Results 161 to 170 of about 2,100 (181)

Correlative In Situ Cryo-ET Reveals Cellular and Viral Remodeling Associated with Selective HIV-1 Core Nuclear Import

Hou Z, Shen Y, Fronik S, Shen J, Shi J, Xu J, Chen L, Hardenbrook N, Thompson C, Neumann S, Engelman AN, Aiken C, Zhang P.   +12 more
europepmc   +1 more source

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

Journal of Virology, 2018
ABSTRACT 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 preintegration complexes. Truncation of the protein at its C-terminal nuclear-targeting arginine/serine-rich (RS) domain produces a protein, CPSF6-358 ...
Jiying Ning, Zhou Zhong, Douglas K Fischer   +2 more
exaly   +6 more sources

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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

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

AIDS 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.
Akatsuki Saito, Hirotaka Ode, Yoshihiro Samune   +2 more
exaly   +3 more sources

Expression of zebrafish cpsf6 in embryogenesis and role of protein domains on subcellular localization

Gene Expression Patterns, 2020
CPSF6 is a component of the CFIm complex, involved in mRNA 3'end processing. Despite increasing interest on this protein as a consequence of proposed roles in cancer and HIV infection, several aspects of CPSF6 biological function are poorly understood.
Borini Etichetti, Carla Maria, Tenaglia, Albano Heraldo, Arroyo, María Nicol, Girardini Brovelli, Javier Enrique   +3 more
exaly   +4 more sources

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

Cell 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.
Vasudevan Achuthan, Gregory A Sowd, William M Mcdougall   +2 more
exaly   +3 more sources

HIV-1 is more dependent on the K182 capsid residue than HIV-2 for interactions with CPSF6

Virology, 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).
Akatsuki Saito, Hirotaka Ode, Emi E Nakayama   +2 more
exaly   +3 more sources

Detection of CPSF6 in Biomolecular Condensates as a Reporter of HIV-1 Nuclear Import

The initial stages of HIV-1 infection involve the transport of the viral core into the nuclear compartment. The presence of the HIV-1 core in the nucleus triggers the translocation of CPSF6/CPSF5 from paraspeckles into nuclear speckles, forming puncta-like structures.
Charlotte, Luchsinger, Felipe, Diaz-Griffero   +1 more
openaire   +2 more sources

[The nuclear translocation of circRNA CPSF6 promotes apoptosis of trophoblast cells induced by homocysteine].

Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology, 2022
Objective To investigate the role of circular RNA cleavage and polyadenylation specificity factor 6 (circRNA CPSF6) in the apoptosis of trophoblast cells induced by homocysteine (Hcy) and its mechanism. Methods HTR-8/SVneo human chorionic trophoblast cells were cultured in vitro and divided into control group (0 mmol/L Hcy treatment) and 1 mmol/L Hcy ...
Lina, Gao, Qirui, Wu, He, Yin, Linying, Liu, Yuzhu, Wu, Yuyue, Zhang, Yanhua, Wang, Kai, Wu, Huiping, Zhang   +8 more
openaire   +1 more source