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Showing 1–7 of 7 results
Advanced filters: Author: Salima Daou Clear advanced filters

  • Structures of an unusual enzymatic domain in PINK1 provide insights into how this protein regulates the function of organelles called mitochondria, and how mutations in PINK1 contribute to Parkinson’s disease.

    • Salima Daou
    • Frank Sicheri
    News & Views
    Nature
    Volume: 552, P: 38-39

  • Additional sex combs-like (ASXLs) stimulate BAP1 deubiquitinase activity to induce tumor suppression, but how these complexes work in coordination in vivo is unclear. Here, the authors show the mutually reinforcing roles of BAP1 and ASXLs such that BAP1 promotes DEUBAD monoubiquitination of ASXL2, which in turn stimulates BAP1 DUB activity.

    • Salima Daou
    • Haithem Barbour
    • El Bachir Affar
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-21

  • tRNA modifications are vital for their function in protein synthesis, one of the most central processes in all living cells. Here the authors show how KEOPS, a multi-subunit tRNA modifying complex, engages and acts on a substrate tRNA.

    • Samara Mishelle Ona Chuquimarca
    • Jonah Beenstock
    • Frank Sicheri
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-20

  • Upon starvation, cells coordinate protein disposal to recycle amino acids, although the role of the proteasome has been unclear. Here, the authors show that in the mammalian nucleus, proteasomes form condensates that dissolve following nutrient replenishment.

    • Maxime Uriarte
    • Nadine Sen Nkwe
    • El Bachir Affar
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-22

  • 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

  • Histone H2A monoubiquitination on lysine 119 in vertebrate and lysine 118 in Drosophila (H2Aub) is an epigenomic mark usually associated with gene repression by Polycomb group factors. Here the authors review the current knowledge on the deposition and removal of H2Aub, its function in transcription and other DNA-associated processes as well as its relevance to human disease.

    • Haithem Barbour
    • Salima Daou
    • El Bachir Affar
    ReviewsOpen Access
    Nature Communications
    Volume: 11, P: 1-16