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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Prevalence and species distribution of the low-complexity, amyloid-like, reversible, kinked segment structural motif in amyloid-like fibrils.
TL;DR: In this article, the authors used computational methods to identify structural motifs termed low-complexity amyloid-like reversible kinked segments (LARKS) that promote phase transition to form hydrogels and that are common in human proteins that participate in Membraneless Organelles.
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Complementary and alternative medicine--an Annals series.
TL;DR: This special series of invited papers consists of reports of original health services research, critical reviews of the literature, and commentary on a variety of CAM-related issues to provide physicians with synoptic reports of the state of the science for commonly used CAM therapies.
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Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer’s disease
Romany Abskharon,Romany Abskharon,Paul M. Seidler,Paul M. Seidler,Michael R. Sawaya,Michael R. Sawaya,Duilio Cascio,Duilio Cascio,Tianxiao P. Yang,Tianxiao P. Yang,Stephan Philipp,Christopher Williams,Kathy L. Newell,Bernardino Ghetti,Michael DeTure,Dennis W. Dickson,Harry V. Vinters,Philip L. Felgner,Rie Nakajima,Charles G. Glabe,David Eisenberg,David Eisenberg +21 more
TL;DR: By binding to oligomers, which are hypothesized to be the earliest seeding-competent species, M204-scFv may have potential as an early-stage diagnostic for AD and tauopathies, and also could guide the development of promising therapeutic antibodies.
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3D structure and significance of the GPhiXXG helix packing motif in tetramers of the E1beta subunit of pyruvate dehydrogenase from the archeon Pyrobaculum aerophilum.
TL;DR: The determination of the 2.0 A structure of the E1beta subunit of pyruvate dehydrogenase from Pyrobaculum aerophilum (PA), a thermophilic archaeon, illustrates that comparative analysis of protein structures can identify the structural significance of a sequence motif.
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Revealing structure–activity links in hydrazine oxidation: doping and nanostructure in carbide–carbon electrocatalysts
TL;DR: In this paper, the effect of doping on carbide-carbon composites was studied and it was shown that doping enhanced activity by nanostructural effects rather than purely catalytic effects, as revealed by electrochemical and material investigations.