M
M. Kroemer
Researcher at Novartis
Publications - 8
Citations - 995
M. Kroemer is an academic researcher from Novartis. The author has contributed to research in topics: Deubiquitinating enzyme & Phosphorylation. The author has an hindex of 6, co-authored 8 publications receiving 914 citations.
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Journal ArticleDOI
Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.
Paul Erbel,Nikolaus Schiering,Allan D'Arcy,Martin Renatus,M. Kroemer,Siew Pheng Lim,Zheng Yin,Thomas H. Keller,Subhash G. Vasudevan,Ulrich Hommel +9 more
TL;DR: In this article, the crystal structures of a dengue NS2B-NS3pro complex and a West Nile virus NS2b-NS 3pro complex with a substrate-based inhibitor were reported.
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Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.
Jean-Michel Rondeau,Francis Bitsch,E. Bourgier,Martin Geiser,Rene Hemmig,M. Kroemer,S. Lehmann,Paul Ramage,S. Rieffel,André Strauss,Jonathan Green,Wolfgang Jahnke +11 more
TL;DR: The crystal structures of human farnesyl pyrophosphate synthase (FPPS) in its unliganded state are solved and the accumulating substrate, IPP, was found to bind to and stabilize the FPPS–N‐BP complexes rather than to compete with and displace the N‐BP inhibitor.
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Structural Basis of Ubiquitin Recognition by the Deubiquitinating Protease USP2
Martin Renatus,Shirley Gil Parrado,Allan D'Arcy,Ulf Eidhoff,Bernd Gerhartz,Ulrich Hassiepen,Benoit Pierrat,Ralph Riedl,D. Vinzenz,Susanne Worpenberg,M. Kroemer +10 more
TL;DR: A general mechanism of water-mediated ubiquitin recognition by USPs is suggested, as several of those molecules are found at identical positions in the previously solved USP7/ubiquitin-aldehyde complex structure.
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Novel 3-aminopyrazole inhibitors of MK-2 discovered by scaffold hopping strategy.
Juraj Velcicky,Roland Feifel,Stuart Hawtin,Richard Heng,Christine Huppertz,Guido Koch,M. Kroemer,Henrik Moebitz,Laszlo Revesz,Clemens Scheufler,Achim Schlapbach +10 more
TL;DR: New, selective 3-aminopyrazole based MK2-inhibitors were discovered by scaffold hopping strategy and proved to inhibit intracellular phosphorylation of hsp27 as well as LPS-induced TNFalpha release in cells.
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In vivo and in vitro SAR of tetracyclic MAPKAP-K2 (MK2) inhibitors. Part II.
Laszlo Revesz,Achim Schlapbach,Reiner Aichholz,Janet Dawson,Roland Feifel,Stuart Hawtin,Amanda Littlewood-Evans,Guido Koch,M. Kroemer,Henrik Möbitz,Clemens Scheufler,Juraj Velcicky,Christine Huppertz +12 more
TL;DR: Pyrrolo[2,3-f]isoquinoline based amino acids, tetracyclic lactams and cyclic ketone analogues are described as novel MK2 inhibitors with IC(50) as low as 5nM and good selectivity profiles against a number of related kinases including ERK, p38alpha and JNKs.