Anke Ohler
University of Mainz
21 Papers
18 Citations
Anke Ohler is an academic researcher from University of Mainz. The author has contributed to research in topics: Medicine & Proteases. The author has an hindex of 7, co-authored 11 publications.
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Papers
Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates
Christoph Becker-Pauly,Olivier Barré,Oliver Schilling,Oliver Schilling,Ulrich auf dem Keller,Ulrich auf dem Keller,Anke Ohler,Claudia Broder,André Schütte,Reinhild Kappelhoff,Walter Stöcker,Christopher M. Overall +11 more
TL;DR: In this paper, the authors used PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000 cleavage sites were proteomically identified for five different metalloproteases.
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The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10
Tamara Jefferson,Ulrich auf dem Keller,Ulrich auf dem Keller,Caroline L. Bellac,Verena V. Metz,Claudia Broder,Jana Hedrich,Anke Ohler,Wladislaw Maier,Viktor Magdolen,Erwin-Ernst Sterchi,Judith S. Bond,Arumugam Jayakumar,Heiko Traupe,Athena Chalaris,Stefan Rose-John,Claus U. Pietrzik,Rolf Postina,Christopher M. Overall,Christoph Becker-Pauly +19 more
TL;DR: The finding of cystatin C, elafin and fetuin-A as substrates and natural inhibitors for meprins reveal new mechanisms in the regulation of protease activity important for understanding pathophysiological processes.
Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation.
TL;DR: A specific interaction between meprin metalloproteases and kallikrein-related peptidases is demonstrated, revealing possible interactions within the proteolytic web.
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for the astacin metalloprotease family reflected by physiological substrates
Christoph Becker-Pauly,Olivier Barré,Oliver Schilling,Anke Ohler,Claudia Broder,André Schütte,Reinhild Kappelhoff,Walter Stöcker,Christopher M,Johannes Gutenberg-University +9 more
- 01 Jan 2011
TL;DR: This specificity characterizes the astacins as unique contributors to extracellular proteolysis that is corroborated by known cleavage sites in procollagen I+III, VEGF (vascular endothelial growth factor)-A, IL (interleukin)-1β, and pro-kallikrein 7.
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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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