ArticleProceedings of the National Academy of Sciences of the United States of America2002
Specific zinc-finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
66 citing papers in PubMed, 112 citations in OpenAlex.
- Characterizing Complex Nucleic Acid Interactions of LINE1 ORF1p by Single-Molecule Force Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Single-molecule measurements of double-stranded DNA condensation.Biophysical journal · 2025Review
- Article
- Exploring the potential function of trace elements in human health: a therapeutic perspective.Molecular and cellular biochemistry · 2023Review
- The human cellular protein NoL12 is a specific partner of the HIV-1 nucleocapsid protein NCp7.Journal of virology · 2023Article
- Probing the structure of human tRNARSC advances · 2023Article
- Tackling COVID-19 Using Antiviral Nanocoating's-Recent Progress and Future Challenges.Particle & particle systems characterization : measurement and description of particle properties and behavior in powders and other disperse systems · 2023Review
- Article
- The HIV-1 nucleocapsid chaperone protein forms locally compacted globules on long double-stranded DNA.Nucleic acids research · 2021Article
- Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States.Viruses · 2020Review
- HIV-1 Nucleocapsid Protein Unfolds Stable RNA G-Quadruplexes in the Viral Genome and Is Inhibited by G-Quadruplex Ligands.ACS infectious diseases · 2019Article
- Protein-nucleic acid interactions of LINE-1 ORF1p.Seminars in cell & developmental biology · 2019Review
- Characterization of a male specific region containing a candidate sex determining gene in Atlantic cod.Scientific reports · 2019Article
- Retroviral nucleocapsid proteins and DNA strand transfers.Biochimie open · 2018Review
- Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018Review
- Pausing kinetics dominates strand-displacement polymerization by reverse transcriptase.Nucleic acids research · 2017Article
- Requirements for nucleocapsid-mediated regulation of reverse transcription during the late steps of HIV-1 assembly.Scientific reports · 2016Article
- Core protein: A pleiotropic keystone in the HBV lifecycle.Antiviral research · 2015Review
- Single aromatic residue location alters nucleic acid binding and chaperone function of FIV nucleocapsid protein.Virus research · 2014Article
- Similarities and differences in the nucleic acid chaperone activity of HIV-2 and HIV-1 nucleocapsid proteins in vitro.Retrovirology · 2014Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
The nucleocapsid protein (NC) of HIV type 1 (HIV-1) is a nucleic acid chaperone that facilitates the rearrangement of nucleic acid secondary structure during reverse transcription. HIV-1 NC contains two CCHC-type zinc binding domains. Here, we use optical tweezers to stretch single lambda-DNA molecules through the helix-to-coil transition in the presence of wild-type and several mutant forms of HIV-1 NC with altered zinc-finger domains. Although all forms of NC lowered the cooperativity of the DNA helix-coil transition, subtle changes in the zinc-finger structures reduced NC's effect on the transition. The change in cooperativity of the DNA helix-coil transition correlates strongly with in vitro nucleic acid chaperone activity measurements and in vivo HIV-1 replication studies using the same NC mutants. Moreover, Moloney murine leukemia virus NC, which contains a single zinc finger, had little effect on transition cooperativity. These results suggest that a specific two-zinc-finger architecture is required to destabilize nucleic acids for optimal chaperone activity during reverse transcription in complex retroviruses such as HIV-1.
Indexed as
Identifiers
What OpenQuestion holds
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.