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Membrane Proteins

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  • MiLoPYP: self-supervised molecular pattern mining and particle localization in situ
    • MiLoPYP: self-supervised molecular pattern mining and particle localization in situ
    • MiLoPYP: self-supervised molecular pattern mining and particle localization in situ

    • Cryo-EM, Machine learning and artificial intelligence, Membrane Proteins, Publications, Ribosome
    •   MiLoPYP: self-supervised molecular pattern mining and particle localization in situ Cryo-electron tomography (CET) allows the routine visualization of cellular landscapes in three dimensions at nanometer-range resolutions. When combined with single-particle tomography (SPT), it is possible to obtain near-atomic resolution structures of frequently occurring macromolecules within their native environment. Two outstanding challenges associated with CET/SPT are the automatic identification and…
  • Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies
    • Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies
    • Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies

    • HIV, Membrane Proteins, Publications, Structures
    •   Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies Natural antibodies (Abs) can target host glycans on the surface of pathogens. We studied the evolution of glycan-reactive B cells of rhesus macaques and humans using glycosylated HIV-1 envelope (Env) as a model antigen. We describe HIV-1 Env Fab-dimerized glycan (FDG)-reactive neutralizing Abs in HIV-1 vaccinated and simian-HIV (SHIV)-infected…
  • Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs
    • Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs
    • Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs

    • Membrane Proteins, Publications, Structures
    •   Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation. eLife, 7:e37558, 2018.
  • Structure of rhodopsin bound to an inhibitory G protein
    • Structure of rhodopsin bound to an inhibitory G protein
    • Structure of rhodopsin bound to an inhibitory G protein

    • Membrane Proteins, Publications, Structures
    •   Cryo-EM structure of human rhodopsin bound to an inhibitory G protein For the first time, scientists have visualized the interaction between two critical components of the body’s vast cellular communication network, a discovery that could lead to more effective medications with fewer side effects for conditions ranging from migraine to cancer. The near-atomic resolution images obtained, show a G-protein coupled…
  • Cryo-EM Analysis of Human P-glycoprotein
    • Cryo-EM Analysis of Human P-glycoprotein
    • Cryo-EM Analysis of Human P-glycoprotein

    • Membrane Proteins, Publications, Structures
    •   Cryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle Molecular Pharmacology, 90(1):35-41, 2016.
  • Structures of Chimeric Hemagglutinin on Influenza Virus
    • Structures of Chimeric Hemagglutinin on Influenza Virus
    • Structures of Chimeric Hemagglutinin on Influenza Virus

    • Membrane Proteins, Publications, Structures
    •   Cryo-electron Microscopy Structures of Chimeric Hemagglutinin Displayed on a Universal Influenza Vaccine Candidate Chimeric hemagglutinin proteins are set to undergo human clinical trials as a universal influenza vaccine candidate, yet no structural information for these proteins is available. Using cryo-electron tomography, we report the first three-dimensional (3D) visualization of chimeric hemagglutinin proteins displayed on the surface of the influenza…
  • Structure of Magnesium Channel CorA
    • Structure of Magnesium Channel CorA
    • Structure of Magnesium Channel CorA

    • Membrane Proteins, Publications, Structures
    •   Cryo-EM Structures of the Magnesium Channel CorA Reveal Symmetry Break upon Gating Magnesium ions (Mg2+) play essential roles in all living organisms. Bacteria and other prokaryotes rely upon the Mg2+-dependent channel CorA, which is composed of five identical subunits (A-E), to obtain these ions from their surroundings. Studies of CorA showed that, in contrast to most ligand-gated ion channels,…
  • Structure of Ebola Glycoprotein Mucin-like Domain
    • Structure of Ebola Glycoprotein Mucin-like Domain
    • Structure of Ebola Glycoprotein Mucin-like Domain

    • Membrane Proteins, Structures
    •   Spatial Localization of the Ebola Glycoprotein Mucin-like Domain using Cryo-Electron Tomography J Virol, 88(18):10958-62, 2014.
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