Functional and structural effects of amyloid-β aggregate on Xenopus laevis oocytes-Reference-Cited by-同舟云学术

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Functional and structural effects of amyloid-β aggregate on Xenopus laevis oocytes

Published:2012-10 Issue:4 Volume:34 Page:349-355
ISSN:1016-8478
Container-title:Molecules and Cells
language:en
Short-container-title:Mol Cells

Author:

Parodi Jorge,Ochoa-de la Paz Lenin,Miledi Ricardo,Martínez-Torres Ataúlfo

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/s10059-012-2247-8.pdf

Reference29 articles.

1. Arellano, R.O., Woodward, R.M., and Miledi, R. (1996). Ion channels and membrane receptors in follicle-enclosed Xenopus oocytes. Ion Channels 4, 203–259.

2. Arellano, R.O., Garay, E., and Miledi, R. (1998). Cl− currents activated via purinergic receptors in Xenopus follicles. Am. J. Physiol. 274, C333–340.

3. Arispe, N. (2004). Architecture of the Alzheimer’s A beta P ion channel pore. J. Membr. Biol. 197, 33–48.

4. Arispe, N., Pollard, H.B., and Rojas, E. (1994). The ability of amyloid beta-protein [A beta P (1–40)] to form Ca2+ channels provides a mechanism for neuronal death in Alzheimer’s disease. Ann. N Y Acad. Sci. 747, 256–266.

5. Avila, M.E., Sepulveda, F.J., Burgos, C.F., Moraga-Cid, G., Parodi, J., Moon, R.T., Aguayo, L.G., Opazo, C., and De Ferrari, G.V. (2010). Canonical Wnt3a modulates intracellular calcium and enhances excitatory neurotransmission in hippocampal neurons. J. Biol. Chem. 285, 18939–18947.

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