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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Journal ArticleDOI
Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels.
Thanh D. Do,Nichole E. LaPointe,Nichole E. LaPointe,Rebecca Nelson,Rebecca Nelson,Pascal Krotee,Pascal Krotee,Eric Y. Hayden,Eric Y. Hayden,Brittany Ulrich,Brittany Ulrich,Sarah Quan,Sarah Quan,Stuart C. Feinstein,Stuart C. Feinstein,David B. Teplow,David B. Teplow,David Eisenberg,David Eisenberg,Joan-Emma Shea,Joan-Emma Shea,Michael T. Bowers,Michael T. Bowers +22 more
TL;DR: It is found that hexamers of C-terminal Aβ fragments, including Aβ(24-34), A β(25-35) and Aβ (26-36), have collision cross sections similar to those of cylindrins and that β-barrels can be formed by folding an out-of-register β-sheet, a common type of structure found in amyloid proteins.
Journal ArticleDOI
Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO
TL;DR: The structure of RuBisCO, the first L8S8 type known from an X-ray crystallographic study at near-atomic resolution, shows that all eight L subunits are elongated along the 4-fold axis so that the molecule cannot be simply described as layers of subunits, as it had been from studies by electron microscopy.
Journal Article
Double-blind placebo-controlled trial of static magnets for the treatment of osteoarthritis of the knee: results of a pilot study.
Peter M. Wolsko,David Eisenberg,Lee S. Simon,Roger B. Davis,Jan Walleczek,Michael F. Mayo-Smith,Ted J. Kaptchuk,Russell S. Phillips +7 more
TL;DR: The sustained efficacy of magnetic therapy for knee osteoarthritis could be assessed in an adequately powered trial utilizing an appropriate control such as a new placebo-magnet device.
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Structure-based inhibitors of amyloid beta core suggest a common interface with tau.
Sarah Griner,Paul M. Seidler,Jeannette Bowler,Kevin A. Murray,Tianxiao Peter Yang,Shruti Sahay,Michael R. Sawaya,Duilio Cascio,Jose A. Rodriguez,Stephan Philipp,Justyna Sosna,Charles G. Glabe,Charles G. Glabe,Tamir Gonen,David Eisenberg +14 more
TL;DR: The ability of these inhibitors to interfere with both Aβ and tau seeds suggests these fibrils share a common epitope, and supports the hypothesis that cross-seeding is one mechanism by which amyloid is linked to tau aggregation and could promote cognitive decline.
Journal ArticleDOI
Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation.
TL;DR: In this article, the crystal structure of glutamine synthetase (GS) from Mycobacterium tuberculosis determined at 2.4 was refined with strict 24-fold non-crystallographic symmetry (NCS) constraints and has an R-factor of 22.7% and R-free of 25.5%.