@misc{AichertStaigerSchulteMaeteretal.2010, author = {Aichert, Ingrid and Staiger, Anja and Schulte-M{\"a}ter, Anne and Becker-Redding, Ulrike and Stahn, Corinna and Peschke, Claudia and Heide, Judith and Ott, Susan and Herrmann, Heike and V{\"o}lsch, Juliane and Mayer, J{\"o}rg and Rohnke, Lucie and Frank, Ulrike and Stadie, Nicole and Jentsch, Nadine and Blech, Anke and Kurtenbach, Stephanie and Thieke, Johanna and Schr{\"o}der, Astrid and Stahn, Corinna and H{\"o}rnig, Robin and Burchert, Frank and De Bleser, Ria and Heister, Julian and Bartels, Luise and W{\"u}rzner, Kay-Michael and B{\"o}hme, Romy and Burmester, Juliane and Krajewski, Melanie and Nager, Wido and Jungeh{\"u}lsing, Gerhard Jan and Wartenburger, Isabell and J{\"o}bges, Michael and Schwilling, Eleonore and Lidzba, Karen and Winkler, Susanne and Konietzko, Andreas and Kr{\"a}geloh-Mann, Ingeborg and Rilling, Eva and Wilken, Rainer and Wismann, Kathrin and Glandorf, Birte and Hoffmann, Hannah and Hinnenkamp, Christiane and Rohlmann, Insa and Ludewigt, Jacqueline and Bittner, Christian and Orlov, Tatjana and Claus, Katrin and Ehemann, Christine and Winnecken, Andreas and Hummel, Katja and Breitenstein, Sarah}, title = {Spektrum Patholinguistik = Schwerpunktthema: Von der Programmierung zur Artikulation : Sprechapraxie bei Kindern und Erwachsenen}, number = {3}, editor = {Wahl, Michael and Stahn, Corinna and Hanne, Sandra and Fritzsche, Tom}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, organization = {Verband f{\"u}r Patholinguistik e. V. (vpl)}, isbn = {978-3-86956-079-3}, issn = {1869-3822}, doi = {10.25932/publishup-4578}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-45470}, year = {2010}, abstract = {Das 3. Herbsttreffen Patholinguistik fand am 21. November 2009 an der Universit{\"a}t Potsdam statt. Der vorliegende Tagungsband enth{\"a}lt die drei Hauptvortr{\"a}ge zum Schwerpunktthema „Von der Programmierung zu Artikulation: Sprechapraxie bei Kindern und Erwachsenen". Dar{\"u}ber hinaus enth{\"a}lt der Band die Beitr{\"a}ge aus dem Spektrum Patholinguistik, sowie die Abstracts der Posterpr{\"a}sentationen.}, language = {de} } @article{SperberWelkePetazzietal.2019, author = {Sperber, Hannah Sabeth and Welke, Robert-William and Petazzi, Roberto Arturo and Bergmann, Ronny and Schade, Matthias and Shai, Yechiel and Chiantia, Salvatore and Herrmann, Andreas and Schwarzer, Roland}, title = {Self-association and subcellular localization of Puumala hantavirus envelope proteins}, series = {Scientific reports}, volume = {9}, journal = {Scientific reports}, publisher = {Nature Publ. Group}, address = {London}, issn = {2045-2322}, doi = {10.1038/s41598-018-36879-y}, pages = {15}, year = {2019}, abstract = {Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number\&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential.}, language = {en} } @article{DunsingLucknerZuehlkeetal.2018, author = {Dunsing, Valentin and Luckner, Madlen and Zuehlke, Boris and Petazzi, Roberto Arturo and Herrmann, Andreas and Chiantia, Salvatore}, title = {Optimal fluorescent protein tags for quantifying protein oligomerization in living cells}, series = {Scientific reports}, volume = {8}, journal = {Scientific reports}, publisher = {Nature Publ. Group}, address = {London}, issn = {2045-2322}, doi = {10.1038/s41598-018-28858-0}, pages = {12}, year = {2018}, abstract = {Fluorescence fluctuation spectroscopy has become a popular toolbox for non-disruptive analysis of molecular interactions in living cells. The quantification of protein oligomerization in the native cellular environment is highly relevant for a detailed understanding of complex biological processes. An important parameter in this context is the molecular brightness, which serves as a direct measure of oligomerization and can be easily extracted from temporal or spatial fluorescence fluctuations. However, fluorescent proteins (FPs) typically used in such studies suffer from complex photophysical transitions and limited maturation, inducing non-fluorescent states. Here, we show how these processes strongly affect molecular brightness measurements. We perform a systematic characterization of non-fluorescent states for commonly used FPs and provide a simple guideline for accurate, unbiased oligomerization measurements in living cells. Further, we focus on novel red FPs and demonstrate that mCherry2, an mCherry variant, possesses superior properties with regards to precise quantification of oligomerization.