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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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Effects of tai chi mind-body movement therapy on functional status and exercise capacity in patients with chronic heart failure: a randomized controlled trial.

TL;DR: Tai chi may be a beneficial adjunctive treatment that enhances quality of life and functional capacity in patients with chronic heart failure who are already receiving standard medical therapy.
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A structure-based mechanism for copper-zinc superoxide dismutase.

TL;DR: The outlines of a structure-based cyclic mechanism for copper-zinc superoxide dismutase (CuZnSOD) are offered, which involves inner sphere electron transfer from superoxide to Cu(II) in one portion of the cycle and outer sphere electrons transfer from Cu(I) to superoxide in the other portion of this cycle.
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Reconstruction of glutamine synthetase using computer averaging.

TL;DR: The axial projection of the glutamine synthetase molecule has been reconstructed from electron micrographs of a stained preparation by using a new method of correlation search and averaging.
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Use of complementary and alternative medical therapies among racial and ethnic minority adults: results from the 2002 National Health Interview Survey.

TL;DR: Excluding prayer, Hispanics and non-Hispanic blacks used CAM less frequently thanNon-Hispanic whites and were less likely to disclose their use to their healthcare provider.
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Three-dimensional Cluster Analysis Identifies Interfaces and Functional Residue Clusters in Proteins

TL;DR: It is found that the regional conservation score (C(R)(x)) identifies functional residue clusters better than a scoring scheme that does not take 3D information into account, and is particularly useful for the prediction of poorly conserved, transient protein-protein interfaces.