Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Dominikus A. Lysek"'
Background: The objective of the present in vitro study was to evaluate the ability of a novel self-assembling peptide matrix gel with calcium phosphate in effectively occluding dentine tubules compared to selected desensitizing toothpastes. Methods:
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e4f85afe24b22baa14ebc0211f5c0b5
https://doi.org/10.21203/rs.2.16822/v1
https://doi.org/10.21203/rs.2.16822/v1
Autor:
Ralf Gutwald, Rainer Schmelzeisen, Jörg Haberstroh, Carola Kister, Sebastian Sauerbier, Michele Maglione, Samuel Porfírio Xavier, Toshiyuki Oshima, Jens Kuschnierz, Dominikus A. Lysek
Publikováno v:
British Journal of Oral and Maxillofacial Surgery. 48:285-290
Our aim was to compare the osteogenic potential of mononuclear cells harvested from the iliac crest combined with bovine bone mineral (BBM) (experimental group) with that of autogenous cancellous bone alone (control group). We studied bilateral augme
Publikováno v:
Gene. 341:249-253
A new determination of the house cat (Felis catus) prion protein gene sequence (fPrnp), which has so far been subject of controversy, is reported. The newly determined fPrnp sequence is similar to dog (Canis familiaris) and mink (Mustela putorius) Pr
Autor:
Dominikus A. Lysek, Kurt Wüthrich
Publikováno v:
Biochemistry. 43:10393-10399
Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified, although the
Autor:
Christopher C. Moser, Tobias W B Ost, Simon Daff, Dominikus A. Lysek, Caroline S Miles, Stephen K Chapman, Kirsty J. McLean, P. Leslie Dutton, David Leys, Ker R. Marshall, Andrew W. Munro, Christopher C. Page
Publikováno v:
Trends in Biochemical Sciences. 27:250-257
Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion
Autor:
Stephen K Chapman, Scott P. Webster, Lisa McIver, Dominikus A. Lysek, Sharon M. Kelly, Robert Baxter, Dominic J. Campopiano, Claire Leadbeater, Michael A. Noble, Nicholas C. Price, Andrew W. Munro
Publikováno v:
Biochemical Journal. 352:257-266
The structure of the Escherichia coli flavodoxin NADP+ oxidoreductase (FLDR) places three arginines (R144, R174 and R184) in the proposed NADPH-binding site. Mutant enzymes produced by site-directed mutagenesis, in which each arginine was replaced by
Autor:
Stephen K Chapman, Dominikus A. Lysek, Robert P. Hanzlik, Michael A. Noble, Caroline S Miles, Angela C. Mackay, Graeme A Reid, Andrew W. Munro
Publikováno v:
Biochemical Journal. 339:371-379
The effects of mutation of key active-site residues (Arg-47, Tyr-51, Phe-42 and Phe-87) in Bacillus megaterium flavocytochrome P450 BM3 were investigated. Kinetic studies on the oxidation of laurate and arachidonate showed that the side chain of Arg-
Publikováno v:
Clinical oral implants research. 21(5)
Background: During a time period of 15 years (1992–2007), 2190 implants were inserted in 983 patients after sinus floor elevation. Materials and methods: One thousand two hundred and seven implants (461 patients) were placed into sites, in which th
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 102(3)
The NMR structure of the recombinant elk prion protein (ePrP), which represents the cellular isoform (ePrP C ) in the healthy organism, is described here. As anticipated from the highly conserved amino acid sequence, ePrP C has the same global fold a
Autor:
Christine von Schroetter, Barbara Christen, Vicent Esteve-Moya, Christian Schorn, Dominikus A. Lysek, Lucas G. Nivón, Torsten Herrmann, Luigi Calzolai, Francesco Fiorito, Peter Güntert, Kurt Wüthrich
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 102(3)
The NMR structures of the recombinant cellular form of the prion proteins (PrP C ) of the cat ( Felis catus ), dog ( Canis familiaris ), and pig ( Sus scrofa ), and of two polymorphic forms of the prion protein from sheep ( Ovis aries ) are presented