Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Behdokht Jan Fada"'
Autor:
Behdokht Jan Fada, Udayan Guha, Yi Zheng, Eleazar Reward, Elie Kaadi, Ayette Dourra, Haidong Gu
Publikováno v:
Viruses, Vol 15, Iss 5, p 1070 (2023)
Upon viral entry, components of ND10 nuclear bodies converge with incoming DNA to repress viral expression. The infected cell protein 0 (ICP0) of herpes simplex virus 1 (HSV-1) contains a RING-type E3 ubiquitin ligase that targets the ND10 organizer,
Externí odkaz:
https://doaj.org/article/15f68de4b94c4d41a506be90d2cb194c
Publikováno v:
Viruses, Vol 13, Iss 2, p 239 (2021)
Nuclear domains 10 (ND10), a.k.a. promyelocytic leukemia nuclear bodies (PML-NBs), are membraneless subnuclear domains that are highly dynamic in their protein composition in response to cellular cues. They are known to be involved in many key cellul
Externí odkaz:
https://doaj.org/article/471ccfebb7a549ccaebdc3c0052acf7b
Autor:
Haidong Gu, Behdokht Jan Fada
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 11, p 4088 (2020)
Ubiquitination is a prominent posttranslational modification, in which the ubiquitin moiety is covalently attached to a target protein to influence protein stability, interaction partner and biological function. All seven lysine residues of ubiquitin
Externí odkaz:
https://doaj.org/article/b472421839174922b0116f096177b9ff
Publikováno v:
J Virol
ND10 nuclear bodies, as part of the intrinsic defenses, impose repression on incoming DNA. Infected cell protein 0 (ICP0), an E3 ubiquitin ligase of herpes simplex virus 1 (HSV-1), can derepress viral genes by degrading ND10 organizers to disrupt ND1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36e844accd11f453b1abd63702e5df18
https://doi.org/10.1128/jvi.00470-20
https://doi.org/10.1128/jvi.00470-20
Autor:
Behdokht Jan Fada, Haidong Gu
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 4088, p 4088 (2020)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
Ubiquitination is a prominent posttranslational modification, in which the ubiquitin moiety is covalently attached to a target protein to influence protein stability, interaction partner and biological function. All seven lysine residues of ubiquitin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54793430a57b3bffad71dbb9d7a2f01c
https://www.mdpi.com/1422-0067/21/11/4088
https://www.mdpi.com/1422-0067/21/11/4088