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pro vyhledávání: '"Maik Annies"'
Autor:
Maik Annies
Publikováno v:
World Patent Information. 34:206-212
Chemical formulations are compositions of active ingredients and inert formulation components (adjuvants), which are more effective in combination than the active ingredients alone. Thus, formulation technology synergistically can improve the propert
Publikováno v:
Biochemical and Biophysical Research Communications. 388:434-438
Regulation of proteolytic cleavage of the amyloid precursor protein by the aspartic protease BACE may occur by alternative splicing and the generation of enzymatically inactive forms. In fact, the presence of exonic donor and acceptor sites for intro
Autor:
Stephan Kröger, Maik Annies
Publikováno v:
Molecular and Cellular Neuroscience. 20:525-535
Several isoforms of chick agrin, which differ in their activity to aggregate AChRs at the neuromuscular junction, are generated by alternative splicing at splice site B. We analyzed the isoform pattern and the functional properties of agrin in a defi
Autor:
Godela Bittcher, Maik Annies, Jürgen Löschinger, Elmar Porten, Stefan Wöll, Rene Ramseger, Stephan Kröger, Christian Abraham, Markus A. Rüegg
The transmembrane form of agrin (TM-agrin) is primarily expressed in the CNS, particularly on neurites. To analyze its function, we clustered TM-agrin on neurons using anti-agrin antibodies. On axons from the chick CNS and PNS as well as on axons and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9e14268220631146377693b1382f40c
Autor:
Godela Bittcher, Maik Annies, Stephan Kröger, Beat Schumacher, Frank Neumann, Markus A. Rüegg
Agrin is a basal lamina-associated heparansulfate proteoglycan that is a key molecule in the formation of the vertebrate neuromuscular junction. The carboxy-terminal part of agrin is involved in its synaptogenic activity. The amino-terminal end of ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9bbc22c2eb02cf4d9622666e7b4cd90