Zobrazeno 1 - 10
of 306
pro vyhledávání: '"Wolfram, Bode"'
Autor:
Mekdes Debela, Viktor Magdolen, Wolfgang Skala, Brigitta Elsässer, Eric L. Schneider, Charles S. Craik, Martin L. Biniossek, Oliver Schilling, Wolfram Bode, Hans Brandstetter, Peter Goettig
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-15 (2018)
Abstract Human KLK8/neuropsin, a kallikrein-related serine peptidase, is mostly expressed in skin and the hippocampus regions of the brain, where it regulates memory formation by synaptic remodeling. Substrate profiles of recombinant KLK8 were analyz
Externí odkaz:
https://doaj.org/article/c16e2c7087564dea9f129dcd30f35722
Publikováno v:
Biological chemistry
Although kallikrein-related peptidase 10 (KLK10) is expressed in a variety of human tissues and body fluids, knowledge of its physiological functions is fragmentary. Similarly, the pathophysiology of KLK10 in cancer is not well understood. In some ca
Autor:
Anna Tochowicz, Klaus Richter, Hideaki Nagase, Wolfram Bode, Robert Visse, Klaus Maskos, Richard Evans, Peter Goettig, Noriko Ito, Yoshifumi Itoh, Daniel Franke, Ralf Palmisano, Yasuyuki Shitomi, Dmitri I. Svergun
Publikováno v:
The journal of biological chemistry 286, 7587-7600 (2011). doi:10.1074/jbc.M110.178434
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of the hemopexin (Hpx) domain-driven dimerization of MT1-MMP
Autor:
F. X. Gomis-Rüth, Walter Stöcker, Ulrich Baumann, Frank Grams, Wolfram Bode, David B. McKay, Peter Reinemer
Publikováno v:
Protein Science. 4:823-840
The three-dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin II from rattle snake venom, alkaline proteinase from Pseudomonas aeruginosa, and astacin from crayfish are topologically similar, with respect to a f
Autor:
Rainer W. Friedrich, Daniel Riester, Wolfram Bode, Marcel Thürk, Andreas Schwienhorst, Peter Göttig
Publikováno v:
European Journal of Medicinal Chemistry. 43:1330-1335
Thrombin, the ultimate proteinase of the coagulation cascade, is an attractive target for the treatment of a variety of cardiovascular diseases. Previously, a series of novel thrombin inhibitors, discovered by employing a powerful and new computer-as
Autor:
Wolfram Bode, Peter Reinemer, Luis Moroder, Sergio A. Cadamuro, Peter Goettig, Holger Steuber, Marion G. Götz, Michael Willem, Christian Renner, Tanja Kohler, Anja Jestel, Alessandra Barazza
Publikováno v:
ChemBioChem. 8:2078-2091
Minimal sequence requirements for binding of substrate-derived statine peptides to the aspartyl enzyme were established on the basis of the X-ray cocrystal structure of the hydroxyethylene-octapeptide OM00-3 in complexation with BACE-1. With this inf
Autor:
Robert Huber, Mekdes Debela, Peter Goettig, Wolfram Bode, Viktor Magdolen, Norman M. Schechter
Publikováno v:
Journal of Molecular Biology. 373:1017-1031
Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases. It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role i
Autor:
Anna, Tochowicz, Klaus, Maskos, Robert, Huber, Ruth, Oltenfreiter, Vincent, Dive, Athanasios, Yiotakis, Matteo, Zanda, Tayebeh, Pourmotabbed, Wolfram, Bode, Peter, Goettig
Publikováno v:
Journal of Molecular Biology. 371:989-1006
Human matrix metalloproteinase 9 (MMP-9), also called gelatinase B, is particularly involved in inflammatory processes, bone remodelling and wound healing, but is also implicated in pathological processes such as rheumatoid arthritis, atherosclerosis
Autor:
D. Zucic, Wolfram Bode, V. Turk, Richard A. Engh, D. Musil, Takae Towatari, Tatjana Popovič, Dušan Turk, Janko Kos, Nobuhiko Katunuma, Robert Huber
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e50b6545e07148f8062770f8ad300607
https://doi.org/10.1159/000423522
https://doi.org/10.1159/000423522