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Schlauderer, F.* ; Lammens, K.* ; Nagel, D. ; Vincendeau, M. ; Eitelhuber, A.C. ; Verhelst, S.H.* ; Kling, D.* ; Chrusciel, A.* ; Ruland, J.* ; Krappmann, D. ; Hopfner, K.-P.*

Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase.

Angew. Chem.-Int. Edit. 52, 10384-10387 (2013)

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Open Access Green as soon as Postprint is submitted to ZB.

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Second site: In the crystal structure of human MALT1casp-Ig3 (mucosa-associated lymphoid tissue lymphoma translocation protein 1) in complex with the tricyclic phenothiazine derivative thioridazine (violet in the picture), the inhibitor is bound in a hydrophobic pocket far from the active site. This explains the action of phenothiazine derivatives as noncompetitive, reversible inhibitors.

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Publication type Article: Journal article

Document type Scientific Article

Keywords Cancer ; Inhibitors ; Medicinal Chemistry ; Multiple Sclerosis ; Thioridazine; Nf-kappa-b; T-cell-activation; Protease Activity; Ubiquitin Ligase; Lymphoma; Identification; Lymphocytes; Regulator; Cleavage; Cancer

ISSN (print) / ISBN 1433-7851

e-ISSN 1521-3773

Journal Angewandte Chemie - Internationale Edition

Quellenangaben Volume: 52, Issue: 39, Pages: 10384-10387

Publisher Wiley

Publishing Place Weinheim

Reviewing status Peer reviewed

Institute(s) Research Unit Signaling and Translation (SAT)