Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Martin Pitschke"'
Publikováno v:
Neuroscience Research Communications. 23:119-128
A fragment of the human prion protein, PrP106-126, has been used model the neurotoxicity of PrPscin vitro. The mechanism of action of PrP106-126 was demonstrated to require the presence of microglia and neuronal expression of PrPc. We show that PrP10
Autor:
Thomas R. Appel, Dieter Kirsch, Oliver Schäfer, Hana Serban, Karin Post, Holger Wille, Ingrid Mehlhorn, Detlev Riesner, Martin Pitschke, Stanley B. Prusiner
Publikováno v:
bchm. 379:1307-1318
The N-terminally truncated form of the prion protein, PrP 27-30, and the corresponding recombinant protein, rPrP, were solubilized in 0.2% SDS, and the transitions induced by changing the conditions from 0.2% SDS to physiological conditions, i.e. rem
Publikováno v:
Analytical Ultracentrifugation IV ISBN: 9783798511064
In order to utilize the high sensitivity of the fluorescence detection system for sedimentation equilibrium in analytical ultracentrifugation, a new evaluation method was developed. In comparison to absorption recording the sensitivity could be raise
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3c9f6b19060e3e5a36e94683829b0485
https://doi.org/10.1007/bfb0118016
https://doi.org/10.1007/bfb0118016
Publikováno v:
Antibodies ISBN: 9781461347019
The quality control of biopharmaceutical antibodies intended for human use are required to follow guidelines and regulations set down by national and international regulatory authorities. The US Food and Drug Administration (FDA) issued a guidance in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a05ed2e5b22a09c2879b1850f23abfce
https://doi.org/10.1007/978-1-4419-8875-1_6
https://doi.org/10.1007/978-1-4419-8875-1_6
Autor:
Stanley B. Prusiner, Darlene Groth, Holger Wille, Hana Serban, Martin Pitschke, Detlev Riesner, Michael A. Baldwin, Karin Post, K. Kellings
Publikováno v:
Prions and Brain Diseases in Animals and Humans ISBN: 9781489918987
Prions are composed largely, if not entirely, of an abnormal isoform of the prion protein (PrP) designated PrPSc. A protease resistant polypeptide, PrP 27–30, can be derived from PrPSc by limited proteolysis with retention of infectivity. Both PrPS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b98ae9342573d6ae2e46a768a9fdc32
https://doi.org/10.1007/978-1-4899-1896-3_23
https://doi.org/10.1007/978-1-4899-1896-3_23