Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Dominique Tripier"'
Autor:
Miguel Beato, Rainer Renkawitz, Joachim Nickel, Martin Eggert, Susanne Schmidt, Rüdiger Arnold, Christian Möws, Dominique Tripier, Jörg Michel
Publikováno v:
ResearcherID
Glucocorticoids influence numerous cell functions by regulating gene activity. The glucocorticoid receptor (GR) is a ligand-activated transcription factor and, like any other transcription factor, does not modulate gene activity just by binding to DN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::397853446456a309e3319216b6009173
https://doi.org/10.1074/jbc.270.51.30755
https://doi.org/10.1074/jbc.270.51.30755
Publikováno v:
Proceedings of the National Academy of Sciences. 92:7956-7960
VASP (vasodilator-stimulated phosphoprotein), an established substrate of cAMP- and cGMP-dependent protein kinases in vitro and in living cells, is associated with focal adhesions, microfilaments, and membrane regions of high dynamic activity. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::209fb71d4439215a8f29e2df282b0bf7
https://doi.org/10.1073/pnas.92.17.7956
https://doi.org/10.1073/pnas.92.17.7956
Autor:
Frank Girbig, Günter Müller, Karin Jouvenal, Simone Kowalewski, Ulrike Gutjahr, Günther Wess, Werner Kramer, Dominique Tripier
Publikováno v:
Scopus-Elsevier
The anatomical localization of the Na+/bile acid cotransport system from rabbit small intestine was determined using brush border membrane vesicles prepared from eight different segments of the small intestine. Na(+)-dependent transport activity for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2672068e710221aa38d1a93605c9bb1a
https://doi.org/10.1016/s0021-9258(17)46808-6
https://doi.org/10.1016/s0021-9258(17)46808-6
Autor:
Torsten Krafft, Felix Dross, Andrea Duchêne, Falk Fahrenholz, Elzbieta Kojro, Achim Kröger, Viktor Geisler, Dominique Tripier, Friedbert Theis, Ruth Lenger, Karin Juvenal
Publikováno v:
Europe PubMed Central
The hydrogenase (Hyd) isolated from the cytoplasmic membrane of Wolinella succinogenes consists of three polypeptides (HydA, HydB and HydC) and contains cytochrome b (6.4 μmol/g protein), which was reduced upon the addition of H2. The enzyme catalyz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d5813d828ae1e9dd3f1c8462fbd812d
https://doi.org/10.1111/j.1432-1033.1992.tb16905.x
https://doi.org/10.1111/j.1432-1033.1992.tb16905.x
Autor:
Kevin A. Mitchell, M. Spannagl, Melitta Just, Mark D. Talbot, J. Bichler, Ron Almquist, Paul H. Johnson, Cris Olsen, M. Koehler, Robert B. Wallis, F. Doutremepuich, C. Vigneron, G. Pindur, M. Siebeck, F. Markwardt, E. Wenzel, Michael Wallock, F.A. Ofosu, Ch. Rauschenbach, J.W. Fenton, Jawed Fareed, K. Stocker, G. Nowak, H. Bichler, H. Fritz, Fritz Markwardt, B. Schulz, J. Walenga, Keith D. Butler, C.M. Kirchmaier, Richard C. Winant, Michael Koza, Dominique Tripier, Ping Sze, K. Narayanan, M.D. Liang, W. Schramm, Christopher M. Lees, K. Rübsamen, P. Zeiller, Jerome B. Lazar, H. Lill, William S. Fields, E. Glusa, M. Basic-Micic, C. Kirchmaier, John Ambler, Morris F. Tweed, V. Eschenfelder, A. Morin, Peter Underhill, E. Bucha, W. Raake, B. Fichtl, G.B. Villanueva, O.K. Bellinger, H. Elling, K. Krupinski, C. Doutremepuich, Debra Hoppensteadt, B. Braun, Dirk Seiffge, Mike Koza, M.C. Lalanne, H.K. Breddin, Debra Hudson, J. Stürzebecher, M. Heiden, J.M. Walenga, M. Marchand-Arvier, Roque Pifarre, Robin F. Peters, Jeanine M. Walenga, K. Breddin, R.J. Klauser, J.M. Maraganore, J. Fareed
