Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–6 of 6 results
Advanced filters: Author: Connor Arkinson Clear advanced filters

  • Here, Arkinson et al. reconstitute NUB1-mediated FAT10 degradation by the human 26S proteasome and use biochemistry, cryo-EM and hydrogen–deuterium exchange to show that NUB1 acts as an ATP-independent chaperone to trap partially folded FAT10 for proteasome delivery.

    • Connor Arkinson
    • Ken C. Dong
    • Andreas Martin
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1752-1765

  • The authors use time-resolved cryo-electron microscopy to reveal the interactions of the redox-active cofactor TXNL1 with the human 26S proteasome and detect ATPase motor states that indicate burst-like mechanisms for hand-over-hand substrate translocation.

    • Connor Arkinson
    • Christine L. Gee
    • Andreas Martin
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 2403-2415

  • Structures of USP1−UAF complexes, including a cryo-EM structure of USP−UAF1 bound to its substrate FANCI−FANCD2, reveal molecular details of USP1−UAF1 regulation and substrate recognition.

    • Martin L. Rennie
    • Connor Arkinson
    • Helen Walden
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 356-364

  • Using Xenopus egg extracts, the authors developed a mass spectrometry method (UBIMAX) to identify proteins ubiquitylated in response to defined DNA lesions. Highlighting UBIMAX’s versatility, they describe the ubiquitylation of the actin regulator Dbn1 in response to DNA double-strand breaks.

    • Camilla S. Colding-Christensen
    • Ellen S. Kakulidis
    • Michael L. Nielsen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • UBE2T adopts an allosteric activation mechanism to mediate site-specific ubiquitination of Fanconi anemia complex. Interaction with FANCL induces a cascade of conformational changes of UBE2T and leads to exposure of substrate-binding sites.

    • Viduth K. Chaugule
    • Connor Arkinson
    • Helen Walden
    Research
    Nature Chemical Biology
    Volume: 16, P: 291-301

  • Most proteins are degraded and regulated by the 26S proteasome. A balance of specificity and promiscuity underlies substrate recognition and ATP-dependent degradation, which can occur in a ubiquitin-dependent or ubiquitin-independent manner. Recent insights into the mechanisms and regulation of substrate delivery, processing and degradation will inform new strategies for the treatment of human diseases.

    • Connor Arkinson
    • Ken C. Dong
    • Andreas Martin
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 26, P: 104-122