To use all functions of this page, please activate cookies in your browser.
My watch list
my.chemeurope.com
my.chemeurope.com
With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.
- My watch list
- My saved searches
- My saved topics
- My newsletter
24 Newest Publications of de Gruyter
rss
matching the following criteria
Purification of the proprotein convertase furin by affinity chromatography based on PC-specific inhibitors
30-08-2011 | Miriam Kuester; Gero L. Becker; Kornelia Hardes; Iris Lindberg; Torsten Steinmetzer; Manuel E. Than, Biological Chemistry, 2011
Abstract In eucaryotes, many secreted proteins and peptides are proteolytically excised from larger precursor proteins by a specific class of serine proteases, the proprotein/prohormone convertases (PCs). This cleavage is essential for substrate activation, making the PCs very interesting ...
Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenesis and cell adhesion
18-06-2011 | reference-global@degruyter.com (Anke Ohler et al), Biological Chemistry, 2011
Biological Chemistry, Volume 392, Issue 7, Page 653-664, July 2011.
Poliovirus 3C proteinase inhibition by organotelluranes
23-05-2011 | Iuri E. Gouvea; Jorge A.N. Santos; Fernanda M. Burlandy; Ivarne L.S. Tersariol; Edson E. da Silva; Maria A. Ju ..., Biological Chemistry, 2011
Abstract The 3C proteinase, essential for human poliovirus (PV) replication, has unique characteristics as its three-dimensional structure resembles chymotrypsin, but its catalytic nucleophile is a cysteine SH group rather than the OH group of serine. Here, we describe the use of tellurium ...
Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence
23-05-2011 | Tomasz Kantyka; Karolina Plaza; Joanna Koziel; Danuta Florczyk; Hennig R. Stennicke; Ida B. Thogersen; Jan J. ..., Biological Chemistry, 2011
Abstract Bacterial proteases are considered virulence factors and it is presumed that by abrogating their activity, host endogenous protease inhibitors play a role in host defense against invading pathogens. Here we present data showing that Staphylococcus aureus cysteine proteases ...
Helicobacter pylori-induced tyrosine phosphorylation of IKKβ contributes to NF-κB activation
23-05-2011 | Cornelia Rieke; Anja Papendieck; Olga Sokolova; Michael Naumann, Biological Chemistry, 2011
Abstract Helicobacter pylori, the etiological agent of several human gastric diseases, induces the transcription factor nuclear factor-κB (NF-κB) in colonized epithelial cells leading to the release of proinflammatory mediators. Activation of NF-κB involves the IκB kinase (IKK)-complex ...
Selective inhibition of dipeptidyl peptidase 4 by targeting a substrate-specific secondary binding site
23-05-2011 | Kerstin Kühn-Wache; Joachim W. Bär; Torsten Hoffmann; Raik Wolf; Jens-Ulrich Rahfeld; Hans-Ulrich Demuth, Biological Chemistry, 2011
Abstract Dipeptidyl peptidase 4/CD26 (DP4) is a multifunctional serine protease liberating dipeptide from the N-terminus of (oligo)peptides which can modulate the activity of these peptides. The enzyme is involved in physiological processes such as blood glucose homeostasis and immune ...
Expression and role of the cell surface protease seprase/fibroblast activation protein-α (FAP-α) in astroglial tumors
23-05-2011 | Rolf Mentlein; Kirsten Hattermann; Charles Hemion; Achim A. Jungbluth; Janka Held-Feindt, Biological Chemistry, 2011
Abstract Seprase or fibroblast activation protein-α (FAP-α) is a cell-surface serine protease that was previously described nearly exclusively on reactive and tumor stromal fibroblasts and thought to be involved in tissue remodeling. We investigated the expression and significance of FAP-α in ...
Expression and spatial heterogeneity of dipeptidyl peptidases in endothelial cells of conduct vessels and capillaries
23-05-2011 | Veerle Matheeussen; Lesley Baerts; Guido De Meyer; Gilles De Keulenaer; Pieter Van der Veken; Koen Augustyns; ..., Biological Chemistry, 2011
Abstract Dipeptidyl peptidase IV (DPPIV)/CD26 is by far the most extensively studied member of the prolyl oligopeptidase family of serine proteases. The discovery of the related enzymes DPP8 and DPP9 necessitates a (re-)evaluation of the DPPIV-like enzymatic activity in cells and organs. In ...
Secretion of hepatoma-derived growth factor is regulated by N-terminal processing
18-11-2010 | Ketan Thakar; Tim Kröcher; Soniya Savant; Doron Gollnast; Sørge Kelm; Frank Dietz, Biological Chemistry, 2010
Abstract Hepatoma-derived growth factor (HDGF) was first purified as a growth factor secreted by hepatoma cells. It promotes angiogenesis and has been related to tumorigenesis. To date, little is known about the molecular mechanisms of HDGF functions and especially its routes or regulation of ...
The substrate specificity profile of human granzyme A
23-08-2010 | Petra Van Damme; Sebastian Maurer-Stroh; Han Hao; Niklaas Colaert; Evy Timmerman; Frank Eisenhaber; Joël ..., Biological Chemistry, 2010
Abstract The exact biological function of granzyme A, a granule-associated serine protease belonging to the tryptase family of proteases, is still a matter of debate because conflicting roles have been suggested, such as initiation of caspase-independent apoptosis-like cell death and ...
Netmeeting
