P
Prasath Somasundaram
Researcher at University of Kiel
Publications - 5
Citations - 266
Prasath Somasundaram is an academic researcher from University of Kiel. The author has contributed to research in topics: Cleavage (embryo) & Sheddase. The author has an hindex of 3, co-authored 5 publications receiving 198 citations.
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Journal ArticleDOI
Phosphatidylserine exposure is required for ADAM17 sheddase function
Anselm Sommer,Felix Kordowski,Joscha Büch,Thorsten Maretzky,Astrid Evers,Jörg Andrä,Stefan Düsterhöft,Matthias Michalek,Inken Lorenzen,Prasath Somasundaram,Andreas Tholey,Frank D. Sönnichsen,Karl Kunzelmann,Lena Heinbockel,Christian Nehls,Thomas Gutsmann,Joachim Grötzinger,Sucharit Bhakdi,Karina Reiss +18 more
TL;DR: Evidence is presented that surface exposure of phosphatidylserine (PS) is pivotal for ADAM17 to exert sheddase activity, and it is speculated that surface-exposed PS directs the protease to its targets where it then executes its shedding function.
Journal ArticleDOI
Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role of N-Glycosylation.
Steffen Riethmueller,Prasath Somasundaram,Johanna C. Ehlers,Chien-Wen Hung,Charlotte M. Flynn,Juliane Lokau,Maria Agthe,Stefan Düsterhöft,Yijue Zhu,Joachim Grötzinger,Inken Lorenzen,Tomas Koudelka,Kosuke Yamamoto,Ute Pickhinke,Rielana Wichert,Christoph Becker-Pauly,Marisa Rädisch,Alexander Albrecht,Markus Hessefort,Dominik Stahnke,Carlo Unverzagt,Stefan Rose-John,Andreas Tholey,Christoph Garbers +23 more
TL;DR: Liquid chromatography–mass spectrometry is used to identify an sIL-6R form in human serum that originates from proteolytic cleavage, map its cleavage site between Pro-355 and Val-356, and determine the occupancy of all O- and N-glycosylation sites of the human sIL -6R.
Journal ArticleDOI
C-Terminal Charge-Reversal Derivatization and Parallel Use of Multiple Proteases Facilitates Identification of Protein C-Termini by C-Terminomics
TL;DR: The derivatization with N,N-dimethylethylenediamine and (4-aminobutyl)guanidine leading to a positively charged C-terminus was investigated and c-terminal charge-reversed peptides showed improved coverage of b- and y-ion series in the MS/MS spectra compared to their noncharged counterparts.
Journal ArticleDOI
Cell Surface Processing of CD109 by Meprin β Leads to the Release of Soluble Fragments and Reduced Expression on Extracellular Vesicles
Wiebke Lückstädt,Simon Bub,Simon Bub,Tomas Koudelka,Egor Pavlenko,Florian Peters,Prasath Somasundaram,Christoph Becker-Pauly,Ralph Lucius,Friederike Zunke,Philipp Arnold +10 more
TL;DR: In this article, the authors identify the metalloproteinase meprin β to cleave CD109 at the cell surface and induce the release of cleavage fragments of different size.
Book ChapterDOI
Quantitative MALDI MS Using Ionic Liquid Matrices
TL;DR: The ionic liquid matrices (ILM) as discussed by the authors are composed of an equimolar mixture of classically used acidic MALDI matrices and organic bases, which allows for an almost infinite number of combinations with different properties.