Searching for harmony in transition-metal signaling

September 17th, 2015 by Christopher J Chang

Nature Chemical Biology 11, 744 (2015). doi:10.1038/nchembio.1913

Author: Christopher J Chang

The recent emergence of signaling roles for transition metals presages a broader contribution of these elements beyond their traditional functions as metabolic cofactors. New chemical approaches to identify the sources, targets and physiologies of transition-metal signaling can help expand understanding of the periodic table in a biological context.

Metabolism: Jump-starting CoA biosynthesis

September 17th, 2015 by Marianne de Villiers

Nature Chemical Biology 11, 757 (2015). doi:10.1038/nchembio.1912

Authors: Marianne de Villiers & Erick Strauss

The essential metabolic cofactor coenzyme A was believed to be produced by biosynthesis from pantothenate in all eukaryotic cells. Rescue experiments in systems depleted of CoA have shown that a phosphorylated CoA biosynthetic intermediate can pass through eukaryotic membranes to serve as an alternative source.

Small-molecule inhibitors: bULKing up mTOR inhibition

September 17th, 2015 by Jonathan M Goodwin

Nature Chemical Biology 11, 758 (2015). doi:10.1038/nchembio.1909

Authors: Jonathan M Goodwin & Leon O Murphy

A new small-molecule inhibitor of the autophagy-initiating kinase ULK1 serves to block a critical survival mechanism activated upon inhibition of mTORC1, potentially enhancing treatment efficacy for mTOR inhibitors currently in clinical trials for cancer treatment.

Host-directed drug therapy for tuberculosis

September 17th, 2015 by Reto Guler

Nature Chemical Biology 11, 748 (2015). doi:10.1038/nchembio.1917

Authors: Reto Guler & Frank Brombacher

Chemical compounds designed to enhance understanding of host-pathogen interaction together with next-generation 'smart drugs' will rationally drive the discovery of promising new host-directed targets against pathogens including Mycobacterium tuberculosis, the causative agent of tuberculosis.

Corrigendum: Structural basis of enzymatic benzene ring reduction

September 17th, 2015 by Tobias Weinert

Nature Chemical Biology 11, 815 (2015). doi:10.1038/nchembio1015-815a

Author: Tobias Weinert, Simona G Huwiler, Johannes W Kung, Sina Weidenweber, Petra Hellwig, Hans-Joachim Stärk, Till Biskup, Stefan Weber, Julien J H Cotelesage, Graham N George, Ulrich Ermler & Matthias Boll

Viral mechanisms: A route to the ER

September 17th, 2015 by Mirella Bucci

Nature Chemical Biology 11, 755 (2015). doi:10.1038/nchembio.1925

Author: Mirella Bucci

Corrigendum: Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain

September 17th, 2015 by Chao Xu

Nature Chemical Biology 11, 815 (2015). doi:10.1038/nchembio1015-815c

Author: Chao Xu, Xiao Wang, Ke Liu, Ian A Roundtree, Wolfram Tempel, Yanjun Li, Zhike Lu, Chuan He & Jinrong Min

  • Posted in Nat Chem Biol, Publications
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Voices of chemical biology

September 17th, 2015 by Nature Chemical Biology - Issue - nature.com science feeds

Nature Chemical Biology 11, 752 (2015). doi:10.1038/nchembio.1919

We asked a collection of chemical biologists: "What do you value most about being part of the chemical biology community?"

Erratum: Pharmacological targeting of the Wdr5-MLL interaction in C/EBPα N-terminal leukemia

September 17th, 2015 by Florian Grebien

Nature Chemical Biology 11, 815 (2015). doi:10.1038/nchembio1015-815b

Author: Florian Grebien, Masoud Vedadi, Matthäus Getlik, Roberto Giambruno, Amit Grover, Roberto Avellino, Anna Skucha, Sarah Vittori, Ekaterina Kuznetsova, David Smil, Dalia Barsyte-Lovejoy, Fengling Li, Gennadiy Poda, Matthieu Schapira, Hong Wu, Aiping Dong, Guillermo Senisterra, Alexey Stukalov, Kilian V M Huber, Andreas Schönegger, Richard Marcellus, Martin Bilban, Christoph Bock, Peter J Brown, Johannes Zuber, Keiryn L Bennett, Rima Al-awar, Ruud Delwel, Claus Nerlov, Cheryl H Arrowsmith & Giulio Superti-Furga

  • Posted in Nat Chem Biol, Publications
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Metalloproteins: Simple structure, complex function

September 17th, 2015 by Angela Lombardi

Nature Chemical Biology 11, 760 (2015). doi:10.1038/nchembio.1918

Author: Angela Lombardi

The four-helix bundle is a simple structural motif, widespread in nature, that is involved in numerous and fundamental processes. This portfolio is now expanded by the report of a four-helix bundle protein able to store copper for particulate methane monooxygenase, an enzyme that catalyzes methane oxidation.