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KHNYN is essential for the zinc finger antiviral protein (ZAP) to restrict HIV-1 containing clustered CpG dinucleotides

Autor: Mattia Ficarelli, Harry Wilson, Rui Pedro Galão, Michela Mazzon, Irati Antzin-Anduetza, Mark Marsh, Stuart JD Neil, Chad M Swanson

Publikováno v: eLife, Vol 8 (2019)

CpG dinucleotides are suppressed in most vertebrate RNA viruses, including HIV-1, and introducing CpGs into RNA virus genomes inhibits their replication. The zinc finger antiviral protein (ZAP) binds regions of viral RNA containing CpGs and targets t

Externí odkaz: https://doaj.org/article/5dd80e2d2db84fe1968a5d9597cac568

CoCUN, a Novel Ubiquitin Binding Domain Identified in N4BP1

Autor: Ridvan Nepravishta, Federica Ferrentino, Walter Mandaliti, Anna Mattioni, Janine Weber, Simona Polo, Luisa Castagnoli, Gianni Cesareni, Maurizio Paci, Elena Santonico

Publikováno v: Biomolecules, Vol 9, Iss 7, p 284 (2019)

Ubiquitin binding domains (UBDs) are modular elements that bind non-covalently to ubiquitin and act as downstream effectors and amplifiers of the ubiquitination signal. With few exceptions, UBDs recognize the hydrophobic path centered on Ile44, inclu

Externí odkaz: https://doaj.org/article/c2a90c2b05d94ff89aad1aebdeeef0ac

CoCUN, a Novel Ubiquitin Binding Domain Identified in N4BP1

Autor: Simona Polo, Anna Mattioni, Federica Ferrentino, Janine Weber, Maurizio Paci, Luisa Castagnoli, Elena Santonico, Walter Mandaliti, Gianni Cesareni, Ridvan Nepravishta

Publikováno v: Archivio Istituzionale della Ricerca dell'Università degli Studi di Milano
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Volume 9
Biomolecules, Vol 9, Iss 7, p 284 (2019)
Issue 7
Biomolecules

Ubiquitin binding domains (UBDs) are modular elements that bind non-covalently to ubiquitin and act as downstream effectors and amplifiers of the ubiquitination signal. With few exceptions, UBDs recognize the hydrophobic path centered on Ile44, inclu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e03f5ccc454a3d063f71bbfd15580b1

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