Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Gaia Fabrizio"'
Autor:
Emilia Mayo, Gaia Fabrizio, Emanuele Salvatore Scarpa, Annalisa Stilla, Nadia Dani, Fulvio Chiacchiera, Henning Kleine, Francesca Attanasio, Bernhard Lüscher, Maria Di Girolamo
Publikováno v:
Challenges, Vol 9, Iss 1, p 22 (2018)
Protein ADP-ribosylation is a reversible post-translational modification of cellular proteins that is catalysed by enzymes that transfer one (mono) or several (poly) units of ADP-ribose from β-NAD+ to a specific amino acid of the target protein. The
Externí odkaz:
https://doaj.org/article/88414ed5e5624b3ea493b401ec9bc290
Autor:
Maria Di Girolamo, Gaia Fabrizio
Publikováno v:
Challenges, Vol 9, Iss 1, p 24 (2018)
Poly-ADP-ribosylation is a post-translational modification that occurs in multicellular organisms, including plants and some lower unicellular eukaryotes. The founding member of the PARP family is PARP1. To date, 17 members of the PARP family have be
Externí odkaz:
https://doaj.org/article/ef0ce059c08a4b4c95329abc4021f686
Autor:
Maria Di Girolamo, Gaia Fabrizio
Publikováno v:
Biochemical pharmacology. 167
Mono-ADP-ribosylation is a reversible post-translational protein modification that modulates the function of proteins involved in different cellular processes, including signal transduction, protein transport, transcription, cell cycle regulation, DN
Autor:
Gaia Fabrizio, Maria Di Girolamo
Publikováno v:
Challenges, Vol 9, Iss 1, p 24 (2018)
Poly-ADP-ribosylation is a post-translational modification that occurs in multicellular organisms, including plants and some lower unicellular eukaryotes. The founding member of the PARP family is PARP1. To date, 17 members of the PARP family have be
Autor:
Fulvio Chiacchiera, Henning Kleine, Emanuele Salvatore Scarpa, Annalisa Stilla, Emilia Mayo, Maria Di Girolamo, Nadia Dani, Francesca Attanasio, Bernhard Lüscher, Gaia Fabrizio
Publikováno v:
Challenges, Vol 9, Iss 1, p 22 (2018)
Challenges; Volume 9; Issue 1; Pages: 22
Challenges; Volume 9; Issue 1; Pages: 22
Protein ADP-ribosylation is a reversible post-translational modification of cellular proteins that is catalysed by enzymes that transfer one (mono) or several (poly) units of ADP-ribose from β-NAD+ to a specific amino acid of the target protein. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b3a7ade6bafb7d0aa623f04176899af
https://hdl.handle.net/11576/2665623
https://hdl.handle.net/11576/2665623
Publikováno v:
Current Topics in Medicinal Chemistry. 13:3001-3010
The post-translational modifications of proteins by mono- and poly-ADP-ribosylation involve the cleavage of βNAD⁺, with the release of its nicotinamide moiety, accompanied by the transfer of a single (mono) or several (poly) ADP-ribose molecules f
ARTC1-mediated ADP-ribosylation of GRP78/BiP: a new player in endoplasmic-reticulum stress responses
Autor:
Monica Giannotta, Stephan Menzel, Gaia Fabrizio, Maria Di Girolamo, Michele Sallese, Carmen Ruggiero, Annalisa Stilla, Friedrich Koch-Nolte, Simone Di Paola
Publikováno v:
Cellular and molecular life sciences : CMLS. 72(6)
Protein mono-ADP-ribosylation is a reversible post-translational modification of cellular proteins. This scheme of amino-acid modification is used not only by bacterial toxins to attack host cells, but also by endogenous ADP-ribosyltransferases (ARTs
Publikováno v:
Current topics in medicinal chemistry. 13(23)
The post-translational modifications of proteins by mono- and poly-ADP-ribosylation involve the cleavage of βNAD⁺, with the release of its nicotinamide moiety, accompanied by the transfer of a single (mono) or several (poly) ADP-ribose molecules f
Publikováno v:
The FEBS journal. 280(15)
During the development, progression and dissemination of neoplastic lesions, cancer cells can hijack normal pathways and mechanisms. This includes the control of the function of cellular proteins through reversible post-translational modifications, s