![The Aβ(1–38) peptide is a negative regulator of the Aβ(1–42) peptide implicated in Alzheimer disease progression | Scientific Reports The Aβ(1–38) peptide is a negative regulator of the Aβ(1–42) peptide implicated in Alzheimer disease progression | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-020-80164-w/MediaObjects/41598_2020_80164_Fig4_HTML.png)
The Aβ(1–38) peptide is a negative regulator of the Aβ(1–42) peptide implicated in Alzheimer disease progression | Scientific Reports
![Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation | Journal of the American Chemical Society Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation | Journal of the American Chemical Society](https://pubs.acs.org/cms/10.1021/ja036813f/asset/images/medium/ja036813ff00009.gif)
Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation | Journal of the American Chemical Society
![Figure 1 from Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. | Semantic Scholar Figure 1 from Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/dcfaca302f14329361847645e1cb52a6cfaf1f1f/5-Figure3-1.png)
Figure 1 from Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. | Semantic Scholar
![Brain Sciences | Free Full-Text | Prognostic Role of CSF β-amyloid 1–42/1–40 Ratio in Patients Affected by Amyotrophic Lateral Sclerosis Brain Sciences | Free Full-Text | Prognostic Role of CSF β-amyloid 1–42/1–40 Ratio in Patients Affected by Amyotrophic Lateral Sclerosis](https://pub.mdpi-res.com/brainsci/brainsci-11-00302/article_deploy/html/images/brainsci-11-00302-ag-550.jpg?1616466416)
Brain Sciences | Free Full-Text | Prognostic Role of CSF β-amyloid 1–42/1–40 Ratio in Patients Affected by Amyotrophic Lateral Sclerosis
![Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures | PNAS Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures | PNAS](https://www.pnas.org/cms/10.1073/pnas.0905007106/asset/0fd877ea-d670-411b-942e-ef2633af1dd5/assets/graphic/zpq9990900970003.jpeg)
Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures | PNAS
![Frontiers | The Acute Effects of Amyloid-Beta1–42 on Glutamatergic Receptor and Transporter Expression in the Mouse Hippocampus Frontiers | The Acute Effects of Amyloid-Beta1–42 on Glutamatergic Receptor and Transporter Expression in the Mouse Hippocampus](https://www.frontiersin.org/files/MyHome%20Article%20Library/494393/494393_Thumb_400.jpg)
Frontiers | The Acute Effects of Amyloid-Beta1–42 on Glutamatergic Receptor and Transporter Expression in the Mouse Hippocampus
![Neurotoxicity and Memory Deficits Induced by Soluble Low-Molecular-Weight Amyloid-β1–42 Oligomers Are Revealed In Vivo by Using a Novel Animal Model | Journal of Neuroscience Neurotoxicity and Memory Deficits Induced by Soluble Low-Molecular-Weight Amyloid-β1–42 Oligomers Are Revealed In Vivo by Using a Novel Animal Model | Journal of Neuroscience](https://www.jneurosci.org/content/jneuro/32/23/7852/F1.large.jpg)
Neurotoxicity and Memory Deficits Induced by Soluble Low-Molecular-Weight Amyloid-β1–42 Oligomers Are Revealed In Vivo by Using a Novel Animal Model | Journal of Neuroscience
Assessments of Aβ-(1-42) under oligomer-and fibril-forming conditions... | Download Scientific Diagram
![Treatment of beta amyloid 1–42 (Aβ1–42)-induced basal forebrain cholinergic damage by a non-classical estrogen signaling activator in vivo | Scientific Reports Treatment of beta amyloid 1–42 (Aβ1–42)-induced basal forebrain cholinergic damage by a non-classical estrogen signaling activator in vivo | Scientific Reports](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fsrep21101/MediaObjects/41598_2016_Article_BFsrep21101_Fig1_HTML.jpg)
Treatment of beta amyloid 1–42 (Aβ1–42)-induced basal forebrain cholinergic damage by a non-classical estrogen signaling activator in vivo | Scientific Reports
![Truncated Amyloid-β(11–40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly* - Journal of Biological Chemistry Truncated Amyloid-β(11–40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly* - Journal of Biological Chemistry](https://www.jbc.org/cms/asset/e13fa711-4677-4866-83db-b3180ed298ef/gr1.jpg)
Truncated Amyloid-β(11–40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly* - Journal of Biological Chemistry
![Frontiers | Detection of Amyloid-β(1–42) Aggregation With a Nanostructured Electrochemical Sandwich Immunoassay Biosensor Frontiers | Detection of Amyloid-β(1–42) Aggregation With a Nanostructured Electrochemical Sandwich Immunoassay Biosensor](https://www.frontiersin.org/files/Articles/853947/fbioe-10-853947-HTML/image_m/fbioe-10-853947-g009.jpg)
Frontiers | Detection of Amyloid-β(1–42) Aggregation With a Nanostructured Electrochemical Sandwich Immunoassay Biosensor
![Figure 1 from Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. | Semantic Scholar Figure 1 from Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/dcfaca302f14329361847645e1cb52a6cfaf1f1f/4-Figure1-1.png)
Figure 1 from Amyloid-beta(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate. | Semantic Scholar
Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils - Chemical Communications (RSC Publishing)
![Peptide dimer conformations in A β (1 – 42) and A β (1 – 40) fibrils.... | Download Scientific Diagram Peptide dimer conformations in A β (1 – 42) and A β (1 – 40) fibrils.... | Download Scientific Diagram](https://www.researchgate.net/publication/281634997/figure/fig2/AS:284449943113729@1444829559114/Peptide-dimer-conformations-in-A-b-1-42-and-A-b-1-40-fibrils-Cross-sections-of.png)