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Volume 5 Issue 1, January 2009

Proteasomal substrate selection. Prakash et al. (p 29) mixed and matched a ubiquitin tag and an unstructured region, two signals for proteasomal targeting, on the protein complex components barnase and barstar. Attaching ubiquitin to barstar and an unstructured region to barnase resulted in degradation of barnase through an in trans targeting mechanism (see also News and Views by Wandless on p 3). Barstar modified with four ubiquitin domains is shown targeting the unstructured region of barnase to the proteasome. Cover art by Erin Boyle based on images provided by Sumit Prakash and Tomonao Inobe.

Volume 5 Issue 1

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Editorial

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Elements

  • A taste of the research at the Monell Center reveals an increased understanding of how we perceive and integrate chemical cues.

    • Catherine Goodman
    Elements
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News & Views

  • Protein ubiquitination is an important degradative signal, yet not all ubiquitinated proteins are degraded. Recent results reveal insights into the proteasome's strategy for integrating biophysical signals when choosing substrates for degradation.

    • Thomas J Wandless
    News & Views

  • Peptidases are enzymes that trim small protein fragments called peptides to regulate their biological functions. A new method opens the door to chasing down and identifying important cutting events mediated by peptidases involved in metabolic regulation.

    • Matthew Bogyo
    News & Views

  • Cytochrome P450 enzymes selectively oxidize relatively unactivated sites in a range of model drug-like substrates in vitro. The hydroxylated products can be transformed into selectively fluorinated systems, providing a rapid sequential method for the identification, activation and fluorination of saturated sites in drug candidates.

    • Graham Sandford
    News & Views

  • Development of an inhibitor of an endocannabinoid-degrading enzyme provides insights into the role of 2-arachidonoylglycerol in the nervous system.

    • Lawrence J Marnett
    News & Views

  • A powerful technology called global protein stability profiling allows rates of protein turnover to be determined for a substantial fraction of the human proteome in a single experiment. This approach sets the stage for systems-level analyses of the dynamics of the mammalian proteome.

    • Xiaolu L Ang
    • J Wade Harper
    News & Views
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