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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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Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation

TL;DR: This study developed an approach that combines the structure-based rational design with chemical modification for the development of amyloid inhibitors, which could be applied to the developed of therapeutics for different amyloids-related diseases.
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Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples

TL;DR: This work reports the 1.0 Å resolution micro-electron diffraction structure of an aggregation-prone segment of tau with the sequence SVQIVY, present in the cores of patient-derived fibrils from AD and tauopathies, and shows that tau-capping inhibitors can be transiently expressed in HEK293 tau biosensor cells, indicating that nucleic acid–based vectors can be used for inhibitor delivery.
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Emerging Credentialing Practices, Malpractice Liability Policies, and Guidelines Governing Complementary and Alternative Medical Practices and Dietary Supplement Recommendations: A Descriptive Study of 19 Integrative Health Care Centers in the United States

TL;DR: Hospitals are using heterogeneous approaches to address licensure, credentialing, scope of practice, malpractice liability, and dietary supplement use in developing models of integrative care.
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A model for oxidative modification of glutamine synthetase, based on crystal structures of mutant H269N and the oxidized enzyme.

TL;DR: Studies of mutant and oxidized enzymes confirm that there are at least two stages of oxidative modification of GS, and suggest that the early modification occurs at the n2 metal ion site, eliminating enzyme activity, and the later modification occursat the n1 metal ions site, relaxing the GS structure, perhaps enabling proteolytic degradation.
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Developing a library of authenticated Traditional Chinese Medicinal (TCM) plants for systematic biological evaluation — Rationale, methods and preliminary results from a Sino-American collaboration

TL;DR: This manuscript summarizes the rationale, methods and preliminary "proof of principle" for the establishment of this prototype, authenticated medicinal plant library and it is hoped that these methods will foster scientific discoveries with therapeutic potential and enhance efforts to systematically evaluate commonly used herbal therapies worldwide.