Publikationen in 2017

  • Abdollahzadeh I, Schwarten M, Gensch T, Willbold D, Weiergräber OH 
    The Atg8 Family of Proteins—Modulating Shape and Functionality of Autophagic Membranes 
    Front. Genet. 8, 109 (2017) 
    https://doi.org/10.3389/fgene.2017.00109  
  • Akers PW, Dingley AJ, Swift S, Nelson ARJ, Martin J, McGillivray DJ. 
    Using Neutron Reflectometry to Characterize Antimicrobial Protein Surface Coatings 
    J Phys Chem B [Epub ahead of print], (2017) 
    http://dx.doi.org/10.1021/acs.jpcb.7b02886  
    https://www.ncbi.nlm.nih.gov/pubmed/28537751  
  • Arinkin V, Granzin J, Röllen K, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R. 
    Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools 
    Scientific Reports 7(42971), (2017) 
    http://dx.doi.org/10.1038/srep42971  
  • Batra-Safferling R and Granzin J.  
    The Structure of the Polar Core Mutant R175E and Its Functional Implications.  
    The Structural Basis Of Arrestin Functions, Vsevolod V. Gurevich (Editor); Springer International Publishing Chapter 11, 143-158 (2017) 
    ISBN: 978-3-319-57552-0 
  • Boeske A, Schwarten M, Ma P, Tusche M, Mötter J, Möller C, Neudecker P, Hoffmann S, Willbold D 
    Direct binding to GABARAP family members is essential for HIV-1 Nef plasma membrane localization 
    Scientific Reports 7, 5979 (2017) 
  • Bradshaw NJ, Yerabham ASK, Marreiros R, Zhang T, Nagel-Steger L, Korth C 
    An unpredicted aggregation-critical region of the actin-polymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure 
    J Biol Chem 292, 9583-9598 (2017) 
    http://dx.doi.org/10.1074/jbc.M116.767939  
  • Brass JRJ, Owens RA, Matoušek J, Steger G 
    Viroid quasispecies revealed by deep sequencing 
    RNA Biology 14, 317-325 (2017) 
    http://dx.doi.org/10.1080/15476286.2016.1272745  
  • Caruso IP, Panwalkar V, Coronado MA, Dingley AJ, Cornélio ML, Willbold D, Arni RK, Eberle RJ. 
    NMR studies of cold shock protein A from Corynebacterium pseudotuberculosis: structure and interaction with Y-box single-stranded DNA fragment. 
    FEBS J. 285, 372-390 (2017) 
  • Dammers C, Reiss K, Gremer L, Lecher J, Ziehm T, Stoldt M, Schwarten M, Willbold D.  
    Pyroglutamate-modified amyloid-β(3-42) shows α-helical intermediates before amyloid formation. 
    Biophys. J. 112, 1621-1633 (2017) 
  • Dammers C, Schwarten M, Buell AK, Willbold D 
    Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways 
    Chem. Sci. 8, 4996-5004 (2017) 
    http://pubs.rsc.org/en/content/articlehtml/2017/sc/c6sc04797a  
  • Elfgen A, Santiago-Schübel B, Gremer L, Kutzsche J, Willbold, D 
    Surprisingly high stability of the Aβ oligomer eliminating all-D-enantiomeric peptide D3 in media simulating the route of orally administered drugs 
    European Journal of Pharmaceutical Sciences 107, 203-207 (2017) 
    https://doi.org/10.1016/j.ejps.2017.07.015  
    https://www.ncbi.nlm.nih.gov/pubmed/28711713  
  • Gremer L, Schölzel D, Schenk C, Reinartz E, Labahn J, Ravelli RB, Tusche M, Lopez-Iglesias C, Hoyer W, Heise H, Willbold D, Schröder GF 
    Fibril structure of amyloid-ß(1-42) by cryoelectron microscopy 
    Science 358, 116-119 (2017) 
    http://dx.doi.org/10.1126/science.aao2825  
    http://science.sciencemag.org/content/early/2017/09/06/science.aao2825  
  • Gushchin I, Melnikov I, Polovinkin V, Ishchenko A, Yuzhakova A, Buslaev P, Bourenkov G, Grudinin S, Round E, Balandin T, Borshchevskiy V, Willbold D, Leonard G, Büldt G, Popov A, Gordeliy V. 
    Mechanism of transmembrane signaling by sensor histidine kinases. 
    Science 356, eaah6345 (2017) 
  • Herrmann Y, Bujnicki T, Zafiu C, Kulawik A, Kühbach K, Peters L, Fabig J, Willbold J, Bannach O, Willbold D. 
    Nanoparticle standards for immuno-based quantitation of α-synuclein oligomers in diagnostics of Parkinson's disease and other synucleinopathies. 
