Publikationen in 2011

  • Alexander K. Buell, Elin K. Esbjörner, Patrick J. Riss, Duncan A. White, Franklin I. Aigbirhio, Gergely Toth, Mark E. Welland, Christopher M. Dobson and Tuomas P.J. Knowles 
    Probing small molecule binding to amyloid fibrils 
    Phys Chem Chem Phys 13, 20044-20052 (2011) 
    https://www.ncbi.nlm.nih.gov/pubmed/22006124  
  • Bajaj P, Steger G, Hammann C 
    Sequence elements outside the catalytic core of natural hairpin ribozymes modulate the reactions differentially 
    Biol. Chem. 392, 593-600 (2011) 
    http://dx.doi.org/10.1515/BC.2011.071  
  • Cong Y, Schröder GF, Meyer AS, Jakana J, Ma B, Dougherty MT, Schmid MF, Reissmann S, Levitt M, Ludtke SL, Frydman J, and Chiu W 
    Symmetry-Free Cryo-EM Structures of the Chaperonin TRiC Along its ATPase-Driven Conformational Cycle. 
    EMBO J 31, 720 (2011) 
  • Feuerstein S, Solyom Z, Aladag A, Hoffmann S, Willbold D, Brutscher B 
    1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus nonstructural protein 5A 
    Biomol. NMR Assign. 53, 241-243 (2011) 
  • Funke SA 
    Detection of Soluble Amyloid-β Oligomers and Insoluble High-Molecular-Weight Particles in CSF: Development of Methods with Potential for Diagnosis and Therapy Monitoring of Alzheimer's Disease. 
    Int J Alzheimers Dis. 2011, 151645 (2011) 
  • Funke SA, Willbold D 
    Quantitation of Amyloid-β oligomers in human body fluids for Alzheimer’s disease early diagnosis or therapy monitoring. 
    Alzheimer's diagnosis. Charles E. Ronson (Ed.), Hauppage, NY, USA (2011) 
    Nova Science Publishers, ISBN 978-1-61209-846-3 
  • Gao S, von der Malsburg A, Dick A, Faelber K, Schröder GF, Haller O, Kochs G, Daumke O 
    Three domain architecture of dynamin-like MxA GTPase. 
    Immunity 35, 514 (2011) 
  • Glück JM 
    Ligand interaction analysis of membrane-anchored proteins. 
    Schriften des Forschungszentrums Jülich Reihe Gesundheit, Band 31, (2011) 
    http://wwwzb1.fz-juelich.de/contentenrichment/inhaltsverzeichnisse/2010/verlag/gesund31_i.pdf  
  • Glück JM, Koenig BW, Willbold D 
    Nanodiscs allow the use of integral membrane proteins as analytes in surface plasmon resonance studies. 
    Anal. Biochem. 408, 46-52 (2011) 
  • Hickman DT, López-Deber MP, Ndao DM, Silva AB, Nand D, Pihlgren M, Giriens V, Madani R, St-Pierre A, Karastan H, Nagel-Steger L, Willbold D, Riesner D, Nicolau C, Baldus M, Pfeifer A, Muhs A 
    Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases. 
    J. Biol.Chem. 286, 13966-13976 (2011) 
  • Hochdörffer K, März-Berberich J, Nagel-Steger L, Epple M, Meyer-Zaika W, Horn AH, Sticht H, Sinha S, Bitan G, Schrader T 
    Rational Design of β-Sheet Ligands Against Aβ(42)-Induced Toxicity. 
    J. Am. Chem. Soc. 133, 4348-4358 (2011) 
  • Hofmann H, Wurm R, Wagner, R 
    The E. coli Anti-Sigma Factor Rsd: Studies on the Specificity and Regulation of its Expression. 
    PLoS ONE 6, e19235 (2011) 
    http://dx.doi.org/10.1371/journal.pone.0019235  
    http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0019235  
  • Jaenicke E, Büchler K, Decker H, Markl J, Barends T, and Schröder GF 
    The Refined Structure of Functional Unit h of Keyhole Limpet Hemocyanin (KLH1-h) Reveals Disulfide Bridges. 
    IUBMB Life 63(3), 183 (2011) 
  • Janssen S, Schudoma C, Steger G, Giegerich R 
    Lost in folding space? Comparing four variants of the thermodynamic model for RNA secondary structure prediction. 
    BMC Bioinformatics 12, 429 (2011) 
    http://dx.doi.org/10.1186/1471-2105-12-429  
  • Jore MM, Lundgren M, van Duin E, Bultema JB, Westra ER, Waghmare SP, Wiedenheft B, Pul U, Wurm R, Wagner R, Beijer M, Barendregt RA, Zhou K, Snijders APL, Dickman MJ, Doudna JA, Boekema EJ, Heck AJR, van der Oost J and Brouns SJJ 
    Structural basis for CRISPR RNA-guided DNA recognition by Cascade. 
    Nat. Struct. Mol. Biol. 18, 529–536 (2011) 
    http://dx.doi.org/10.1038/nsmb.2019  
    http://www.nature.com/nsmb/journal/v18/n5/full/nsmb.2019.html  
