Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Ryota, Shimaya"'
Autor:
Haruna Tamano, Atsushi Takeda, Ashley I. Bush, Ryusei Itoh, Mako Egawa, Yudai Ishikawa, Paul A. Adlard, Ryota Shimaya, Aoi Shioya, Naoya Oneta
Publikováno v:
NeuroToxicology. 79:177-183
Adrenergic β receptor activation prevents human soluble amyloid β (Aβ)-induced impairment of long-term potentiation (LTP) in slices. On the basis of the evidence that human Aβ1-42-induced impairment of LTP is due to Aβ1-42-mediated Zn2+ toxicity
Publikováno v:
Biochemical and Biophysical Research Communications. 514:888-892
Human amyloid-β1-40 (Aβ1-40) and rat Aβ1-42 have lower affinity for extracellular Zn2+ than human Aβ1-42. Here we report extracellular Zn2+-independent attenuation of dentate gyrus long-term potentiation (LTP) by human Aβ1-40 and rat Aβ1-42. On
Autor:
Haruna, Tamano, Yudai, Ishikawa, Aoi, Shioya, Ryusei, Itoh, Naoya, Oneta, Ryota, Shimaya, Mako, Egawa, Paul A, Adlard, Ashley I, Bush, Atsushi, Takeda
Publikováno v:
Neurotoxicology. 79
Adrenergic β receptor activation prevents human soluble amyloid β (Aβ)-induced impairment of long-term potentiation (LTP) in slices. On the basis of the evidence that human Aβ
Autor:
Ryusei Itoh, Ashley I. Bush, Mitsuyasu Kubota, Paul A. Adlard, Atsushi Takeda, Ryota Shimaya, Yuki Fujise, Haruna Tamano, Miki Suzuki
Publikováno v:
Neurochemistry International. 120:43-48
On the basis of the evidence that the basolateral amygdala (BLA) modulates hippocampal memory processes via synaptic plasticity, here we report that adrenergic β receptor activation in the BLA rescues amyloid β1-42 (Aβ1-42)-induced attenuation of
Autor:
Haruna, Tamano, Mako, Takiguchi, Ryota, Shimaya, Paul A, Adlard, Ashley I, Bush, Atsushi, Takeda
Publikováno v:
Biochemical and biophysical research communications. 514(3)
Human amyloid-β
Autor:
Haruna, Tamano, Mitsuyasu, Kubota, Yuki, Fujise, Ryota, Shimaya, Ryusei, Itoh, Miki, Suzuki, Paul A, Adlard, Ashley I, Bush, Atsushi, Takeda
Publikováno v:
Neurochemistry international. 120
On the basis of the evidence that the basolateral amygdala (BLA) modulates hippocampal memory processes via synaptic plasticity, here we report that adrenergic β receptor activation in the BLA rescues amyloid β