    Clin Chim Acta 466, 152–159 (2017) 
    http://dx.doi.org/10.1016/j.cca.2017.01.010  
    http://www.sciencedirect.com/science/article/pii/S0009898117300104  
  • Herrmann Y, Kulawik A, Kühbach K, Hülsemann M, Peters L, Bujnicki T, Kravchenko K, Linnartz C, Willbold J, Zafiu C, Bannach O, Willbold D. 
    sFIDA automation yields sub-femtomolar limit of detection for Aβ aggregates in body liquids. 
    Clinical Biochem. 50(4-5), 244-247 (2017) 
    http://dx.doi.org/10.1016/j.clinbiochem.2016.11.001  
    http://www.sciencedirect.com/science/article/pii/S0009912016305008  
  • Hupert M, Elfgen A, Schartmann E, Schemmert S, Buscher B, Kutzsche J, Willbold D, Santiago-Schübel B 
    Development and Validation of an UHPLC-ESI-QTOF-MS method for quantification of the highly hydrophilic amyloid-β oligomer eliminating all-D-enantiomeric peptide RD2 in mouse plasma 
    Journal of Chromatography B 1073, 123-129 (2017) 
    https://doi.org/10.1016/j.jchromb.2017.12.009  
    https://www.sciencedirect.com/science/article/pii/S1570023217316562  
  • Klein AN, Ziehm T, van Groen T, Kadish I, Elfgen A, Tusche M, Thomaier M, Reiss K, Brener O, Gremer L, Kutzsche J, Willbold D 
    Optimization of D-peptides for Aβ monomer binding specificity enhances their potential to eliminate toxic Aβ oligomers 
    ACS Chem Neurosci 8, 1889-1900 (2017) 
  • Kravchenko K, Kulawik A, Hülsemann M, Kühbach K, Zafiu C, Herrmann Y, Linnartz C, Peters L, Bujnicki T, Willbold J, Bannach O, Willbold D.  
    Analysis of anticoagulants for blood-based quantitation of amyloid β oligomers in the sFIDA assay. 
    Biol. Chem. 398(4), 465-475 (2017) 
    https://dx.doi.org/10.1515/hsz-2016-0153  
    https://www.degruyter.com/view/j/bchm.ahead-of-print/hsz-2016-0153/hsz-2016-0153.xml  
  • Kroeger T, Frieg B, Zhang T, Hansen FK, Marmann A, Proksch P, Nagel-Steger L, Groth G, Smits SHJ, Gohlke H 
    EDTA aggregates induce SYPRO orange-based fluorescence in thermal shift assay 
    PLoS One 12, e0177024 (2017) 
    http://dx.doi.org/10.1371/journal.pone.0177024  
  • Kühbach K, Hülsemann M, Herrmann Y, Kravchenko K, Kulawik A, Linnartz C, Peters L, Wang K, Willbold J, Willbold D, Bannach O.  
    Application of an amyloid beta oligomer standard in the sFIDA assay. 
    In: Biomarkers of Alzheimer's Disease: The Present and the Future. Eds. Sylvain Lehmann, Charlotte Elisabeth Teunissen. , 39-44 (2017) 
    ISBN 9782889450411  
  • Kutzsche J, Schemmert S, Tusche M, Neddens J, Rabl R, Jürgens D, Brener O, Willuweit A, Hutter-Paier B, Willbold D. 
    Large-Scale Oral Treatment Study with the Four Most Promising D3-Derivatives for the Treatment of Alzheimer's Disease. 
    Molecules 22(10), (2017) 
    http://10.3390/molecules22101693  
    https://www.ncbi.nlm.nih.gov/pubmed/28994710  
  • Matoušek J, Siglová K, Jakše J, Radišek S, Brass JR, Tsushima T, Guček T, Duraisamy GS, Sano T, Steger G 
    Propagation and some physiological effects of Citrus bark cracking viroid and Apple fruit crinkle viroid in multiple infected hop (Humulus lupulus L.) 
    J. Plant Physiol. 213, 166-177 (2017) 
    http://dx.doi.org/10.1016/j.jplph.2017.02.014  
  • Nikolaev M, Round E, Gushchin I, Polovinkin V, Balandin T, Kuzmichev P, Shevchenko V, Borshchevskiy V, Kuklin A, Round A, Bernhard F, Willbold D, Büldt G, Gordeliy V.  
    Integral membrane proteins can be crystallized directly from nanodiscs. 
    Cryst. Growth Des. 17, 945-948 (2017) 
  • Panwalkar V, Neudecker P, Willbold D, Dingley AJ. 
    Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding. 
