Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores.
PublicMLA citation style (9th ed.)
. 3242. marian.palni-palci-staging.notch8.cloud/concern/generic_works/4c58baac-0f89-4021-9298-a0fd4f6f9976?locale=en. Amyloid-beta Alzheimer Targets - Protein Processing, Lipid Rafts, and Amyloid-beta Pores.APA citation style (7th ed.)
(3242). Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores. https://marian.palni-palci-staging.notch8.cloud/concern/generic_works/4c58baac-0f89-4021-9298-a0fd4f6f9976?locale=enChicago citation style (CMOS 17, author-date)
Amyloid-Beta Alzheimer Targets - Protein Processing, Lipid Rafts, and Amyloid-Beta Pores. 3242. https://marian.palni-palci-staging.notch8.cloud/concern/generic_works/4c58baac-0f89-4021-9298-a0fd4f6f9976?locale=en.Note: These citations are programmatically generated and may be incomplete.
Amyloid beta (A?), the hallmark of Alzheimer's Disease (AD), now appears to be deleterious in its low number aggregate form as opposed to the macroscopic A? fibers historically seen postmortem. While Alzheimer targets, such as the tau protein, amyloid precursor protein (APP) processing, and immune system activation continue to be investigated, the recent discovery that amyloid beta aggregates at lipid rafts and likely forms neurotoxic pores has led to a new paradigm regarding why past therapeutics may have failed and how to design the next round of compounds for clinical trials. An atomic resolution understanding of A? aggregates, which appear to exist in multiple conformations, is most desirable for future therapeutic development. The investigative difficulties, structures of these small A? aggregates, and current therapeutics are summarized in this review.
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- The Yale Journal of Biology and Medicine
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Amyloid-beta_Alzheimer_Arbor_2016.pdf | 2021-05-03 | Public | Download |