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Showing 1–12 of 12 results
Advanced filters: Author: Radoslav I. Enchev Clear advanced filters

  • Cullin-RING ligases are regulated by the COP9 signalosome (CSN) through deneddylation. Here, authors report high-resolution cryo-EM structures that capture catalytic and dissociation intermediates, identify CSNAP within the complex, and reveal a stepwise pathway for CSN disengagement.

    • Shan Ding
    • Julie A. Clapperton
    • Radoslav I. Enchev
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-15

  • The GroEL/ES chaperonin can act during protein synthesis to promote folding. Here, Roeselová et al. show how GroEL captures, remodels and sequesters nascent proteins in its central chamber, while they remain tethered to the ribosome.

    • Alžběta Roeselová
    • Sarah L. Maslen
    • David Balchin
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • There is a growing interest in performing time-resolved cryo-EM studies. Here, the authors present a time-resolved sample preparation method for cryo-EM called trEM, which uses a microfluidic device to initiate the biochemical reaction by rapid mixing of the components and then spraying the sample onto a cryo-EM grid to snap-freeze it in a blot-free, automated manner within several milliseconds.

    • Märt-Erik Mäeots
    • Byungjin Lee
    • Radoslav I. Enchev
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • Post-translational modification of proteins by NEDD8 has been mainly characterized in terms of the cullin–RING E3 ligase family. However, recent studies have indicated that there might be non-cullin neddylation targets that require further verification.

    • Radoslav I. Enchev
    • Brenda A. Schulman
    • Matthias Peter
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 16, P: 30-44

  • CtIP has a key role in DNA double-strand break repair as its role in resecting DNA at the break commits a cell to homologous recombination. Here the authors show that KLHL15 interacts with CtIP and regulates repair by controlling protein turnover.

    • Lorenza P. Ferretti
    • Sarah-Felicitas Himmels
    • Alessandro A. Sartori
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-16

  • The APC/C is a large multiprotein complex that functions as an E3 ubiquitin ligase to regulate the cell cycle. Here, the entire APC/C complex is reconstituted, and in combination with structural studies a pseudo-atomic model for 70% of the complex is provided. These results contribute towards a molecular understanding of the roles of individual subunits in APC/C assembly and their interactions with co-activators, substrates and regulatory proteins.

    • Anne Schreiber
    • Florian Stengel
    • David Barford
    Research
    Nature
    Volume: 470, P: 227-232

  • It has previously been established that DNA end resection in yeast and in humans is under CDK control. Here the authors explain how phosphorylation regulates the capacity of Sae2 — the yeast orthologue of human CtIP — to promote DNA end resection.

    • Elda Cannavo
    • Dominic Johnson
    • Petr Cejka
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-14

  • Although focal adhesions (FAs) and microtubules (MTs) are known to associate, the underlying regulation of this dynamic interaction is not understood. Here the authors discover that the CRL3KLHL21E3 ubiquitin ligase localises to FAs and ubiquitinates the MT plus-tip binding protein EB1, thereby promoting MT and FA dynamics and cell migration.

    • Thibault Courtheoux
    • Radoslav I. Enchev
    • Matthias Peter
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-13

  • Different mutations found in endometrial and prostate tumors affecting the substrate-recognition domain of SPOP, a component of the E3 ubiquitin ligase complex, result in opposing degradation activity of BET proteins and response to BET inhibitors. This work, along with findings by Zhang et al. and Dai et al., highlights the divergent effects of recurrent mutations affecting different residues within the same functional domain of SPOP and provides scientific rationale to guide the administration of BET inhibitors in endometrial and prostate cancer patients harboring SPOP mutations.

    • Hana Janouskova
    • Geniver El Tekle
    • Jean-Philippe P Theurillat
    Research
    Nature Medicine
    Volume: 23, P: 1046-1054