Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Urs Röthlisberger"'
Autor:
Hans Werner Lahm, Pat Eyers, Brown Paul Anthony, Michael J. Broadhurst, L H Elliott, John M. Budd, Trevor J. Hallam, Urs Röthlisberger, David Bradshaw, Geoffrey Lawton, Amanda Whittle, J. S. Nixon, Maisie James, Hill Christopher Huw, Janet E. Merritt, Neera Borkakoti, William Henry Johnson, Balraj Krishnan Handa, K. M. K. Bottomley
Publikováno v:
Biochemical Journal. 323:483-488
N-terminal analysis of aggrecan fragments lost from bovine nasal cartilage cultured in the presence of recombinant human interleukin 1alpha revealed a predominant ARGSVIL sequence with an additional ADLEX sequence. Production of the ARGSVIL-containin
Autor:
Cesura Andrea, Mosé Da Prada, Urs Röthlisberger, Hans-Werner Lahm, Rene Imhof, J. Gottowik, Gabrielle Lang, Pari Malherbe
Publikováno v:
European Journal of Biochemistry. 236:996-1002
The structural features of the active site of human monoamine oxidase B (MAO-B) were investigated by affinity labeling and site-directed mutagenesis. The pseudosubstrate inhibitor N-[2-aminoethyl]-5-chloro-2-pyridine carboxamide HCl (lazabemide) can
Autor:
Eric Kusznir, Michel Tessier, Hans-Werner Lahm, Urs Röthlisberger, Francis Müller, Guido Wahl, Alexandra Kronenberger, Arno Friedlein, R. Remy, Luis Pasamontes, Markus Wyss, Kurt Vogel, Adolphus P. G. M. van Loon, Anke Middendorf, Line Schnoebelen, Martin Lehmann
Publikováno v:
Applied and environmental microbiology. 65(2)
Phytases ( myo -inositol hexakisphosphate phosphohydrolases) are found naturally in plants and microorganisms, particularly fungi. Interest in these enzymes has been stimulated by the fact that phytase supplements increase the availability of phospho
Autor:
E J Schlaeger, Hans-Werner Lahm, E N Hatada, Robert B. Meyer, Urs Röthlisberger, M. Haiker, C Bartsch, A. P. G. M. Van Loon, Claus Scheidereit, Hans-Peter Hohmann
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 88(3)
The DNA binding subunit of nuclear factor kappa B (NF-kappa B), a B-cell protein that interacts with the immunoglobulin kappa light-chain gene enhancer, has been purified from nuclei of human HL-60 cells stimulated with tumor necrosis factor alpha (T