Výsledky vyhledávání - "Behdokht Jan Fada"

Akademický článek

A Novel Recognition by the E3 Ubiquitin Ligase of HSV-1 ICP0 Enhances the Degradation of PML Isoform I to Prevent ND10 Reformation in Late Infection

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

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Akademický článek

The Role of ND10 Nuclear Bodies in Herpesvirus Infection: A Frenemy for the Virus?

Autor: Behdokht Jan Fada, Eleazar Reward, Haidong Gu

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

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Effect of SUMO-SIM Interaction on the ICP0-Mediated Degradation of PML Isoform II and Its Associated Proteins in Herpes Simplex Virus 1 Infection

Autor: Haidong Gu, Behdokht Jan Fada, Elie Kaadi, Yi Zheng, Subodh Kumar Samrat

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

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Specificity in Ubiquitination Triggered by Virus Infection

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

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

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