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

August 2011

  • Internal organization of large protein families: Relationship between the sequence, structure, and function-based clustering

    Cai X., Jaroszewski L., Wooley J. and Godzik A.

    Proteins 79, 2389 - 2402 (2011)

    [doi: http://dx.doi.org/10.1002/prot.23049]

  • Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production

    Filippova E., Shuvalova L., Minasov G., Kiryukhina O., Zhang Y. et al.

    Proteins 79, 2566 - 2577 (2011)

    [doi: http://dx.doi.org/10.1002/prot.23062]

  • Crystal structure of the novel PaiB transcriptional regulator from Geobacillus stearothermophilus

    Filippova E., Brunzelle J., Cuff M., Li H., Joachimiak A. et al.

    Proteins 79, 2578 - 2582 (2011)

    [doi: http://dx.doi.org/10.1002/prot.23061]

  • Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria

    Kim Y., Joachimiak G., Ye Z., Binkowski T., Zhang R. et al.

    Proc Natl Acad Sci USA 108, 10109 - 10114 (2011)

    [doi: http://dx.doi.org/10.1073/pnas.1106840108]

  • NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554

    Wahab A., Serrano P., Geralt M. and Wüthrich K.

    Protein Sci 20, 1137 - 1144 (2011)

    [doi: http://dx.doi.org/10.1002/pro.641]

  • Crystal structure of secretory protein Hcp3 from Pseudomonas aeruginosa

    Osipiuk J., Xu X., Cui H., Savchenko A., Edwards A. et al.

    J Struct Funct Genomics 12, 21 - 26 (2011)

    [doi: http://dx.doi.org/10.1007/s10969-011-9107-1]

  • Catalytic mechanism and three-dimensional structure of adenine deaminase

    Kamat S., Bagaria A., Kumaran D., Holmes-Hampton G., Fan H. et al.

    Biochemistry 50, 1917 - 1927 (2011)

    [doi: http://dx.doi.org/10.1021/bi101788n]

  • A dual function of the CRISPR-Cas system in bacterial antivirus immunity and DNA repair

    Babu M., Beloglazova N., Flick R., Graham C., Skarina T. et al.

    Mol Microbiol 79, 484 - 502 (2011)

    [doi: http://dx.doi.org/10.1111/j.1365-2958.2010.07465.x]

  • Structural and functional studies of fatty acyl adenylate ligases from E. coli and L. pneumophila

    Zhang Z., Zhou R., Sauder J., Tonge P., Burley S. et al.

    J Mol Biol 406, 313 - 324 (2011)

    [doi: http://dx.doi.org/10.1016/j.jmb.2010.12.011]

  • Crystal structure of a metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity

    Han G., Ko J., Farr C., Deller M., Xu Q. et al.

    Proteins 79, 2146 - 2160 (2011)

    [doi: http://dx.doi.org/10.1002/prot.23035]

  • Eisosome-driven plasma membrane organization is mediated by BAR domains

    Ziółkowska N., Karotki L., Rehman M., Huiskonen J. and Walther T.

    Nat Struct Mol Biol 18, 854 - 856 (2011)

    [doi: http://dx.doi.org/10.1038/nsmb.2080]

  • Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction

    Phan A., Kuryavyi V., Darnell J., Serganov A., Majumdar A. et al.

    Nat Struct Mol Biol 18, 796 - 804 (2011)

    [doi: http://dx.doi.org/10.1038/nsmb.2064]

  • Recognition of the F&H motif by the Lowe syndrome protein OCRL

    Pirruccello M., Swan L., Folta-Stogniew E. and de Camilli P.

    Nat Struct Mol Biol 18, 789 - 795 (2011)

    [doi: http://dx.doi.org/10.1038/nsmb.2071]

  • Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin

    Eustermann S., Yang J., Law M., Amos R., Chapman L. et al.

    Nat Struct Mol Biol 18, 777 - 782 (2011)

    [doi: http://dx.doi.org/10.1038/nsmb.2070]

  • ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome

    Iwase S., Xiang B., Ghosh S., Ren T., Lewis P. et al.

    Nat Struct Mol Biol 18, 769 - 776 (2011)

    [doi: http://dx.doi.org/10.1038/nsmb.2062]

  • The structural basis of modularity in ECF-type ABC transporters

    Erkens G., Berntsson R.P., Fulyani F., Majsnerowska M., Vujičić-Žagar A. et al.

    Nat Struct Mol Biol 18, 755 - 760 (2011)

    [doi: http://dx.doi.org/10.1038/nsmb.2073]

  • Endotoxin-Induced Structural Transformations in Liquid Crystalline Droplets

    Lin I., Miller D., Bertics P., Murphy C., de Pablo J. et al.

    Science 332, 1297 - 1300 (2011)

    [doi: http://dx.doi.org/10.1126/science.1195639]

  • Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

    Sievers S., Karanicolas J., Chang H., Zhao A., Jiang L. et al.

    Nature 475, 96 - 100 (2011)

    [doi: http://dx.doi.org/10.1038/nature10154]

  • Structure of the human histamine H1 receptor complex with doxepin

    Shimamura T., Shiroishi M., Weyand S., Tsujimoto H., Winter G. et al.

    Nature 475, 65 - 70 (2011)

    [doi: http://dx.doi.org/10.1038/nature10236]

  • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation

    Lebon G., Warne T., Edwards P., Bennett K., Langmead C. et al.

    Nature 474, 521 - 525 (2011)

    [doi: http://dx.doi.org/10.1038/nature10136]

  • Structural insight into brassinosteroid perception by BRI1

    She J., Han Z., Kim T., Wang J., Cheng W. et al.

    Nature 474, 472 - 476 (2011)

    [doi: http://dx.doi.org/10.1038/nature10178]

  • Structural basis of steroid hormone perception by the receptor kinase BRI1

    Hothorn M., Belkhadir Y., Dreux M., Dabi T., Noel J. et al.

    Nature 474, 467 - 471 (2011)

    [doi: http://dx.doi.org/10.1038/nature10153]

  • X-ray structure of a bacterial oligosaccharyltransferase

    Lizak C., Gerber S., Numao S., Aebi M. and Locher K.

    Nature 474, 350 - 355 (2011)

    [doi: http://dx.doi.org/10.1038/nature10151]

  • Latent TGF-β structure and activation

    Shi M., Zhu J., Wang R., Chen X., Mi L. et al.

    Nature 474, 343 - 349 (2011)

    [doi: http://dx.doi.org/10.1038/nature10152]

  • Structure and function of a membrane component SecDF that enhances protein export

    Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S. et al.

    Nature 474, 235 - 238 (2011)

    [doi: http://dx.doi.org/10.1038/nature09980]

  • Improved technologies now routinely provide protein NMR structures useful for molecular replacement

    Mao B., Guan R. and Montelione G.

    Structure 19, 757 - 766 (2011)

    [doi: http://dx.doi.org/10.1016/j.str.2011.04.005]

  • Crystal structure of a copper-transporting PIB-type ATPase

    Gourdon P., Liu X., Skjorringe T., Morth J., Moller L. et al.

    Nature 475, 59 - 64 (2011)

    [doi: http://dx.doi.org/10.1038/nature10191]

  • Distributed structure determination at the JCSG.

    van den Bedem H., Wolf G., Xu Q. and Deacon A.

    Acta crystallographica. Section D, Biological crystallography 67, 368 - 375 (2011)

    [doi: http://dx.doi.org/10.1107/S0907444910039934]

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