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

December 2010

  • Homologue structure of the SLAC1 anion channel for closing stomata in leaves

    Chen Y.H., Hu L., Punta M., Bruni R., Hillerich B., et al.

    Nature 467, 1074 - 1080 (2010)

    [doi: http://dx.doi.org/10.1038/nature09487]

  • The crystal structure of a bacterial Sufu-like protein defines a novel group of bacterial proteins that are similar to the N-terminal domain of human Sufu

    Das D., Finn R.D., Abdubek P., Astakhova T., Axelrod H.L., et al.

    Protein Sci 19, 2131 - 2140 (2010)

    [doi: http://dx.doi.org/10.1002/pro.497]

  • Substrate and drug binding sites in LeuT

    Nyola A., Karpowich N.K., Zhen J., Marden J., Reith M.E., et al.

    Curr Opin Struct Biol 20, 415 - 422 (2010)

    [doi: http://dx.doi.org/10.1016/j.sbi.2010.05.007]

  • TOPSAN: a collaborative annotation environment for structural genomics

    Weekes D., Krishna S.S., Bakolitsa C., Wilson I.A., Godzik A., et al.

    BMC Bioinformatics. 11, 426 (2010)

    [doi: http://dx.doi.org/10.1186/1471-2105-11-426]

  • Structural insight into the mechanism of c-di-GMP hydrolysis by EAL domain phosphodiesterases

    Tchigvintsev A., Xu X., Singer A., Chang C., Brown G., et al.

    J Mol Biol. 402, 524 - 538 (2010)

    [doi: http://dx.doi.org/10.1016/j.jmb.2010.07.050]

  • Dead-end filling of SlipChip evaluated theoretically and experimentally as a function of the surface chemistry and the gap size between the plates for lubricated and dry SlipChips

    Li L., Karymov M.A., Nichols K.P., Ismagilov R.F.

    Langmuir. 26, 12465 - 12471 (2010)

    [doi: http://dx.doi.org/10.1021/la101460z]

  • Heme proteins--diversity in structural characteristics, function, and folding

    Smith L.J., Kahraman A., Thornton J.M.

    Proteins 78, 2349 - 2368 (2010)

    [doi: http://dx.doi.org/10.1002/prot.22747]

  • New surface contacts formed upon reductive lysine methylation: improving the probability of protein crystallization

    Sledz P., Zheng H., Murzyn K., Chruszcz M., Zimmerman M.D., et al.

    Protein Sci 19, 1395 - 1404 (2010)

    [doi: http://dx.doi.org/10.1002/pro.420]

  • Molecular mechanism of MLL PHD3 and RNA recognition by the Cyp33 RRM domain

    Hom R.A., Chang P.Y., Roy S., Musselman C.A., Glass K.C., et al.

    J Mol Biol 400, 145 - 154 (2010)

    [doi: http://dx.doi.org/10.1016/j.jmb.2010.04.067]

  • X-ray structure determination of the glycine cleavage system protein H of Mycobacterium tuberculosis using an inverse Compton synchrotron X-ray source

    Abendroth J., McCormick M.S., Edwards T.E., Staker B., Loewen R., et al.

    J Struct Funct Genomics 11, 91 - 100 (2010)

    [doi: http://dx.doi.org/10.1007/s10969-010-9087-6]

  • ArchSchema: a tool for interactive graphing of related Pfam domain architectures

    Tamuri A.U., Laskowski R.A.

    Bioinformatics 26, 1260 - 1261 (2010)

    [doi: http://dx.doi.org/10.1093/bioinformatics/btq119]

  • Visualization of macromolecular structures

    O'Donoghue S.I., Goodsell D.S., Frangakis A.S., Jossinet F., Laskowski R.A., et al.

    Nat Methods 7, S42 - 55 (2010)

    [doi: http://dx.doi.org/10.1038/nmeth.1427]

  • The structure of DinB from Geobacillus stearothermophilus: a representative of a unique four-helix-bundle superfamily

    Cooper D.R., Grelewska K., Kim C.Y., Joachimiak A., Derewenda Z.S.

    Acta Crystallogr Sect F Struct Biol Cryst Commun 66, 219 - 224 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109053913]

  • Structure of bovine pancreatic ribonuclease complexed with uridine 5'-monophosphate at 1.60 A resolution

    Larson S.B., Day J.S., Nguyen C., Cudney R., McPherson A.

    Acta Crystallogr Sect F Struct Biol Cryst Commun 66, 113 - 120 (2010)

    [doi: http://dx.doi.org/10.1107/S174430910905194X]

  • Protein crystallization analysis on the World Community Grid

    Cumbaa C.A., Jurisica I

    J Struct Funct Genomics 11, 61 - 69 (2010)

    [doi: http://dx.doi.org/10.1007/s10969-009-9076-9]

  • Purification of transmembrane proteins from Saccharomyces cerevisiae for X-ray crystallography

    Clark K.M., Fedoriw N., Robinson K., Connelly S.M., Randles J., et al.