}, language = {en} } @article{GoetzSuopankiSchuleretal.2005, author = {Goetz, C. and Suopanki, J. and Schuler, Benjamin and Wanker, E. and Herrmann, Andreas}, title = {Perturbation of brain lipid membrane by soluble Huntingtin depends on its polyproline tract}, issn = {0006-3495}, year = {2005}, language = {en} } @inproceedings{TavangarianSchroederIgeletal.2013, author = {Tavangarian, Djamshid and Schroeder, Ulrik and Igel, Christoph and Magenheim, Johannes and Kundisch, Dennis and Beutner, Marc and Herrmann, Philipp and Whittaker, Michael and Reinhardt, Wolfgang and Zoyke, Andrea and Elbeshausen, Stefanie and Griesbaum, Joachim and Koelle, Ralph and Kneiphoff, Anika Hanna and Mauch, Martina and H{\"u}bner, Sandra and Walter, Satjawan and Dittler, Ullrich and Baumann, Annette and Reeh, Lucas and Beuster, Liane and Elkina, Margarita and Fortenbacher, Albrecht and Kappe, Leonard and Merceron, Agathe and Pursian, Andreas and Schwarzrock, Sebastian and Wenzlaff, Boris and Hilse, Michael and Lucke, Ulrike}, title = {E-Learning Symposium 2012}, editor = {Lucke, Ulrike}, publisher = {Universit{\"a}tsverlag Potsdam}, address = {Potsdam}, doi = {10.25932/publishup-6162}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-62661}, pages = {77}, year = {2013}, abstract = {Dieser Tagungsband beinhaltet die auf dem E-Learning Symposium 2012 an der Universit{\"a}t Potsdam vorgestellten Beitr{\"a}ge zu aktuellen Anwendungen, innovativen Prozesse und neuesten Ergebnissen im Themenbereich E-Learning. Lehrende, E-Learning-Praktiker und -Entscheider tauschten ihr Wissen {\"u}ber etablierte und geplante Konzepte im Zusammenhang mit dem Student-Life-Cycle aus. Der Schwerpunkt lag hierbei auf der unmittelbaren Unterst{\"u}tzung von Lehr- und Lernprozessen, auf Pr{\"a}sentation, Aktivierung und Kooperation durch Verwendung von neuen und etablierten Technologien.}, language = {de} } @article{RistowHerrmannIlligetal.2006, author = {Ristow, Michael and Herrmann, Andreas and Illig, Hubert and Klemm, Gunther and Kummer, Volker and Kl{\"a}ge, Hans-Christian and Machatzi, Bernd and Raetzel, Stefan and Schwarz, R. and Zimmermann, Friedrich}, title = {Liste und Rote Liste der etablierten Gef{\"a}ßpflanzen Brandenburgs}, year = {2006}, language = {de} } @article{MemczakLausterKaretal.2016, author = {Memczak, Henry and Lauster, Daniel and Kar, Parimal and Di Lella, Santiago and Volkmer, Rudolf and Knecht, Volker and Herrmann, Andreas and Ehrentreich-Foerster, Eva and Bier, Frank Fabian and Stoecklein, Walter F. M.}, title = {Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding}, series = {PLoS one}, volume = {11}, journal = {PLoS one}, publisher = {PLoS}, address = {San Fransisco}, issn = {1932-6203}, doi = {10.1371/journal.pone.0159074}, pages = {82 -- 90}, year = {2016}, abstract = {Antibodies against spike proteins of influenza are used as a tool for characterization of viruses and therapeutic approaches. However, development, production and quality control of antibodies is expensive and time consuming. To circumvent these difficulties, three peptides were derived from complementarity determining regions of an antibody heavy chain against influenza A spike glycoprotein. Their binding properties were studied experimentally, and by molecular dynamics simulations. Two peptide candidates showed binding to influenza A/Aichi/2/68 H3N2. One of them, termed PeB, with the highest affinity prevented binding to and infection of target cells in the micromolar region without any cytotoxic effect. PeB matches best the conserved receptor binding site of hemagglutinin. PeB bound also to other medical relevant influenza strains, such as human-pathogenic A/California/7/2009 H1N1, and avian-pathogenic A/MuteSwan/Rostock/R901/2006 H7N1. Strategies to improve the affinity and to adapt specificity are discussed and exemplified by a double amino acid substituted peptide, obtained by substitutional analysis. The peptides and their derivatives are of great potential for drug development as well as biosensing.