@article {64833,
	title = {Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.},
	journal = {Nature Communications},
	volume = {10},
	year = {2019},
	month = {2019 Mar 07},
	pages = {1104},
	abstract = {<p>Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, we report the purification and electron cryo-microscopy analysis of amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The obtained resolutions are 3.0 {\r A} and 2.7 {\r A} for the murine and human fibril, respectively. The two fibrils differ in fundamental properties, such as presence of right-hand or left-hand twisted cross-β sheets and overall fold of the fibril proteins. Yet, both proteins adopt highly similar β-arch conformations within the N-terminal ~21 residues. Our data demonstrate the importance of the fibril protein N-terminus for the stability of the analyzed amyloid fibril morphologies and suggest strategies of combating this disease by interfering with specific fibril polymorphs.</p>
},
	issn = {2041-1723},
	doi = {10.1038/s41467-019-09033-z},
	author = {Liberta, Falk and Loerch, Sarah and Rennegarbe, Matthies and Schierhorn, Angelika and Westermark, Per and Westermark, Gunilla T and Hazenberg, Bouke P C and Grigorieff, Nikolaus and F{\"a}ndrich, Marcus and Schmidt, Matthias}
}
@article {48156,
	title = {Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.},
	journal = {eLife},
	volume = {6},
	year = {2017},
	month = {2017 Jan 03},
	abstract = {<p>hIAPP fibrils are associated with Type-II Diabetes, but the link of hIAPP structure to islet cell death remains elusive. Here we observe that hIAPP fibrils are cytotoxic to cultured pancreatic β-cells, leading us to determine the structure and cytotoxicity of protein segments composing the amyloid spine of hIAPP. Using the cryoEM method MicroED, we discover that one segment, 19-29 S20G, forms pairs of β-sheets mated by a dry interface that share structural features with and are similarly cytotoxic to full-length hIAPP fibrils. In contrast, a second segment, 15-25 WT, forms non-toxic labile β-sheets. These segments possess different structures and cytotoxic effects, however, both can seed full-length hIAPP, and cause hIAPP to take on the cytotoxic and structural features of that segment. These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of hIAPP.</p>
},
	issn = {2050-084X},
	doi = {10.7554/eLife.19273},
	author = {Krotee, Pascal and Rodriguez, Jose A and Sawaya, Michael R and Cascio, Duilio and Reyes, Francis E and Shi, Dan and Hattne, Johan and Nannenga, Brent L and Oskarsson, Marie E and Philipp, Stephan and Griner, Sarah and Jiang, Lin and Glabe, Charles G and Westermark, Gunilla T and Gonen, Tamir and Eisenberg, David S}
}
