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

Yield Improvement of the Anti-MRSA Antibiotics WAP-8294A by CRISPR/dCas9 Combined with Refactoring Self-Protection Genes in Lysobacter enzymogenes OH11

November 20th, 2017 by Lingjun Yu, Wei Su, Paul D. Fey, Fengquan Liu and Liangcheng Du

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ACS Synthetic Biology
DOI: 10.1021/acssynbio.7b00293
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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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Repair of a Site-Specific DNA Cleavage: Old-School Lessons for Cas9-Mediated Gene Editing

November 14th, 2017 by Danielle N. Gallagher and James E. Haber

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ACS Chemical Biology
DOI: 10.1021/acschembio.7b00760

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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Nonimmune cells equipped with T-cell-receptor-like signaling for cancer cell ablation

November 13th, 2017 by Ryosuke Kojima

Nonimmune cells equipped with T-cell-receptor-like signaling for cancer cell ablation

Nonimmune cells equipped with T-cell-receptor-like signaling for cancer cell ablation, Published online: 13 November 2017; doi:10.1038/nchembio.2498

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Engineering of nonimmune cells with a cell-contact sensor and antigen recognition domains enables cell-contact-dependent sensor cell signaling and effector molecule production directed to attack target cells, providing an alternative strategy to chimeric antigen receptor T-cell (CAR-T) technology.

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Top-down characterization of endogenous protein complexes with native proteomics

November 13th, 2017 by Owen S Skinner

Top-down characterization of endogenous protein complexes with native proteomics

Top-down characterization of endogenous protein complexes with native proteomics, Published online: 13 November 2017; doi:10.1038/nchembio.2515

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A multistage tandem mass spectrometry approach enables the application of native proteomics to characterize intact endogenous protein complexes in discovery mode, including covalent modifications as well as noncovalently bound cofactors and ligands.

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