ArticleJournal of virology2008
Retroviral nucleocapsid proteins display nonequivalent levels of nucleic acid chaperone activity.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
64 citing papers in PubMed, 91 citations in OpenAlex.
- Human RPL7 and DDX21 function synergistically with HTLV-1 Gag to overcome genomic RNA structural barriers that block tRNAPro primer annealing.Nucleic acids research · 2026Article
- Human T-cell leukemia virus type 1 uses a specific tRNARNA (New York, N.Y.) · 2024Article
- The human cellular protein NoL12 is a specific partner of the HIV-1 nucleocapsid protein NCp7.Journal of virology · 2023Article
- Phosphomimetic S207D Lysyl-tRNA Synthetase Binds HIV-1 5'UTR in an Open Conformation and Increases RNA Dynamics.Viruses · 2022Article
- RNA Structural Requirements for Nucleocapsid Protein-Mediated Extended Dimer Formation.Viruses · 2022Article
- HIV-1 Nucleocapsid Protein Binds Double-Stranded DNA in Multiple Modes to Regulate Compaction and Capsid Uncoating.Viruses · 2022Article
- Structural maturation of the HIV-1 RNA 5' untranslated region by Pr55RNA biology · 2022Article
- Article
- An Infectious Rous Sarcoma Virus Gag Mutant That Is Defective in Nuclear Cycling.Journal of virology · 2021Article
- The HIV-1 nucleocapsid chaperone protein forms locally compacted globules on long double-stranded DNA.Nucleic acids research · 2021Article
- Dengue virus strain 2 capsid protein switches the annealing pathway and reduces intrinsic dynamics of the conserved 5' untranslated region.RNA biology · 2021Article
- The nucleic acid chaperone activity of the HIV-1 Gag polyprotein is boosted by its cellular partner RPL7: a kinetic study.Nucleic acids research · 2020Article
- Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking.Cell reports · 2020Article
- Article
- Retroviral Gag protein-RNA interactions: Implications for specific genomic RNA packaging and virion assembly.Seminars in cell & developmental biology · 2019Review
- Retroviral nucleocapsid proteins and DNA strand transfers.Biochimie open · 2018Review
- Human T-cell leukemia virus type 1 Gag domains have distinct RNA-binding specificities with implications for RNA packaging and dimerization.The Journal of biological chemistry · 2018Article
- SAMHD1 Impairs HIV-1 Gene Expression and Negatively Modulates Reactivation of Viral Latency in CD4Journal of virology · 2018Article
- Conservation of tRNA mimicry in the 5'-untranslated region of distinct HIV-1 subtypes.RNA (New York, N.Y.) · 2017Article
- Inhibition of HIV-1 Gag-membrane interactions by specific RNAs.RNA (New York, N.Y.) · 2017Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein (NC) is a nucleic acid chaperone that facilitates the remodeling of nucleic acids during various steps of the viral life cycle. Two main features of NC's chaperone activity are its abilities to aggregate and to destabilize nucleic acids. These functions are associated with NC's highly basic character and with its zinc finger domains, respectively. While the chaperone activity of HIV-1 NC has been extensively studied, less is known about the chaperone activities of other retroviral NCs. In this work, complementary experimental approaches were used to characterize and compare the chaperone activities of NC proteins from four different retroviruses: HIV-1, Moloney murine leukemia virus (MLV), Rous sarcoma virus (RSV), and human T-cell lymphotropic virus type 1 (HTLV-1). The different NCs exhibited significant differences in their overall chaperone activities, as demonstrated by gel shift annealing assays, decreasing in the order HIV-1 approximately RSV > MLV >> HTLV-1. In addition, whereas HIV-1, RSV, and MLV NCs are effective aggregating agents, HTLV-1 NC, which exhibits poor overall chaperone activity, is unable to aggregate nucleic acids. Measurements of equilibrium binding to single- and double-stranded oligonucleotides suggested that all four NC proteins have moderate duplex destabilization capabilities. Single-molecule DNA-stretching studies revealed striking differences in the kinetics of nucleic acid dissociation between the NC proteins, showing excellent correlation between nucleic acid dissociation kinetics and overall chaperone activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.