Errata: Functional annotation of chemical libraries across diverse biological processes

November 21st, 2017 by Jeff S Piotrowski

Errata: Functional annotation of chemical libraries across diverse biological processes

Errata: Functional annotation of chemical libraries across diverse biological processes, Published online: 21 November 2017; doi:10.1038/nchembio1217-1286b

Errata: Functional annotation of chemical libraries across diverse biological processes
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Genetic code expansion: Synthetases pick up the PACE

November 21st, 2017 by Jeffery M Tharp

Genetic code expansion: Synthetases pick up the PACE

Genetic code expansion: Synthetases pick up the PACE, Published online: 21 November 2017; doi:10.1038/nchembio.2516

Phage-assisted evolution can rapidly improve the efficiency and substrate specificity of orthogonal aminoacyl-tRNA synthetases. Furthermore, the crystal structure of the pyrrolysyl-tRNA synthetase N-terminal domain reveals the basis for these improvements and provides a structural rationale for orthogonality.

Nucleic acids: mRNAs get a TREAT

November 21st, 2017 by Grant Miura

Nucleic acids: mRNAs get a TREAT

Nucleic acids: mRNAs get a TREAT, Published online: 21 November 2017; doi:10.1038/nchembio.2522

Nucleic acids: mRNAs get a TREAT

Cancer systems biology: Harnessing off-target effects

November 21st, 2017 by Gaye Saginc

Cancer systems biology: Harnessing off-target effects

Cancer systems biology: Harnessing off-target effects, Published online: 21 November 2017; doi:10.1038/nchembio.2519

The 'off-targets' of a drug are often poorly characterized yet could be harnessed in the treatment of complex diseases. A recent study used a small-molecule screening in non-small-cell lung cancer to repurpose an FDA-approved ALK/IGF1R inhibitor and uncover its mechanism of action.

Host–pathogen interactions: A ubiquitin defense

November 21st, 2017 by Mirella Bucci

Host–pathogen interactions: A ubiquitin defense

Host–pathogen interactions: A ubiquitin defense, Published online: 21 November 2017; doi:10.1038/nchembio.2524

Host–pathogen interactions: A ubiquitin defense

Enzymology: I want my cluster back

November 21st, 2017 by Caitlin Deane

Enzymology: I want my cluster back

Enzymology: I want my cluster back, Published online: 21 November 2017; doi:10.1038/nchembio.2525

Enzymology: I want my cluster back

Monobactam formation in sulfazecin by a nonribosomal peptide synthetase thioesterase

November 20th, 2017 by Ryan A Oliver

Monobactam formation in sulfazecin by a nonribosomal peptide synthetase thioesterase

Monobactam formation in sulfazecin by a nonribosomal peptide synthetase thioesterase, Published online: 20 November 2017; doi:10.1038/nchembio.2526

Biosynthesis of the antibiotic sulfazecin involves N-sulfonation in trans of the tripeptide intermediate before synthesis of the β-lactam ring by a noncanonical thioesterase domain, demonstrating a new enzymatic route to the azetidinone moiety.
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Engineering peptide ligase specificity by proteomic identification of ligation sites

November 20th, 2017 by Amy M Weeks

Engineering peptide ligase specificity by proteomic identification of ligation sites

Engineering peptide ligase specificity by proteomic identification of ligation sites, Published online: 20 November 2017; doi:10.1038/nchembio.2521

A comprehensive characterization of peptide ligase specificity using proteome-derived peptide libraries enables the identification of 72 new subtiligases and their application to site-specific bioconjugation and sequencing of the cellular N terminome.
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Small-molecule inhibition of TLR8 through stabilization of its resting state

November 20th, 2017 by Shuting Zhang

Small-molecule inhibition of TLR8 through stabilization of its resting state

Small-molecule inhibition of TLR8 through stabilization of its resting state, Published online: 20 November 2017; doi:10.1038/nchembio.2518

High-throughput screening identified potent small-molecule inhibitors of the endosomal Toll-like receptor TLR8 that stabilize the preformed TLR8 dimer in its resting state by binding to a unique site on the inactive dimer interface.
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Synthetic microbial consortia enable rapid assembly of pure translation machinery

November 13th, 2017 by Fernando Villarreal

Synthetic microbial consortia enable rapid assembly of pure translation machinery

Synthetic microbial consortia enable rapid assembly of pure translation machinery, Published online: 13 November 2017; doi:10.1038/nchembio.2514

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Strains of Escherichia coli, each expressing a subset of the 34 translation machinery proteins, are grown in synthetic microbial consortia to enable the efficient isolation of the full machinery from a single culturing, lysis, and purification procedure.

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