Stabilizing Inactive Conformations of MALT1 as an Effective Approach to Inhibit Its Protease Activity-Reference-Cited by-同舟云学术

Stabilizing Inactive Conformations of MALT1 as an Effective Approach to Inhibit Its Protease Activity

Published:2020-06-17 Issue:9 Volume:3 Page:2000078
ISSN:2366-3987
Container-title:Advanced Therapeutics
language:en
Short-container-title:Adv. Therap.

Author:

Hughes Nicola¹,Erbel Paul¹,Bornancin Frédéric¹,Wiesmann Christian¹,Schiering Nikolaus¹,Villard Frédéric¹,Decock Arnaud¹,Rubi Bertran²,Melkko Samu¹,Spanka Carsten¹,Buschmann Nicole¹,Pissot‐Soldermann Carole¹,Simic Oliver¹,Beerli René¹,Sorge Mickael¹,Tintelnot‐Blomley Marina¹,Beltz Karen¹,Régnier Catherine H.¹,Quancard Jean¹,Schlapbach Achim¹,Langlois Jean‐Baptiste¹^ORCID,Renatus Martin¹

Affiliation:

1. Novartis Institutes for Biomedical Reseach (NIBR) Novartis Campus Basel CH‐4002 Switzerland

2. Laboratorium für Organische Chemie Zürich CH‐8093 Switzerland

Publisher

Wiley

Subject

Pharmacology (medical),Biochemistry, medical,Genetics(clinical),Pharmaceutical Science,Pharmacology,Medicine (miscellaneous)

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/adtp.202000078

Reference49 articles.

1. Classification and Nomenclature of Metacaspases and Paracaspases: No More Confusion with Caspases

2. Ancient Origin of the CARD–Coiled Coil/Bcl10/MALT1-Like Paracaspase Signaling Complex Indicates Unknown Critical Functions

3. Structural Architecture of the CARMA1/Bcl10/MALT1 Signalosome: Nucleation-Induced Filamentous Assembly

4. Assembly mechanism of the CARMA1–BCL10–MALT1–TRAF6 signalosome

5. Molecular architecture and regulation of BCL10-MALT1 filaments

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