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Author Details

David Eisenberg
university of california los angeles
1963
415
125
PMIDPaper TitleJournal TitlePublished Year
38072051Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation.J Biol Chem2024
36757890Small molecules disaggregate alpha-synuclein and prevent seeding from patient brain-derived fibrils.Proc Natl Acad Sci U S A2023
38077690Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method.PNAS Nexus2023
37801475Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils.Proc Natl Acad Sci U S A2023
37185252Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils.Nat Commun2023
37398204CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis.bioRxiv2023
34954854Atomic view of an amyloid dodecamer exhibiting selective cellular toxic vulnerability in acute brain slices.Protein Sci2022
35405097Bioinformatic identification of previously unrecognized amyloidogenic proteins.J Biol Chem2022
35377792Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation.Proc Natl Acad Sci U S A2022
35344984Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43.Nature2022
35637421Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies.Nat Struct Mol Biol2022
36420821Amyloid nomenclature 2022: update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee.Amyloid2022
35969734De novo designed protein inhibitors of amyloid aggregation and seeding.Proc Natl Acad Sci U S A2022
35988647Micro-electron diffraction structure of the aggregation-driving N terminus of Drosophila neuronal protein Orb2A reveals amyloid-like β-sheets.J Biol Chem2022
36091211The rippled β-sheet layer configuration-a novel supramolecular architecture based on predictions by Pauling and Corey.Chem Sci2022
36114178Structure-based discovery of small molecules that disaggregate Alzheimer's disease tissue derived tau fibrils in vitro.Nat Commun2022
35132852Extended β-Strands Contribute to Reversible Amyloid Formation.ACS Nano2022
33372136Intrinsic electronic conductivity of individual atomically resolved amyloid crystals reveals micrometer-long hole hopping via tyrosines.Proc Natl Acad Sci U S A2021
33688654Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2.bioRxiv2021
34518699Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores.Nat Struct Mol Biol2021
34537246Prevalence and species distribution of the low-complexity, amyloid-like, reversible, kinked segment structural motif in amyloid-like fibrils.J Biol Chem2021
34534463The expanding amyloid family: Structure, stability, function, and pathogenesis.Cell2021
32541896Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils.Nat Struct Mol Biol2020
31895037Inhibition of synucleinopathic seeding by rationally designed inhibitors.Elife2020
32015135The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure.Proc Natl Acad Sci U S A2020
33100054Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee.Amyloid2020
32632432Half a century of amyloids: past, present and future.Chem Soc Rev2020
32796831CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid.Nat Commun2020
32284600Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core.Nat Struct Mol Biol2020
32493775Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease.J Biol Chem2020
30419243Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3, and ESX-5 Type VII Secretion Systems.J Mol Biol2019
31695184Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs.Nat Struct Mol Biol2019
31748568Mechanically rigid supramolecular assemblies formed from an Fmoc-guanine conjugated peptide nucleic acid.Nat Commun2019
31742246Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure.Nat Catal2019
31530939Author Correction: Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation.Nat Struct Mol Biol2019
31612856Structure-based inhibitors of amyloid beta core suggest a common interface with tau.Elife2019
31350392Structure of amyloid-β (20-34) with Alzheimer's-associated isomerization at Asp23 reveals a distinct protofilament interface.Nat Commun2019
31235914Cryo-EM structures of four polymorphic TDP-43 amyloid cores.Nat Struct Mol Biol2019
31537646Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples.J Biol Chem2019
30886570Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation.Front Mol Neurosci2019
30733338A pair of peptides inhibits seeding of the hormone transporter transthyretin into amyloid fibrils.J Biol Chem2019
29237120Ultrafast Time-Resolved Studies on Fluorescein for Recognition Strands Architecture in Amyloid Fibrils.J Phys Chem B2018
30190461Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel.Nat Commun2018
30213731Assessment of the effects of transthyretin peptide inhibitors in Drosophila models of neuropathic ATTR.Neurobiol Dis2018
30076408Atomic insights into the genesis of cellular filaments by globular proteins.Nat Struct Mol Biol2018
30049866Paul D. Boyer (1918-2018).Science2018
29954863Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition.Proc Natl Acad Sci U S A2018
30464263TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle.Nature2018
30297750Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design.Nat Chem2018
30420778Author Correction: Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design.Nat Chem2018
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Collaborators

Co-authored papers 67
university of california los angeles
Co-authored papers 19
Co-authored papers 13
Los Alamos National Laboratory
Co-authored papers 13
University of Lausanne
Co-authored papers 13
University of Texas
Co-authored papers 11
Department of Pharmaceutical Chemistry, University of California san francisco
Co-authored papers 11
Quantitative Biosciences Institute (QBI), University of California San Francisco
Co-authored papers 9
ETH Zurich
Co-authored papers 9
Co-authored papers 9
Howard Hughes Medical Institute, University of California los angeles
Co-authored papers 8
Stanford University
Co-authored papers 7
Co-authored papers 6
University of Missouri
Co-authored papers 5
University of Virginia
Co-authored papers 5
Co-authored papers 5
European Bioinformatics Institute (EMBL-EBI)
Co-authored papers 5
European Institute of Oncology IRCCS
Co-authored papers 5
Co-authored papers 5
University of Rome 'Tor Vergata'
Co-authored papers 5
University of California irvine
Co-authored papers 5
University of Colorado Denver.
Co-authored papers 4
Mayo Clinic Jacksonville
Co-authored papers 4
University of Toronto
Co-authored papers 4
Institute for Research in Immunology and Cancer (IRIC), Universite de Montreal
Co-authored papers 4
EMBL's European Bioinformatics Institute (EMBL-EBI)
Co-authored papers 4
Co-authored papers 4
University of Washington
Co-authored papers 4
Ecole polytechnique federale de Lausanne (EPFL)
Co-authored papers 3
National University of Singapore
Co-authored papers 3