}, language = {en} } @misc{MemczakLausterKaretal.2016, author = {Memczak, Henry and Lauster, Daniel and Kar, Parimal and Di Lella, Santiago and Volkmer, Rudolf and Knecht, Volker and Herrmann, Andreas and Ehrentreich-F{\"o}rster, Eva and Bier, Frank Fabian and St{\"o}cklein, Walter F. M.}, title = {Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding}, series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, journal = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, number = {536}, issn = {1866-8372}, doi = {10.25932/publishup-41087}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-410872}, pages = {24}, year = {2016}, abstract = {Antibodies against spike proteins of influenza are used as a tool for characterization of viruses and therapeutic approaches. However, development, production and quality control of antibodies is expensive and time consuming. To circumvent these difficulties, three peptides were derived from complementarity determining regions of an antibody heavy chain against influenza A spike glycoprotein. Their binding properties were studied experimentally, and by molecular dynamics simulations. Two peptide candidates showed binding to influenza A/Aichi/2/68 H3N2. One of them, termed PeB, with the highest affinity prevented binding to and infection of target cells in the micromolar region without any cytotoxic effect. PeB matches best the conserved receptor binding site of hemagglutinin. PeB bound also to other medical relevant influenza strains, such as human-pathogenic A/California/7/2009 H1N1, and avian-pathogenic A/MuteSwan/Rostock/R901/2006 H7N1. Strategies to improve the affinity and to adapt specificity are discussed and exemplified by a double amino acid substituted peptide, obtained by substitutional analysis. The peptides and their derivatives are of great potential for drug development as well as biosensing.}, language = {en} } @inproceedings{MemczakLausterHerrmannetal.2013, author = {Memczak, Henry and Lauster, Daniel and Herrmann, Andreas and St{\"o}cklein, Walter F. M. and Bier, Frank Fabian}, title = {Novel hemagglutinin-binding peptides for biosensing and inhibition of Influenza Viruses}, series = {Biopolymers}, volume = {100}, booktitle = {Biopolymers}, number = {3}, publisher = {Wiley-Blackwell}, address = {Hoboken}, issn = {0006-3525}, pages = {255 -- 255}, year = {2013}, language = {en} } @article{GrimmMeyerCzaplaetal.2013, author = {Grimm, Christiane and Meyer, Thomas and Czapla, Sylvia and Nikolaus, J{\"o}rg and Scheidt, Holger A. and Vogel, Alexander and Herrmann, Andreas and Wessig, Pablo and Huster, Daniel and M{\"u}ller, Peter}, title = {Structure and dynamics of molecular rods in membranes application of a Spin-Labeled rod}, series = {Chemistry - a European journal}, volume = {19}, journal = {Chemistry - a European journal}, number = {8}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {0947-6539}, doi = {10.1002/chem.201202500}, pages = {2703 -- 2710}, year = {2013}, abstract = {Molecular rods consisting of a hydrophobic backbone and terminally varying functional groups have been synthesized for applications for the functionalization of membranes. In the present study, we employ a spin-labeled analogue of a recently described new class of molecular rods to characterize their dynamic interactions with membranes. By using the different approaches of ESR and NMR spectroscopy, we show that the spin moiety of the membrane-embedded spin-labeled rod is localized in the upper chain/glycerol region of membranes of different compositions. The rod is embedded within the membrane in a tilted orientation to adjust for the varying hydrophobic thicknesses of these bilayers. This orientation does not perturb the membrane structure. The water solubility of the rod is increased significantly in the presence of certain cyclodextrins. These cyclodextrins also allow the rods to be extracted from the membrane and incorporated into preformed membranes. The latter will improve the future applications of these rods in cellular systems as stable membrane-associated anchors for the functionalization of membrane surfaces.}, language = {en} }