Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Claudia Scheckel"'
Publikováno v:
eLife, Vol 9 (2020)
Prion diseases are caused by PrPSc, a self-replicating pathologically misfolded protein that exerts toxicity predominantly in the brain. The administration of PrPSc causes a robust, reproducible and specific disease manifestation. Here, we have appli
Externí odkaz:
https://doaj.org/article/de672fd344864dc7a7212250e349b3e5
Autor:
Silvia Sorce, Mario Nuvolone, Giancarlo Russo, Andra Chincisan, Daniel Heinzer, Merve Avar, Manuela Pfammatter, Petra Schwarz, Mirzet Delic, Micha Müller, Simone Hornemann, Despina Sanoudou, Claudia Scheckel, Adriano Aguzzi
Publikováno v:
PLoS Pathogens, Vol 16, Iss 6, p e1008653 (2020)
The clinical course of prion diseases is accurately predictable despite long latency periods, suggesting that prion pathogenesis is driven by precisely timed molecular events. We constructed a searchable genome-wide atlas of mRNA abundance and splici
Externí odkaz:
https://doaj.org/article/3378ce74ef8f40b7a548373f25fdab25
Autor:
Anna Henzi, Assunta Senatore, Asvin K K Lakkaraju, Claudia Scheckel, Jonas Mühle, Regina Reimann, Silvia Sorce, Gebhard Schertler, Klaus V Toyka, Adriano Aguzzi
Publikováno v:
PLoS ONE, Vol 15, Iss 11, p e0242137 (2020)
The adhesion G-protein coupled receptor Adgrg6 (formerly Gpr126) is instrumental in the development, maintenance and repair of peripheral nervous system myelin. The prion protein (PrP) is a potent activator of Adgrg6 and could be used as a potential
Externí odkaz:
https://doaj.org/article/95263374d6fd48b09546525b07214cbc
Autor:
Claudia Scheckel, Elodie Drapeau, Maria A Frias, Christopher Y Park, John Fak, Ilana Zucker-Scharff, Yan Kou, Vahram Haroutunian, Avi Ma'ayan, Joseph D Buxbaum, Robert B Darnell
Publikováno v:
eLife, Vol 5 (2016)
Neuronal ELAV-like (nELAVL) RNA binding proteins have been linked to numerous neurological disorders. We performed crosslinking-immunoprecipitation and RNAseq on human brain, and identified nELAVL binding sites on 8681 transcripts. Using knockout mic
Externí odkaz:
https://doaj.org/article/f8f66784b59a431fa82b2f6d7b921ab3
Publikováno v:
PLoS Genetics, Vol 8, Iss 5, p e1002742 (2012)
Translational repression is often accompanied by mRNA degradation. In contrast, many mRNAs in germ cells and neurons are "stored" in the cytoplasm in a repressed but stable form. Unlike repression, the stabilization of these mRNAs is surprisingly lit
Externí odkaz:
https://doaj.org/article/ab21effbb14049828fb6f79586bdccbb
Autor:
Valeria Eckhardt, Claudia Scheckel, Marc Emmenegger, Daniel Patrick Pease, Ioannis Xenarios, Elke Schaper, Adriano Aguzzi
Publikováno v:
Brain Pathology. 29:232-244
The cellular prion protein (PrPC ) is best known for its misfolded disease-causing conformer, PrPS c . Because the availability of PrPC is often limiting for prion propagation, understanding its regulation may point to possible therapeutic targets. W
Publikováno v:
eLife
eLife, Vol 9 (2020)
eLife, Vol 9 (2020)
Prion diseases are caused by PrPSc, a self-replicating pathologically misfolded protein that exerts toxicity predominantly in the brain. The administration of PrPSc causes a robust, reproducible and specific disease manifestation. Here, we have appli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c859b17c6b41b75541b5db79c32ecf06
https://doi.org/10.5167/uzh-190429
https://doi.org/10.5167/uzh-190429
Dimeric prion protein ligand activates Adgrg6 but does not rescue myelinopathy of PrP-deficient mice
Autor:
Silvia Sorce, Asvin K. K. Lakkaraju, Claudia Scheckel, Assunta Senatore, Anna Henzi, Jonas Mühle, Gebhard F. X. Schertler, Adriano Aguzzi, Regina Reimann, Klaus V. Toyka
The adhesion G-protein coupled receptor Adgrg6 (formerly Gpr126) is instrumental in the development, maintenance and repair of peripheral nervous system myelin. The prion protein (PrP) is a potent activator of Adgrg6 and could be used as a potential
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fa547761a38742d0d4f5bc80ebd60d73
https://doi.org/10.1101/2020.07.07.191452
https://doi.org/10.1101/2020.07.07.191452