David S. Eisenberg

David Eisenberg

David S. Eisenberg


Division: 
Biochemistry
Academic titles: 
Distinguished Professor
P.D. Boyer Chair
 
Specialties: 
Biochemistry
Biophysics
Structural and Computational Biology
Bioenergy and the Environment
Proteomics and Bioinformatics
Theory
Lab: 
Boyer Hall 201A
(310) 825-3754
Short Biography: 

David Eisenberg is a Professor of Chemistry and Biochemistry and of Biological Chemistry at the University of California, Los Angeles, and Director of the UCLA-DOE Institute for Genomics and Proteomics. He received his undergraduate degree in biochemical sciences from Harvard College and his D.Phil. degree in theoretical chemistry from Oxford University. His postdoctoral research was on ice and water with Walter Kauzmann at Princeton and in protein crystallography with Richard Dickerson. Dr. Eisenberg is a member of the National Academy of Sciences and the Institute of Medicine. He is a recipient of the 2004 UCLA Seaborg Medal, the 2005 Harvard Westheimer Medal, and the 2008 Emily Gray Award from the Biophysical Society.

Biography

Research Interest: 

David Eisenberg and his research group focus on protein interactions. In their experiments they study the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. In bioinformatic work, they derive information on protein interactions from genomic and proteomic data, and design inhibitors of amyloid toxicity.

Amyloid and prion diseases are diseases of protein aggregation in which a normal, functional protein converts to an abnormal, aggregated protein. The systemic amyloid diseases, such as dialysis-related amyloidosis, are apparently caused by the accumulation of fibers until organs fail. The neurodegenerative amyloid diseases, such as Alzheimer's, Parkinson's, amyotrophic lateral sclerosis (ALS), and the prion conditions, seem to be caused by smaller oligomers, intermediate in size between monomers and fibers. Our goals are to understand the general features of the conversion to the amyloid state, why some of the diseases are transmissible between organisms and others not, what the structures of the toxic units are, and how they exert their toxic actions.

 

In 2005, we determined the atomic-level structure for the spine of an amyloid fiber. This structure shows that the spine consists of two parallel beta sheets, packed across a tight, dry interface that we call a steric zipper. The structure of the spine explains the stability of amyloid, gives hints about the conversion process, and suggests why some proteins form amyloid while others do not. Since 2005, we have determined some 90 amyloid spines from 15 disease-related proteins, using a combination of bioinformatics and structural tools. In 2010, we determined the structure of a small toxic amyloid-related oligomer, consisting of six anti-parallel beta strands forming a cylindrical barrel. This structure may suggest models for the toxic oligomers associated with amyloid diseases.

Honors/Awards: 
  • UCLA McCoy Award
  • Amgen Award of the Protein Society
  • Pierce Award of the Immunotoxin Society
  • Biophysical Society Emily M. Gray Award
  • Technion - Israel Institute of Technology Harvey Prize in Human Health
  • Preceptor for the 2009 Nobel Laureate Signature Award for Graduate Education in Chemistry
  • Harvard Westheimer Medal
  • UCLA Seaborg Medal
  • Howard Hughes Medical Institute Investigator
  • National Academy of Sciences Elected Member
  • American Association for the Advancement of Science Fellow
  • American Philosophical Society Member
  • Institute of Medicine Member
Publications: 

2014

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1967

Other

Rokito AS, Zuckerman JD, Shaari JM, Eisenberg DP, Cuomo F, Gallagher MA. (Other). A comparison of nonoperative and operative treatment of type II distal clavicle fractures.Bull Hosp Jt Dis. . 61(1-2):32-9. [Abstract]