Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Annika Hornberger"'
Autor:
Shu Liu, André Hossinger, Stefanie-Elisabeth Heumüller, Annika Hornberger, Oleksandra Buravlova, Katerina Konstantoulea, Stephan A. Müller, Lydia Paulsen, Frederic Rousseau, Joost Schymkowitz, Stefan F. Lichtenthaler, Manuela Neumann, Philip Denner, Ina M. Vorberg
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Pathologic protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells via extracellular vesicles or direct cell-to-cell contact. Here, Liu et al. show that viral glycoproteins can contribute to inte
Externí odkaz:
https://doaj.org/article/3c987601848e42e7821270559f3b20a9
Autor:
Luke J. Fulcher, Thomas Macartney, Polyxeni Bozatzi, Annika Hornberger, Alejandro Rojas-Fernandez, Gopal P. Sapkota
Publikováno v:
Open Biology, Vol 6, Iss 10 (2016)
The von Hippel–Lindau (VHL) protein serves to recruit the hypoxia-inducible factor alpha (HIF1α) protein under normoxia to the CUL2 E3 ubiquitin ligase for its ubiquitylation and degradation through the proteasome. In this report, we modify VHL to
Externí odkaz:
https://doaj.org/article/918e264883224f3ca11632628853105e
Autor:
Shu Liu, Annika Hornberger, Katerina Konstantoulea, Philip Denner, Stefan F. Lichtenthaler, Stefanie-Elisabeth Heumüller, Lydia Paulsen, André Hossinger, Joost Schymkowitz, Frederic Rousseau, Ina Vorberg, Manuela Neumann, Oleksandra Buravlova, Stephan A. Müller
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications 12(1), 5739 (2021). doi:10.1038/s41467-021-25855-2
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications 12(1), 5739 (2021). doi:10.1038/s41467-021-25855-2
Protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells, thereby templating their own aberrant conformation onto soluble homotypic proteins. Proteopathic seeds can be released into the extracellu
Autor:
Manuela Neumann, André Hossinger, Stefan F. Lichtenthaler, Philip Denner, Annika Hornberger, Ina Vorberg, Shu Liu, Oleksandra Buravlova, Stephan A. Müller
SUMMARYPathological protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells, thereby templating their own aberrant conformation onto soluble proteins of the same kind. Proteopathic seeds can be r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e9e1c87efcb9c00bfa539cb49e8d91b
https://doi.org/10.1101/2020.06.26.173070
https://doi.org/10.1101/2020.06.26.173070
Autor:
Shu Liu, Yvonne Duernberger, Katrin Riemschoss, Benedetta Bolognesi, Annika Hornberger, Oleksandra Buravlova, Stephan A. Müller, Lydia Paulsen, Ina Vorberg, Philipp von Eisenhart-Rothe, Stefan F. Lichtenthaler, André Hossinger, Gian Gaetano Tartaglia, Verena Arndt, Sebastian Hogl, Nieves Lorenzo-Gotor
Publikováno v:
Life Science Alliance
Recercat. Dipósit de la Recerca de Catalunya
instname
Life science alliance 2(4), e201800280 (2019). doi:10.26508/lsa.201800280
Recercat. Dipósit de la Recerca de Catalunya
instname
Life science alliance 2(4), e201800280 (2019). doi:10.26508/lsa.201800280
This study provides evidence that exogenous proteinaceous seeds can induce protein aggregates that sequester stress granule components independent of stress granule assembly.
Prions of lower eukaryotes are self-templating protein aggregates that
Prions of lower eukaryotes are self-templating protein aggregates that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::519833838ae0f8065a48060f79452133
http://hdl.handle.net/10230/42509
http://hdl.handle.net/10230/42509
Autor:
Alejandro Rojas-Fernandez, Annika Hornberger, Polyxeni Bozatzi, Gopal P. Sapkota, Luke J. Fulcher, Thomas Macartney
Publikováno v:
Open Biology
Open Biology, Vol 6, Iss 10 (2016)
Open Biology, Vol 6, Iss 10 (2016)
The von Hippel–Lindau (VHL) protein serves to recruit the hypoxia-inducible factor alpha (HIF1α) protein under normoxia to the CUL2 E3 ubiquitin ligase for its ubiquitylation and degradation through the proteasome. In this report, we modify VHL to