Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Rana Dilara Incebacak Eltemur"'
Autor:
Priscila Pereira Sena, Jonasz Jeremiasz Weber, Sercan Bayezit, Rafael Saup, Rana Dilara Incebacak Eltemur, Xiaoling Li, Ana Velic, Jaqueline Jung, Boris Macek, Huu Phuc Nguyen, Olaf Riess, Thorsten Schmidt
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 16 (2023)
Lysine residues are one of the main sites for posttranslational modifications of proteins, and lysine ubiquitination of the Machado-Joseph disease protein ataxin-3 is implicated in its cellular function and polyglutamine expansion-dependent toxicity.
Externí odkaz:
https://doaj.org/article/ab398446675b41ffa6299a6e3522a89b
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 15 (2022)
Among posttranslational modifications, directed proteolytic processes have the strongest impact on protein integrity. They are executed by a variety of cellular machineries and lead to a wide range of molecular consequences. Compared to other forms o
Externí odkaz:
https://doaj.org/article/d73f02fd395b4896a1b7ffd8fc9ceb68
Autor:
Jonasz Jeremiasz Weber, Stefanie Cari Anger, Priscila Pereira Sena, Rana Dilara Incebacak Eltemur, Chrisovalantou Huridou, Florian Fath, Caspar Gross, Nicolas Casadei, Olaf Riess, Huu Phuc Nguyen
Publikováno v:
A: Pathogenic mechanisms.
Autor:
Jonasz Jeremiasz Weber, Stefanie Cari Anger, Priscila Pereira Sena, Rana Dilara Incebacak Eltemur, Chrisovalantou Huridou, Florian Fath, Caspar Gross, Nicolas Casadei, Olaf Riess, Huu Phuc Nguyen
Publikováno v:
Cellular and Molecular Life Sciences. 79
Spinocerebellar ataxia type 17 (SCA17) is a neurodegenerative disease caused by a polyglutamine-encoding trinucleotide repeat expansion in the gene of transcription factor TATA box-binding protein (TBP). While its underlying pathomechanism is elusive