K
Klaus Schilling
Researcher at University of Jena
Publications - 17
Citations - 858
Klaus Schilling is an academic researcher from University of Jena. The author has contributed to research in topics: Cathepsin L & Cathepsin. The author has an hindex of 14, co-authored 17 publications receiving 807 citations. Previous affiliations of Klaus Schilling include Schiller International University.
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Journal ArticleDOI
Modulation of Human T Cell Responses and Macrophage Functions by Onchocystatin, a Secreted Protein of the Filarial Nematode Onchocerca volvulus
Annett A. Schönemeyer,Richard Lucius,Bettina Sonnenburg,Norbert Brattig,Robert Sabat,Klaus Schilling,Janette E. Bradley,Susanne Hartmann +7 more
TL;DR: Recombinant onchocystatin has the potential to contribute to a state of cellular hyporesponsiveness and is a possible pathogenicity factor essential for the persistence of O. volvulus within its human host.
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Parasite-Specific Immunomodulatory Functions of Filarial Cystatin
Peter Schierack,Peter Schierack,Richard Lucius,Bettina Sonnenburg,Klaus Schilling,Susanne Hartmann +5 more
TL;DR: Cystatins of parasitic nematodes are well-described pathogenicity factors which contribute to downregulation of T-cell proliferation of their hosts and induce anti-inflammatory cytokine responses, but not C. elegans cystatins downregulate proliferative responses of host cells due to characteristics which might reflect an adaptation of filariae to their parasitic life style.
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Functions of Propeptide Parts in Cysteine Proteases
TL;DR: Experimental data concerning three functions of propeptides of clan CA family C1 cysteine peptidases (papain family) are summarized, namely the selectivity of their inhibitory potency, the participation in correct intracellular targeting and assistance in folding of the mature enzyme.
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Interaction of papain-like cysteine proteases with dipeptide-derived nitriles.
TL;DR: A series of 44 dipeptide nitriles with various amino acids at the P2 position and glycine nitrile at position P1 were prepared and evaluated as inhibitors of cysteine proteinases to introduce structural diversity into the P1 side chain.
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Azadipeptide nitriles: highly potent and proteolytically stable inhibitors of papain-like cysteine proteases.
TL;DR: Despite a methylated P-P peptide bond, the azadipeptide nitriles show a strong inhibitory activity against cysteine proteases, and a high stability towards chymotryptic hydrolysis.