David S. Eisenberg
· DPhil, Paul D. Boyer Professor of Molecular Biology and BiochemistryUniversity of California, Los Angeles · Chemistry and Biochemistry
Active 1963–2026
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About
David S. Eisenberg is a Professor of Chemistry and Biochemistry and Biological Chemistry at UCLA, serving as a HHMI Investigator and Director of the UCLA-DOE Institute for Genomics and Proteomics. His educational background includes an A.B. in Biochemical Sciences from Harvard College and a D.Phil. in Theoretical Chemistry from Oxford University, earned on a Rhodes Scholarship. He completed postdoctoral studies at Princeton University, focusing on water and hydrogen bonding, and at Caltech on protein crystallography before joining UCLA's faculty. Eisenberg's research centers on protein interactions, with a particular emphasis on amyloid-forming proteins. His work involves studying the structural basis for the conversion of normal proteins to the amyloid state and the transformation of prions into infectious forms, utilizing techniques such as X-ray crystallography, bioinformatics, and biochemistry. He has contributed significantly to understanding diseases related to protein aggregation, including systemic amyloidosis and neurodegenerative disorders like Alzheimer's, Parkinson's, and ALS. His research has led to the determination of the atomic structure of amyloid fibers and toxic oligomers, providing insights into their stability, formation, and toxicity. Eisenberg has published over 300 papers and reviews, holds multiple patents, and has received numerous awards, including membership in the National Academy of Sciences, the American Academy of Arts and Sciences, and the…
Research topics
- Chemistry
- Medicine
- Biology
- Computational biology
- Environmental science
- Pathology
- Environmental chemistry
Selected publications
Half a century of amyloids: past, present and future
Chemical Society Reviews · 2020 · 576 citations
Amyloid diseases are global epidemics with profound health, social and economic implications and yet remain without a cure. This dire situation calls for research into the origin and pathological manifestations of amyloidosis to stimulate continued development of new therapeutics. In basic science and engineering, the cross-β architecture has been a constant thread underlying the structural characteristics of pathological and functional amyloids, and realizing that amyloid structures can be both…
Amyloid · 2020 · 406 citations
amyloid, were discussed. It was decided to include fibulin-like extracellular matrix protein 1 (amyloid protein: AEFEMP1), which appears as localised amyloid in portal veins. There are several possible amyloid proteins under investigation, and these are included in a new Table.
Amyloid · 2024-09-30 · 126 citations
articleThe ISA Nomenclature Committee met at the XIX International Symposium of Amyloidosis in Rochester, MN, 27 May 2024. The in-person event was followed by many electronic discussions, resulting in the current updated recommendations. The general nomenclature principles are unchanged. The total number of human amyloid fibril proteins is now 42 of which 19 are associated with systemic deposition, while 4 occur with either localised or systemic deposits. Most systemic amyloidoses are caused by the pre…
Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy
Nature Communications · 2024-01-17 · 62 citations
articleOpen accessATTR amyloidosis is caused by the deposition of transthyretin in the form of amyloid fibrils in virtually every organ of the body, including the heart. This systemic deposition leads to a phenotypic variability that has not been molecularly explained yet. In brain amyloid conditions, previous studies suggest an association between clinical phenotype and the molecular structures of their amyloid fibrils. Here we investigate whether there is such an association in ATTRv amyloidosis patients carryi…
Science Advances · 2024-05-01 · 17 citations
articleOpen accessSenior authorCorrespondingAmyloid fibrils of tau are increasingly accepted as a cause of neuronal death and brain atrophy in Alzheimer's disease (AD). Diminishing tau aggregation is a promising strategy in the search for efficacious AD therapeutics. Previously, our laboratory designed a six-residue, nonnatural amino acid inhibitor D-TLKIVW peptide (6-DP), which can prevent tau aggregation in vitro. However, it cannot block cell-to-cell transmission of tau aggregation. Here, we find D-TLKIVWC (7-DP), a d-cysteine extensio…
Recent grants
Reversible Amyloid-Like Fibrils in Membraneless Organelles
NSF · $829k · 2016–2022
NIH · $3.9M · 2018
Development of inhibitors for systemic amyloid diseases
NIH · $1.9M · 2014–2019
Frequent coauthors
- 324 shared
M.R. Sawaya
Howard Hughes Medical Institute
- 158 shared
Duilio Cascio
University of California, Los Angeles
- 81 shared
David R. Boyer
University of California, Los Angeles
- 55 shared
José A. Rodríguez
Universidad de Alcalá
- 49 shared
Tamir Gonen
University of California, Los Angeles
- 47 shared
Michael P. Hughes
St. Jude Children's Research Hospital
- 44 shared
Lin Jiang
Xinjiang Medical University
- 43 shared
Lukasz Goldschmidt
University of Washington
Awards & honors
- Passano Laureate
- Thomson Reuters Most Highly Cited Author
- Bert and Natalie Vallee Award in Biomedical Science
- UCLA Switzer Prize
- Harvey Prize in Human Health
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