Publikationen von C Hopf
Alle Typen
Zeitschriftenartikel (8)
1.
Zeitschriftenartikel
122 (3), S. 659 - 668 (2003)
Calcium-dependent maintenance of agrin-induced postsynaptic specializations. Neuroscience 2.
Zeitschriftenartikel
16 (3), S. 269 - 281 (2000)
Nitric oxide synthase (NOS-1) coclustered with agrin-induced AChR-specializations on cultured skeletal myotubes. Molecular and Cellular Neuroscience 3.
Zeitschriftenartikel
253 (2), S. 382 - 389 (1998)
Tyrosine phosphorylation of the muscle-specific kinase is exclusively induced by acetylcholine receptor-aggregating agrin fragments. European Journal of Biochemistry 4.
Zeitschriftenartikel
273 (11), S. 6467 - 6473 (1998)
Dimerization of the muscle-specific kinase induces tyrosine phosphorylation of acetylcholine receptors and their aggregation on the surface of myotubes. The Journal of Biological Chemistry 5.
Zeitschriftenartikel
239 (2), S. 214 - 225 (1998)
Formation of Postsynaptic-Like Membranes during Differentiation of Embryonic Stem Cellsin Vitro. Experimental Cell Research 6.
Zeitschriftenartikel
239 (2), S. 214 - 225 (1998)
Formation of postsynaptic-like membranes during differentiation of embryonic stem cells in vitro. Experimental Cell Research 7.
Zeitschriftenartikel
9 (6), S. 1170 - 1177 (1997)
Heparin inhibits acetylcholine receptor aggregation at two distinct steps in the agrin-induced pathway. European Journal of Neuroscience 8.
Zeitschriftenartikel
271 (9), S. 5231 - 5236 (1996)
Agrin binding to alpha-dystroglycan. Domains of agrin necessary to induce acetylcholine receptor clustering are overlapping but not identical to the alpha-dystroglycan-binding region. The Journal of Biological Chemistry Meeting Abstract (1)
9.
Meeting Abstract
23 (2), 557.10, S. 1410. 27th Annual Meeting of the Society for Neuroscience (Neuroscience 1997), New Orleans, LA, USA, 25. Oktober 1997 - 30. Oktober 1997. Society for Neuroscience, Bethesda, MD, USA (1997)
Antibodies against the muscle specific kinase (MUSK) induce tyrosine phosphorylation of acetylcholine receptors and their aggregation on the surface of myotubes. In Society for Neuroscience Abstracts,