  • Kirchberg K, Kim TY, Möller M, Skegro D, Dasara Raju G, Granzin J, Büldt G, Schlesinger R, Alexiev U 
    Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process. 
    Proc Natl Acad Sci U S A 108(46), 18690-5 (2011) 
    http://dx.doi.org/10.1073/pnas.1015461108  
  • Kolmsee, T, Delic, D, Agyenim, T, Calles, C and Wagner, R 
    Differential stringent control of E. coli rRNA promoters: effects of ppGpp, DksA and the initiating nucleotides. 
    Microbiology 157, 2871-2879 (2011) 
  • Lecher J, Stoldt M, Schwarz CKW, Smits SHJ, Schmitt L, Willbold D 
    ¹H, ¹⁵N and ¹³C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB). 
    Biomol. NMR Assign. 53, 199-201 (2011) 
  • Pfannkuche A, Büther K, Karthe J, Poenisch M, Bartenschlager R, Trilling M, Hengel H, Willbold D, Häussinger D, Bode JG 
    c-Src is required for complex formation between the hepatitis C virus encoded proteins NS5A and NS5B – a prerequisite for replication. 
    Hepatology 53, 1127-1136 (2011) 
  • Sabir T, Schröder GF, Toulmin A, McGlynn P, and Magennis SW 
    Global Structure of Forked DNA in Solution Revealed by High-Resolution Single-Molecule Fluorescence Resonance Energy Transfer. 
    J. Am. Chem. Soc. 135(5), 1188 (2011) 
  • Schünke S 
    NMR solution structures of the MloK1 cyclic nucleotide-gated ion channel binding domain. 
    Schriften des Forschungszentrums Jülich, Reihe Schlüsseltechnologien, Band 26 , (2011) 
    http://wwwzb.zb.kfa-juelich.de/publikationen/schriftreihe.asp?Schriftreihe=65  
  • Schünke S, Stoldt M, Lecher J, Kaupp UB, Willbold D 
    Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. 
    Proc. Natl. Acad. Sci. USA 108, 6121-6126 (2011) 
  • Schwarz CKW, Tschapek B, Jumpertz T, Jenewein S, Lecher J, Willbold D, Panjikar S, Halland B, Smits SHJ, Schmitt L 
    Crystallisation and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter Haemolysin B 
    Acta Cryst. F67, 630-633 (2011) 
  • Seebahn A, Dinkel H, Mohrlüder J, Hartmann R, Vogel N, Becker CM, Sticht H, Enz R 
    Structural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors 
    FEBS Lett 585, 511-516 (2011) 
  • Seehafer C, Kalweit A, Steger G, Gräf S, Hammann C 
    From alpaca to zebrafish: hammerhead ribozymes wherever you look 
    RNA 17, 21-26 (2011) 
    http://dx.doi.org/10.1261/rna.2429911  
  • Stöhr J, Elfrink K, Weinmann N, Wille H, Willbold D, Birkmann E and Riesner D 
    In vitro conversion of the posttranslationally modified prion protein. 
    Biol. Chem. 392, 415-421 (2011) 
  • van Groen T, Kadish I, Funke A and Willbold D 
    Staining of Amyloid Beta (Abeta) Using (Immuno) Histochemical Techniques and Abeta42 Specific Peptides 
    In: Neuroimaging for Clinicians - Combining Research and Practice. In Tech. Editor: Julio F. P. Peres; ISBN 978-953-307-450-4, Chapter 4 (2011) 
    free download  
  • VE Galkin, A Orlova, D Kudryashov, A Solodukhin, E Reisler, GF Schröder, and EH Egelman 
    Remodeling of Actin Filaments by ADF/Cofilin Proteins. 
    PNAS 108(51), 20568 (2011) 
  • Wagner R, Pul U 
    Mikrobielles "Immunsystem": Abwehr gegen Fremd-DNA durch das bakterielle CRISPR/Cas-System. 
    BIOspektrum 4, 393-395 (2011) 
  • Wang W, Dong H, Pacheco V, Willbold D, Zhang Y, Offenhausser A, Hartmann R, Weirich T, Ma P, Krause H, Gu Z 
    Relaxation behavior study of ultra-small superparamagnetic iron oxide nanoparticles at ultra-low and ultra-high magnetic fields. 
    J. Phys. Chem.B 115, 14789-14793 (2011) 
  • Zerrad L, Merli A, Schröder GF, Varga A, Gráczer E, Pernot P, Round A, Vas M, and Bowler MW 
    A Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase. 
    JBC 286, 14040 (2011) 

Physikalische Biologie
Heinrich-Heine-Universität
Gebäude 26.12, Ebene U1
Universitätsstraße 1
40225 Düsseldorf
Deutschland

Institutsleitung
Prof. Dr. D. Willbold
Gebäude 26.12
Ebene U1, Raum 84
Telefon: +49-(0)211 / 81-11390
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