Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Nicolette A. Ender"'
Autor:
Phillip R. Woolley, Xuemei Wen, Olivia M. Conway, Nicolette A. Ender, Ji-Hoon Lee, Tanya T. Paull
Publikováno v:
Cell Reports, Vol 43, Iss 3, Pp 113896- (2024)
Summary: The ataxia telangiectasia mutated (ATM) protein kinase is a master regulator of the DNA damage response and also an important sensor of oxidative stress. Analysis of gene expression in ataxia-telangiectasia (A-T) patient brain tissue shows t
Externí odkaz:
https://doaj.org/article/6b926ebf0e18404b93723ed8d502abf8
Autor:
Seung W Ryu, Rose Stewart, D Chase Pectol, Nicolette A Ender, Oshadi Wimalarathne, Ji-Hoon Lee, Carlos P Zanini, Antony Harvey, Jon M Huibregtse, Peter Mueller, Tanya T Paull
Publikováno v:
PLoS Biology, Vol 18, Iss 7, p e3000606 (2020)
The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protection from stress-induced misfolding and aggregation of polypeptides in most organisms and are responsible for promoting the stability, folding, and degradation of
Externí odkaz:
https://doaj.org/article/316dda2e58104b5c83edc6755636be78
Autor:
Antony Harvey, Oshadi Wimalarathne, Peter R. Mueller, Rose Stewart, Ji-Hoon Lee, Tanya T. Paull, Jon M. Huibregtse, Carlos P. Zanini, Nicolette A. Ender, Seung Woo Ryu, Chase Pectol
The HSP70 family of chaperones are the front-line of protection from stress-induced misfolding and aggregation of polypeptides in most organisms and are responsible for promoting the stability, folding, and degradation of clients to maintain cellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0912db619440b04a5eb19a7c083e2e5b
https://doi.org/10.1101/865030
https://doi.org/10.1101/865030
Publikováno v:
Molecular Cell. 81:1515-1533.e5
SummaryLoss of the ataxia-telangiectasia mutated (ATM) kinase causes cerebellum-specific neurodegeneration in humans. We previously demonstrated that deficiency in ATM activation via oxidative stress generates high levels of insoluble protein aggrega
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e413b38fae8d3129169deeaa0117bae1
https://doi.org/10.1016/j.molcel.2021.01.019
https://doi.org/10.1016/j.molcel.2021.01.019
Autor:
Rose Stewart, Antony Harvey, Oshadi Wimalarathne, Tanya T. Paull, Ji-Hoon Lee, Peter R. Mueller, Seung Woo Ryu, Jon M. Huibregtse, Nicolette A. Ender, D Chase Pectol, Carlos P. Zanini
Publikováno v:
PLoS Biology
PLoS Biology, Vol 18, Iss 7, p e3000606 (2020)
PLoS Biology, Vol 18, Iss 7, p e3000606 (2020)
The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protection from stress-induced misfolding and aggregation of polypeptides in most organisms and are responsible for promoting the stability, folding, and degradation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3eb869ce8e21bfbef439eba196b42989
https://doi.org/10.1371/journal.pbio.3000606
https://doi.org/10.1371/journal.pbio.3000606