Nature Chemical Biology - Engineered aminoacyl-tRNA synthetase (aaRS) mutants have been developed that facilitate ultrafast bioorthogonal noncanonical amino acid tagging (BONCAT) of newly...

N-glycosylation of secretory pathway proteins in the ER is crucial for their maturation and quality control. Recent insights into the enzymes and chaperones that facilitate N-glycosylation have expand...

The Alzheimer's Association calls on HHS Secretary Kennedy to stop dangerous fabrications about the state of Alzheimer’s and dementia research.

The development of targeted protein degradation by recruiting a protein of interest to a ubiquitin ligase to facilitate its degradation has become a powerful therapeutic tool. The potential of this approach is limited to proteins that can be readily ubiquitinated and relies on having a ligand with the various E3 ligases. Here, we describe a new methodology for targeted protein degradation that directly recruits a protein of interest to the proteasome for degradation. We generated bifunctional molecules that incorporate a small molecule ligand into a subunit on the 26S proteasome that recruits the protein directly for degradation. ByeTAC degradation requires binding to Rpn-13, a nonessential ubiquitin receptor of the 26S proteasome, and the protein of interest and does not have to rely on the E ligase cascade for ubiquitination. The ByeTAC methodology demonstrates the application of directly recruiting a protein to the proteasome via interactions with Rpn-13 for degradation.

Nature - A study describes the split integrated stress response, a cellular stress response mechanism characterized by reduced eIF2B activity without eIF2α phosphorylation, which activates the...

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