for Journals by Title or ISSN
for Articles by Keywords
help
Similar Journals
Journal Cover
Nature Structural & Molecular Biology
Journal Prestige (SJR): 10.873
Citation Impact (citeScore): 10
Number of Followers: 241  
 
  Full-text available via subscription Subscription journal
ISSN (Print) 1545-9993 - ISSN (Online) 1545-9985
Published by NPG Homepage  [138 journals]
  • Structures of MERS-CoV spike glycoprotein in complex with sialoside
           attachment receptors
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0334-7

      Cryo-EM structures of MERS-CoV S glycoprotein trimer in complex with different sialosides reveal how the virus engages with sialylated receptors, providing insight into receptor specificity and selectivity.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0334-72019-12-02
      DOI: 10.1038/s41594-019-0334-7
       
  • Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking
           antibody
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0344-5

      Cryo-EM resolution of HIV-1 Env trimer bound to CD4 and a tyrosine-sulfated, coreceptor-mimicking antibody reveals two configurations of gp120–gp41 protomers that create asymmetric Env trimer conformations on the path to membrane fusion.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0344-52019-12-02
      DOI: 10.1038/s41594-019-0344-5
       
  • The structure and oxidation of the eye lens chaperone αA-crystallin
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0332-9

      Oligomers of human αA-crystallin are characterized structurally via a hybrid approach, combining cryo-EM, cross-linking/mass spectrometry, NMR and modeling, providing insight into their dynamic behavior and heterogeneity and revealing that oxidized oligomers can also act as chaperones.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0332-92019-12-02
      DOI: 10.1038/s41594-019-0332-9
       
  • High-affinity recognition of specific tRNAs by an mRNA anticodon-binding
           groove
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0335-6

      The cocrystal structure of the Nocardia farcinica ileS T-box in complex with its cognate tRNA illustrates how mRNA junctions can create specific binding sites for interacting RNAs.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0335-62019-12-02
      DOI: 10.1038/s41594-019-0335-6
       
  • InsP6 binding to PIKK kinases revealed by the cryo-EM structure of an
           SMG1–SMG8–SMG9 complex
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0342-7

      The structure of human SMG1–SMG8–SMG9, a PI(3)K-related protein kinase complex central to mRNA surveillance, uncovers an InsP6-binding site in the SMG1 kinase that is conserved in mTOR and important for kinase activity.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0342-72019-12-02
      DOI: 10.1038/s41594-019-0342-7
       
  • T-box RNA gets boxed
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0340-9

      Bacterial T-boxes are regulatory mRNA regions that control the transcription or translation of factors involved in amino acid supply. T-boxes act by directly binding to non-aminoacylated tRNA in response to amino acid starvation. Three studies now capture three-dimensional structures of tRNA–T-box complexes and reveal a set of RNA features that are required for the recognition of specific tRNAs and modulation of gene expression.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0340-92019-12-02
      DOI: 10.1038/s41594-019-0340-9
       
  • 53BP1–RIF1: sculpting the DNA repair focus in 3D
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0348-1

      Stabilization of the 3D genome architecture surrounding DNA lesions is critical for the maintenance of genome integrity. A new report by Ochs et al. shows how 53BP1 and RIF1 assemble a higher-order structure in the vicinity of damaged chromatin to protect it from unscheduled DNA-end resection.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0348-12019-12-02
      DOI: 10.1038/s41594-019-0348-1
       
  • Structural basis of antagonism of human APOBEC3F by HIV-1 Vif
    • Nature Structural & Molecular Biology, Published online: 02 December 2019; doi:10.1038/s41594-019-0343-6

      Cryo-EM structure of the C-terminal domain of human APOBEC3F in complex with HIV-1 Vif and CFBβ, along with functional analyses, reveals how Vif targets a host restriction protein.Nature Structural & Molecular Biology, Published online: 2019-12-02; doi:10.1038/s41594-019-0343-62019-12-02
      DOI: 10.1038/s41594-019-0343-6
       
 
 
JournalTOCs
School of Mathematical and Computer Sciences
Heriot-Watt University
Edinburgh, EH14 4AS, UK
Email: journaltocs@hw.ac.uk
Tel: +00 44 (0)131 4513762
Fax: +00 44 (0)131 4513327
 
Home (Search)
Subjects A-Z
Publishers A-Z
Customise
APIs
Your IP address: 3.94.129.211
 
About JournalTOCs
API
Help
News (blog, publications)
JournalTOCs on Twitter   JournalTOCs on Facebook

JournalTOCs © 2009-