Motor proteins: Kinesin’s gait captured

February 29th, 2016 by Erwin J G Peterman

Nature Chemical Biology 12, 206 (2016). doi:10.1038/nchembio.2038

Author: Erwin J G Peterman

Kinesin is a motor protein that drives intracellular transport by stepping along microtubules in a hand-over-hand manner. Advanced dark-field microscopy has made it possible to capture the gait of this motor with unprecedented resolution.

Direct observation of intermediate states during the stepping motion of kinesin-1

February 29th, 2016 by Hiroshi Isojima

Nature Chemical Biology 12, 290 (2016). doi:10.1038/nchembio.2028

Authors: Hiroshi Isojima, Ryota Iino, Yamato Niitani, Hiroyuki Noji & Michio Tomishige

  • Posted in Nat Chem Biol, Publications
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The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases

February 29th, 2016 by Kristian E H Frandsen

Nature Chemical Biology 12, 298 (2016). doi:10.1038/nchembio.2029

Authors: Kristian E H Frandsen, Thomas J Simmons, Paul Dupree, Jens-Christian N Poulsen, Glyn R Hemsworth, Luisa Ciano, Esther M Johnston, Morten Tovborg, Katja S Johansen, Pernille von Freiesleben, Laurence Marmuse, Sébastien Fort, Sylvain Cottaz, Hugues Driguez, Bernard Henrissat, Nicolas Lenfant, Floriana Tuna, Amgalanbaatar Baldansuren, Gideon J Davies, Leila Lo Leggio & Paul H Walton

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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 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.