketoamide Inhibitors Bridging the Unprimed to the Primed Site of the Proteasome β5 Subunit;ChemMedChem;2019-11-12

2. Activity-based probes for the multicatalytic proteasome;The FEBS Journal;2017-02-07