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

April 2009

  • Gating Mechanism of the Influenza A M2 Channel Revealed by 1D and 2D IR Spectroscopies.

    Manor J., Mukherjee P., Lin Y., Leonov H., Skinner J. et al.

    Structure 17, 247 - 254 (2009)

    [doi: http://dx.doi.org/10.1016/j.str.2008.12.015]

  • Modification by Single Ubiquitin Moieties Rather Than Polyubiquitination Is Sufficient for Proteasomal Processing of the p105 NF-κB Precursor

    Kravtsova-Ivantsiv Y., Cohen S. and Ciechanover A.

    Mol Cell 33, 496 - 504 (2009)

    [doi: http://dx.doi.org/10.1016/j.molcel.2009.01.023]

  • E2-RING Expansion of the NEDD8 Cascade Confers Specificity to Cullin Modification

    Huang D., Ayrault O., Hunt H., Taherbhoy A., Duda D. et al.

    Mol Cell 33, 483 - 495 (2009)

    [doi: http://dx.doi.org/10.1016/j.molcel.2009.01.011]

  • Nanomole-scale protein solid-state NMR by breaking intrinsic 1H T1 boundaries

    Wickramasinghe N., Parthasarathy S., Jones C., Bhardwaj C., Long F. et al.

    Nat Meth 6, 215 - 218 (2009)

    [doi: http://dx.doi.org/10.1038/nmeth.1300]

  • Quantitative interaction proteomics using mass spectrometry

    Wepf A., Glatter T., Schmidt A., Aebersold R. and Gstaiger M.

    Nat Meth 6, 203 - 205 (2009)

    [doi: http://dx.doi.org/10.1038/nmeth.1302]

  • AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis

    Schmelz S., Kadi N., McMahon S., Song L., Oves-Costales D. et al.

    Nat Chem Biol 5, 174 - 182 (2009)

    [doi: http://dx.doi.org/10.1038/nchembio.145]

  • Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis

    Arora P., Goyal A., Natarajan V., Rajakumara E., Verma P. et al.

    Nat Chem Biol 5, 166 - 173 (2009)

    [doi: http://dx.doi.org/10.1038/nchembio.143]

  • Cocrystal structure of a class I preQ1 riboswitch reveals a pseudoknot recognizing an essential hypermodified nucleobase

    Klein D., Edwards T. and Ferre-D'Amare A.

    Nat Struct Mol Biol 16, 343 - 344 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1563]

  • Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride

    Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A. et al.

    Nat Struct Mol Biol 16, 334 - 342 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1559]

  • Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

    Chang Y., Zhang X., Horton J., Upadhyay A., Spannhoff A. et al.

    Nat Struct Mol Biol 16, 312 - 317 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1560]

  • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses

    Sui J., Hwang W., Perez S., Wei G., Aird D. et al.

    Nat Struct Mol Biol 16, 265 - 273 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1566]

  • The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner

    von Moeller H., Basquin C. and Conti E.

    Nat Struct Mol Biol 16, 247 - 254 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1561]

  • Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding

    Diaz-Moreno I., Hollingworth D., Frenkiel T., Kelly G., Martin S. et al.

    Nat Struct Mol Biol 16, 238 - 246 (2009)

    [doi: http://dx.doi.org/10.1038/nsmb.1558]

  • The Fas-FADD death domain complex structure unravels signalling by receptor clustering

    Scott F., Stec B., Pop C., Dobaczewska M., Lee J. et al.

    Nature 457, 1019 - 1022 (2009)

    [doi: http://dx.doi.org/10.1038/nature07606]

  • High-resolution multi-dimensional NMR spectroscopy of proteins in human cells

    Inomata K., Ohno A., Tochio H., Isogai S., Tenno T. et al.

    Nature 458, 106 - 109 (2009)

    [doi: http://dx.doi.org/10.1038/nature07839]

  • Protein structure determination in living cells by in-cell NMR spectroscopy

    Sakakibara D., Sasaki A., Ikeya T., Hamatsu J., Hanashima T. et al.

    Nature 458, 102 - 105 (2009)

    [doi: http://dx.doi.org/10.1038/nature07814]

  • Molecular basis of transport and regulation in the Na+/betaine symporter BetP

    Ressl S., van Scheltinga A., Vonrhein C., Ott V. and Ziegler C.

    Nature 458, 47 - 52 (2009)

    [doi: http://dx.doi.org/10.1038/nature07819]

  • Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 A resolution

    Das D., Krishna S., McMullan D., Miller M., Xu Q. et al.

    Proteins 75, 264 - 271 (2009)

    [doi: http://dx.doi.org/10.1002/prot.22338]

  • Structural and Biochemical Characterization of the Type II Fructose-1,6-bisphosphatase GlpX from Escherichia coli

    Brown G., Singer A., Lunin V., Proudfoot M., Skarina T. et al.

    J Biol Chem 284, 3784 - 3792 (2009)

    [doi: http://dx.doi.org/10.1074/jbc.M808186200]

  • Two poplar methyl salicylate esterases display comparable biochemical properties but divergent expression patterns

    Zhao N., Guan J., Forouhar F., Tschaplinski T., Cheng Z. et al.

    Phytochemistry 70, 37 - 44 (2009)

    [doi: http://dx.doi.org/10.1016/j.phytochem.2008.11.014]

  • Clean absorption-mode NMR data acquisition

    Wu Y., Ghosh A. and Szyperski T.

    Angew Chem Int Ed Engl 48, 1479 - 1483 (2009)

    [doi: http://dx.doi.org/10.1002/anie.200804927]

  • Structural genomics is the largest contributor of novel structural leverage

    Nair R., Liu J., Soong T., Acton T., Everett J. et al.

    J Struc Funct Genomics 10, 181 (2009)

    [doi: http://dx.doi.org/10.1007/s10969-008-9055-6]

  • Outcome of a workshop on applications of protein models in biomedical research

    Schwede T., Sali A., Honig B., Levitt M., Berman H. et al.

    Structure 17, 151 - 159 (2009)

    [doi: http://dx.doi.org/10.1016/j.str.2008.12.014]

  • Pyrrolysyl-tRNA synthetase-tRNAPyl structure reveals the molecular basis of orthogonality

    Nozawa K., O/'Donoghue P., Gundllapalli S., Araiso Y., Ishitani R. et al.

    Nature 457, 1163 - 1167 (2009)

    [doi: http://dx.doi.org/10.1038/nature07611]

  • Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold

    Chatterjee A., Johnson M., Serrano P., Pedrini B., Joseph J. et al.

    J Virol 83, 1823 - 1836 (2009)

    [doi: http://dx.doi.org/10.1128/JVI.01781-08]

  • The Protein Model Portal

    Arnold K., Kiefer F., Kopp J., Battey J., Podvinec M. et al.

    J Struct Funct Genomics 10, 1 - 8 (2008)

    [doi: http://dx.doi.org/10.1007/s10969-008-9048-5]

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