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Showing 1–8 of 8 results
Advanced filters: Author: Igor Kurinov Clear advanced filters

  • RING E3 ligases mediate transfer of ubiquitin-like proteins from an E2 ligase to a substrate, but how this occurs is a long-standing mystery. Docking E2-RING structures onto a new crystal structure of the C-terminal domain of the E3-RING CUL1 in complex with the RBX1 RING protein now shows how a conformational change in RBX1 allows for the transfer by closing a gap between CUL1 and the E2.

    • Matthew F Calabrese
    • Daniel C Scott
    • Brenda A Schulman
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 947-949

  • The anaphase promoting complex (APC) is a key cell-cycle regulator that has ubiquitin-ligase activity. The first structure of a complex formed between APC subunits, that of CDC26 and APC6, provides detailed structural information of APC components and suggests how CDC26 may stabilize APC6 and other complex subunits.

    • Jing Wang
    • Billy T Dye
    • Brenda A Schulman
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 987-989

  • Using biochemistry, cell biological, X-ray crystallography and cryo-EM methods, Maisonneuve et al. reveal how the scaffolding proteins CNK and HYP enhance the binding of KSR to MEK, which in turn allosterically controls RAF activation in Drosophila.

    • Pierre Maisonneuve
    • Malha Sahmi
    • Marc Therrien
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 1028-1038

  • A PROTAC termed P4B targeting BRAF V600E mutant has been developed, which displays enhanced inhibitory function in cell lines carrying BRAF mutations that impart resistance to conventional BRAF inhibitors.

    • Ganna Posternak
    • Xiaojing Tang
    • Frank Sicheri
    Research
    Nature Chemical Biology
    Volume: 16, P: 1170-1178

  • Modulation of the unfolded protein response by targeting IRE1 has several potential therapeutic applications. Here, the authors provide a first structural view of inhibitors engaging the RNase-active site of IRE1 that suggests avenues towards the generation of analogues with increased potency and selectivity.

    • Mario Sanches
    • Nicole M. Duffy
    • Frank Sicheri
    Research
    Nature Communications
    Volume: 5, P: 1-16

  • An early step in the autophagy process is the conjugation of the ubiquitin-like proteins (UBLs) Atg8 and Atg12 to their targets. Structural and functional experiments reveal how the autophagy E1 Atg7 uses a trans mechanism to catalyze the charging of the autophagy UBLs onto their respective carrier E2 proteins, Atg3 and Atg10.

    • Stephen E Kaiser
    • Kai Mao
    • Brenda A Schulman
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 1242-1249

  • KSR–MEK complexes allosterically activate BRAF through the action of N-terminal regulatory region and kinase domain contacts, thus challenging the accepted role of KSR as a scaffold for MEK recruitment to RAF.

    • Hugo Lavoie
    • Malha Sahmi
    • Marc Therrien
    Research
    Nature
    Volume: 554, P: 549-553