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The collection includes articles from PSI research groups and the broader community

August 2009

  • Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F

    Agarwal R., Schmidt J., Stafford R. and Swaminathan S.

    Nat Struct Mol Biol 16, 789 - 794 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1626]

  • Structural basis for ESCRT-III protein autoinhibition

    Bajorek M., Schubert H., McCullough J., Langelier C., Eckert D. et al.

    Nat Struct Mol Biol 16, 754 - 762 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1621]

  • Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA

    Liang B., Zhou J., Kahen E., Terns R., Terns M. et al.

    Nat Struct Mol Biol 16, 740 - 746 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1624]

  • Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2

    Zhang L., Xu T., Maeder C., Bud L., Shanks J. et al.

    Nat Struct Mol Biol 16, 731 - 739 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1625]

  • Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen

    Velikovsky C., Deng L., Tasumi S., Iyer L., Kerzic M. et al.

    Nat Struct Mol Biol 16, 725 - 730 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1619]

  • Structural insights into hedgehog ligand sequestration by the human hedgehog-interacting protein HHIP

    Bishop B., Aricescu A., Harlos K., O'Callaghan C., Jones E. et al.

    Nat Struct Mol Biol 16, 698 - 703 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1607]

  • The structure of SHH in complex with HHIP reveals a recognition role for the Shh pseudo active site in signaling

    Bosanac I., Maun H., Scales S., Wen X., Lingel A. et al.

    Nat Struct Mol Biol 16, 7, 691 - 697 (2009).

    [doi: http://dx.doi.org/10.1038/nsmb.1632]

  • Structural insight into the autoinhibition mechanism of AMP-activated protein kinase

    Chen L., Jiao Z., Zheng L., Zhang Y., Xie S. et al.

    Nature 459, 1146 - 1149 (2009)

    [doi: http://dx.doi.org/10.1038/nature08075]

  • Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase

    Barends T., Hartmann E., Griese J., Beitlich T., Kirienko N. et al.

    Nature 459, 1015 - 1018 (2009)

    [doi: http://dx.doi.org/10.1038/nature07966]

  • The Thermotoga maritima Trk potassium transporter--from frameshift to function

    Johnson H., Hampton E. and Lesley S.

    J Bacteriol 191, 2276 - 2284 (2009)

    [doi: http://dx.doi.org/10.1128/JB.01367-08]

  • The structural basis of gas-responsive transcription by the human nuclear hormone receptor REV-ERBbeta

    Pardee K., Xu X., Reinking J., Schuetz A., Dong A. et al.

    PLoS Biol 7, e43 (2009)

    [doi: http://dx.doi.org/10.1371/journal.pbio.1000043]

  • Structure of Thermotoga maritima TM0439: implications for the mechanism of bacterial GntR transcription regulators with Zn2+-binding FCD domains

    Zheng M., Cooper D., Grossoehme N., Yu M., Hung L. et al.

    Acta Crystallogr D Biol Crystallogr 65, 356 - 365 (2009)

    [doi: http://dx.doi.org/10.1107/S0907444909004727]

  • An unusual mechanism of thymidylate biosynthesis in organisms containing the thyX gene

    Koehn E., Fleischmann T., Conrad J., Palfey B., Lesley S. et al.

    Nature 458, 919 - 923 (2009)

    [doi: http://dx.doi.org/10.1038/nature07973]

  • Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins

    Park S., Fung P., Nishimura N., Jensen D., Fujii H. et al.

    Science 324, 1068 - 1071 (2009)

    [doi: http://dx.doi.org/10.1126/science.1173041]

  • Mixing and matching detergents for membrane protein NMR structure determination

    Columbus L., Lipfert J., Jambunathan K., Fox D., Sim A. et al.

    J Am Chem Soc 131, 7320 - 7326 (2009)

    [doi: http://dx.doi.org/10.1021/ja808776j]

  • Empirical correlation between protein backbone 15N and 13C secondary chemical shifts and its application to nitrogen chemical shift re-referencing

    Wang L. and Markley J.

    J Biomol NMR 44, 95 - 99 (2009)

    [doi: http://dx.doi.org/10.1007/s10858-009-9324-0]

  • Oxidase activity of a flavin-dependent thymidylate synthase

    Wang Z., Chernyshev A., Koehn E., Manuel T., Lesley S. et al.

    FEBS J 276, 2801 - 2810 (2009)

    [doi: http://dx.doi.org/10.1111/j.1742-4658.2009.07003.x]

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