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.
Papers
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Journal ArticleDOI
Mining literature for protein–protein interactions
TL;DR: It is shown that the frequencies of words in Medline abstracts can be used to determine whether or not a given paper discusses protein-protein interactions, and the relevant information can be captured for the Database of Interacting Proteins.
Journal ArticleDOI
Crystal structure of a synthetic triple-stranded alpha-helical bundle
Brett Lovejoy,Seunghyon Choe,Duilio Cascio,Donald K. McRorie,William F. DeGrado,David Eisenberg +5 more
TL;DR: The x-ray crystal structure of a peptide designed to form a double-stranded parallel coiled coil shows that it is actually a triple- Stranded coiled Coil formed by three alpha-helices, suggesting that hydrophobic interactions are a dominant factor in the stabilization of coiled coils.
Book ChapterDOI
Oligomer Formation By 3D Domain Swapping: A Model For Protein Assembly And Misassembly
TL;DR: The chapter closes with a brief consideration of the possibility that 3D domain swapping is a mechanism for the formation of amyloid or other pathological aggregates of proteins.
Journal ArticleDOI
Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability.
Michael Thompson,David Eisenberg +1 more
TL;DR: In this paper, a comparative analysis of 20 complete genomes for mesophilic, thermophilic and hyperthermophilic organisms was performed, showing a trend towards shortened thermophilicity relative to their mesophilous homologs.
Journal ArticleDOI
Toward rational protein crystallization: A Web server for the design of crystallizable protein variants
TL;DR: A Web server, the surface entropy reduction prediction server (SERp server), designed to identify mutations that may facilitate crystallization and an attempt to benchmark the server by comparing the server's predictions with successful SER structures.