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Results: 7

1.
FIGURE 2.

FIGURE 2. From: Conformational Differences between Two Amyloid ? Oligomers of Similar Size and Dissimilar Toxicity.

AFM analysis of Aβ oligomerization. Aβ42 (25 μm) was assembled without agitation, deposited on mica substrates, and imaged using AFM. Each image is 3 × 3 μm, and the inset images are 0.5 × 0.5 μm.

Ali Reza A. Ladiwala, et al. J Biol Chem. 2012 July 13;287(29):24765-24773.
2.
FIGURE 4.

FIGURE 4. From: Conformational Differences between Two Amyloid ? Oligomers of Similar Size and Dissimilar Toxicity.

Impact of Aβ oligomers on lipid bilayer conductance. A, Aβ42 conformers (250 nm) were added to a reservoir on one side of the lipid bilayer (l-α-phosphocholine), and the membrane conductance was measured. B, Aβ A+ oligomers (12.5 μm) were mixed with the A11 antibody (0.2–3 μm) and diluted into a reservoir on one side of the lipid bilayer (50× dilution), and the membrane conductance was measured.

Ali Reza A. Ladiwala, et al. J Biol Chem. 2012 July 13;287(29):24765-24773.
3.
FIGURE 1.

FIGURE 1. From: Conformational Differences between Two Amyloid ? Oligomers of Similar Size and Dissimilar Toxicity.

Conformation-specific antibody analysis of Aβ assembly. Aβ42 conformers (1–75 μm) were assembled for 10 days (without agitation), and periodically deposited on nitrocellulose membranes. Afterward, the membranes were probed with conformation-specific (A11, prefibrillar oligomers (top), and OC, fibrillar conformers (middle)) and sequence-specific (6E10, N terminus of Aβ (bottom)) antibodies.

Ali Reza A. Ladiwala, et al. J Biol Chem. 2012 July 13;287(29):24765-24773.
4.
FIGURE 3.

FIGURE 3. From: Conformational Differences between Two Amyloid ? Oligomers of Similar Size and Dissimilar Toxicity.

Toxicity analysis of Aβ oligomers and fibrils. Aβ42 (25 μm) was assembled without agitation and added to rat adrenal medulla cells (A and B) and rat primary cortical neuronal cells (C), and the relative toxicity was evaluated (n = 3). Error bars, S.D.

Ali Reza A. Ladiwala, et al. J Biol Chem. 2012 July 13;287(29):24765-24773.
5.
FIGURE 7.

FIGURE 7. From: Conformational Differences between Two Amyloid ? Oligomers of Similar Size and Dissimilar Toxicity.

Characterization of the secondary structure and seeding activity of Aβ oligomers. Aβ42 (25 μm) was assembled without agitation (0–6 days), and its extent of fibrillization and secondary structure were evaluated using ThT fluorescence (A) and circular dichroism (B). C, Aβ fibrils and oligomers were mixed with Aβ monomers (25 μm, 5% seed), and their ThT fluorescence was monitored. RFU, relative fluorescence units. Error bars, S.D.

Ali Reza A. Ladiwala, et al. J Biol Chem. 2012 July 13;287(29):24765-24773.
6.
FIGURE 6.

FIGURE 6. From: Conformational Differences between Two Amyloid ? Oligomers of Similar Size and Dissimilar Toxicity.

Analysis of hydrophobicity and conformational stability of Aβ oligomers. A, Aβ42 (25 μm) was assembled without agitation, and the hydrophobicity of Aβ conformers formed each day was evaluated using ANS fluorescence. The wavelength corresponding to the maximum ANS fluorescence is reported on the y axis. B and C, Aβ conformers (25 μm) were incubated with variable amounts of guanidine hydrochloride, and then their relative degree of unfolding was evaluated using ANS fluorescence (B) and antibodies (A11, prefibrillar oligomers; OC, fibrillar conformers; 6E10, N terminus of Aβ) (C). Error bars, S.D.

Ali Reza A. Ladiwala, et al. J Biol Chem. 2012 July 13;287(29):24765-24773.
7.
FIGURE 5.

FIGURE 5. From: Conformational Differences between Two Amyloid ? Oligomers of Similar Size and Dissimilar Toxicity.

Rate of proteolytic fragmentation of Aβ peptide segments within Aβ oligomers. Aβ42 (25 μm) was incubated with Proteinase K (0.5 μg/ml), deposited periodically on nitrocellulose (every 10–30 min), and probed with antibodies specific for N-terminal (Aβ(3–10); 6E10), central (Aβ(18–22); 4G8), and C-terminal (Aβ(35–39); 9F1) Aβ epitopes. The time intervals were 0, 10, 20, 30, 40, 50, 60, 70, 80, 90, 120, and 150 min.

Ali Reza A. Ladiwala, et al. J Biol Chem. 2012 July 13;287(29):24765-24773.

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