Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Thomas Wiglenda"'
Autor:
Antonia Nicole Klein, Tamar Ziehm, Markus Tusche, Johan Buitenhuis, Dirk Bartnik, Annett Boeddrich, Thomas Wiglenda, Erich Wanker, Susanne Aileen Funke, Oleksandr Brener, Lothar Gremer, Janine Kutzsche, Dieter Willbold
Publikováno v:
PLoS ONE, Vol 11, Iss 4, p e0153035 (2016)
The aggregation of amyloid-β (Aβ) is postulated to be the crucial event in Alzheimer's disease (AD). In particular, small neurotoxic Aβ oligomers are considered to be responsible for the development and progression of AD. Therefore, elimination of
Externí odkaz:
https://doaj.org/article/083680e70c82443787f8e0d46841487d
Autor:
Annett Böddrich, Domenico Rizzo, Iryna Benilova, Bettina Purfürst, Sara Bologna, Claudio Luchinat, Linda Cerofolini, Bart De Strooper, Leonardo Gonnelli, Gianluca Gallo, Erich E. Wanker, Marco Fragai, Thomas Wiglenda, Enrico Ravera, Magdalena Korsak
Publikováno v:
Chemical Communications
Recent structural studies show distinct morphologies for the fibrils of Aβ(1-42) and Aβ(1-40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1 : 1 mixed fibrillar species, which differs from both pure fibri
Autor:
Thomas, Wiglenda, Nicole, Groenke, Waldemar, Hoffmann, Christian, Manz, Lisa, Diez, Alexander, Buntru, Lydia, Brusendorf, Nancy, Neuendorf, Sigrid, Schnoegl, Christian, Haenig, Peter, Schmieder, Kevin, Pagel, Erich E, Wanker
Publikováno v:
Journal of molecular biology. 432(7)
The self-assembly of the 42-residue amyloid-β peptide, Aβ42, into fibrillar aggregates is associated with neuronal dysfunction and toxicity in Alzheimer's disease (AD) patient brains, suggesting that small molecules acting on this process might int
Autor:
Nancy Neuendorf, Miguel A. Andrade-Navarro, Nicole Groenke, Erich E. Wanker, David P. Wolfer, Eric Blanc, Sigrid Schnoegl, Wilfried Nietfeld, Christian Erck, Elisabetta Vannoni, Dieter Beule, Christian Haenig, Beate Friedrich, Annett Boeddrich, Julius Tachu Babila, Henrik Martens, Manuela Jacob, Alexander Buntru, Jochen C. Meier, Thomas Wiglenda, Maarten Loos, Lisa Diez, Matthew R. Huska
Self-propagating amyloid-β (Aβ) aggregates or seeds possibly drive pathogenesis of Alzheimer's disease (AD). Small molecules targeting such structures might act therapeutically in vivo. Here, a fluorescence polarization assay was established that e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86a69b46279601dc0db4c44c0dadefcc
https://www.zora.uzh.ch/id/eprint/159044/
https://www.zora.uzh.ch/id/eprint/159044/
Autor:
Diana Flores-Dominguez, Alina Dagane, Judith Schilling, Nelli Blank, Sybille Krauss, Ina Vorberg, Erich E. Wanker, Frank Matthes, Moritz M. Hettich, Hanna Wolf, Dan Ehninger, Gunnar Dittmar, Stephanie Weber, Alexander Buntru, Thomas Wiglenda
Publikováno v:
Cell Death Discovery
Cell death discovery 4(1), 4 (2018). doi:10.1038/s41420-017-0003-8
Cell Death Discovery, Vol 4, Iss 1, Pp 1-19 (2018)
Cell death discovery 4(1), 4 (2018). doi:10.1038/s41420-017-0003-8
Cell Death Discovery, Vol 4, Iss 1, Pp 1-19 (2018)
Alzheimer’s disease (AD) is characterized by two neuropathological hallmarks: senile plaques, which are composed of amyloid-β (Aβ) peptides, and neurofibrillary tangles, which are composed of hyperphosphorylated tau protein. Aβ peptides are deri
Autor:
Steffen, Goerke, Katharina S, Milde, Raul, Bukowiecki, Patrick, Kunz, Karel D, Klika, Thomas, Wiglenda, Axel, Mogk, Erich E, Wanker, Bernd, Bukau, Mark E, Ladd, Peter, Bachert, Moritz, Zaiss
Publikováno v:
NMR in biomedicine. 30(1)
Chemical exchange saturation transfer (CEST) is an MRI technique that allows mapping of biomolecules (small metabolites, proteins) with nearly the sensitivity of conventional water proton MRI. In living organisms, several tissue-specific CEST effects
Autor:
Juan Miguel López del Amo, Ronald Frank, Bernd Reif, Marcus Fändrich, Björn Grüning, Stefan Günther, Jan Bieschke, Erich E. Wanker, Michael Schmidt, Franziska Schiele, Annett Boeddrich, Thomas Wiglenda, Qinwen Wang, Roger Anwyl, Rudi Lurz, Daniela Kleckers, Sigrid Schnoegl, Dominic M. Walsh, Ralf P. Friedrich, Martin Herbst
Publikováno v:
Nature Chemical Biology; Vol 8
Nature Chemical Biology
Nature Chemical Biology
Several lines of evidence indicate that prefibrillar assemblies of amyloid-β (Aβ) polypeptides, such as soluble oligomers or protofibrils, rather than mature, end-stage amyloid fibrils cause neuronal dysfunction and memory impairment in Alzheimer's
Autor:
Yacine Bounab, Gillian P. Bates, Ralf P. Friedrich, David Fournier, Josef Priller, Miguel A. Andrade-Navarro, Konrad Klockmeier, Christian Haenig, Matthias E. Futschik, Franziska Hesse, Sean Patrick Riechers, Erich E. Wanker, Stephan J. Sigrist, Sargon Yigit, Martin Stroedicke, Nadine U. Strempel, Michael R. Hayden, Rona K. Graham, Sigrid Schnoegl, Annett Boeddrich, Shuang Li, Jenny Russ, Thomas Wiglenda, Cecilia Nicoletti, Gautam Chaurasia
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Assemblies of huntingtin (HTT) fragments with expanded polyglutamine (polyQ) tracts are a pathological hallmark of Huntington's disease (HD). The molecular mechanisms by which these structures are formed and cause neuronal dysfunction and toxicity ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11b6410b3bf5fa81355c1008e6a41ee2
https://hdl.handle.net/10400.1/11700
https://hdl.handle.net/10400.1/11700
Publikováno v:
Helvetica Chimica Acta. 89:598-613
Triplex-forming oligonucleotides (TFOs) containing 9-deazaguanine N7-(2′-deoxyribonucleoside) 1a and halogenated derivatives 1b,c were synthesized employing solid-phase oligonucleotide synthesis. For that purpose, the phosphoramidite building block
Autor:
Ronald Gust, Ingo Ott, Petra Schumacher, Thierry Langer, Brigitte Kircher, Daniela Schuster, Thomas Wiglenda
Publikováno v:
Journal of Medicinal Chemistry. 48:6516-6521
The 1H-imidazoles 7a-e were synthesized and tested for biological activity in vitro. The results pointed to a clear structure-activity relationship. The introduction of an ethyl chain at C5 of the 1,2,4-tris(4-hydroxyphenyl)-1H-imidazole 7a caused ho