    FEBS Lett. 591(11), 1573-1583 (2017) 
    http://dx.doi.org/10.1002/1873-3468.12664  
    https://www.ncbi.nlm.nih.gov/pubmed/28471472  
  • Ricardo Gaspar, Georg Meisl, Alexander K Buell, Laurence Young, Clemens F Kaminski, Tuomas PJ Knowles, Emma Sparr, Sara Linse 
    Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification 
    Quarterly Reviews in Biophysics 50, (2017) 
    https://doi.org/10.1017/S0033583516000172  
    https://www.cambridge.org/core/journals/quarterly-reviews-of-biophysics/article/div-classtitlesecondary-nucleation-of-monomers-on-fibril-surface-dominates-span-classitalicspan-synuclein-aggregation-and-provides-autocatalytic-amyloid-amplificationdiv/36C95  
  • Ricardo Gaspar, Georg Meisl, Alexander K. Buell, Laurie Young, Clemens F. Kaminski, Tuomas P. J.Knowles, Emma Sparr and Sara Linse 
    Secondary nucleation of monomers on fibril surface dominates α- synuclein aggregation and provides autocatalytic amyloid amplification 
    Quart Rev Biophys 50, e6, 1-12 (2017) 
    https://doi.org/10.1017/S0033583516000172  
  • Schartmann E, Schemmert S, Ziehm T, Leithold LHE, Jiang N, Tusche M, Shah NJ, Langen KJ, Kutzsche J, Willbold D, Willuweit A. 
    Comparison of blood-brain barrier penetration efficiencies between linear and cyclic all-d-enantiomeric peptides developed for the treatment of Alzheimer's disease. 
    Eur J Pharm Sci. 17, 0928-0987 (2017) 
    https://doi.org/10.1016/j.ejps.2017.12.005  
    https://www.ncbi.nlm.nih.gov/pubmed/29225107  
  • Steger G 
    Modelling the three-dimensional structure of the right-terminal domain of pospiviroids. 
    Sci. Rep. 7, 711 (2017) 
    http://dx.doi.org/10.1038/s41598-017-00764-x  
  • Steger G, Riesner D, Maurel M-C, Perreault J-P 
    Viroid structure 
    In Viroids and Satellites; Hadidi A, Flores, R, Randles JW, Palukaitis P (eds), Oxford: Academic Press , 63-70 (2017) 
    https://www.elsevier.com/books/viroids-and-satellites/hadidi/978-0-12-801498-1  
  • van Groen T, Schemmert S, Brener O, Gremer L, Ziehm T, Tusche M, Nagel-Steger L, Kadish I, Schartmann E, Elfgen A, Jürgens D, Willuweit A, Kutzsche J, Willbold D. 
    The Aβ oligomer eliminating D-enantiomeric peptide RD2 improves cognition without changing plaque pathology. 
    Sci Rep. 7, 16275 (2017) 
    https://doi.org/10.1038/s41598-017-16565-1  
    https://www.nature.com/articles/s41598-017-16565-1  
  • Vasudevan JAA, Hofmann H, Willbold D, Häussinger D, Koenig BW, Münk C. 
    Enhancing the catalytic deamination activity of APOBEC3C is insufficient to inhibit Vif-deficient HIV-1. 
    J. Mol. Biol. 429, 1171-1191 (2017) 
  • Victor J, Steger G, Riesner D 
    Inability of DNAzymes to cleave RNA in vivo is due to limited Mg2+ concentration in cells 
    Eur Biophys J , (2017) 
    https://doi.org/10.1007/s00249-017-1270-2  
  • Volkov O, Kovalev K, Polovinkin V, Borshchevskiy V, Bamann C, Astashkin R, Marin E, Popov A, Balandin T, Willbold D, Büldt G, Bamberg E, Gordeliy V 
    Structural insights into ion conduction by channelrhodopsin 2 
    Science 358, eaan8862, (2017) 
  • Weiergräber OH, Schwarten M, Strodel B, Willbold D.  
    Investigating Structure and Dynamics of Atg8 Family Proteins. 
    Methods Enzymol. 587, 115-142 (2017) 
  • Wolff M, Zhang-Haagen B, Decker C, Barz B, Schneider M, Biehl R, Radulescu A, Strodel B, Willbold D, Nagel-Steger L 
    Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution 
    Sci Rep 7, 2493 (2017) 
    http://dx.doi.org/10.1038/s41598-017-02370-3  
  • Wördehoff M, Shaykhalishahi H, Groß L, Gremer L, Stoldt M, Buell AK, Willbold D, Hoyer W 
    Opposed effects of dityrosine formation in soluble and aggregated α-synuclein on fibril growth 
    Journal of Molecular Biology , (2017) 
    https://doi.org/10.1016/j.jmb.2017.09.005  
    http://www.sciencedirect.com/science/article/pii/S0022283617304278  
  • Yerabham ASK, Mas PJ, Decker C, Soares DC, Weiergräber OH, Nagel-Steger L, Willbold D, Hart DJ, Bradshaw NJ, Korth C. 
    A structural organization for Disrupted in Schizophrenia 1 protein, identified by high-throughput screening, reveals distinctly folded regions which are bisected by mental illness related mutations.  
    J Biol Chem 292, 6468-6477 (2017) 
    http://dx.doi.org/10.1074/jbc.M116.773903  

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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