Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Christian Haenig"'
Autor:
Annett Boeddrich, Christian Haenig, Nancy Neuendorf, Eric Blanc, Andranik Ivanov, Marieluise Kirchner, Philipp Schleumann, Irem Bayraktaroğlu, Matthias Richter, Christine Mirjam Molenda, Anje Sporbert, Martina Zenkner, Sigrid Schnoegl, Christin Suenkel, Luisa-Sophie Schneider, Agnieszka Rybak-Wolf, Bianca Kochnowsky, Lauren M. Byrne, Edward J. Wild, Jørgen E. Nielsen, Gunnar Dittmar, Oliver Peters, Dieter Beule, Erich E. Wanker
Publikováno v:
Genome Medicine, Vol 15, Iss 1, Pp 1-32 (2023)
Abstract Background Alzheimer’s disease (AD) is characterized by the intra- and extracellular accumulation of amyloid-β (Aβ) peptides. How Aβ aggregates perturb the proteome in brains of patients and AD transgenic mouse models, remains largely u
Externí odkaz:
https://doaj.org/article/84f66523eef540e7aa35e8b03a0fbf0e
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:
Stephanie Plassmann, Juan Manuel Ramírez-Anguita, Annett Boeddrich, Elsa Sanchez-Garcia, Jana Wolf, Erich E. Wanker, Kenny Bravo-Rodriguez, Nadine U. Strempel, Antonio Z. Politi, Anne Ast, Konrad Klockmeier, Katharina Baum, Alexander Buntru, Anne S. Wagner, Christian Haenig, Lydia Brusendorf
Huntingtin (HTT) fragments with extended polyglutamine (polyQ) tracts self-assemble into amyloid-like fibrillar aggregates. Elucidating the fibril formation mechanism is critical for understanding Huntington’s disease pathology and for developing n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72958ae99f7a7d477ada0313341725a6
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=85045543107
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=85045543107
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
Autor:
Eberhard Scherzinger, Claudia Abraham, Stephanie Waelter, Martin Stroedicke, Christian Haenig, Anja Droege, Erich E. Wanker, Renate Hasenbank, Sarah H. Coleman, Anja Fritzsche, Hans Lehrach, Jaana Suopanki, Katrin S. Lindenberg, Ulrich Stelzl, Heike Goehler, Bernhard Landwehrmeyer, Bianca Bauer, Uwe Worm, Maciej Lalowski, Martin Herbst, Andreas H. Ludewig, Maria Knoblich, Claire-Anne Gutekunst, Konrad Buessow
Publikováno v:
Molecular Cell. 15:853-865
Analysis of protein-protein interactions (PPIs) is a valuable approach for characterizing proteins of unknown function. Here, we have developed a strategy combining library and matrix yeast two-hybrid screens to generate a highly connected PPI networ
Autor:
Walter Birchmeier, Felix H. Brembeck, Martin Stroedicke, Sylvia Krobitsch, Jan Timm, Martina Zenkner, Bernhard Korn, Nicole Bock, Anja Droege, Erich E. Wanker, Uwe Worm, Christian Haenig, Susanne Koeppen, Engin Toksöz, Maciej Lalowski, Claudia Abraham, Hans Lehrach, Anke Schoenherr, Sascha Mintzlaff, Astrid Goedde, Heike Goehler, Ulrich Stelzl, Silvia Kietzmann
Publikováno v:
Cell
SummaryProtein-protein interaction maps provide a valuable framework for a better understanding of the functional organization of the proteome. To detect interacting pairs of human proteins systematically, a protein matrix of 4456 baits and 5632 prey