@article {49117,
	title = {Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2.},
	journal = {Nature Structural \& Molecular Biology},
	year = {2018},
	month = {2018 Mar 12},
	abstract = {<p>Proteins in the fibrous amyloid state are a major hallmark of neurodegenerative disease. Understanding the multiple conformations, or polymorphs, of amyloid proteins at the molecular level is a challenge of amyloid research. Here, we detail the wide range of polymorphs formed by a segment of human TAR DNA-binding protein 43 (TDP-43) as a model for the polymorphic capabilities of pathological amyloid aggregation. Using X-ray diffraction, microelectron diffraction (MicroED) and single-particle cryo-EM, we show that theDLIIKGISVHIsegment from the second RNA-recognition motif (RRM2) forms an array of amyloid polymorphs. These associations include seven distinct interfaces displaying five different symmetry classes of steric zippers. Additionally, we find that this segment can adopt three different backbone conformations that contribute to its polymorphic capabilities. The polymorphic nature of this segment illustrates at the molecular level how amyloid proteins can form diverse fibril structures.</p>
},
	issn = {1545-9985},
	doi = {10.1038/s41594-018-0045-5},
	author = {Guenther, Elizabeth L and Ge, Peng and Trinh, Hamilton and Sawaya, Michael R and Cascio, Duilio and Boyer, David R and Gonen, Tamir and Zhou, Z Hong and Eisenberg, David S}
}
@article {49006,
	title = {Sub-{\r a}ngstr{\"o}m cryo-EM structure of a prion protofibril reveals a polar clasp.},
	journal = {Nature Structural \& Molecular Biology},
	year = {2018},
	month = {2018 Jan 15},
	abstract = {<p>The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-{\r a}ngstr{\"o}m-resolution structure of a protofibril formed by a wild-type segment from the β2-α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named {\textquoteright}polar clasps{\textquoteright}.</p>
},
	issn = {1545-9985},
	doi = {10.1038/s41594-017-0018-0},
	author = {Gallagher-Jones, Marcus and Glynn, Calina and Boyer, David R and Martynowycz, Michael W and Hernandez, Evelyn and Miao, Jennifer and Zee, Chih-Te and Novikova, Irina V and Goldschmidt, Lukasz and McFarlane, Heather T and Helguera, Gustavo F and Evans, James E and Sawaya, Michael R and Cascio, Duilio and Eisenberg, David S and Gonen, Tamir and Rodriguez, Jose A}
}
