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Nature Structural & Molecular Biology
Journal Prestige (SJR): 10.873
Citation Impact (citeScore): 10
Number of Followers: 187  
 
  Full-text available via subscription Subscription journal
ISSN (Print) 1545-9993 - ISSN (Online) 1545-9985
Published by NPG Homepage  [144 journals]
  • Elisa Izaurralde 1959–2018
    • Elisa Izaurralde 1959–2018

      Elisa Izaurralde 1959–2018, Published online: 18 June 2018; doi:10.1038/s41594-018-0081-1

      Elisa Izaurralde 1959–2018Elisa Izaurralde 1959–2018, Published online: 2018-06-18; doi:10.1038/s41594-018-0081-12018-06-18
      DOI: 10.1038/s41594-018-0081-1
       
  • Structural basis of meiotic chromosome synapsis through SYCP1
           self-assembly
    • Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly

      Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly, Published online: 18 June 2018; doi:10.1038/s41594-018-0078-9

      The structural basis for self-assembly of human SYCP1, the core architectural element of the meiotic synaptonemal complex, reveals an obligate tetrameric structure that assembles into a zipper-like supramolecular lattice.Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly, Published online: 2018-06-18; doi:10.1038/s41594-018-0078-92018-06-18
      DOI: 10.1038/s41594-018-0078-9
       
  • Cryo-EM structures of complex I from mouse heart mitochondria in two
           biochemically defined states
    • Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states

      Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states, Published online: 18 June 2018; doi:10.1038/s41594-018-0073-1

      Cryo-EM analyses of mitochondrial complex I (NADH:ubiquinone oxidoreductase) isolated from mouse heart allow comparisons between the active and deactive states and provide new mechanistic insights into this important complex.Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states, Published online: 2018-06-18; doi:10.1038/s41594-018-0073-12018-06-18
      DOI: 10.1038/s41594-018-0073-1
       
  • Molecular mechanism of modulating arrestin conformation by GPCR
           phosphorylation
    • Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation

      Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation, Published online: 05 June 2018; doi:10.1038/s41594-018-0071-3

      Analysis of 18 available structures and other data reveals a new, conserved structural motif in arrestins and suggests that different phosphorylation patterns of the GPCR C terminus can drive distinct arrestin conformations and functional outcomes.Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation, Published online: 2018-06-05; doi:10.1038/s41594-018-0071-32018-06-05
      DOI: 10.1038/s41594-018-0071-3
       
  • Cryo-EM structure of the human neutral amino acid transporter ASCT2
    • Cryo-EM structure of the human neutral amino acid transporter ASCT2

      Cryo-EM structure of the human neutral amino acid transporter ASCT2, Published online: 05 June 2018; doi:10.1038/s41594-018-0076-y

      A cryo-EM structure of the human SLC1 transporter ASCT2 in the inward-facing conformation reveals the retrovirus-docking site and helps to elucidate the transport cycle. The transport domain is more solvent exposed than in most of the homolog structures.Cryo-EM structure of the human neutral amino acid transporter ASCT2, Published online: 2018-06-05; doi:10.1038/s41594-018-0076-y2018-06-05
      DOI: 10.1038/s41594-018-0076-y
       
  • Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the
           cytosol-open state
    • Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state

      Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state, Published online: 05 June 2018; doi:10.1038/s41594-018-0072-2

      The crystal structure of SLC38A9 from Danio rerio in complex with arginine in the cytosol-open conformation reveals the mechanism of substrate binding.Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state, Published online: 2018-06-05; doi:10.1038/s41594-018-0072-22018-06-05
      DOI: 10.1038/s41594-018-0072-2
       
  • Strength in numbers—an arrestin interaction code
    • Strength in numbers—an arrestin interaction code

      Strength in numbers—an arrestin interaction code, Published online: 05 June 2018; doi:10.1038/s41594-018-0077-x

      Activation signals from GPCRs, the largest receptor family, are transmitted to heterotrimeric G proteins and arrestins, and can be differentially modulated by GPCR phosphorylation. In a recent article, available data, including multiple arrestin structures, are analyzed to decipher common and state-specific conformational changes in arrestins and how these depend on patterns of receptor phosphorylation.Strength in numbers—an arrestin interaction code, Published online: 2018-06-05; doi:10.1038/s41594-018-0077-x2018-06-05
      DOI: 10.1038/s41594-018-0077-x
       
  • Controlling load-dependent kinetics of β-cardiac myosin at the
           single-molecule level
    • Controlling load-dependent kinetics of β-cardiac myosin at the single-molecule level

      Controlling load-dependent kinetics of β-cardiac myosin at the single-molecule level, Published online: 04 June 2018; doi:10.1038/s41594-018-0069-x

      The load-dependence of the detachment rate of single molecules of human β-cardiac myosin from actin, and the effects of small-molecule compounds and cardiomyopathy-causing mutations, are investigated using harmonic force spectroscopy.Controlling load-dependent kinetics of β-cardiac myosin at the single-molecule level, Published online: 2018-06-04; doi:10.1038/s41594-018-0069-x2018-06-04
      DOI: 10.1038/s41594-018-0069-x
       
 
 
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