David Eisenberg
Affiliations: | University of California, Los Angeles, Los Angeles, CA |
Area:
protein interactionsWebsite:
http://www.chemistry.ucla.edu/directory/eisenberg-david-sGoogle:
"David Eisenberg"Bio:
http://www.nasonline.org/member-directory/members/7987.html
http://www.doe-mbi.ucla.edu/People/Eisenberg/
http://www.hhmi.org/scientists/david-eisenberg
Mean distance: 16.11 (cluster 11) | S | N | B | C | P |
Cross-listing: Neurotree
Parents
Sign in to add mentorJohn Tileston Edsall | research assistant | Harvard | |
Charles Alfred Coulson | grad student | 1964 | Oxford |
Walter Kauzmann | post-doc | 1964-1966 | Princeton |
Richard E. Dickerson | post-doc | 1966-1969 | Caltech |
Children
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Publications
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Rosenberg GM, Abskharon R, Boyer DR, et al. (2023) Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method. Pnas Nexus. 2: pgad402 |
Tayeb-Fligelman E, Bowler JT, Tai CE, et al. (2023) Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils. Nature Communications. 14: 2379 |
Ryder BD, Boyer DR, Ustyantseva E, et al. (2023) DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity. Biorxiv : the Preprint Server For Biology |
Buxbaum JN, Dispenzieri A, Eisenberg DS, et al. (2022) Amyloid nomenclature 2022: update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 1-7 |
Bowler JT, Sawaya MR, Boyer DR, et al. (2022) Micro-electron diffraction structure of the aggregation-driving N-terminus of Drosophila neuronal protein Orb2A reveals amyloid-like β-sheets. The Journal of Biological Chemistry. 102396 |
Murray KA, Hu CJ, Griner SL, et al. (2022) De novo designed protein inhibitors of amyloid aggregation and seeding. Proceedings of the National Academy of Sciences of the United States of America. 119: e2206240119 |
Murray KA, Evans D, Hughes MP, et al. (2022) Extended β-Strands Contribute to Reversible Amyloid Formation. Acs Nano |
Hughes MP, Goldschmidt L, Eisenberg DS. (2021) Prevalence and species distribution of the low-complexity, amyloid-like, reversible, kinked segment (LARKS) structural motif in amyloid-like fibrils. The Journal of Biological Chemistry. 101194 |
Sawaya MR, Hughes MP, Rodriguez JA, et al. (2021) The expanding amyloid family: Structure, stability, function, and pathogenesis. Cell. 184: 4857-4873 |
Lu J, Cao Q, Hughes MP, et al. (2020) CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid. Nature Communications. 11: 4090 |