    Protein Expr Purif 71, 207 - 223 (2010)

    [doi: http://dx.doi.org/10.1016/j.pep.2009.12.012]

  • Crystal structure and molecular modeling study of N-carbamoylsarcosine amidase Ta0454 from Thermoplasma acidophilum

    Luo H.B., Zheng H., Zimmerman M.D., Chruszcz M., Skarina T., et al.

    J Struct Biol 169, 304 - 311 (2010)

    [doi: http://dx.doi.org/10.1016/j.jsb.2009.11.008]

  • A comprehensive analysis of structural and sequence conservation in the TetR family transcriptional regulators

    Yu Z., Reichheld S.E., Savchenko A., Parkinson J., Davidson A.R.

    J Mol Biol 400, 847 - 864 (2010)

    [doi: http://dx.doi.org/10.1016/j.jmb.2010.05.062]

  • Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

    Daugherty M.D., Liu B., Frankel A.D.

    Nat Struct Mol Biol 17, 1337 - 1342 (2010)

    [doi: http://dx.doi.org/10.1038/nsmb.1902]

  • Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation

    Wang T., Darwin K.H., Li H.

    Nat Struct Mol Biol 17, 1352 - 1357 (2010)

    [doi: http://dx.doi.org/10.1038/nsmb.1918]

  • NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1

    Guttler T., Madl T., Neumann P., Deichsel D., Corsini L., et al.

    Nat Struct Mol Biol 17, 1367 - 1376 (2010)

    [doi: http://dx.doi.org/10.1038/nsmb.1931]

  • Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes

    Arnett K.L., Hass M., McArthur D.G., Ilagan M.X.G., Aster J.C., et al.

    Nat Struct Mol Biol 17, 1312 - 1317 (2010)

    [doi: http://dx.doi.org/10.1038/nsmb.1938]

  • Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers

    Feld G.K., Thoren K.L., Kintzer A.F., Sterling H.J., Tang I.I., et al.

    Nat Struct Mol Biol 17, 1383 - 1390 (2010)

    [doi: http://dx.doi.org/10.1038/nsmb.1923]

  • The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations

    Wang L., Yang J.K., Kabaleeswaran V., Rice A.J., Cruz A.C., et al.

    Nat Struct Mol Biol 17, 1324 - 1329 (2010)

    [doi: http://dx.doi.org/10.1038/nsmb.1920]

  • Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel

    Hilf R.J.C., Bertozzi C., Zimmermann I., Reiter A., Trauner D., et al.

    Nat Struct Mol Biol 17, 1330 - 1336 (2010)

    [doi: http://dx.doi.org/10.1038/nsmb.1933]

  • Structure of a Eukaryotic CLC Transporter Defines an Intermediate State in the Transport Cycle

    Feng L., Campbell EB., Hsiung Y., MacKinnon R.

    Science 330, 635-641 (2010)

    [doi: http://dx.doi.org/10.1126/science.1195230]

  • Insights into Egg Coat Assembly and Egg-Sperm Interaction from the X-Ray Structure of Full-Length ZP3

    Han L., Monne M., Okumura H., Schwend T., Cherry AL., et al.

    Cell 143, 404-415 (2010)

    [doi: http://dx.doi.org/10.1016/j.cell.2010.09.041]

  • Crystal structure of Spot 14, a modulator of fatty acid synthesis

    Colbert CL., Kim C-W., Moon Y-A., Henry L., Palnitkar M., et al.

    PNAS 107, 18820-18825 (2010)

    [doi: http://dx.doi.org/10.1073/pnas.1012736107]

  • Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure

    Wu S-R., Loving R., Lindqvist B., Hebert H., Koeck PJB., et al.

    PNAS 107, 18844-18849 (2010)

    [doi: http://dx.doi.org/10.1073/pnas.1007227107]

  • Structural basis of semaphorin-plexin signalling

    Janssen BJC., Robinson RA., Perez-Branguli F., Bell CH., Mitchell KJ., et al.

    Nature 467, 1118-1122 (2010)

    [doi: http://dx.doi.org/10.1038/nature09468]

  • Structural basis for semaphorin signalling through the plexin receptor

    Nogi T., Yasui N., Mihara E., Matsunaga Y., Noda M., et al.

    Nature 467, 1123-1127 (2010)

    [doi: http://dx.doi.org/10.1038/nature09473]

  • Structure of a cation-bound multidrug and toxic compound extrusion transporter

    He X., Szewczyk P., Karyakin A., Evin M., Hong W-X., et al.

    Nature 467, 991-994 (2010)

    [doi: http://dx.doi.org/10.1038/nature09408]

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