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

The Research Library is no longer being updated. Please explore the previous submissions, or find the PSI’s latest research articles in the PSI Publications Portal.

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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