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Journal Cover Nature Structural & Molecular Biology
  [SJR: 12.548]   [H-I: 222]   [183 followers]  Follow
    
   Full-text available via subscription Subscription journal
   ISSN (Print) 1545-9993 - ISSN (Online) 1545-9985
   Published by NPG Homepage  [135 journals]
  • APOBEC3 induces mutations during repair of CRISPR–Cas9-generated DNA
           breaks
    • APOBEC3 induces mutations during repair of CRISPR–Cas9-generated DNA breaks

      APOBEC3 induces mutations during repair of CRISPR–Cas9-generated DNA breaks, Published online: 11 December 2017; doi:10.1038/s41594-017-0004-6

      The APOBEC-AID family of cytidine deaminases target single-stranded nucleic acids for cytidine-to-uridine deamination and can thereby affect DNA repair processes that occur during CRISPR–Cas9-mediated genome editing.APOBEC3 induces mutations during repair of CRISPR–Cas9-generated DNA breaks, Published online: 2017-12-11; doi:10.1038/s41594-017-0004-62017-12-11
      DOI: 10.1038/s41594-017-0004-6
       
  • Histone octamer rearranges to adapt to DNA unwrapping
    • Histone octamer rearranges to adapt to DNA unwrapping

      Histone octamer rearranges to adapt to DNA unwrapping, Published online: 11 December 2017; doi:10.1038/s41594-017-0005-5

      Cryo-EM structures of nucleosomes in partially unwrapped, transient states reveal intrinsic plasticity that is required for nucleosome stability and can be exploited by chromatin-remodeling factors.Histone octamer rearranges to adapt to DNA unwrapping, Published online: 2017-12-11; doi:10.1038/s41594-017-0005-52017-12-11
      DOI: 10.1038/s41594-017-0005-5
       
  • Dominant-negative SMARCA4 mutants alter the accessibility landscape of
           tissue-unrestricted enhancers
    • Dominant-negative SMARCA4 mutants alter the accessibility landscape of tissue-unrestricted enhancers

      Dominant-negative SMARCA4 mutants alter the accessibility landscape of tissue-unrestricted enhancers, Published online: 11 December 2017; doi:10.1038/s41594-017-0007-3

      Heterozygous cancer-associated SMARCA4 missense mutations disrupt conserved ATPase surfaces of this chromatin remodeler and alter the open chromatin landscape, thus inducing pro-oncogenic gene expression.Dominant-negative SMARCA4 mutants alter the accessibility landscape of tissue-unrestricted enhancers, Published online: 2017-12-11; doi:10.1038/s41594-017-0007-32017-12-11
      DOI: 10.1038/s41594-017-0007-3
       
  • Polθ helicase: drive or reverse
    • Polθ helicase: drive or reverse

      Polθ helicase: drive or reverse, Published online: 07 December 2017; doi:10.1038/nsmb.3510

      The helicase intrinsic to DNA polymerase θ (Polθ), the versatile mediator of microhomology-based repair of DNA double-strand breaks and stalled replication forks, is now revealed to be a member of an elite group of proteins known as annealing helicases. This small family of enzymes remodels DNA intermediates in multiple repair processes that are crucial to preserving genome stability and warding off cancer and aging.Polθ helicase: drive or reverse, Published online: 2017-12-07; doi:10.1038/nsmb.35102017-12-07
      DOI: 10.1038/nsmb.3510
       
  • One flexible loop in OST lassos both substrates
    • One flexible loop in OST lassos both substrates

      One flexible loop in OST lassos both substrates, Published online: 07 December 2017; doi:10.1038/nsmb.3508

      The crystal structure of an oligosaccharyltransferase in complex with a sugar donor and an acceptor peptide provides insight into the mechanism of protein glycosylation and reveals how lipid-linked oligosaccharides are positioned in the enzyme active site.One flexible loop in OST lassos both substrates, Published online: 2017-12-07; doi:10.1038/nsmb.35082017-12-07
      DOI: 10.1038/nsmb.3508
       
  • The ribosome moves: RNA mechanics and translocation
    • The ribosome moves: RNA mechanics and translocation

      The ribosome moves: RNA mechanics and translocation, Published online: 07 December 2017; doi:10.1038/nsmb.3505

      The mechanics and mechanisms of ribosomal translocation, including the conformational rearrangements in the ribosome and the roles of EF-G and tRNAs, are discussed in this Perspective by Mohan, Noller and colleagues.The ribosome moves: RNA mechanics and translocation, Published online: 2017-12-07; doi:10.1038/nsmb.35052017-12-07
      DOI: 10.1038/nsmb.3505
       
  • Catching DNA with hoops—biophysical approaches to clarify the
           mechanism of SMC proteins
    • Catching DNA with hoops—biophysical approaches to clarify the mechanism of SMC proteins

      Catching DNA with hoops—biophysical approaches to clarify the mechanism of SMC proteins, Published online: 07 December 2017; doi:10.1038/nsmb.3507

      In this Review, the authors consider how single-molecule biophysical approaches can inform our understanding of the ring-shaped structural maintenance of chromosome (SMC) complexes and their function in chromosome organization.Catching DNA with hoops—biophysical approaches to clarify the mechanism of SMC proteins, Published online: 2017-12-07; doi:10.1038/nsmb.35072017-12-07
      DOI: 10.1038/nsmb.3507
       
  • Poly(A) tails: longer is not always better
    • Poly(A) tails: longer is not always better

      Poly(A) tails: longer is not always better, Published online: 07 December 2017; doi:10.1038/nsmb.3509

      Deadenylation of mRNAs is generally associated with translational inhibition and mRNA decay. A study now reports that, unexpectedly, highly expressed genes tend to have shorter poly(A) tails and suggests that poly(A) tails can be 'pruned', generating a 30-nucleotide-biased phased distribution, likely due to protection by poly(A)-binding proteins.Poly(A) tails: longer is not always better, Published online: 2017-12-07; doi:10.1038/nsmb.35092017-12-07
      DOI: 10.1038/nsmb.3509
       
 
 
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