J
Johanna Tüshaus
Researcher at German Center for Neurodegenerative Diseases
Publications - 16
Citations - 201
Johanna Tüshaus is an academic researcher from German Center for Neurodegenerative Diseases. The author has contributed to research in topics: Biology & ADAM10. The author has an hindex of 5, co-authored 11 publications receiving 90 citations. Previous affiliations of Johanna Tüshaus include Technische Universität München.
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Journal ArticleDOI
Functions of 'A disintegrin and metalloproteases (ADAMs)' in the mammalian nervous system.
Hung-En Hsia,Johanna Tüshaus,Johanna Tüshaus,Tobias Brummer,Tobias Brummer,Yuanpeng Zheng,Yuanpeng Zheng,Simone D. Scilabra,Simone D. Scilabra,Simone D. Scilabra,Stefan F. Lichtenthaler,Stefan F. Lichtenthaler +11 more
TL;DR: Among the proteolytic ADAMs, ADAM10 is the best characterized one due to its substrates Notch and amyloid precursor protein, where cleavage is required for nervous system development or linked to Alzheimer’s disease (AD), respectively.
Journal ArticleDOI
An optimized quantitative proteomics method establishes the cell type-resolved mouse brain secretome
Johanna Tüshaus,Johanna Tüshaus,Stephan A. Müller,Stephan A. Müller,Evans Kataka,Jan Zaucha,Laura Sebastian Monasor,Minhui Su,Minhui Su,Gökhan Güner,Gökhan Güner,Georg Jocher,Georg Jocher,Sabina Tahirovic,Dmitrij Frishman,Mikael Simons,Mikael Simons,Stefan F. Lichtenthaler,Stefan F. Lichtenthaler +18 more
TL;DR: This work miniaturized secretome analysis by developing the “high‐performance secretome protein enrichment with click sugars” (hiSPECS) method, which revealed that an unexpectedly high number of secreted proteins in vitro and in vivo are proteolytically cleaved membrane protein ectodomains.
Journal ArticleDOI
The tetraspanin Tspan15 is an essential subunit of an ADAM10 scissor complex
Chek Ziu Koo,Chek Ziu Koo,Neale Harrison,Peter J. Noy,Justyna Szyroka,Alexandra L. Matthews,Hung-En Hsia,Stephan A. Mueller,Johanna Tüshaus,Joelle Goulding,Katie Willis,Clara Apicella,Bethany Cragoe,Edward T Davis,Murat Keles,Antonia Malinova,Thomas A. McFarlane,Philip R. Morrison,Hanh T.H. Nguyen,Michael C. Sykes,Haroon Ahmed,Alessandro Di Maio,Lisa Seipold,Paul Saftig,Eleanor Cull,Christos Pliotas,Eric Rubinstein,Natalie S. Poulter,Natalie S. Poulter,Stephen J. Briddon,Nicholas D. Holliday,Stefan F. Lichtenthaler,Michael G. Tomlinson,Michael G. Tomlinson +33 more
TL;DR: An immunogen is designed to generate the first monoclonal antibodies targeting Tspan15, a model TspanC8, and it is shown that endogenous T span15 and ADAM10 co-localize on the cell surface, thatADAM10 is the principal Tspan 15-interacting protein, and that a synthetic ADAM 10/Tspan15 fusion protein is a functional scissor.
Journal ArticleDOI
Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3
Martina Pigoni,Martina Pigoni,Hung-En Hsia,Hung-En Hsia,Jana Hartmann,Jasenka Rudan Njavro,Jasenka Rudan Njavro,Merav D. Shmueli,Merav D. Shmueli,Merav D. Shmueli,Stephan A. Müller,Stephan A. Müller,Gökhan Güner,Gökhan Güner,Johanna Tüshaus,Johanna Tüshaus,Peer-Hendrik Kuhn,Peer-Hendrik Kuhn,Rohit Kumar,Rohit Kumar,Rohit Kumar,Pan Gao,Pan Gao,Mai Ly Tran,Mai Ly Tran,Bulat Ramazanov,Birgit Blank,Agnes L. Hipgrave Ederveen,Julia von Blume,Julia von Blume,Christophe Mulle,Jenny M. Gunnersen,Jenny M. Gunnersen,Manfred Wuhrer,Gerhard Rammes,Marc Aurel Busche,Thomas Koeglsperger,Thomas Koeglsperger,Stefan F. Lichtenthaler +38 more
TL;DR: It is demonstrated that SEZ6 controls glycosylation and cell surface localization of kainate receptors composed of GluK2/3 subunits, which may help to better understand the role of SEZ 6 in neurologic and psychiatric diseases.
Journal ArticleDOI
ADAM17 stabilizes its interacting partner inactive Rhomboid 2 (iRhom2) but not inactive Rhomboid 1 (iRhom1)
Gisela Weskamp,Johanna Tüshaus,Daniel Li,Regina Feederle,Thorsten Maretzky,Steven Swendemann,Erik Falck-Pedersen,David R. McIlwain,Tak W. Mak,Jane E. Salmon,Stefan F. Lichtenthaler,Carl P. Blobel +11 more
TL;DR: Findings support a model in which iRhom2 and ADAM17 are obligate binding partners and indicate that iR Hom2 stability requires the presence of ADAM 17, whereas iRHom1 is stable in the absence of ADam17.