Zobrazeno 1 - 10
of 51
pro vyhledávání: '"W. Schiebler"'
Autor:
Paul Greengard, F J Kézdy, M F Ho, Emil Thomas Kaiser, Andrew J. Czernik, W Schiebler, Martin Bähler
Publikováno v:
Journal of Biological Chemistry. 266:5600-5607
Synapsin I is a neuron-specific phosphoprotein localized on the surface of small synaptic vesicles to which it binds with high affinity (Kd = 10 nM). Synapsin I exhibits a tendency to self-associate, suggesting that it might have amphiphilic properti
Akademický článek
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Publikováno v:
European journal of cell biology. 56(2)
Membranes from human placenta contain proteins which inhibit the activity of phospholipases A2 by binding to phospholipid thus impeding substrate availability. We used unilamellar mixed liposomes and a partially purified cytosolic phospholipase A2 fr
Publikováno v:
The Journal of biological chemistry. 266(9)
Synapsin I is a neuron-specific phosphoprotein localized on the surface of small synaptic vesicles to which it binds with high affinity (Kd = 10 nM). Synapsin I exhibits a tendency to self-associate, suggesting that it might have amphiphilic properti
Akademický článek
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Publikováno v:
European Journal of Biochemistry. 177:657-664
Bovine brain cytosol is shown to contain two heat-resistant inhibitors of protein kinase C, with the following characteristics: 1. One protein kinase C inhibitor can be easily purified to homogeneity. Evidence is presented that this polypeptide of Mr
Publikováno v:
The Journal of Cell Biology
Synapsin I (protein I) is a neuron-specific phosphoprotein, which is a substrate for cAMP-dependent and Ca/calmodulin-dependent protein kinases. In two accompanying studies (De Camilli, P., R. Cameron, and P. Greengard, and De Camilli, P., S. M. Harr
Certain Neurotoxins may be used as tools for the characterization of molecular components involved in nerve impuls propagation. We intend to use them for the investigation of receptor-ion channel relationships in excitable membranes. α-Neurotoxins f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24c01d41254c22f884b93b9d20ffc3bf
https://doi.org/10.1016/b978-0-08-024952-0.50088-0
https://doi.org/10.1016/b978-0-08-024952-0.50088-0
A major calmodulin-binding protein (CaM-BP) of Mr 240,000 was demonstrated in various rat tissues by using a 125I-labeled CaM gel overlay technique. This protein (designated p240) was detected in the particulate fraction and to a lesser extent in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c8942089a1c1f4455123282917fc156
https://europepmc.org/articles/PMC346511/
https://europepmc.org/articles/PMC346511/