Publikováno v:
Pathophysiology of Haemostasis and Thrombosis. 21:I-IV
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::982bc78c67558a86681f7a8ed1feda41
https://doi.org/10.1159/000216257
https://doi.org/10.1159/000216257
Publikováno v:
Biological Chemistry Hoppe-Seyler. 372:187-192
To study disulphide bridge formation by Streptomyces lividans TK 24 in secreted single chain precursors of insulin a fusion protein (PTF 1) was investigated consisting of monkey proinsulin and the aminoterminal sequence Asp1 to Gly43 of the alpha-amy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2fd4308766de28dbc86182d49555b5a
https://doi.org/10.1515/bchm3.1991.372.1.187
https://doi.org/10.1515/bchm3.1991.372.1.187
Publikováno v:
European journal of biochemistry. 213(2)
We report the distribution of phosphorylation sites in murine lamins A and C (A-type lamins) in vitro and in vivo followed by reverse-phase high-performance liquid chromatography and microsequencing of peptides spanning the almost complete lamin sequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a2ebea7c999bb5a2450109ffbb61c0e
https://pubmed.ncbi.nlm.nih.gov/8477740
https://pubmed.ncbi.nlm.nih.gov/8477740
Publikováno v:
Haemostasis. 21
The effect of recombinant hirudin (r-hirudin; HBW 023) was studied in four different models of thrombosis as well as on bleeding time. Arteriolar thrombus formation was induced in rats either by argon laser injury or by photochemical reaction. r-Hiru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3aacf18aa83ae8d78f47e720259c5a9
https://pubmed.ncbi.nlm.nih.gov/1716605
https://pubmed.ncbi.nlm.nih.gov/1716605
Autor:
J. Stürzebecher, Peter Underhill, K. Rübsamen, B. Fichtl, B. Schulz, O.K. Bellinger, Dominique Tripier, J.M. Maraganore, P. Zeiller, H.K. Breddin, Robert B. Wallis, F. Doutremepuich, Keith D. Butler, Jerome B. Lazar, Morris F. Tweed, K. Narayanan, W. Schramm, Debra Hudson, R.J. Klauser, John Ambler, G.B. Villanueva, Paul H. Johnson, M. Heiden, Richard C. Winant, Cris Olsen, E. Wenzel, C.M. Kirchmaier, C. Doutremepuich, H. Elling, G. Pindur, K. Stocker, Ron Almquist, M. Marchand-Arvier, Ping Sze, H. Lill, M. Basic-Micic, Robin F. Peters, Jawed Fareed, V. Eschenfelder, B. Braun, Mark D. Talbot, Christopher M. Lees, Dirk Seiffge, W. Raake, J. Bichler, Roque Pifarre, C. Vigneron, Kevin A. Mitchell, J. Fareed, Jeanine M. Walenga, M. Spannagl, J. Walenga, Melitta Just, K. Breddin, M.C. Lalanne, M. Koehler, Debra Hoppensteadt, M.D. Liang, Michael Wallock, Ch. Rauschenbach, J.W. Fenton, H. Fritz, Michael Koza, Mike Koza, E. Glusa, Fritz Markwardt, C. Kirchmaier, F. Markwardt, E. Bucha, William S. Fields, M. Siebeck, H. Bichler, F.A. Ofosu, G. Nowak, A. Morin, J.M. Walenga, K. Krupinski
Publikováno v:
Pathophysiology of Haemostasis and Thrombosis. 21:174-174
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a00ec50207b5d8a5e05e8274b3edb74
https://doi.org/10.1159/000216282
https://doi.org/10.1159/000216282
Publikováno v:
European Journal of Biochemistry. 166:447-452
The fumarate reductase complex of the anaerobic bacterium Wolinella succinogenes catalyzes the electron transfer from menaquinol to fumarate. Two structural genes coding for subunits of the enzyme have been cloned in Escherichia coli. The genes were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfec7db9b8af0ac6a80368b31469d710
https://doi.org/10.1111/j.1432-1033.1987.tb13536.x
https://doi.org/10.1111/j.1432-1033.1987.tb13536.x