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Journal Cover Nature Structural & Molecular Biology
  [SJR: 12.548]   [H-I: 222]   [181 followers]  Follow
    
   Full-text available via subscription Subscription journal
   ISSN (Print) 1545-9993 - ISSN (Online) 1545-9985
   Published by NPG Homepage  [135 journals]
  • Class 2 CRISPR–Cas RNA-guided endonucleases: Swiss Army knives of
           genome editing
    • Class 2 CRISPR–Cas RNA-guided endonucleases: Swiss Army knives of genome editing

      Nature Structural & Molecular Biology, Published online: 16 October 2017; doi:10.1038/nsmb.3486

      This review highlights recent mechanistic insights into the CRISPR class 2 type V enzymes Cpf1 and C2c1, which are crucial for improving these genome engineering tools and expanding the genomic editing space.

      Nature Structural & Molecular Biology, Published online: 16 October 2017; doi:10.1038/nsmb.34862017-10-16
      DOI: 10.1038/nsmb.3486
       
  • MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear
           NAD+ consumption
    • MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear NAD+ consumption

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.3481

      Histone variant macroH2A1.1 inhibits PARP activity to maintain mitochondrial NAD+ pools in muscle cells, thus linking chromatin state to optimal energy metabolism.

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.34812017-10-09
      DOI: 10.1038/nsmb.3481
       
  • A structural model for microtubule minus-end recognition and protection by
           CAMSAP proteins
    • A structural model for microtubule minus-end recognition and protection by CAMSAP proteins

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.3483

      Combined structural and microscopy approaches provide a model for how CAMSAP proteins recognize microtubule minus ends through their conserved CCK domains and protect microtubules from depolymerizing kinesin-13.

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.34832017-10-09
      DOI: 10.1038/nsmb.3483
       
  • Architectural alterations of the fission yeast genome during the cell
           cycle
    • Architectural alterations of the fission yeast genome during the cell cycle

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.3482

      Analysis of the 3D genomic organization of Schizosaccharomyces pombe during the cell cycle reveals that condensin mediates formation of large domains that serve as chromosomal compaction units, whereas cohesin forms smaller, more stable domains.

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.34822017-10-09
      DOI: 10.1038/nsmb.3482
       
  • Structural basis for GABAA receptor potentiation by
           neurosteroids
    • Structural basis for GABAA receptor potentiation by neurosteroids

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.3484

      Crystal structures and functional assays of a chimeric GABAA receptor in apo and pregnanolone-bound states reveal how neurosteroid binding alters receptor conformation to modulate channel opening.

      Nature Structural & Molecular Biology, Published online: 9 October 2017; doi:10.1038/nsmb.34842017-10-09
      DOI: 10.1038/nsmb.3484
       
  • A glimpse into the C-type-inactivated state for a Potassium Channel
    • A glimpse into the C-type-inactivated state for a Potassium Channel

      Nature Structural & Molecular Biology, Published online: 5 October 2017; doi:10.1038/nsmb.3480

      C-type inactivation is a process by which ion flux through a voltage-gated K+ channel is regulated at the selectivity filter. A recent structure of the Kv1.2 channel provides a view into the structural changes of the selectivity filter during C-type inactivation.

      Nature Structural & Molecular Biology, Published online: 5 October 2017; doi:10.1038/nsmb.34802017-10-05
      DOI: 10.1038/nsmb.3480
       
  • Fine-tuning PERK signaling to control cell fate under stress
    • Fine-tuning PERK signaling to control cell fate under stress

      Nature Structural & Molecular Biology, Published online: 5 October 2017; doi:10.1038/nsmb.3478

      PERK is a major sensor of the unfolded protein response controlling cell fate under endoplasmic reticulum (ER) stress. A new study reveals an additional step for optimal PERK signaling, involving the binding of CNPY2 to PERK's luminal domain. The PERK–CNPY2 axis was shown to enhance cell death under ER stress in vivo influence liver disease.

      Nature Structural & Molecular Biology, Published online: 5 October 2017; doi:10.1038/nsmb.34782017-10-05
      DOI: 10.1038/nsmb.3478
       
  • Cryo-electron microscopy snapshots of the spliceosome: structural insights
           into a dynamic ribonucleoprotein machine
    • Cryo-electron microscopy snapshots of the spliceosome: structural insights into a dynamic ribonucleoprotein machine

      Nature Structural & Molecular Biology, Published online: 5 October 2017; doi:10.1038/nsmb.3463

      Nature Structural & Molecular Biology, Published online: 5 October 2017; doi:10.1038/nsmb.34632017-10-05
      DOI: 10.1038/nsmb.3463
       
 
 
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