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To mark the 100th anniversary of the 1918 influenza pandemic, Nature Reviews Microbiology presents a collection including Reviews and research articles from across Nature Research to showcase the latest advances in our understanding of influenza virus biology, evolution and adaptation, and advances in surveillance and drug and vaccine development. Access the collection online. | | |
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TABLE OF CONTENTS
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February 2018 Volume 25, Issue 2 |
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| Review Articles Brief Communications Articles Technical Reports | | Advertisement | | | | Nature Research ‘lab health’ survey 2018 The Nature Research’s lab health survey aims to find out what makes a research group supportive, productive, and rigorous. The survey should take 10 to 15 minutes to complete and you’ll have the chance to win a £100/$150 Amazon gift card. Your entries will be confidential and results will be featured in Nature. Complete the survey today >> | | | |
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Review Articles | |
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| | Structural insights into the design of novel anti-influenza therapies pp115 - 121 Nicholas C. Wu & Ian A. Wilson doi:10.1038/s41594-018-0025-9 Wu and Wilson review our structural knowledge of influenza virus HA and broadly neutralizing antibodies, which have opened the way for design of novel vaccines and therapeutics. | | | | The ring-shaped hexameric helicases that function at DNA replication forks pp122 - 130 Michael E. O'Donnell & Huilin Li doi:10.1038/s41594-018-0024-x In this Review, the authors discuss our current understanding of how the hexameric helicases that catalyze helix unwinding during DNA replication are physically and functionally integrated with other replisome components. | | Brief Communications | | | | | Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp pp131 - 134 Marcus Gallagher-Jones, Calina Glynn, David R. Boyer, Michael W. Martynowycz, Evelyn Hernandez et al. doi:10.1038/s41594-017-0018-0 MicroED structure of a peptide from the β2-α2 loop of the bank vole prion protein reveals a protofibril stabilized by a dense network of hydrogen bonds. | | | | Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex pp135 - 138 doi:10.1038/s41594-017-0020-6 The cryo-EM structure of the human core CPSF complex, containing CPSF160, WDR33, CPSF30 and Fip1 subunits, bound to its RNA target reveals the mechanism of PAS recognition. | | | | | |
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A new open access, multi- and interdisciplinary journal dedicated to publishing the highest quality papers on aging and age-related diseases, the journal is now open for submissions. | | |
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Articles | |
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Cryo-EM structure of the exocyst complex pp139 - 146 Kunrong Mei, Yan Li, Shaoxiao Wang, Guangcan Shao, Jia Wang et al. doi:10.1038/s41594-017-0016-2 The structure of the fully assembled yeast exocyst complex, which mediates the tethering of secretory vesicles to the plasma membrane during exocytosis, provides new insights to hierarchical complex assembly and the mechanism of vesicle tethering. |
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TRF1 participates in chromosome end protection by averting TRF2-dependent telomeric R loops pp147 - 153 Yong Woo Lee, Rajika Arora, Harry Wischnewski & Claus M. Azzalin doi:10.1038/s41594-017-0021-5 In vitro and cellular assays unexpectedly reveal that shelterin protein TRF2 binds TERRA and stimulates strand invasion within telomere repeats and that TRF1 suppresses this activity to prevent telomere loss and genome instability. |
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Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes pp154 - 162 Simon Poepsel, Vignesh Kasinath & Eva Nogales doi:10.1038/s41594-018-0023-y Cryo-EM analyses of human PRC2 bound to dinucleosomes with one unmodified (substrate) and one H3K27me3-containing (activating) nucleosome support a model for H3K27me3-based PRC2 activation and spreading. |
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Solution structure and elevator mechanism of the membrane electron transporter CcdA pp163 - 169 Yunpeng Zhou & John H. Bushweller doi:10.1038/s41594-018-0022-z An NMR structure of Thermus thermophilus membrane electron transporter CcdA in an oxidized, outward-facing state suggests an elevator-type mechanism shuttles reactive cysteines to relay reducing equivalents across the membrane. |
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Structural basis for recognition of diverse antidepressants by the human serotonin transporter pp170 - 175 Jonathan A. Coleman & Eric Gouaux doi:10.1038/s41594-018-0026-8 The X-ray structures of engineered variants of the human serotonin transporter show that the antidepressants sertraline, fluvoxamine and paroxetine occupy the central substrate-binding site and stabilize the transporter in an outward-open conformation. |
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Technical Reports | |
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Spatiotemporal allele organization by allele-specific CRISPR live-cell imaging (SNP-CLING) pp176 - 184 Philipp G. Maass, A. Rasim Barutcu, David M. Shechner, Catherine L. Weiner, Marta Melé et al. doi:10.1038/s41594-017-0015-3 An allele-specific CRISPR-based DNA imaging technique provides insights into allelic positioning in live mouse cells. Spatiotemporal monitoring reveals that allele positions may fluctuate during cell state transitions. |
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Visualization and analysis of non-covalent contacts using the Protein Contacts Atlas pp185 - 194 Melis Kayikci, A. J. Venkatakrishnan, James Scott-Brown, Charles N. J. Ravarani, Tilman Flock et al. doi:10.1038/s41594-017-0019-z The Protein Contacts Atlas is an interactive resource of non-covalent contacts that can generate multiple representations of non-covalent contacts from PDB structures at different scales, from atoms to subunits and entire complexes. |
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| | | | | | 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. For event advertising opportunities across the Nature Publishing Group portfolio please contact natureevents@nature.com | | | | | | |
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