S
Stuart A. Sievers
Researcher at California Institute of Technology
Publications - 33
Citations - 4855
Stuart A. Sievers is an academic researcher from California Institute of Technology. The author has contributed to research in topics: Chimeric antigen receptor & Amyloid. The author has an hindex of 18, co-authored 33 publications receiving 4316 citations. Previous affiliations of Stuart A. Sievers include Howard Hughes Medical Institute & University of California, Los Angeles.
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Journal ArticleDOI
Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
Michael R. Sawaya,S. Sambashivan,Rebecca Nelson,Magdalena I. Ivanova,Stuart A. Sievers,Marcin I. Apostol,Michael J. Thompson,Melinda Balbirnie,Jed J.W. Wiltzius,Heather T. McFarlane,Anders Ø. Madsen,Anders Ø. Madsen,Christian Riekel,David Eisenberg +13 more
TL;DR: Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.
Journal ArticleDOI
Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation
Stuart A. Sievers,John Karanicolas,John Karanicolas,Howard W. Chang,Anni Zhao,Lin Jiang,Onofrio Zirafi,Jason T. Stevens,Jan Münch,David Baker,David Eisenberg +10 more
TL;DR: The results indicate that peptides from structure-based designs can disrupt the fibril formation of full-length proteins, including those, such as tau protein, that lack fully ordered native structures.
Journal ArticleDOI
The 3D profile method for identifying fibril-forming segments of proteins
Michael Thompson,Stuart A. Sievers,John Karanicolas,Magdalena I. Ivanova,David Baker,David Eisenberg +5 more
TL;DR: Based on the crystal structure of the cross-beta spine formed by the peptide NNQQNY, a computational approach for identifying those segments of amyloidogenic proteins that themselves can form amyloids-like fibrils is developed.
Journal ArticleDOI
Molecular basis for insulin fibril assembly.
TL;DR: It is found that the segment of the insulin B-chain with sequence LVEALYL is the smallest segment that both nucleates and inhibits the fibrillation of full-length insulin in a molar ratio–dependent manner, suggesting that this segment is central to the cross-β spine of the pancreatic fibril.
Journal ArticleDOI
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin).
Jed J.W. Wiltzius,Stuart A. Sievers,Michael R. Sawaya,Duilio Cascio,Dmitriy Popov,Christian Riekel,David Eisenberg +6 more
TL;DR: The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full‐length IAPP polymorph.