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David Eisenberg

Researcher at Technion – Israel Institute of Technology

Publications -  719
Citations -  120468

David Eisenberg is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: Amyloid & Protein structure. The author has an hindex of 156, co-authored 697 publications receiving 112460 citations. Previous affiliations of David Eisenberg include Howard Hughes Medical Institute & Hebrew University of Jerusalem.

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Identifying the amylome, proteins capable of forming amyloid-like fibrils

TL;DR: The amylome is the universe of proteins that are capable of forming amyloid-like fibrils and the presence in the protein of a segment that can form a tightly complementary interface with an identical segment permits the formation of a steric zipper.
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3D domain swapping: As domains continue to swap

TL;DR: It is suggested that 3D domain swapping can occur under appropriate conditions in any protein with an unconstrained terminus and that the swapped domains are diverse in their primary and secondary structures.
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The crystal structure of diphtheria toxin

TL;DR: The crystal structure of the diphtheria toxin dimer at 2.5 Å resolution reveals a Y-shaped molecule of three domains that can be useful in designing chimaeric proteins, such as immunotoxins, in which the receptor-binding domain is substituted with antibodies to target other cell types.