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Michael R. Sawaya

Researcher at University of California, Los Angeles

Publications -  255
Citations -  28324

Michael R. Sawaya is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Amyloid & Fibril. The author has an hindex of 78, co-authored 238 publications receiving 24515 citations. Previous affiliations of Michael R. Sawaya include University of Ulm & University of California, San Diego.

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers.

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.
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Structure of the cross-beta spine of amyloid-like fibrils.

TL;DR: The atomic structure of the cross-β spine illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.
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Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

TL;DR: It is discovered that exposure of cell or tissue lysates to a biotinylated isoxazole (b-isox) chemical precipitated hundreds of RNA-binding proteins with significant overlap to the constituents of RNA granules, offering a framework for understanding the function of LC sequences as well as an organizing principle for cellular structures that are not membrane bound.
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Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules

TL;DR: It is found that peptide and protein hormones in secretory granules of the endocrine system are stored in an amyloid-like cross–β-sheet–rich conformation, which means functional amyloids in the pituitary and other organs can contribute to normal cell and tissue physiology.
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Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis

TL;DR: This work bridges structural genomics to structural biology with a procedure for determining protein complexes of previously unknown function from any organism with a sequenced genome and its entire procedure can be scaled to a genome-wide level.