Methods: A small-molecule SMASh hit

August 18th, 2015 by Jeffrey Hannah

Nature Chemical Biology 11, 637 (2015). doi:10.1038/nchembio.1886

Authors: Jeffrey Hannah & Pengbo Zhou

There are many techniques that can be employed to control gene expression at the post-translational level. However, a novel system called SMASh (small molecule–assisted shutoff), which allows for chemically-induced degradation of target proteins, presents some distinct advantages.

Proteostasis: Death by cytoplasmic accumulation

August 18th, 2015 by Mirella Bucci

Nature Chemical Biology 11, 633 (2015). doi:10.1038/nchembio.1903

Author: Mirella Bucci

Minimum Information about a Biosynthetic Gene cluster

August 18th, 2015 by Marnix H Medema

Nature Chemical Biology 11, 625 (2015). doi:10.1038/nchembio.1890

Authors: Marnix H Medema, Renzo Kottmann, Pelin Yilmaz, Matthew Cummings, John B Biggins, Kai Blin, Irene de Bruijn, Yit Heng Chooi, Jan Claesen, R Cameron Coates, Pablo Cruz-Morales, Srikanth Duddela, Stephanie Düsterhus, Daniel J Edwards, David P Fewer, Neha Garg, Christoph Geiger, Juan Pablo Gomez-Escribano, Anja Greule, Michalis Hadjithomas, Anthony S Haines, Eric J N Helfrich, Matthew L Hillwig, Keishi Ishida, Adam C Jones, Carla S Jones, Katrin Jungmann, Carsten Kegler, Hyun Uk Kim, Peter Kötter, Daniel Krug, Joleen Masschelein, Alexey V Melnik, Simone M Mantovani, Emily A Monroe, Marcus Moore, Nathan Moss, Hans-Wilhelm Nützmann, Guohui Pan, Amrita Pati, Daniel Petras, F Jerry Reen, Federico Rosconi, Zhe Rui, Zhenhua Tian, Nicholas J Tobias, Yuta Tsunematsu, Philipp Wiemann, Elizabeth Wyckoff, Xiaohui Yan, Grace Yim, Fengan Yu, Yunchang Xie, Bertrand Aigle, Alexander K Apel, Carl J Balibar, Emily P Balskus, Francisco Barona-Gómez, Andreas Bechthold, Helge B Bode, Rainer Borriss, Sean F Brady, Axel A Brakhage, Patrick Caffrey, Yi-Qiang Cheng, Jon Clardy, Russell J Cox, René De Mot, Stefano Donadio, Mohamed S Donia, Wilfred A van der Donk, Pieter C Dorrestein, Sean Doyle, Arnold J M Driessen, Monika Ehling-Schulz, Karl-Dieter Entian, Michael A Fischbach, Lena Gerwick, William H Gerwick, Harald Gross, Bertolt Gust, Christian Hertweck, Monica Höfte, Susan E Jensen, Jianhua Ju, Leonard Katz, Leonard Kaysser, Jonathan L Klassen, Nancy P Keller, Jan Kormanec, Oscar P Kuipers, Tomohisa Kuzuyama, Nikos C Kyrpides, Hyung-Jin Kwon, Sylvie Lautru, Rob Lavigne, Chia Y Lee, Bai Linquan, Xinyu Liu, Wen Liu, Andriy Luzhetskyy, Taifo Mahmud, Yvonne Mast, Carmen Méndez, Mikko Metsä-Ketelä, Jason Micklefield, Douglas A Mitchell, Bradley S Moore, Leonilde M Moreira, Rolf Müller, Brett A Neilan, Markus Nett, Jens Nielsen, Fergal O'Gara, Hideaki Oikawa, Anne Osbourn, Marcia S Osburne, Bohdan Ostash, Shelley M Payne, Jean-Luc Pernodet, Miroslav Petricek, Jörn Piel, Olivier Ploux, Jos M Raaijmakers, José A Salas, Esther K Schmitt, Barry Scott, Ryan F Seipke, Ben Shen, David H Sherman, Kaarina Sivonen, Michael J Smanski, Margherita Sosio, Evi Stegmann, Roderich D Süssmuth, Kapil Tahlan, Christopher M Thomas, Yi Tang, Andrew W Truman, Muriel Viaud, Jonathan D Walton, Christopher T Walsh, Tilmann Weber, Gilles P van Wezel, Barrie Wilkinson, Joanne M Willey, Wolfgang Wohlleben, Gerard D Wright, Nadine Ziemert, Changsheng Zhang, Sergey B Zotchev, Rainer Breitling, Eriko Takano & Frank Oliver Glöckner

A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters. Information about these clusters, pathways and metabolites is currently dispersed throughout the literature, making it difficult to exploit. To facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters, we propose the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard.

Looking for logic

August 18th, 2015 by Nature Chemical Biology - Issue - nature.com science feeds

Nature Chemical Biology 11, 619 (2015). doi:10.1038/nchembio.1905

Improved tools and expanding knowledge are enabling new insights into the biochemical basis, ecological roles and promising applications of natural product biosynthesis.

Protein degradation: Prime time for PROTACs

August 18th, 2015 by Raymond J Deshaies

Nature Chemical Biology 11, 634 (2015). doi:10.1038/nchembio.1887

Author: Raymond J Deshaies

PROTACs are heterobifunctional small molecules that simultaneously bind a target protein and a ubiquitin ligase, enabling ubiquitination and degradation of the target. Major progress in developing potent and specific PROTACs has recently been reported, invigorating prospects for novel PROTAC-based therapies.

The structural biology of biosynthetic megaenzymes

August 18th, 2015 by Kira J Weissman

Nature Chemical Biology 11, 660 (2015). doi:10.1038/nchembio.1883

Author: Kira J Weissman

Cancer metabolism: Two sides of a coin

August 18th, 2015 by Grant Miura

Nature Chemical Biology 11, 632 (2015). doi:10.1038/nchembio.1899

Author: Grant Miura

LAPTM4B facilitates late endosomal ceramide export to control cell death pathways

August 17th, 2015 by Tomas Blom

Nature Chemical Biology 11, 799 (2015). doi:10.1038/nchembio.1889

Authors: Tomas Blom, Shiqian Li, Andrea Dichlberger, Nils Bäck, Young Ah Kim, Ursula Loizides-Mangold, Howard Riezman, Robert Bittman & Elina Ikonen

  • Posted in Nat Chem Biol, Publications
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A fungal monooxygenase-derived jasmonate attenuates host innate immunity

August 10th, 2015 by Rajesh N Patkar

Nature Chemical Biology 11, 733 (2015). doi:10.1038/nchembio.1885

Authors: Rajesh N Patkar, Peter I Benke, Ziwei Qu, Yuan Yi Constance Chen, Fan Yang, Sanjay Swarup & Naweed I Naqvi

  • Posted in Nat Chem Biol, Publications
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An excess of catalytically required motions inhibits the scavenger decapping enzyme

August 10th, 2015 by Ancilla Neu

Nature Chemical Biology 11, 697 (2015). doi:10.1038/nchembio.1866

Authors: Ancilla Neu, Ursula Neu, Anna-Lisa Fuchs, Benjamin Schlager & Remco Sprangers

  • Posted in Nat Chem Biol, Publications
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