Author Correction: Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex

January 15th, 2020 by Dirksen E. Bussiere

Nature Chemical Biology, Published online: 15 January 2020; doi:10.1038/s41589-020-0471-7

Author Correction: Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex
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Publisher Correction: An efficient gene knock-in strategy using 5′-modified double-stranded DNA donors with short homology arms

January 15th, 2020 by Yi Yu

Nature Chemical Biology, Published online: 15 January 2020; doi:10.1038/s41589-020-0470-8

Publisher Correction: An efficient gene knock-in strategy using 5′-modified double-stranded DNA donors with short homology arms
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Molecular basis for fibroblast growth factor 23 <i>O</i>-glycosylation by GalNAc-T3

January 13th, 2020 by Matilde de las Rivas

Nature Chemical Biology, Published online: 13 January 2020; doi:10.1038/s41589-019-0444-x

Polypeptide GalNAc-transferase T3 catalyzes the specific glycosylation of threonine-178 of fibroblast growth factor 23, and structural insights reveal a unique lectin-based mechanism of substrate recognition.
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Reprogramming fatty acyl specificity of lipid kinases via C1 domain engineering

January 13th, 2020 by Timothy B. Ware

Nature Chemical Biology, Published online: 13 January 2020; doi:10.1038/s41589-019-0445-9

A chemoproteomics and protein engineering strategy to investigate metabolic activity of lipid kinases led to assignment of a key role for atypical C1 domains in directing fatty acyl specificity of diacylglycerol kinase function in live cells.
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A fungal family of lytic polysaccharide monooxygenase-like copper proteins

January 13th, 2020 by Aurore Labourel

Nature Chemical Biology, Published online: 13 January 2020; doi:10.1038/s41589-019-0438-8

The X325 protein family is highly similar to lytic polysaccharide monooxygenases (LPMOs) in regulation, structure and copper coordination by a histidine brace, yet lacks LPMO activity and suggests the evolution of an alternative function in fungi.
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Rewiring E2 enzymes

January 13th, 2020 by Koichi Sato

Nature Chemical Biology, Published online: 13 January 2020; doi:10.1038/s41589-019-0454-8

The site-specific monoubiquitination of FANCD2 is crucial for the Fanconi anemia DNA repair pathway and tumor suppression. This modification is mediated by the E2 enzyme UBE2T and the E3 ligase FANCL through a novel allosteric mechanism.

Lipid droplets can promote drug accumulation and activation

January 13th, 2020 by Ramin Dubey

Nature Chemical Biology, Published online: 13 January 2020; doi:10.1038/s41589-019-0447-7

Lasonolide A is hydrolyzed into a cytotoxic metabolite by a lipid droplet-associated orphan serine hydrolase, showing that lipid droplets can promote drug toxicity by both accumulating and metabolizing drugs in cells.

A lytic polysaccharide monooxygenase-like protein functions in fungal copper import and meningitis

January 13th, 2020 by Sarela Garcia-Santamarina

Nature Chemical Biology, Published online: 13 January 2020; doi:10.1038/s41589-019-0437-9

In the fungal pathogen Cryptococcus neoformans, Bim1 is a copper-binding lytic polysaccharide monooxygenase-like protein that participates in copper uptake in concert with the Ctr1 importer to drive virulence mechanisms during fungal meningitis.
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Chain alignment of collagen I deciphered using computationally designed heterotrimers

January 6th, 2020 by Abhishek A. Jalan

Nature Chemical Biology, Published online: 06 January 2020; doi:10.1038/s41589-019-0435-y

Designed heterotrimers of collagen I, locked in three possible chain registers, enable structural and functional characterization of each permutation, leading to identification of the AAB heterotrimer as the most active and therefore likely to occur biologically.
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A tunable orthogonal coiled-coil interaction toolbox for engineering mammalian cells

January 6th, 2020 by Tina Lebar

Nature Chemical Biology, Published online: 06 January 2020; doi:10.1038/s41589-019-0443-y

A set of orthogonal coiled-coil peptide heterodimers were developed to enable control of protein localization as well as transcriptional regulation by enhancing effector recruitment to TALE and CRISPR–dCas9 systems in mammalian cells and in vivo.
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