Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Sarah M. Prophet"'
Publikováno v:
Biomolecules, Vol 10, Iss 3, p 468 (2020)
Torsin ATPases are members of the AAA+ (ATPases associated with various cellular activities) superfamily of proteins, which participate in essential cellular processes. While AAA+ proteins are ubiquitously expressed and demonstrate distinct subcellul
Externí odkaz:
https://doaj.org/article/f96827af7bb946ac9a6207afa850e93c
Autor:
Sarah M. Prophet, Anthony J. Rampello, Robert F. Niescier, Juliana E. Gentile, Sunanda Mallik, Anthony J. Koleske, Christian Schlieker
Publikováno v:
Nat Cell Biol
DYT1 dystonia is a debilitating neurological movement disorder arising from mutation in the AAA+ ATPase TorsinA. The hallmark of Torsin dysfunction is nuclear envelope blebbing resulting from defects in nuclear pore complex biogenesis. Whether blebs
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 9; Pages: 4627
DYT1 dystonia is a debilitating neurological movement disorder that arises upon Torsin ATPase deficiency. Nuclear envelope (NE) blebs that contain FG-nucleoporins (FG-Nups) and K48-linked ubiquitin are the hallmark phenotype of Torsin manipulation ac
Autor:
Anthony J. Koleske, Christian Schlieker, Anthony J Rampello, Juliana E. Shaw, Robert F. Niescier, Sarah M Prophet
DYT1 dystonia is a highly debilitating neurological movement disorder arising from mutation in the AAA+ ATPase TorsinA. The hallmark of Torsin dysfunction is nuclear envelope blebbing resulting from defects in nuclear pore complex biogenesis. Whether
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::48f933f2b2d4f5f63c0f97ed8eb166b1
https://doi.org/10.1101/2021.10.26.465916
https://doi.org/10.1101/2021.10.26.465916
Autor:
Sarah M, Prophet, Anthony J, Rampello, Robert F, Niescier, Juliana E, Gentile, Sunanda, Mallik, Anthony J, Koleske, Christian, Schlieker
Publikováno v:
Nature cell biology. 24(11)
DYT1 dystonia is a debilitating neurological movement disorder arising from mutation in the AAA+ ATPase TorsinA. The hallmark of Torsin dysfunction is nuclear envelope blebbing resulting from defects in nuclear pore complex biogenesis. Whether blebs
Autor:
Anthony J Rampello, Christian Schlieker, Lin Shao, C. Patrick Lusk, Ethan Laudermilch, Chenguang Zhao, Sarah M Prophet, Nidhi Vishnoi
Publikováno v:
The Journal of Cell Biology
Rampello et al. demonstrate that Torsin ATPases play a critical role in nuclear pore assembly and thus present mechanistic insight into DYT1 dystonia etiology. Moreover, an MLF2-based live-cell imaging platform provides temporally resolved informatio
Autor:
Sarah M Prophet, Christian Schlieker
Publikováno v:
The Journal of clinical investigation. 129(11)
Deciphering novel pathways that regulate liver lipid content has profound implications for understanding the pathophysiology of nonalcoholic fatty liver disease (NAFLD) and nonalcoholic steatohepatitis (NASH). Recent evidence suggests that the nuclea