![Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β40 (Aβ40) by the peptide fragment Aβ16–22 | Science Advances Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β40 (Aβ40) by the peptide fragment Aβ16–22 | Science Advances](https://www.science.org/cms/10.1126/sciadv.aav8216/asset/99b31615-823b-41c3-8755-1783c4eef017/assets/graphic/aav8216-f1.jpeg)
Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β40 (Aβ40) by the peptide fragment Aβ16–22 | Science Advances
![Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation | PNAS Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation | PNAS](https://www.pnas.org/cms/10.1073/pnas.0711731105/asset/1ce45235-4067-4d66-aed5-b99b81ba395e/assets/graphic/zpq0100898160003.jpeg)
Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation | PNAS
![Sequence alignment of IAPP and A-(1– 40). The sequence alignment of... | Download Scientific Diagram Sequence alignment of IAPP and A-(1– 40). The sequence alignment of... | Download Scientific Diagram](https://www.researchgate.net/publication/8895683/figure/fig1/AS:394514310156297@1471070949873/Sequence-alignment-of-IAPP-and-A-1-40-The-sequence-alignment-of-IAPP-and-A-1-40.png)
Sequence alignment of IAPP and A-(1– 40). The sequence alignment of... | Download Scientific Diagram
![Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage | Nature Communications Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage | Nature Communications](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41467-020-16566-1/MediaObjects/41467_2020_16566_Fig1_HTML.png)
Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage | Nature Communications
![Sequence of Ab 1-42 and N-terminal truncated Ab starting at position 3.... | Download Scientific Diagram Sequence of Ab 1-42 and N-terminal truncated Ab starting at position 3.... | Download Scientific Diagram](https://www.researchgate.net/publication/246987877/figure/fig1/AS:669004217716750@1536514443528/Sequence-of-Ab-1-42-and-N-terminal-truncated-Ab-starting-at-position-3-a-Ab-1-42-starts.png)
Sequence of Ab 1-42 and N-terminal truncated Ab starting at position 3.... | Download Scientific Diagram
![Beta-amyloid A β 1-40 amino acid sequence (active fragment A β 16-22 in... | Download Scientific Diagram Beta-amyloid A β 1-40 amino acid sequence (active fragment A β 16-22 in... | Download Scientific Diagram](https://www.researchgate.net/publication/273752134/figure/fig1/AS:294717100183556@1447277440326/Beta-amyloid-A-b-1-40-amino-acid-sequence-active-fragment-A-b-16-22-in-blue-balls.png)
Beta-amyloid A β 1-40 amino acid sequence (active fragment A β 16-22 in... | Download Scientific Diagram
![Are N- and C-terminally truncated Aβ species key pathological triggers in Alzheimer's disease? - ScienceDirect Are N- and C-terminally truncated Aβ species key pathological triggers in Alzheimer's disease? - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0021925820352455-gr1.jpg)
Are N- and C-terminally truncated Aβ species key pathological triggers in Alzheimer's disease? - ScienceDirect
![Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils | Nature Structural & Molecular Biology Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils | Nature Structural & Molecular Biology](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fnsmb.1799/MediaObjects/41594_2010_Article_BFnsmb1799_Fig1_HTML.jpg)
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils | Nature Structural & Molecular Biology
![Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface | Science Advances Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface | Science Advances](https://www.science.org/cms/10.1126/sciadv.aaz6014/asset/c59ced8e-f730-4db2-84bc-31931ec7456e/assets/graphic/aaz6014-f1.jpeg)
Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface | Science Advances
![Dominance of Amyloid Precursor Protein Sequence over Host Cell Secretases in Determining β-Amyloid Profiles Studies of Interspecies Variation and Drug Action by Internally Standardized Immunoprecipitation/Mass Spectrometry | Journal of Pharmacology and ... Dominance of Amyloid Precursor Protein Sequence over Host Cell Secretases in Determining β-Amyloid Profiles Studies of Interspecies Variation and Drug Action by Internally Standardized Immunoprecipitation/Mass Spectrometry | Journal of Pharmacology and ...](https://jpet.aspetjournals.org/content/jpet/320/3/1144/F1.large.jpg)
Dominance of Amyloid Precursor Protein Sequence over Host Cell Secretases in Determining β-Amyloid Profiles Studies of Interspecies Variation and Drug Action by Internally Standardized Immunoprecipitation/Mass Spectrometry | Journal of Pharmacology and ...
![Amyloid beta: structure, biology and structure-based therapeutic development | Acta Pharmacologica Sinica Amyloid beta: structure, biology and structure-based therapeutic development | Acta Pharmacologica Sinica](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Faps.2017.28/MediaObjects/41401_2017_Article_BFaps201728_Fig3_HTML.jpg)
Amyloid beta: structure, biology and structure-based therapeutic development | Acta Pharmacologica Sinica
![Figure 1 from How do membranes initiate Alzheimer's Disease? Formation of toxic amyloid fibrils by the amyloid β-protein on ganglioside clusters. | Semantic Scholar Figure 1 from How do membranes initiate Alzheimer's Disease? Formation of toxic amyloid fibrils by the amyloid β-protein on ganglioside clusters. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/d315aeb12a281c1d0faeac68c86e2b75c9b752e6/2-Figure1-1.png)
Figure 1 from How do membranes initiate Alzheimer's Disease? Formation of toxic amyloid fibrils by the amyloid β-protein on ganglioside clusters. | Semantic Scholar
![Refining the amyloid β peptide and oligomer fingerprint ambiguities in Alzheimer's disease: Mass spectrometric molecular characterization in brain, cerebrospinal fluid, blood, and plasma - Michno - 2021 - Journal of Neurochemistry - Wiley Online Library Refining the amyloid β peptide and oligomer fingerprint ambiguities in Alzheimer's disease: Mass spectrometric molecular characterization in brain, cerebrospinal fluid, blood, and plasma - Michno - 2021 - Journal of Neurochemistry - Wiley Online Library](https://onlinelibrary.wiley.com/cms/asset/90191c73-6946-48c7-8f9a-7e6734a9aa10/jnc15466-fig-0002-m.jpg)