Production and purification of homogenous recombinant human selenoproteins reveals a unique codon skipping event in E. coli and GPX4-specific affinity to bromosulfophthalein

Autor: Qing Cheng, Antonella Roveri, Giorgio Cozza, Luciana Bordin, Isabelle Rohn, Tanja Schwerdtle, Anna Kipp, Fulvio Ursini, Matilde Maiorino, Giovanni Miotto, Elias S.J. Arnér

Publikováno v: Redox Biology, Vol 46, Iss , Pp 102070- (2021)

Selenoproteins are translated via animal domain-specific elongation machineries that redefine dedicated UGA opal codons from termination of translation to selenocysteine (Sec) insertion, utilizing specific tRNA species and Sec-specific elongation fac

Externí odkaz: https://doaj.org/article/1f6c69bfec4246ab9b89587e51908e46

Redox homeostasis: The Golden Mean of healthy living

Autor: Fulvio Ursini, Matilde Maiorino, Henry Jay Forman

Publikováno v: Redox Biology, Vol 8, Iss C, Pp 205-215 (2016)

The notion that electrophiles serve as messengers in cell signaling is now widely accepted. Nonetheless, major issues restrain acceptance of redox homeostasis and redox signaling as components of maintenance of a normal physiological steady state. Th

Externí odkaz: https://doaj.org/article/16dfb33f9a654e709ab35522bb837b33

A white paper on Phospholipid Hydroperoxide Glutathione Peroxidase (GPx4) forty years later

Autor: Fulvio Ursini, Valentina Bosello Travain, Giorgio Cozza, Giovanni Miotto, Antonella Roveri, Stefano Toppo, Matilde Maiorino

The purification of a protein inhibiting lipid peroxidation led to the discovery of the selenoperoxidase GPx4 forty years ago. Thus, the evidence of the enzymatic activity was reached after identifying the biological effect and unambiguously defined

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10399d684d8ade0e8a1438dbd87a40b6
http://hdl.handle.net/11577/3454547

A dual attack on the peroxide bond. The common principle of peroxidatic cysteine or selenocysteine residues

Autor: Leopold Flohé, F.M. Bickelhaupt, Matilde Maiorino, Laura Orian, Fulvio Ursini, M. Dalla Tiezza

Publikováno v: Redox Biology, 34:101540, 1-9. Elsevier
Dalla Tiezza, M, Bickelhaupt, F M, Flohé, L, Maiorino, M, Ursini, F & Orian, L 2020, ' A dual attack on the peroxide bond. The common principle of peroxidatic cysteine or selenocysteine residues ', Redox Biology, vol. 34, 101540, pp. 1-9 . https://doi.org/10.1016/j.redox.2020.101540
Redox Biology, 34
Redox Biology
Redox Biology, Vol 34, Iss, Pp 101540-(2020)

The (seleno)cysteine residues in some protein families react with hydroperoxides with rate constants far beyond those of fully dissociated low molecular weight thiol or selenol compounds. In case of the glutathione peroxidases, we could demonstrate t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::123ec6113c73d627a549bc17870f2198
https://research.vu.nl/en/publications/fc3cd324-06d7-4e11-9ba1-357888acaf93

Lack of glutathione peroxidase-8 in the ER impacts on lipid composition of HeLa cells microsomal membranes

Autor: Antonella Roveri, Giorgio Cozza, Ana-Marija Vučković, Matilde Maiorino, Valentina Bosello Travain, Mattia Zaccarin, Fulvio Ursini, Stefano Toppo, Rina Venerando, Giovanni Miotto

GPx8 is a glutathione peroxidase homolog inserted in the membranes of endoplasmic reticulum (ER), where it seemingly plays a role in controlling redox status by preventing the spill of H2O2. We addressed the impact of GPx8 silencing on the lipidome o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b5c52d605fc7e59bf663d33ce83a11d
https://www.bib.irb.hr/1147205