Emerging roles of i-motif in gene expression and disease treatment

X Luo, J Zhang, Y Gao, W Pan, Y Yang, X Li… - Frontiers in …, 2023 - frontiersin.org
As non-canonical nucleic acid secondary structures consisting of cytosine-rich nucleic acids,
i-motifs can form under certain conditions. Several i-motif sequences have been identified in …

Post-translational modifications of retroviral HIV-1 gag precursors: an overview of their biological role

C Bussienne, R Marquet, JC Paillart… - International Journal of …, 2021 - mdpi.com
Protein post-translational modifications (PTMs) play key roles in eukaryotes since they finely
regulate numerous mechanisms used to diversify the protein functions and to modulate their …

Phenotypical characterization of the nuclear egress of recombinant cytomegaloviruses reveals defective replication upon ORF-UL50 deletion but not pUL50 …

S Häge, E Sonntag, A Svrlanska, EM Borst, AC Stilp… - Viruses, 2021 - mdpi.com
Nuclear egress is a common herpesviral process regulating nucleocytoplasmic capsid
release. For human cytomegalovirus (HCMV), the nuclear egress complex (NEC) is …

The phosphorylation of HIV-1 Gag by atypical protein kinase C facilitates viral infectivity by promoting Vpr incorporation into virions

A Kudoh, S Takahama, T Sawasaki, H Ode… - Retrovirology, 2014 - Springer
Background Human immunodeficiency virus type 1 (HIV-1) Gag is the main structural protein
that mediates the assembly and release of virus-like particles (VLPs) from an infected cell …

HIV-1 Gag recruits oligomeric Vpr via two binding sites in p6, but both mature p6 and Vpr are rapidly lost upon target cell entry

M Wanaguru, KN Bishop - Journal of virology, 2021 - Am Soc Microbiol
The p12 region of murine leukemia virus (MLV) Gag and the p6 region of HIV-1 Gag contain
late domains required for virus budding. Additionally, the accessory protein Vpr is recruited …

[HTML][HTML] HIV-1 Vpr drives a tissue residency-like phenotype during selective infection of resting memory T cells

AK Reuschl, D Mesner, M Shivkumar, MVX Whelan… - Cell Reports, 2022 - cell.com
Summary HIV-1 replicates in CD4+ T cells, leading to AIDS. Determining how HIV-1 shapes
its niche to create a permissive environment is central to informing efforts to limit …

The nucleocapsid domain of Gag is dispensable for actin incorporation into HIV-1 and for association of viral budding sites with cortical F-actin

S Stauffer, SA Rahman, A de Marco, LA Carlson… - Journal of …, 2014 - Am Soc Microbiol
Actin and actin-binding proteins are incorporated into HIV-1 particles, and F-actin has been
suggested to bind the NC domain in HIV-1 Gag. Furthermore, F-actin has been frequently …

RNA and nucleocapsid are dispensable for mature HIV-1 capsid assembly

S Mattei, A Flemming, M Anders-Össwein… - Journal of …, 2015 - Am Soc Microbiol
Human immunodeficiency virus type 1 (HIV-1) is released from infected cells in an immature,
noninfectious form in which the structural polyprotein Gag is arranged in a hexameric lattice …

Glutamic acid residues in HIV-1 p6 regulate virus budding and membrane association of Gag

M Friedrich, C Setz, F Hahn, A Matthaei, K Fraedrich… - Viruses, 2016 - mdpi.com
The HIV-1 Gag p6 protein regulates the final abscission step of nascent virions from the cell
membrane by the action of its two late (l-) domains, which recruit Tsg101 and ALIX …

Mass spectrometry-based proteomic approaches for discovery of HIV–host interactions

Y Luo, MA Muesing - Future virology, 2014 - Taylor & Francis
ABSTRACT A molecular understanding of viral infection requires a multi-disciplinary
approach. Mass spectrometry has emerged as an indispensable tool to investigate the …