TABLE OF CONTENTS
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April 2017 Volume 24, Issue 4 |
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News and Views | Top |
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Articles | Top |
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TOP2 synergizes with BAF chromatin remodeling for both resolution and formation of facultative heterochromatin pp344 - 352 Erik L Miller, Diana C Hargreaves, Cigall Kadoch, Chiung-Ying Chang, Joseph P Calarco et al. doi:10.1038/nsmb.3384 TOP2 collaborates with the BAF complex genome-wide to form and resolve facultative heterochromatin at transcriptional regulatory elements recognized by pluripotency factors. |
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Genome-wide mapping of long-range contacts unveils clustering of DNA double-strand breaks at damaged active genes pp353 - 361 François Aymard, Marion Aguirrebengoa, Emmanuelle Guillou, Biola M Javierre, Beatrix Bugler et al. doi:10.1038/nsmb.3387 Capture Hi-C analysis reveals that DNA double-strand breaks within transcriptionally active regions of the human genome form clusters that exhibit delayed repair in the G1 phase of the cell cycle. |
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Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode pp362 - 369 Baobin Li, Hao Li, Lei Lu and Jiaoyang Jiang doi:10.1038/nsmb.3390 Human OGA forms an unusual arm-in-arm homodimer with a substrate-binding cleft that affords extensive interactions with the peptide substrate in a recognition mode distinct from that of its bacterial homologs. |
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Quaternary contact in the initial interaction of CD4 with the HIV-1 envelope trimer pp370 - 378 Qingbo Liu, Priyamvada Acharya, Michael A Dolan, Peng Zhang, Christina Guzzo et al. doi:10.1038/nsmb.3382 Cryo-EM analyses of the initial contact of the HIV-1 Env trimer with the CD4 receptor reveal that CD4 interacts with two gp120 protomers; these quaternary contacts are important for viral infectivity. |
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HIV Tat protein and amyloid-β peptide form multifibrillar structures that cause neurotoxicity pp379 - 386 Alina Hategan, Mario A Bianchet, Joseph Steiner, Elena Karnaukhova, Eliezer Masliah et al. doi:10.1038/nsmb.3379 HIV Tat binding to the exterior of Aβ fibrils induces lateral aggregation and formation of fibers with increased adhesion, rigidity and mechanical resistance, thus potentially accounting for their higher neurotoxicity. |
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MHC-I peptides get out of the groove and enable a novel mechanism of HIV-1 escape pp387 - 394 Phillip Pymm, Patricia T Illing, Sri H Ramarathinam, Geraldine M O'Connor, Victoria A Hughes et al. doi:10.1038/nsmb.3381 Structural determination and analysis of HLA-I that presents an HIV-derived peptide to an NK cell receptor reveal that N-terminal extended epitope conformations contribute to immune recognition and mechanisms of HIV immune escape.
See also: News and Views by Dash & Thomas |
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Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8+ T cell epitope pp395 - 406 InYoung Song, Anna Gil, Rabinarayan Mishra, Dario Ghersi, Liisa K Selin et al. doi:10.1038/nsmb.3383 Crystal structure analysis combined with sequencing approaches uncover a broad T cell receptor repertoire and reveal the structural basis of influenza M1 epitope recognition.
See also: News and Views by Dash & Thomas |
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Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90 pp407 - 413 Javier Oroz, Jin Hae Kim, Bliss J Chang and Markus Zweckstetter doi:10.1038/nsmb.3380 The interaction of Hsp90 with misfolded monomeric transthyretin is characterized via biophysical approaches, and the data indicate that Hsp90 may have a distinct recognition mode for aggregation-prone proteins. |
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Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution pp414 - 418 Andreas Boland, Thomas G Martin, Ziguo Zhang, Jing Yang, Xiao-chen Bai et al. doi:10.1038/nsmb.3386 Cryo-EM analyses provide a near-atomic view of the C. elegans securin-separase complex, with insights into the mechanism by which securin inhibits separase's protease activity.
See also: News and Views by Singleton & Uhlmann |
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A mammalian nervous-system-specific plasma membrane proteasome complex that modulates neuronal function pp419 - 430 Kapil V Ramachandran and Seth S Margolis doi:10.1038/nsmb.3389 A 20S proteasome complex localizes to neuronal plasma membrane, where it produces and releases extracellular peptides that induce neuronal calcium signaling. |
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