Host-pathogen interactions: A cholera surveillance system

February 22nd, 2016 by Aaron T Wright

Nature Chemical Biology 12, 203 (2016). doi:10.1038/nchembio.2039

Author: Aaron T Wright

Bacterial pathogen–secreted proteases may have a key role in inhibiting a potentially widespread host-pathogen interaction. Activity-based protein profiling enabled the identification of a major Vibrio cholerae serine protease that limits the ability of a host-derived intestinal lectin to bind to the bacterial pathogen in vivo.

Chemoproteomic profiling of host and pathogen enzymes active in cholera

February 22nd, 2016 by Stavroula K Hatzios

Nature Chemical Biology 12, 268 (2016). doi:10.1038/nchembio.2025

Authors: Stavroula K Hatzios, Sören Abel, Julianne Martell, Troy Hubbard, Jumpei Sasabe, Diana Munera, Lars Clark, Daniel A Bachovchin, Firdausi Qadri, Edward T Ryan, Brigid M Davis, Eranthie Weerapana & Matthew K Waldor

  • Posted in Nat Chem Biol, Publications
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Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway

February 22nd, 2016 by PuiYee Chan

Nature Chemical Biology 12, 282 (2016). doi:10.1038/nchembio.2036

Authors: PuiYee Chan, Xiao Han, Baohui Zheng, Michael DeRan, Jianzhong Yu, Gopala K Jarugumilli, Hua Deng, Duojia Pan, Xuelian Luo & Xu Wu

  • Posted in Nat Chem Biol, Publications
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Pooled screening for antiproliferative inhibitors of protein-protein interactions

February 22nd, 2016 by Satra Nim

Nature Chemical Biology 12, 275 (2016). doi:10.1038/nchembio.2026

Authors: Satra Nim, Jouhyun Jeon, Carles Corbi-Verge, Moon-Hyeong Seo, Ylva Ivarsson, Jason Moffat, Nadya Tarasova & Philip M Kim

  • Posted in Nat Chem Biol, Publications
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RNA conformation: Lightening up invisible states

February 16th, 2016 by Yun-Xing Wang

Nature Chemical Biology 12, 126 (2016). doi:10.1038/nchembio.2030

Author: Yun-Xing Wang

The versatility of RNA is achieved in part through its ability to adopt various shapes of structures. A new technology called X-ray scattering interferometry enables the detection of 'invisible' states by lighting up gold pairs tagged to RNA molecules.

Development and application of bond cleavage reactions in bioorthogonal chemistry

February 16th, 2016 by Jie Li

Nature Chemical Biology 12, 129 (2016). doi:10.1038/nchembio.2024

Authors: Jie Li & Peng R Chen

  • Posted in Nat Chem Biol, Publications
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Optogenetics: Follow the PIF

February 16th, 2016 by Grant Miura

Nature Chemical Biology 12, 125 (2016). doi:10.1038/nchembio.2031

Author: Grant Miura

RNA modification: Translating for growth

February 16th, 2016 by Grant Miura

Nature Chemical Biology 12, 125 (2016). doi:10.1038/nchembio.2034

Author: Grant Miura

Target identification: Getting cholesterol out

February 16th, 2016 by Mirella Bucci

Nature Chemical Biology 12, 125 (2016). doi:10.1038/nchembio.2032

Author: Mirella Bucci

Translation: Ribosomes make sweeping arrests

February 16th, 2016 by Diego A Alonzo

Nature Chemical Biology 12, 127 (2016). doi:10.1038/nchembio.2027

Authors: Diego A Alonzo & T Martin Schmeing

The arrest peptides that function with the macrolide antibiotic erythromycin stall translating ribosomes in the presence of the antibiotic, leading to remodeling of the downstream mRNA and enhancement of the translation of resistance genes. Current work suggests that small changes in the nascent peptide dictate the ability of ribosomes to respond to this and other small molecules.