Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Alexander Buntru"'
Autor:
Philipp Trepte, Sabrina Kruse, Simona Kostova, Sheila Hoffmann, Alexander Buntru, Anne Tempelmeier, Christopher Secker, Lisa Diez, Aline Schulz, Konrad Klockmeier, Martina Zenkner, Sabrina Golusik, Kirstin Rau, Sigrid Schnoegl, Craig C Garner, Erich E Wanker
Publikováno v:
Molecular Systems Biology, Vol 14, Iss 7, Pp 1-20 (2018)
Abstract Information on protein–protein interactions (PPIs) is of critical importance for studying complex biological systems and developing therapeutic strategies. Here, we present a double‐readout bioluminescence‐based two‐hybrid technology
Externí odkaz:
https://doaj.org/article/6a2435b9498b4222843c1f79d478cf6f
Autor:
Christopher Secker, Angelika Y. Motzny, Simona Kostova, Alexander Buntru, Lucas Helmecke, Laura Reus, Robert Steinfort, Lydia Brusendorf, Annett Boeddrich, Nancy Neuendorf, Lisa Diez, Peter Schmieder, Aline Schulz, Constantin Czekelius, Erich E. Wanker
Publikováno v:
Journal of Neurochemistry.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::641a47457871028f637027ea07e53870
https://doi.org/10.1111/jnc.15842
https://doi.org/10.1111/jnc.15842
Autor:
Barbara Mlody, Josef Priller, Manuel Iburg, Janine Kirstein, Alexander Buntru, Maria Lucia Pigazzini, Katrin Juenemann, Anne Ast, Alessandro Prigione, Erich E. Wanker, Annika Scior, Kristin Arnsburg, Dmytro Puchkov
Publikováno v:
EMBO J
Huntington9s disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin gene ( HTT ). Molecular chaperones have been implicated in suppressing or delaying the aggregation of mutant Htt. Using in vitr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::454bf88c184e1f306444a067dbf67a0b
https://doi.org/10.15252/embj.2021109413
https://doi.org/10.15252/embj.2021109413
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::daf7796ce544bbd001f55a5b056d0b65
https://pubmed.ncbi.nlm.nih.gov/32061932
https://pubmed.ncbi.nlm.nih.gov/32061932
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:
Kirstin Rau, Sabrina Kruse, Craig C. Garner, Sabrina Golusik, Martina Zenkner, Simona Kostova, Erich E. Wanker, Sheila Hoffmann, Aline Schulz, Christopher Secker, Anne Tempelmeier, Konrad Klockmeier, Philipp Trepte, Alexander Buntru, Sigrid Schnoegl, Lisa Diez
Publikováno v:
Molecular systems biology 14(7), e8071 (2018). doi:10.15252/msb.20178071
Molecular Systems Biology
Molecular Systems Biology
Information on protein–protein interactions (PPIs) is of critical importance for studying complex biological systems and developing therapeutic strategies. Here, we present a double‐readout bioluminescence‐based two‐hybrid technology, termed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ea7927e62de6c0b937b1ca46d16ec18
http://edoc.mdc-berlin.de/17591/1/17591oa.pdf
http://edoc.mdc-berlin.de/17591/1/17591oa.pdf
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1780
N-terminal mutant huntingtin (mHTT) fragments with pathogenic polyglutamine (polyQ) tracts spontaneously form stable, amyloidogenic protein aggregates with a fibrillar morphology. Such structures are detectable in brains of Huntington's disease (HD)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cc873855c55e441d0745cd10dea06942
https://pubmed.ncbi.nlm.nih.gov/29856013
https://pubmed.ncbi.nlm.nih.gov/29856013
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
Publikováno v:
Methods in Molecular Biology ISBN: 9781493978243
N-terminal mutant huntingtin (mHTT) fragments with pathogenic polyglutamine (polyQ) tracts spontaneously form stable, amyloidogenic protein aggregates with a fibrillar morphology. Such structures are detectable in brains of Huntington's disease (HD)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77c58ee940c3fd154409309e4839ca97
https://doi.org/10.1007/978-1-4939-7825-0_3
https://doi.org/10.1007/978-1-4939-7825-0_3
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c41aed3ff0e3a0bfa0e0ed3090c0528a
https://pubmed.ncbi.nlm.nih.gov/29531801
https://pubmed.ncbi.nlm.nih.gov/29531801