Nature Chemical Biology Contents: May 2015, Volume 11 No 5 pp 301 - 361

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TABLE OF CONTENTS May 2015 Volume 11, Issue 5 Editorial Correspondence Research Highlights News and Views Perspective Brief Communication Articles Addendum Subscribe   Facebook   RSS   Recommend to library   Twitter   Advertisement Nature Outlook Biomaterials The Nature Outlook: Biomaterials examines the many ways in which solutions created by the natural world — by spiders, mussels, geckos, lotus leaves and more — are inspiring technological imitations that surpass some of the best existing human-engineered substances.  Access the Outlook free online for six months. Produced with support from: KISCO Ltd. in association with Spiber Inc.     Editorial Top Structures under scrutiny   p301 doi:10.1038/nchembio.1808 Structural biology advances have democratized access to biomolecular snapshots, but high standards must be maintained to ensure their utility. Correspondence Top Carbohydrate anomalies in the PDB   p303 Jon Agirre, Gideon Davies, Keith Wilson and Kevin Cowtan doi:10.1038/nchembio.1798 Research Highlights Top Structural biology: A racemate to the rescue | Metabolic regulation: Go fish | Neuroscience: An epileptic target | Riboswitches: Manganese management | Cell biology: Not the same | Wnt signaling: Trimming the fat News and Views Top Bioconjugation: How to pick a single amine?   pp306 - 307 Floris P J T Rutjes doi:10.1038/nchembio.1791 Single-step site-specific labeling of native proteins is one of the holy grails in the chemical biology field. 2-Pyridinecarboxyaldehyde derivatives are shown to react selectively at the N terminus of proteins to form stable conjugates, irrespective of the nature of the N-terminal amino acid, enabling the straightforward introduction of useful functional groups into a wide array of proteins. See also: Article by MacDonald et al. Translation: An O-GlcNAc stamp of approval   pp307 - 308 Evan T Powers doi:10.1038/nchembio.1777 Cytosolic proteins can be modified cotranslationally by the installation of O-GlcNAc groups onto serine and threonine residues. This modification suppresses cotranslational ubiquitination and stabilizes proteins against proteasomal degradation. See also: Article by Zhu et al. Chemical Biology JOBS of the week Research Associate: Chemist / Chemical Biologist - The Chemical Biology of the Epigenome (fixed-term) University of Cambridge Funded PhD project in Chemical Biology Cardiff University Post-doctoral position in Biomedical Research Case Western Reserve University Senior Scientist - Tenure Track Paul Scherrer Institut (PSI) ERC-funded PhD studentship in Molecular Cell Biology Max Planck Institute of Molecular Physiology More Science jobs from Chemical Biology EVENT The Expanding Toolbox of Medicinal Chemistry: From Chemical Biology to Clinical Applications 16 October 2015 Dijon, France More science events from Perspective Top Toward spinning artificial spider silk   pp309 - 315 Anna Rising and Jan Johansson doi:10.1038/nchembio.1789 Spider silks have enormous potential as strong yet flexible biomaterials, but obtaining artificial silk polymers has proven challenging. Recent advances in our understanding of natural silk processing may inform techniques for silk production. Brief Communication Top Small molecule–triggered Cas9 protein with improved genome-editing specificity   pp316 - 318 Kevin M Davis, Vikram Pattanayak, David B Thompson, John A Zuris and David R Liu doi:10.1038/nchembio.1793 Post-translational regulation of Cas9 activity may improve the specificity of genomic targeting. A modified version of Cas9 with an insertion of a small molecule–regulated intein allows temporal control of Cas9 activity and reduces off-target activity. Articles Top O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains   pp319 - 325 Yanping Zhu, Ta-Wei Liu, Samy Cecioni, Razieh Eskandari, Wesley F Zandberg et al. doi:10.1038/nchembio.1774 O-GlcNAcylation is a known post-translational modification, but analysis of nascent proteins now demonstrates that it also occurs during translation, preventing proteolytic degradation of modified proteins by blocking ubiquitination. Chemical compounds See also: News and Views by Powers One-step site-specific modification of native proteins with 2-pyridinecarboxyaldehydes   pp326 - 331 James I MacDonald, Henrik K Munch, Troy Moore and Matthew B Francis doi:10.1038/nchembio.1792 Bioconjugation methods enable a variety of applications, but it remains difficult to modify many proteins in a single location with a single functional group. A serendipitous discovery of aldehyde reactivity now leads to reagents for the selective labeling of protein N termini under mild conditions. Chemical compounds See also: News and Views by Rutjes Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors   pp332 - 338 Lionel Tarrago, Zalán Péterfi, Byung Cheon Lee, Thomas Michel and Vadim N Gladyshev doi:10.1038/nchembio.1787 The lack of existing tools has made it difficult to detect and quantify methionine sulfoxide in cells. The introduction of the MetSOx and MetROx fluorescent sensors allows detection of stereospecific forms of methionine sulfoxide in cells. Impeding the interaction between Nur77 and p38 reduces LPS-induced inflammation   pp339 - 346 Li Li, Yuan Liu, Hang-zi Chen, Feng-wei Li, Jian-feng Wu et al. doi:10.1038/nchembio.1788 The orphan nuclear receptor Nur77 blocks inflammation through inhibition of p65 DNA binding and is suppressed by p38α-mediated phosphorylation. A small-molecule compound, PDNPA, disrupts p38α-Nur77 interactions and alleviates mouse models of sepsis. siRNA screen identifies QPCT as a druggable target for Huntington's disease   pp347 - 354 Maria Jimenez-Sanchez, Wun Lam, Michael Hannus, Birte Sönnichsen, Sara Imarisio et al. doi:10.1038/nchembio.1790 An siRNA screen for genes that suppress mutant huntingtin toxicity in both mammalian cells and Drosophila identifies glutaminyl cyclase (QPCT). Newly generated small-molecule inhibitors further identify QPCT as a druggable target for Huntington′s disease. Chemical compounds A pentose bisphosphate pathway for nucleoside degradation in Archaea   pp355 - 360 Riku Aono, Takaaki Sato, Tadayuki Imanaka and Haruyuki Atomi doi:10.1038/nchembio.1786 Genetic, biochemical and bioinformatic data define a pathway in Archaea that links the ribose moieties of nucleosides to central carbon metabolism, substituting for the classical pentose phosphate pathway found in Bacteria and Eukarya. Addendum Top Addendum: Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds   p361 Yu-Chen Liu, Yi-Shan Li, Syue-Yi Lyu, Li-Jen Hsu, Yu-Hou Chen et al. doi:10.1038/nchembio0515-361 Top Advertisement Epigenome Roadmap Nature Publishing Group presents an online portal - the Epigenome Roadmap - which collects key research papers from The NIH Roadmap Epigenomics Program, complemented by thematical 'threads' to help the readers mine the wealth of available information. Access the Epigenome Roadmap for FREE at:  nature.com/epigenomeroadmap Produced with exclusive support from  Illumina   Natureevents is a fully searchable, multi-disciplinary database designed to maximise exposure for events organisers. The contents of the Natureevents Directory are now live. The digital version is available here. Find the latest scientific conferences, courses, meetings and symposia on natureevents.com. 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