M
Malte Gersch
Researcher at Max Planck Society
Publications - 33
Citations - 1872
Malte Gersch is an academic researcher from Max Planck Society. The author has contributed to research in topics: Deubiquitinating enzyme & Ubiquitin. The author has an hindex of 18, co-authored 31 publications receiving 1439 citations. Previous affiliations of Malte Gersch include Center for Integrated Protein Science Munich & Laboratory of Molecular Biology.
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Journal ArticleDOI
Molecular basis of USP7 inhibition by selective small-molecule inhibitors
Andrew P. Turnbull,Stephanos Ioannidis,Wojciech W. Krajewski,Adan Pinto-Fernandez,Claire Heride,Agnes C. L. Martin,Louise M. Tonkin,Elizabeth C. Townsend,Shane M. Buker,David R. Lancia,Caravella Justin Andrew,Angela V. Toms,Thomas M. Charlton,Johanna Lahdenranta,Erik W. Wilker,Bruce Follows,Nicola J. Evans,Lucy Stead,Cristina Alli,Vladislav V. Zarayskiy,Adam C. Talbot,Alexandre J. Buckmelter,Minghua Wang,Crystal McKinnon,Fabienne Saab,Joanna F. McGouran,Hannah Century,Malte Gersch,Marc S. Pittman,C. Gary Marshall,Tony Raynham,Mary Simcox,Lorna M. D. Stewart,Sheila B. McLoughlin,Jaime Escobedo,Kenneth W. Bair,Christopher J. Dinsmore,Tim Hammonds,Sunkyu Kim,Sylvie Urbé,Michael J. Clague,Benedikt M. Kessler,David Komander +42 more
TL;DR: Two compounds are reported that inhibit ubiquitin-specific protease 7 with high affinity and specificity in vitro and within human cells, and co-crystal structures reveal that both compounds target a dynamic pocket near the catalytic centre of the auto-inhibited apo form of USP7, which differs from other USP deubiquitinases.
Journal ArticleDOI
Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis.
Tobias Wauer,Kirby N. Swatek,Jane L. Wagstaff,Christina Gladkova,Jonathan N. Pruneda,Martin A. Michel,Malte Gersch,Christopher M. Johnson,Stefan M.V. Freund,David Komander +9 more
TL;DR: It is shown that PINK1 can phosphorylate every Ub in Ub chains, and phosphoUb has no effect on E1‐mediated E2 charging but can affect discharging of E2 enzymes to form polyUb chains.
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Electrophilic natural products and their biological targets
TL;DR: A comprehensive compilation of electrophilic natural products from all major chemical classes together with their biological targets, with special emphasis on the elucidation of their respective biological targets via activity-based protein profiling.
Journal ArticleDOI
Mechanism and regulation of the Lys6-selective deubiquitinase USP30
Malte Gersch,Christina Gladkova,Alexander F. Schubert,Martin A. Michel,Sarah L. Maslen,David Komander +5 more
TL;DR: Details are provided into the architecture, activity and regulation of USP30, which will aid drug design against this and related enzymes, and Lys6-linkage-specific affimers identify numerous mitochondrial substrates for this modification.
Journal ArticleDOI
Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne
Tycho E. T. Mevissen,Yogesh Kulathu,Monique P. C. Mulder,Monique P. C. Mulder,Paul P. Geurink,Paul P. Geurink,Sarah L. Maslen,Malte Gersch,Paul R. Elliott,John E. Burke,Bianca D. M. van Tol,Masato Akutsu,Masato Akutsu,Farid El Oualid,Masato Kawasaki,Stefan M.V. Freund,Huib Ovaa,Huib Ovaa,David Komander +18 more
TL;DR: This work reveals how the deubiquitinase Cezanne (also known as OTUD7B) specifically targets Lys11-linked polyubiquITin and indicates that new conformational states can occur when a true substrate, such as diubiqueitin, is bound at the active site.