Results 151 to 160 of about 2,267 (171)

Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner. [PDF]

open access: yesMBio, 2021
Human immunodeficiency virus type 1 (HIV-1) capsid binds host proteins during infection, including cleavage and polyadenylation specificity factor 6 (CPSF6) and cyclophilin A (CypA).
Zhou Zhong   +2 more
exaly   +6 more sources

Truncated CPSF6 Forms Higher-Order Complexes That Bind and Disrupt HIV-1 Capsid. [PDF]

open access: yesJournal of Virology, 2018
Cleavage and polyadenylation specificity factor 6 (CPSF6) is a human protein that binds HIV-1 capsid and mediates nuclear transport and integration targeting of HIV-1 pre-integration complexes.
Zhou Zhong, Gemma Harris, Hannah Fischer
exaly   +6 more sources

HIV-1-Induced Translocation of CPSF6 to Biomolecular Condensates

Trends in Microbiology
Cleavage and polyadenylation specificity factor subunit 6 (CPSF6, also known as CFIm68) is a 68 kDa component of the mammalian cleavage factor I (CFIm) complex that modulates mRNA alternative polyadenylation (APA) and determines 3' untranslated region (UTR) length, an important gene expression control mechanism.
Felipe Diaz-Griffero
exaly   +3 more sources

Capsid-CPSF6 Interaction Licenses Nuclear HIV-1 Trafficking to Sites of Viral DNA Integration [PDF]

open access: yesCell Host and Microbe, 2018
HIV-1 integration into the host genome favors actively transcribed genes. Prior work indicated that the nuclear periphery provides the architectural basis for integration site selection, with viral capsid-binding host cofactor CPSF6 and viral integrase-binding cofactor LEDGF/p75 contributing to selection of individual sites.
Stefan G. Sarafianos   +2 more
exaly   +3 more sources

The 4th and 112th Residues of Viral Capsid Cooperatively Modulate Capsid-CPSF6 Interactions of HIV-1 [PDF]

open access: yesAIDS Research and Human Retroviruses, 2020
Binding of HIV-1 capsid (CA) to cleavage and polyadenylation specificity factor 6 (CPSF6) is hypothesized to provide a significant fitness advantage to in vivo viral replication, explaining why CA-CPSF6 interactions are strictly conserved in primate lentiviruses.
Hirotaka Ode   +2 more
exaly   +3 more sources

HIV-1 Is More Dependent on the K182 Capsid Residue Than HIV-2 for Interactions With CPSF6

open access: yesVirology, 2019
The HIV-1 capsid (CA) utilizes CPSF6 for nuclear entry and integration site targeting. Previous studies demonstrated that the HIV-1 CA C-terminal domain (CTD) contains a highly conserved K182 residue involved in interaction with CPSF6. In contrast, certain HIV-2 strains possess a substitution at this residue (K182R).
Hirotaka Ode   +2 more
exaly   +3 more sources

A Critical Role for Alternative Polyadenylation Factor CPSF6 in Targeting HIV-1 Integration to Transcriptionally Active Chromatin [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2016
Significance HIV-1 requires integration for efficient gene expression, and the local chromatin environment significantly influences the level of HIV-1 transcription. Silent, integrated proviruses constitute the latent HIV reservoir. As HIV-1 commandeers cellular factors to dictate its preferred integration sites, these interactions ...
Gregory Alan Sowd   +2 more
exaly   +3 more sources

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