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Showing 1–13 of 13 results
Advanced filters: Author: Shira Albeck Clear advanced filters

  • Polymerization-inducing chimeras are a novel bifunctional modality that uses protein symmetry to sequester targets by forming insoluble supramolecular assemblies. This approach overcomes reliance on accessory proteins and differs functionally from conventional inhibitors.

    • Ella Livnah
    • Ohad Suss
    • Nir London
    ResearchOpen Access
    Nature Chemical Biology
    P: 1-11

  • Enzymes are viscoelastic, deformable machines. Mutating high-strain regions in these machines affect their catalytic function.

    • Eyal Weinreb
    • John M. McBride
    • Tsvi Tlusty
    Research
    Nature Physics
    Volume: 21, P: 787-798

  • The molecular basis of ultrahigh specificity in protein-protein interactions remains obscure. The authors present a computational method to design atomically accurate new pairs exhibiting >100,000-fold specificity switches, generating a large and complex interaction network.

    • Ravit Netzer
    • Dina Listov
    • Sarel J. Fleishman
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13

  • Vinculin binding to talin is a key event in focal adhesion dynamics; yet, how vinculin is activated to recruit actin remains unknown. Here, the authors use a multiscale approach to reveal that talin activates vinculin through an intricate allosteric mechanism tightly regulated by force.

    • Florian Franz
    • Rafael Tapia-Rojo
    • Frauke Gräter
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-16

  • A computational protein design was used to generate eight enzymes that were able to catalyse the Kemp elimination, a model reaction for proton transfer from carbon. Directed evolution was used to enhance the catalytic activity of the designed enzymes, demonstrating that the combination of computational protein design and directed evolution is a highly effective strategy to create novel enzymes.

    • Daniela Röthlisberger
    • Olga Khersonsky
    • David Baker
    Research
    Nature
    Volume: 453, P: 190-195

  • Computationally designed enzymes often show lower activity or stability than their natural counterparts. Here, the authors present an evolution-inspired method for automated enzyme design, creating stable enzymes with accurate active site architectures and wild-type-like activities.

    • Gideon Lapidoth
    • Olga Khersonsky
    • Sarel J. Fleishman
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-9

  • The type-I fatty acid synthase (FAS-I) complex is essential for Mycobacterium tuberculosis (Mtb) and mediates the production of C26 fatty acids that are precursors for the synthesis of mycolic acids. Here the authors present the 3.3 Å resolution cryo-EM structure of Mtb FAS-I, which is of interest for tuberculosis drug development.

    • Nadav Elad
    • Szilvia Baron
    • Ron Diskin
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-6

  • Colicins are secreted bacterial toxins. To avoid killing the producer organism, each colicin is coexpressed with a high-affinity inhibitor, or immunity protein (Im). The evolution of Im-Colicin interfaces and the evolvability traits of protein-protein interactions are now examined using in vitro evolution and structural analyses.

    • Kalia Bernath Levin
    • Orly Dym
    • Dan S Tawfik
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 1049-1055

  • Some phages—viruses that infect bacteria—encode peptides that are secreted from infected cells and that, beyond a certain threshold, stimulate other viruses to switch from the lytic (killing the host cell) to lysogenic (dormant) phase.

    • Zohar Erez
    • Ida Steinberger-Levy
    • Rotem Sorek
    Research
    Nature
    Volume: 541, P: 488-493