Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Ralph Zahn"'
Autor:
Nicola Franscini, Ahmed El Gedaily, Ulrich Matthey, Susanne Franitza, Man-Sun Sy, Alexander Bürkle, Martin Groschup, Ueli Braun, Ralph Zahn
Publikováno v:
PLoS ONE, Vol 1, p e71 (2006)
BACKGROUND: Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmi
Externí odkaz:
https://doaj.org/article/332fa1232a7d49f582e72c6fd8bfeb8e
Autor:
Edith Lubos, Andreas E. May, Holger Eggebrecht, Ralph Stephan von Bardeleben, Jochen Senges, Axel Bauer, Ralph Zahn, Christine S. Zuern, Miriam Puls, Christian Butter, Peter Boekstegers, Taoufik Ouarrak, Georg Nickenig
Publikováno v:
Clinical Research in Cardiology. 104:1044-1053
To investigate the influence of non-cardiac comorbidities on outcomes of patients enrolled in the German transcatheter mitral valve interventions (TRAMI) registry. Intrahospital and 30-day MACCE rates (death of all causes, stroke and myocardial infar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5521703588f70527030fb726688927d6
https://doi.org/10.1007/s00392-015-0872-x
https://doi.org/10.1007/s00392-015-0872-x
Autor:
Susanne Franitza, E Berli, Nicola Franscini, Ueli Braun, Ulrich Matthey, Michael Hässig, Ralph Zahn, A C Tschuor, A El Gedaily
Publikováno v:
Schweizer Archiv für Tierheilkunde. 151:433-436
The goal of the present study was to investigate whether protease-resistant prion protein (PrPres) occurs in plasma samples of offspring of cows that developed bovine spongiform encephalopathy (BSE; group A) and to compare the prevalence with that of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::37c1fbadc1c1b1bf671dd6077accefe5
https://doi.org/10.1024/0036-7281.151.9.433
https://doi.org/10.1024/0036-7281.151.9.433
Publikováno v:
Journal of Molecular Neuroscience
Journal of Molecular Neuroscience, Humana Press, 2008, 34 (1), pp.9-15. ⟨10.1007/s12031-007-0011-x⟩
Journal of Molecular Neuroscience, Humana Press, 2008, 34 (1), pp.9-15. ⟨10.1007/s12031-007-0011-x⟩
The cellular prion protein (PrP(C)) is found prominently at the synapse. However, its role at the nerve termini and elsewhere is unknown. Here we discuss research presented at the 2005 International Institute for Complex Adaptive Matter (I2CAM) first
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::913f8657e26567af86be057ca304ad99
https://doi.org/10.1007/s12031-007-0011-x
https://doi.org/10.1007/s12031-007-0011-x
Autor:
Jochen Senges, Martin Gottwitz, Anselm K. Gitt, Tobias Heer, Claus Juenger, Harm Wienbergen, Uwe Zeymer, Rudolf Schiele, Ralph Zahn, Frank Towae
Publikováno v:
The American Journal of Cardiology. 98:160-166
To assess gender-based differences in presentation and outcome after non-ST-elevation myocardial infarction (NSTEMI) in clinical practice, this study examined data from the Acute Coronary Syndrome registry, which enrolled 16,817 patients from 2000 th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5436934bd23567d59fa8dd6031d81dc
https://doi.org/10.1016/j.amjcard.2006.01.072
https://doi.org/10.1016/j.amjcard.2006.01.072
Autor:
Ralph Zahn
Publikováno v:
Journal of Molecular Biology. 334:477-488
Structural studies of mammalian prion protein at pH values between 4.5 and 5.5 established that the N-terminal 100 residue domain is flexibly disordered. Here, we show that at pH values between 6.5 and 7.8, i.e. the pH at the cell membrane, the octap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6cb9f12542f9791ab8b278fd3d635e5
https://doi.org/10.1016/j.jmb.2003.09.048
https://doi.org/10.1016/j.jmb.2003.09.048
Autor:
Luigi Calzolai, Ralph Zahn
Publikováno v:
Journal of Biological Chemistry. 278:35592-35596
The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f491f63f2b1c9542672fcb9fccbba28a
https://doi.org/10.1074/jbc.m303005200
https://doi.org/10.1074/jbc.m303005200
Publikováno v:
Journal of Molecular Biology. 326:225-234
The nuclear magnetic resonance structure of the globular domain with residues 121–230 of a variant human prion protein with two disulfide bonds, hPrP(M166C/E221C), shows the same global fold as wild-type hPrP(121–230). It contains three α-helice
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::277d369395193b1d22acc3c41f7d9005
https://doi.org/10.1016/s0022-2836(02)01332-3
https://doi.org/10.1016/s0022-2836(02)01332-3
Autor:
Fred F. Damberger, Kurt Wüthrich, Graziano Di Giuseppe, Pierangelo Luporini, Cristina Miceli, Ralph Zahn
Publikováno v:
Scopus-Elsevier
Pheromones of Euplotes raikovi form a homologous family of proteins with 37- to 40-amino acid residues, including six cysteines that form three strictly conserved disulfide bridges. The determination of the primary structure of the pheromone Er-23, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94562a885135a765492c123b3510143d
https://doi.org/10.1111/j.1550-7408.2002.tb00347.x
https://doi.org/10.1111/j.1550-7408.2002.tb00347.x
Publikováno v:
Journal of Molecular Biology. 313:923-931
The NMR solution structure of the 51 residue pheromone Er-23 from the ciliated protozoan Euplotes raikovi (Er) was calculated with the torsion angle dynamics program DYANA from 582 nuclear Overhauser enhancement (NOE) upper limit distance constraints
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::105216fea58eee5830345e502208c3dd
https://doi.org/10.1006/jmbi.2001.5099
https://doi.org/10.1006/jmbi.2001.5099