Zobrazeno 1 - 10
of 124
pro vyhledávání: '"SIT4"'
Autor:
Telma S. Martins, Miguel Correia, Denise Pinheiro, Carolina Lemos, Marta Vaz Mendes, Clara Pereira, Vítor Costa
Publikováno v:
Cells, Vol 13, Iss 8, p 655 (2024)
The Sit4 protein phosphatase plays a key role in orchestrating various cellular processes essential for maintaining cell viability during aging. We have previously shown that SIT4 deletion promotes vacuolar acidification, mitochondrial derepression,
Externí odkaz:
https://doaj.org/article/61fe05bfd68e4f5db6a4daf7bbe62a24
Akademický článek
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Autor:
Francisca Randez-Gil, Lino Bojunga, Francisco Estruch, Joris Winderickx, Maurizio Del Poeta, Jose A. Prieto
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 8 (2020)
Hyperphosphorylation of protein tau is a hallmark of Alzheimer’s disease (AD). Changes in energy and lipid metabolism have been correlated with the late onset of this neurological disorder. However, it is uncertain if metabolic dysregulation is a c
Externí odkaz:
https://doaj.org/article/c86081aa29014a8d99917c9d39db9ed6
Publikováno v:
Frontiers in Microbiology, Vol 10 (2019)
PP2A-like phosphatases share high homology with PP2A enzymes and are composed of a catalytic subunit and a regulatory subunit. In Candida albicans, the PP2A-like catalytic subunit SIT4 regulates cell growth, morphogenesis, and virulence. However, the
Externí odkaz:
https://doaj.org/article/1e04bbc5e39d45f0a18eecc8018c59bf
Publikováno v:
Microbial Cell, Vol 1, Iss 12, Pp 416-424 (2014)
Previous work in yeast has suggested that modification of tRNAs, in particular uridine bases in the anticodon wobble position (U34), is linked to TOR (target of rapamycin) signaling. Hence, U34 modification mutants were found to be hypersensitive to
Externí odkaz:
https://doaj.org/article/98092d59c1704f1aa9026d421e1f8202
Autor:
Bruno Leonardo Bozaquel-Morais, Leonie Vogt, Valentina D’Angelo, Raffael Schaffrath, Roland Klassen, Mónica Montero-Lomelí
Publikováno v:
Biomolecules, Vol 8, Iss 3, p 49 (2018)
The protein phosphatase Sit4 has been shown to be required for lipogenesis and resistance against the acetyl-CoA carboxylase inhibitor soraphen A. Since Sit4 is also required for biosynthesis of Elongator dependent tRNA modifications such as 5-methox
Externí odkaz:
https://doaj.org/article/13b57e4a55c642baa2db95a833a248c0
Akademický článek
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Autor:
Maurizio Del Poeta, Lino Bojunga, Joris Winderickx, Jose Antonio Prieto, Francisca Randez-Gil, Francisco Estruch
Publikováno v:
Frontiers in Cell and Developmental Biology
Digital.CSIC. Repositorio Institucional del CSIC
instname
Rández-Gil, Francisca Bojunga, Lino Estruch Ros, Francisco Winderickx, Joris Del Poeta, Maurizio Prieto Alamán, José Antonio 2020 Sphingolipids and inositol phosphates regulate the tau protein phosphorylation status in humanized yeast Frontiers In Cell And Developmental Biology 8 592159
RODERIC. Repositorio Institucional de la Universitat de Valéncia
Frontiers in Cell and Developmental Biology, Vol 8 (2020)
RODERIC: Repositorio Institucional de la Universitat de Valéncia
Digital.CSIC. Repositorio Institucional del CSIC
instname
Rández-Gil, Francisca Bojunga, Lino Estruch Ros, Francisco Winderickx, Joris Del Poeta, Maurizio Prieto Alamán, José Antonio 2020 Sphingolipids and inositol phosphates regulate the tau protein phosphorylation status in humanized yeast Frontiers In Cell And Developmental Biology 8 592159
RODERIC. Repositorio Institucional de la Universitat de Valéncia
Frontiers in Cell and Developmental Biology, Vol 8 (2020)
RODERIC: Repositorio Institucional de la Universitat de Valéncia
Hyperphosphorylation of protein tau is a hallmark of Alzheimer’s disease (AD). Changes in energy and lipid metabolism have been correlated with the late onset of this neurological disorder. However, it is uncertain if metabolic dysregulation is a c
Publikováno v:
Frontiers in Microbiology, Vol 10 (2019)
PP2A-like phosphatases share high homology with PP2A enzymes and are composed of a catalytic subunit and a regulatory subunit. In Candida albicans, the PP2A-like catalytic subunit SIT4 regulates cell growth, morphogenesis, and virulence. However, the
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.