Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Marie-Helene Kabbaj"'
Publikováno v:
Autophagy Reports, Vol 2, Iss 1 (2023)
Protein misfolding, aggregation, and accumulation cause neurodegenerative disorders. One such disorder, Huntington’s disease, is caused by an increased number of glutamine-encoding trinucleotide repeats CAG in the first exon of the huntingtin (HTT)
Externí odkaz:
https://doaj.org/article/a5e6406a761c4f5fb9b6fb5f8a0a5d84
Publikováno v:
PLoS Genetics, Vol 17, Iss 5, p e1009592 (2021)
The spindle assembly checkpoint (SAC) prevents anaphase onset in response to chromosome attachment defects, and SAC silencing is essential for anaphase onset. Following anaphase onset, activated Cdc14 phosphatase dephosphorylates the substrates of cy
Externí odkaz:
https://doaj.org/article/0a654c7c0fe94b3d895312070436e9d9
Autor:
Ryan Higgins, Marie-Helene Kabbaj, Delaney Sherwin, Lauren A. Howell, Alexa Hatcher, Robert J. Tomko, Jr., Yanchang Wang
Publikováno v:
Cell Reports, Vol 32, Iss 2, Pp 107898- (2020)
Summary: The accumulation of misfolded proteins is associated with multiple neurodegenerative disorders, but it remains poorly defined how this accumulation causes cytotoxicity. Here, we demonstrate that the Cdc48/p97 segregase machinery drives the c
Externí odkaz:
https://doaj.org/article/64665d8392944950b3c1f13929211b39
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0191490 (2018)
The functionality of a protein depends on its correct folding, but newly synthesized proteins are susceptible to aberrant folding and aggregation. Heat shock proteins (HSPs) function as molecular chaperones that aid in protein folding and the degrada
Externí odkaz:
https://doaj.org/article/eb7c3b585edd40f1a6ca202a0e7f8f4d