Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Jacques J. H. Hens"'
Autor:
Marieke A M Frasa, Lale Erdem-Eraslan, André P. van Rossum, Jeffrey F W Keuren, Jacques J H Hens
Publikováno v:
British Journal of Haematology, 183(4), 681-683. Wiley-Blackwell Publishing Ltd
Autor:
Arnoud Marquart, Jacques J. H. Hens, Willem Hendrik Gispen, Henk Zwiers, Pierre N. E. De Graan, A. Beate Oestreicher, Marc Mercken
Publikováno v:
Journal of Neurochemistry. 62:881-889
Mouse monoclonal B-50 antibodies (Mabs) were screened to select a Mab that may interfere with suggested functions of B-50 (GAP-43), such as involvement in neurotransmitter release. Because the Mab NM2 reacted with peptide fragments of rat B-50 contai
Autor:
Wati Dimjati, Jacques J. H. Hens, A. Beate Oestreicher, Victor M. Wiegant, W.E.J.M. Ghijsen, Pierre N. E. De Graan, Willem Hendrik Gispen
Publikováno v:
Journal of Neurochemistry. 61:602-609
To study the involvement of the protein kinase C (PKC) substrate B-50 [also known as growth-associated protein-43 (GAP-43), neuromodulin, and F1] in presynaptic cholecystokinin-8 (CCK-8) release, highly purified synaptosomes from rat cerebral cortex
Publikováno v:
Neuroscience Research Communications. 19:9-17
Autor:
W.E.J.M. Ghijsen, W.H. Gispen, F.H. Lopes da Silva, Matthijs Verhage, Victor M. Wiegant, Frans Boomsma, Jacques J. H. Hens, P.N.E. de Graan
Publikováno v:
European journal of pharmacology, 291, 387. Elsevier
European Journal of Pharmacology. Molecular Pharmacology Section, 291, 387-398. Elsevier
European Journal of Pharmacology. Molecular Pharmacology Section, 291, 387-398. Elsevier
Exocytosis from nerve terminals is triggered by depolarization-evoked Ca 2+ entry, which also activates calmodulin and stimulates protein phosphorylation. Ba 2+ is believed to replace Ca 2+ in triggering exocytosis without activation of calmodulin an
Autor:
Willem Hendrik Gispen, Pierre N. E. De Graan, Frans Boomsma, Frank L. Margolis, Lodewijk V. Dekker, Marina de Wit, A. Beate Oestreicher, Jacques J. H. Hens
Publikováno v:
Journal of Neurochemistry. 60:1264-1273
The involvement of B-50, protein kinase C (PKC), and PKC-mediated B-50 phosphorylation in the mechanism of Ca(2+)-induced noradrenaline (NA) release was studied in highly purified rat cerebrocortical synaptosomes permeated with streptolysin-O. Under
Publikováno v:
Life Sciences. 52:1013-1022
ACTH-(1-24), 1 microM, enhanced the Ca(2+)-dependent release of [3H]dopamine ([3H]DA) from intact septal synaptosomes by approximately 30%, but had no effect on the release of [3H]noradrenaline ([3H]NA) from intact cortical synaptosomes. Since a stro
Publikováno v:
Journal of Neurochemistry. 54:1645-1652
We studied the molecular events underlying K(+)-induced phosphorylation of the neuron-specific protein kinase C substrate B-50. Rat cortical synaptosomes were prelabelled with 32P-labelled orthophosphate. B-50 phosphorylation was measured by an immun
Autor:
P.N.E. de Graan, W.E.J.M. Ghijsen, M. de Wit, R. Kissmehl, A.G.M. Leenders, Jacques J. H. Hens, Victor M. Wiegant, Hendrikus Boddeke, W.H. Gispen, Ulrich Weller
Publikováno v:
Journal of neurochemistry, 71(5), 1978. Blackwell Science
Journal of Neurochemistry, 71(5), 1978-1986. Blackwell Publishing Ltd
Journal of Neurochemistry, 71(5), 1978-1986. Blackwell Publishing Ltd
Neurotransmission requires rapid docking, fusion, and recycling of neurotransmitter vesicles. Several of the proteins involved in this complex Ca2+-regulated mechanism have been identified as substrates for protein kinases and phosphatases, e.g., the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb25cebddd62b23d351e253d0590a1cc
https://dspace.library.uu.nl/handle/1874/4051
https://dspace.library.uu.nl/handle/1874/4051