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Edward H. Egelman

Edward H. Egelman

· Professor of Structure and Function of Macromolecular Complexes Using Electron Microscopy

University of Virginia · Biochemistry and Molecular Genetics

Active 1980–2026

h-index93
Citations25.4k
Papers40887 last 5y
Funding$36.6M1 active

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Edward H. Egelman is a professor in the Department of Biochemistry and Molecular Genetics at the University of Virginia School of Medicine. He holds a BA in Physics and a PhD in Biophysics from Brandeis University, and completed postdoctoral training in Biophysics at the MRC Laboratory of Molecular Biology in Cambridge, UK. His research focuses on the structure and function of macromolecular assemblies, utilizing electron cryo-microscopy and three-dimensional reconstruction techniques. His work has historically concentrated on protein-DNA complexes and F-actin, with recent advancements enabling near-atomic resolution of many filamentous biological assemblies. Egelman's research explores themes such as the lability of quaternary structures, the impact of small sequence changes on protein assembly and evolution, and the extraordinary conservation of actin sequences over hundreds of millions of years. His studies have provided insights into how minor sequence variations can lead to significant structural and functional divergence, and how extensive allosteric networks within actin contribute to its remarkable properties. His contributions have advanced understanding of macromolecular complex architecture and dynamics, with implications for evolutionary biology and cellular function.

Research topics

  • Biology
  • Chemistry
  • Biophysics
  • Biochemistry
  • Genetics
  • Cell biology
  • Evolutionary biology
  • Anatomy
  • Polymer chemistry
  • Neuroscience

Selected publications

  • Cryo-EM structure of an extracellular Geobacter OmcE cytochrome filament reveals tetrahaem packing

    Nature Microbiology · 2022 · 114 citations

  • Mating pair stabilization mediates bacterial conjugation species specificity

    Nature Microbiology · 2022 · 101 citations

    interacts with OmpK36 through the insertion of a β-hairpin in the tip of TraN into a monomer of the OmpK36 porin trimer. Combining bioinformatic analysis with AlphaFold structural predictions, we identified a fourth TraN structural variant that mediates mating pair stabilization by binding OmpF. Accordingly, we devised a classification scheme for TraN homologues on the basis of structural similarity and their associated receptors: TraNα (OmpW), TraNβ (OmpK36), TraNγ (OmpA), TraNδ (OmpF). These T…

  • Artificial Intracellular Filaments

    Cell Reports Physical Science · 2020 · 73 citations

    formation of self-limiting intracellular filaments of a small peptide via enzymatic morphological transition of a phosphorylated and trimethylated heterochiral tetrapeptide. Enzymatic dephosphorylation reduces repulsive intermolecular electrostatic interactions and converts the peptidic nanoparticles into filaments, which exhibit distinct types of cross-β structures with either C7 or C2 symmetries, with the hydrophilic C-terminal residues at the periphery of the helix. Macromolecular crowding pr…

  • Osteogenesis imperfecta mutations in plastin 3 lead to impaired calcium regulation of actin bundling

    Bone Research · 2020 · 37 citations

    .

  • The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage

    Proceedings of the National Academy of Sciences · 2020 · 36 citations

    Lipases are enzymes necessary for the proper distribution and utilization of lipids in the human body. Lipoprotein lipase (LPL) is active in capillaries, where it plays a crucial role in preventing dyslipidemia by hydrolyzing triglycerides from packaged lipoproteins. Thirty years ago, the existence of a condensed and inactive LPL oligomer was proposed. Although recent work has shed light on the structure of the LPL monomer, the inactive oligomer remained opaque. Here we present a cryo-EM reconst…

Recent grants

Frequent coauthors

  • Albina Orlova

    University of Virginia

    93 shared
  • Xiong Yu

    Guiyang Medical University

    89 shared
  • Fengbin Wang

    University of Alabama at Birmingham

    67 shared
  • Vitold E. Galkin

    Eastern Virginia Medical School

    65 shared
  • Mart Krupovìč

    Institut Pasteur

    53 shared
  • Virginija Cvirkaitė‐Krupovič

    Institut Pasteur

    38 shared
  • Emil Reisler

    University of California, Los Angeles

    35 shared
  • Weili Zheng

    University of Virginia

    29 shared

Education

  • Postdoc

    MRC Laboratory of Molecular Biology

    1984
  • Ph.D.

    Brandeis University

    1982

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