HUWE1 employs a giant substrate-binding ring to feed and regulate its HECT E3 domain

Nature Chemical Biology, Published online: 22 July 2021; doi:10.1038/s41589-021-00831-5The full-length structure of HUWE1 reveals the bipartite organization of a giant E3 ubiquitin ligase, comprising a catalytic HECT domain and a large, ring-shaped scaffold that provides docking sites for various substrates and regulates E3 activity.

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HUWE1 employs a giant substrate-binding ring to feed and regulate its HECT E3 domain

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Imaging and targeting LOX-mediated tissue remodeling with a reactive collagen peptide

Nature Chemical Biology, Published online: 12 July 2021; doi:10.1038/s41589-021-00830-6Collagen cross-linking, mediated by lysyl oxidases (LOX), is critical for the stability of the extracellular matrix. Aldehyde-reactive sensors and collagen peptide probes for monitoring LOX activity enable direct in vivo imaging of collagen maturation.

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Mechanical strength of RNA knot in Zika virus protects against cellular defenses

Nature Chemical Biology, Published online: 12 July 2021; doi:10.1038/s41589-021-00829-zA knot-like RNA from Zika virus is shown to evade digestion by host RNases through its extreme resistance to mechanical unfolding. Weakening the knot mechanically or reducing the likelihood of knot formation lowers the RNase resistance.

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Imaging and targeting LOX-mediated tissue remodeling with a reactive collagen peptide

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Mechanical strength of RNA knot in Zika virus protects against cellular defenses

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Linking K29-Ub chains to biology

Nature Chemical Biology, Published online: 08 July 2021; doi:10.1038/s41589-021-00833-3Different ubiquitin chain types serve as distinct cellular signals. A new synthetic antigen-binding fragment, sAB-K29, specifically recognizes K29-linked diubiquitin and links K29 chains to proteotoxic stress and their accumulation in midbodies during mitosis.

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K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle

Nature Chemical Biology, Published online: 08 July 2021; doi:10.1038/s41589-021-00823-5A linkage-specific tool for K29-linked polyubiquitin was developed, enabling the discovery that K29-linked ubiquitination participates in multiple cellular pathways, including the proteotoxic stress response and cell cycle regulation.

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Linking K29-Ub chains to biology

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K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle

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