Proteases articles within Nature

Featured

  • Article |

    The cryo-electron microscopy structure of human γ-secretase in complex with its substrate Notch reveals pronounced structural rearrangements compared to the apo enzyme, including formation of a β-sheet involving residues from both enzyme and substrate.

    • Guanghui Yang
    • , Rui Zhou
    •  & Yigong Shi

  • Article |

    Cryo-electron microscopy structures and dynamics of a substrate-engaged human 26S proteasome reveal in atomic detail three principal modes of coordinated ATP hydrolysis that regulate different steps in the degradation of a ubiquitylated protein.

    • Yuanchen Dong
    • , Shuwen Zhang
    •  & Youdong Mao

  • Article |

    Chemical optimization of arylomycins results in an inhibitor of bacterial type I signal peptidase that shows activity both against multidrug-resistant clinical isolates of Gram-negative bacteria in vitro and in several in vivo infection models.

    • Peter A. Smith
    • , Michael F. T. Koehler
    •  & Christopher E. Heise

  • Letter |

    OTULIN, which removes ubiquitin chains deposited by LUBAC, promotes LUBAC activity by preventing its auto-ubiquitination, thereby supporting normal mouse embryo development and preventing pro-inflammatory cell death in adult mice.

    • Klaus Heger
    • , Katherine E. Wickliffe
    •  & Vishva M. Dixit

  • Letter |

    The proteasome-associated enzyme USP14 regulates protein degradation by removing ubiquitin from proteins; here it is shown that USP14 removes ubiquitin chains from in vitro generated cyclin B conjugates en bloc and within milliseconds, before the proteasome has a chance to initiate degradation, and proceeds until a single chain remains.

    • Byung-Hoon Lee
    • , Ying Lu
    •  & Daniel Finley

  • Letter |

    The crystal structures of the protease domain of separase are reported, showing how separase recognizes cohesin, and how phosphorylation of the cleavage site enhances separase activity.

    • Zhonghui Lin
    • , Xuelian Luo
    •  & Hongtao Yu

  • Article |

    The atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.

    • Xiao-chen Bai
    • , Chuangye Yan
    •  & Yigong Shi

  • Article |

    The three-dimensional structure of intact human γ-secretase complex at 4.5 Å resolution is revealed by cryo-electron-microscopy single-particle analysis; the complex comprises a horseshoe-shaped transmembrane domain containing 19 transmembrane segments, and a large extracellular domain from nicastrin, which sits immediately above the hollow space formed by the horseshoe.

    • Peilong Lu
    • , Xiao-chen Bai
    •  & Yigong Shi

  • Article |

    Presenilin, the catalytic component of γ-secretase, cleaves amyloid precursor protein into short peptides that form the plaques that are found in the brains of patients with Alzheimer’s disease; here the structure of a presenilin homologue is described, which will serve as a framework for understanding the mechanisms of action of presenilin and γ-secretase.

    • Xiaochun Li
    • , Shangyu Dang
    •  & Yigong Shi

  • News & Views |

    The protein OTUB1 inhibits DNA repair without using its enzymatic activity. Instead, it sequesters a protein that is required for the assembly of certain forms of ubiquitin chain, which function as key signals during repair.

    • April Rose
    •  & Christian Schlieker

  • Article |

    To survive and evade host responses, malaria parasites export several hundred proteins into the host cell on infection. A feature of these proteins is a conserved, pentameric motif that is cleaved by an unknown protease before export. This is one of two independent studies revealing the identity of the protease as plasmepsin V, an aspartic acid protease located in the endoplasmic reticulum. This enzyme is essential for parasite viability and is an attractive candidate for drug development.

    • Ilaria Russo
    • , Shalon Babbitt
    •  & Daniel E. Goldberg

  • Article |

    To survive and evade host responses, malaria parasites export several hundred proteins into the host cell on infection. A feature of these proteins is a conserved, pentameric motif that is cleaved by an unknown protease before export. This is one of two independent studies revealing the identity of the protease as plasmepsin V, an aspartic acid protease located in the endoplasmic reticulum. This enzyme is essential for parasite viability and is an attractive candidate for drug development.

    • Justin A. Boddey
    • , Anthony N. Hodder
    •  & Alan F. Cowman

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