New IDH1 mutant inhibitors for treatment of acute myeloid leukemia

October 5th, 2015 by Ujunwa C Okoye-Okafor

Nature Chemical Biology 11, 878 (2015). doi:10.1038/nchembio.1930

Authors: Ujunwa C Okoye-Okafor, Boris Bartholdy, Jessy Cartier, Enoch N Gao, Beth Pietrak, Alan R Rendina, Cynthia Rominger, Chad Quinn, Angela Smallwood, Kenneth J Wiggall, Alexander J Reif, Stanley J Schmidt, Hongwei Qi, Huizhen Zhao, Gerard Joberty, Maria Faelth-Savitski, Marcus Bantscheff, Gerard Drewes, Chaya Duraiswami, Pat Brady, Arthur Groy, Swathi-Rao Narayanagari, Iléana Antony-Debre, Kelly Mitchell, Heng Rui Wang, Yun-Ruei Kao, Maximilian Christopeit, Luis Carvajal, Laura Barreyro, Elisabeth Paietta, Hideki Makishima, Britta Will, Nestor Concha, Nicholas D Adams, Benjamin Schwartz, Michael T McCabe, Jaroslav Maciejewski, Amit Verma & Ulrich Steidl

Crystal structure of the Varkud satellite ribozyme

September 28th, 2015 by Nikolai B Suslov

Nature Chemical Biology 11, 840 (2015). doi:10.1038/nchembio.1929

Authors: Nikolai B Suslov, Saurja DasGupta, Hao Huang, James R Fuller, David M J Lilley, Phoebe A Rice & Joseph A Piccirilli

Ribozymes: How RNA catalyzes cyclization

September 28th, 2015 by Zhensheng Zhong

Nature Chemical Biology 11, 830 (2015). doi:10.1038/nchembio.1928

Authors: Zhensheng Zhong & Gang Chen

The long-awaited crystal structure of the Varkud satellite (VS) ribozyme dimer provides atomic-level insights into how the VS ribozyme folds and catalyzes RNA circularization during rolling circle replication, as well as revealing convergent evolution used by RNAs to catalyze an SN2 reaction.

Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism

September 28th, 2015 by Hongjun Yu

Nature Chemical Biology 11, 847 (2015). doi:10.1038/nchembio.1927

Authors: Hongjun Yu, Megumi Takeuchi, Jamie LeBarron, Joshua Kantharia, Erwin London, Hans Bakker, Robert S Haltiwanger, Huilin Li & Hideyuki Takeuchi

  • Posted in Nat Chem Biol, Publications
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Two cytochromes P450 catalyze S-heterocyclizations in cabbage phytoalexin biosynthesis

September 21st, 2015 by Andrew P Klein

Nature Chemical Biology 11, 837 (2015). doi:10.1038/nchembio.1914

Authors: Andrew P Klein & Elizabeth S Sattely

Phytoalexins are abundant in edible crucifers and have important biological activities, yet no dedicated gene for their biosynthesis is known. Here, we report two new cytochromes P450 from Brassica rapa (Chinese cabbage) that catalyze unprecedented S-heterocyclizations in cyclobrassinin and spirobrassinin biosynthesis. Our results provide genetic and biochemical insights into the biosynthesis of a prominent pair of dietary metabolites and have implications for pathway discovery across >20 recently sequenced crucifers.

  • Posted in Nat Chem Biol, Publications
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Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes

September 21st, 2015 by Mahesh K Chand

Nature Chemical Biology 11, 870 (2015). doi:10.1038/nchembio.1926

Authors: Mahesh K Chand, Neha Nirwan, Fiona M Diffin, Kara van Aelst, Manasi Kulkarni, Christian Pernstich, Mark D Szczelkun & Kayarat Saikrishnan

  • Posted in Nat Chem Biol, Publications
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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.