Výsledky vyhledávání - "Ceh‐Pavia, Efrain"

Akademický článek

Regulating behavior with the flip of a translational switch

Autor: Ceh-Pavia, Efraín, Partch, Carrie L.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 2018 Dec . 115(52), 13151-13153.

Externí odkaz: https://www.jstor.org/stable/26573906

Zobrazit plný text záznamu

Akademický článek

Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria.

Autor: Ceh‐Pavia, Efrain¹ (AUTHOR), Tang, Xiaofan^1,2 (AUTHOR), Liu, Yawen³ (AUTHOR), Heyes, Derren J.⁴ (AUTHOR), Zhao, Bing³ (AUTHOR), Xiao, Ping² (AUTHOR), Lu, Hui¹ (AUTHOR) hui.lu@manchester.ac.uk

Publikováno v: FEBS Journal. Jun2020, Vol. 287 Issue 11, p2281-2291. 11p.

Zobrazit plný text záznamu

Akademický článek

Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.

Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria:Electron flow mechanism of MIA40 pathway

Autor: Ceh Pavia, Efrain, Tang, Xiaofan, Liu, Yawen, Heyes, Derren, Zhao, Bing, Xiao, Ping, Lu, Hui

Publikováno v: Ceh Pavia, E, Tang, X, Liu, Y, Heyes, D, Zhao, B, Xiao, P & Lu, H 2019, ' Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria : Electron flow mechanism of MIA40 pathway ', The FEBS Journal . https://doi.org/10.1111/febs.15136

The mitochondrial import and assembly (MIA) pathway plays a vitally important role in import and oxidative folding of mitochondrial proteins. Erv1, a member of the FAD-dependent Erv1/ALR disulphide bond generating enzyme family, is a key player of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3818::1359093195ee9b5a0e0cbceea84c0048
https://doi.org/10.1111/febs.15136

Zobrazit plný text záznamu

Akademický článek

Folding and Biogenesis of Mitochondrial Small Tim Proteins.

Autor: Ceh-Pavia, Efrain¹ efrain.cehpavia@postgrad.manchester.ac.uk, Spiller, Michael P.¹ michael.spiller@manchester.ac.uk, Hui Lu¹ hui.lu@manchester.ac.uk

Publikováno v: International Journal of Molecular Sciences. Aug2013, Vol. 14 Issue 8, p16685-16705. 21p. 5 Diagrams.

Zobrazit plný text záznamu

Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function

Autor: Wang, Qi, Ang, Swee Kim, Ceh-Pavia, Efrain, Pang, Jiayun, Lu, Hui

Erv1 is an FAD-dependent sulphydryl oxidase of the ERV/ALR sub-family, and an essential component of the mitochondrial import and assembly pathway. Erv1 contains six tryptophan residues, which are all located in the highly conserved C-terminal FAD-bi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::d9337303b39a41428b42970e33ee0af5

Zobrazit plný text záznamu

INSIGHTS INTO THE MOLECULAR MECHANISM OF THE MITOCHONDRIAL INTERMEMBRANE SPACE SULPHYDRYL OXIDASE ERV1

Autor: Ceh Pavia, Efrain

Mitochondria are involved in numerous cellular processes such as respiration, ATP production, calcium signalling and apoptosis. About 99% of mitochondrial proteins are nuclear-encoded and need to be imported into mitochondria for their function. The

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2295::520739f582f23f9679fec020586d6831
http://www.manchester.ac.uk/escholar/uk-ac-man-scw:231484

Zobrazit plný text záznamu