ArticleVirology2013
The ATPase of the phi29 DNA packaging motor is a member of the hexameric AAA+ superfamily.
Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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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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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.
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Who cites it
38 citing papers in PubMed, 47 citations in OpenAlex.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Developing Potent Therapeutics for Liver Cancer Chemoresistance via an RNA Nanotech and Series-Circuit-Christmas-Bulb Mechanism Targeting ABC Transporters.Molecular pharmaceutics · 2026Review
- Duck Plague Virus Full-Length UL15 Protein Is a Multifunctional Enzyme Which Not Only Possesses Nuclease Activity but Also Exerts ATPase and DNA-Binding Activity.Veterinary sciences · 2025Article
- DNA/RNA hybrids avoid channel gating that leads to the continued packaging of numerous hybrids into the phi29 protein shell.Nucleic acids research · 2025Article
- Revolving hexameric ATPases as asymmetric motors to translocate double-stranded DNA genome along one strand.iScience · 2023Review
- Revolving ATPase motors as asymmetrical hexamers in translocating lengthy dsDNA via conformational changes and electrostatic interactions in phi29, T7, herpesvirus, mimivirus,Exploration (Beijing, China) · 2023Review
- Computational modeling of protracted HCMV replication using genome substrates and protein temporal profiles.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Controlling the Revolving and Rotating Motion Direction of Asymmetric Hexameric Nanomotor by Arginine Finger and Channel Chirality.ACS nano · 2019Review
- Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017Review
- Construction of Asymmetrical Hexameric Biomimetic Motors with Continuous Single-Directional Motion by Sequential Coordination.Small (Weinheim an der Bergstrasse, Germany) · 2017Article
- An Arginine Finger Regulates the Sequential Action of Asymmetrical Hexameric ATPase in the Double-Stranded DNA Translocation Motor.Molecular and cellular biology · 2016Article
- Development of Potent Antiviral Drugs Inspired by Viral Hexameric DNA-Packaging Motors with Revolving Mechanism.Journal of virology · 2016Review
- Biological Nanomotors with a Revolution, Linear, or Rotation Motion Mechanism.Microbiology and molecular biology reviews : MMBR · 2016Review
- Article
- Phi29 Connector-DNA Interactions Govern DNA Crunching and Rotation, Supporting the Check-Valve Model.Biophysical journal · 2016Article
- Discovery of a new method for potent drug development using power function of stoichiometry of homomeric biocomplexes or biological nanomotors.Expert opinion on drug delivery · 2016Article
- Mechanisms of DNA Packaging by Large Double-Stranded DNA Viruses.Annual review of virology · 2015Review
- Thermodynamic Interrogation of the Assembly of a Viral Genome Packaging Motor Complex.Biophysical journal · 2015Article
- RNA as a stable polymer to build controllable and defined nanostructures for material and biomedical applications.Nano today · 2015Article
- New approach to develop ultra-high inhibitory drug using the power function of the stoichiometry of the targeted nanomachine or biocomplex.Nanomedicine (London, England) · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The AAA+ superfamily of proteins is a class of motor ATPases performing a wide range of functions that typically exist as hexamers. The ATPase of phi29 DNA packaging motor has long been a subject of debate in terms of stoichiometry and mechanism of action. Here, we confirmed the stoichiometry of phi29 motor ATPase to be a hexamer and provide data suggesting that the phi29 motor ATPase is a member of the classical hexameric AAA+ superfamily. Native PAGE, EMSA, capillary electrophoresis, ATP titration, and binomial distribution assay show that the ATPase is a hexamer. Mutations in the known Walker motifs of the ATPase validated our previous assumptions that the protein exists as another member of this AAA+ superfamily. Our data also supports the finding that the phi29 DNA packaging motor uses a revolution mechanism without rotation or coiling (Schwartz et al., this issue).
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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.