OpenSSL SSL_connect: Connection reset by peer in connection to v2.sherpa.ac.uk:443 PuSH - Publikationsserver des Helmholtz Zentrums München: Use of non-natural amino acids for the design and synthesis of a selective, cell-permeable MALT1 activity-based probe.

PuSH - Publikationsserver des Helmholtz Zentrums München

van de Plassche, M.A.T.* ; O'Neill, T.J. ; Seeholzer, T. ; Turk, B.* ; Krappmann, D. ; Verhelst, S.H.L.*

Use of non-natural amino acids for the design and synthesis of a selective, cell-permeable MALT1 activity-based probe.

J. Med. Chem. 63, 3996-4004 (2020)
Postprint DOI PMC
Open Access Green
Constitutive proteolytic activity of MALT1 is associated with highly aggressive B-cell lymphomas. Chemical tools that detect active MALT1 have been reported, but suffer from poor cell permeability and/or cross-reactivity with the cysteine protease cathepsin B. Here, we report that the non-natural amino acid pipecolinic acid in the P2 position of substrates and chemical probes leads to improved selectivity toward MALT1 and results in cell-permeable fluorescent probes.
Altmetric
Weitere Metriken?
[➜Einloggen]
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Protease; Paracaspase; Specificity; Activation
ISSN (print) / ISBN 0022-2623
e-ISSN 1520-4804
Zeitschrift Journal of Medicinal Chemistry
Quellenangaben Band: 63, Heft: 8, Seiten: 3996-4004 Artikelnummer: , Supplement: ,
Verlag American Chemical Society (ACS)
Verlagsort 1155 16th St, Nw, Washington, Dc 20036 Usa
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Research Unit Signaling and Translation (SAT)