Marit Stirnberg
University of Bonn
28 Papers
325 Citations
Marit Stirnberg is an academic researcher from University of Bonn. The author has contributed to research in topics: Serine protease & Protease. The author has an hindex of 16, co-authored 28 publications.
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Papers
Development of Nitrile-Based Peptidic Inhibitors of Cysteine Cathepsins
TL;DR: This review summarizes the development of peptidic and peptidomimetic compounds with an electrophilic nitrile 'warhead' as inhibitors of the cysteine cathepsins B, S, L, C, and K.
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Identification of the first low-molecular-weight inhibitors of matriptase-2.
Mihiret T. Sisay,Torsten Steinmetzer,Marit Stirnberg,Eva Maurer,Maya Hammami,Jürgen Bajorath,Michael Gütschow +6 more
TL;DR: A comparative three-dimensional model of the catalytic domain of matriptase-2 was generated and utilized for structure-based virtual screening in combination with similarity searching and knowledge-based compound design, and two N-protected dipeptide amides containing a 4-amidinobenzylamide as P1 residue were identified.
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Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.
Marit Stirnberg,Eva Maurer,Angelika Horstmeyer,Sonja Kolp,Stefan Frank,Tobias Bald,Katharina Arenz,Andreas Janzer,Kai Prager,Patrick Wunderlich,Jochen Walter,Michael Gütschow +11 more
TL;DR: The subcellular localization of the monomeric and multimeric form of matriptase-2 was characterized and it was identified as a defining point in its proteolytic processing, indicating a transactivation and trans-shedding mechanism.
Matriptase-2 (TMPRSS6) is directly up-regulated by hypoxia inducible factor-1: identification of a hypoxia-responsive element in the TMPRSS6 promoter region
TL;DR: The action of HIF-1α on TMPRSS6 promoter activity reveals a new regulative element for the suppression of hepcidin synthesis, providing a new link between hypoxia signaling and iron homeostasis.
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Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.
Felix Jäckle,Frederike Schmidt,Rielana Wichert,Philipp Arnold,Johannes Prox,Martin Mangold,Anke Ohler,Claus U. Pietrzik,Tomas Koudelka,Andreas Tholey,Michael Gütschow,Marit Stirnberg,Christoph Becker-Pauly +12 more
TL;DR: It is shown that MT2, but not TMPRSS4 or pancreatic trypsin, is capable of activating full-length meprin β at the cell surface, analysed by specific fluorogenic peptide cleavage assay, Western blotting and confocal laser scanning microscopy (CLSM).
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