The natural product betulinic acid rapidly promotes amyloid-β fibril formation at the expense of soluble oligomers.

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The unfolded protein response in the therapeutic effect of hydroxy-DHA against Alzheimer's disease.Ring-like N-fold Models of Aβ42 fibrils.

P2860

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The natural product betulinic acid rapidly promotes amyloid-β fibril formation at the expense of soluble oligomers.

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http://www.wikidata.org/entity/Q37642967

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2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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The natural product betulinic ...... expense of soluble oligomers.

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The natural product betulinic ...... expense of soluble oligomers.

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The natural product betulinic ...... expense of soluble oligomers.

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The natural product betulinic ...... expense of soluble oligomers.

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The natural product betulinic ...... expense of soluble oligomers.

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The natural product betulinic ...... expense of soluble oligomers.

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P1476

The natural product betulinic ...... expense of soluble oligomers.

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P2093

Amit Kumar

http://www.w3.org/2001/XMLSchema#string

Matthew S Planchard

http://www.w3.org/2001/XMLSchema#string

Michael A Samel

http://www.w3.org/2001/XMLSchema#string

Vijayaraghavan Rangachari

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P2860

Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Selective cytotoxicity of betulinic acid on tumor cell lines, but not on normal cells

Betulinic acid triggers CD95 (APO-1/Fas)- and p53-independent apoptosis via activation of caspases in neuroectodermal tumors

Discovery of betulinic acid as a selective inhibitor of human melanoma that functions by induction of apoptosis

A specific amyloid-beta protein assembly in the brain impairs memory

Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins

Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo

N-Methylated peptide inhibitors of beta-amyloid aggregation and toxicity. Optimization of the inhibitor structure.

Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formation

Amyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins.

P304

900-908

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scholarly article

P356

10.1021/CN300030A

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P478

http://www.w3.org/2001/XMLSchema#string

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2012-11-01T00:00:00Z

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230692582

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23401880

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P932

3957411

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The natural product betulinic acid rapidly promotes amyloid-β fibril formation at the expense of soluble oligomers.

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P2860

P2860

The natural product betulinic acid rapidly promotes amyloid-β fibril formation at the expense of soluble oligomers.

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P1433

P1476

P2093

P2860

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P698

P932

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P2860

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P932