Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Monaldi I."'
Publikováno v:
6th IBRO World Congress of Neuroscience, Praga, Repubblica Ceca, 2003
info:cnr-pdr/source/autori:Nobile M., Alloisio S., Monaldi I., Cugnoli C., Ferroni S./congresso_nome:6th IBRO World Congress of Neuroscience/congresso_luogo:Praga, Repubblica Ceca/congresso_data:2003/anno:2003/pagina_da:/pagina_a:/intervallo_pagine
info:cnr-pdr/source/autori:Nobile M., Alloisio S., Monaldi I., Cugnoli C., Ferroni S./congresso_nome:6th IBRO World Congress of Neuroscience/congresso_luogo:Praga, Repubblica Ceca/congresso_data:2003/anno:2003/pagina_da:/pagina_a:/intervallo_pagine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::5c4ed76d47313a190d8d384af95c0d13
https://publications.cnr.it/doc/101260
https://publications.cnr.it/doc/101260
Publikováno v:
FEBS letters
538 (2003): 71–76.
info:cnr-pdr/source/autori:Nobile M. 1, Monaldi I. 1, Alloisio S. 1, Cugnoli C. 1, Ferroni S. 2/titolo:ATP-induced, sustained calcium signalling in cultured rat cortical astrocytes: evidence for a non capacitative, P2X7-like-mediated entry./doi:/rivista:FEBS letters (Print)/anno:2003/pagina_da:71/pagina_a:76/intervallo_pagine:71–76/volume:538
538 (2003): 71–76.
info:cnr-pdr/source/autori:Nobile M. 1, Monaldi I. 1, Alloisio S. 1, Cugnoli C. 1, Ferroni S. 2/titolo:ATP-induced, sustained calcium signalling in cultured rat cortical astrocytes: evidence for a non capacitative, P2X7-like-mediated entry./doi:/rivista:FEBS letters (Print)/anno:2003/pagina_da:71/pagina_a:76/intervallo_pagine:71–76/volume:538
The receptor mechanisms regulating the ATP-induced free cytosolic Ca(2+) concentration ([Ca(2+)](i)) changes in cultured rat cortical type-1 astrocytes were analyzed using fura-2-based Ca(2+) imaging microscopy. Upon prolonged ATP challenge (1-100 mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::5117681f008a2688917631a30f368fe2
https://publications.cnr.it/doc/9350
https://publications.cnr.it/doc/9350
Akademický článek
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Akademický článek
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Akademický článek
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Autor:
Silvia Giovedì, Enrico Millo, Flavia Valtorta, Massimo Vassalli, Roberto Raiteri, Angela Bachi, Fabio Benfenati, Ilaria Monaldi, Anna Fassio
Publikováno v:
Biochemical journal (Lond., 1984) 426 (2010): 55–64. doi:10.1042/BJ20090762
info:cnr-pdr/source/autori:Ilaria MONALDI; Massimo VASSALLI; Angela BACHI; Silvia GIOVEDI'; Enrico MILLO; Flavia VALTORTA; Roberto RAITERI; Fabio BENFENATI; Anna FASSIO/titolo:The highly conserved synapsin domain E mediates synapsin dimerization and phospholipid vesicle clustering/doi:10.1042%2FBJ20090762/rivista:Biochemical journal (Lond., 1984)/anno:2010/pagina_da:55/pagina_a:64/intervallo_pagine:55–64/volume:426
info:cnr-pdr/source/autori:Ilaria MONALDI; Massimo VASSALLI; Angela BACHI; Silvia GIOVEDI'; Enrico MILLO; Flavia VALTORTA; Roberto RAITERI; Fabio BENFENATI; Anna FASSIO/titolo:The highly conserved synapsin domain E mediates synapsin dimerization and phospholipid vesicle clustering/doi:10.1042%2FBJ20090762/rivista:Biochemical journal (Lond., 1984)/anno:2010/pagina_da:55/pagina_a:64/intervallo_pagine:55–64/volume:426
Synapsins are abundant SV (synaptic vesicle)-associated phosphoproteins that regulate synapse formation and function. The highly conserved C-terminal domain E was shown to contribute to several synapsin functions, ranging from formation of the SV res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44af82107c5ffb08726415fd573ce8ce
Autor:
Thierry Galli, Marc Tramier, Sun Joo Park, Toshiki Itoh, Ottavio Cremona, Kohji Takei, Fabio Benfenati, Ilaria Monaldi, Maïté Coppey-Moisan, Sergi Padilla-Parra, Pietro De Camilli, Mathilde Chaineau, Hiroshi Yamada
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (49), pp.34244-56. ⟨10.1074/jbc.M109.064204⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (49), pp.34244-56. ⟨10.1074/jbc.M109.064204⟩
International audience; Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependent fission, was also shown to have a regulatory role in actin dynamics. Here, we report that amphiphysin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d4ceef494610039dd04489dfa19aaa6
http://hdl.handle.net/11567/223168
http://hdl.handle.net/11567/223168