D
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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Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure.
Pandeeswar Makam,Sharma S. R. K. C. Yamijala,Kai Tao,Linda J. W. Shimon,David Eisenberg,Michael R. Sawaya,Bryan M. Wong,Ehud Gazit +7 more
TL;DR: Evidence is presented for the ability of a single amino acid to self-assemble into a potent and stable catalytic structural entity showing catalytic properties similar to those of the natural enzyme carbonic anhydrase.
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An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (Antigen 85B), a mycolyl transferase.
TL;DR: Two crystal structures of M. tuberculosis antigen 85B are determined and a new class of antituberculous drugs are suggested, made by connecting two trehalose molecules by an amphipathic linker, minimizes aqueous exposure of the apolar mycolates.
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Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta
Lin Jiang,Cong Liu,David J. Leibly,Meytal Landau,Minglei Zhao,Michael P. Hughes,David Eisenberg +6 more
TL;DR: Structural-activity relationship studies of the fiber-binding compounds and their derivatives suggest that compound binding increases fiber stability and decreases fiber toxicity, perhaps by shifting the equilibrium of Aβ from oligomers to fibers.
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Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs
TL;DR: Cryo-EM analyses of α-synuclein fibrils formed with hereditary Parkinson's disease mutant H50Q reveal features that help explain the mutant’s properties in vitro and in cells.
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Structures of the two 3D domain-swapped RNase A trimers.
TL;DR: The first example of a protein that can form both a linear and a cyclic domain‐swapped oligomer is revealed, permit interpretation of the enzymatic activities of the RNase A oligomers on double‐stranded RNA.