ArticleJournal of virology2001
Amino-terminal domain exchange redirects origin-specific interactions of adeno-associated virus rep78 in vitro.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- The Expression and Function of the Small Nonstructural Proteins of Adeno-Associated Viruses (AAVs).Viruses · 2024Review
- Exchange of functional domains between a bacterial conjugative relaxase and the integrase of the human adeno-associated virus.PloS one · 2018Article
- Novel Mutant AAV2 Rep Proteins Support AAV2 Replication without Blocking HSV-1 Helpervirus Replication.PloS one · 2017Article
- DNA Binding and Cleavage by the Human Parvovirus B19 NS1 Nuclease Domain.Biochemistry · 2016Article
- Structural Studies of AAV2 Rep68 Reveal a Partially Structured Linker and Compact Domain Conformation.Biochemistry · 2015Article
- Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding.Virology · 2015Article
- Adeno-associated virus Rep represses the human integration site promoter by two pathways that are similar to those required for the regulation of the viral p5 promoter.Journal of virology · 2014Article
- The interdomain linker of AAV-2 Rep68 is an integral part of its oligomerization domain: role of a conserved SF3 helicase residue in oligomerization.PLoS pathogens · 2012Article
- Parvovirus B19 genotype specific amino acid substitution in NS1 reduces the protein's cytotoxicity in culture.International journal of medical sciences · 2010Article
- Article
- DNA structure modulates the oligomerization properties of the AAV initiator protein Rep68.PLoS pathogens · 2009Article
- Four-dimensional visualization of the simultaneous activity of alternative adeno-associated virus replication origins.Journal of virology · 2005Article
- The expression strategy of goose parvovirus exhibits features of both the Dependovirus and Parvovirus genera.Journal of virology · 2005Article
- Structure of adeno-associated virus type 2 Rep40-ADP complex: insight into nucleotide recognition and catalysis by superfamily 3 helicases.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Characterization of the mouse adeno-associated virus AAVS1 ortholog.Journal of virology · 2004Article
- Reannotation of the CELO genome characterizes a set of previously unassigned open reading frames and points to novel modes of host interaction in avian adenoviruses.BMC bioinformatics · 2003Article
- Cross-packaging of a single adeno-associated virus (AAV) type 2 vector genome into multiple AAV serotypes enables transduction with broad specificity.Journal of virology · 2002Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The unique ability of adeno-associated virus type 2 (AAV) to site-specifically integrate its genome into a defined sequence on human chromosome 19 (AAVS1) makes it of particular interest for use in targeted gene delivery. The objective underlying this study is to provide evidence for the feasibility of retargeting site-specific integration into selected loci within the human genome. Current models postulate that AAV DNA integration is initiated through the interactions of the products of a single viral open reading frame, REP, with sequences present in AAVS1 that resemble the minimal origin for AAV DNA replication. Here, we present a cell-free system designed to dissect the Rep functions required to target site-specific integration using functional chimeric Rep proteins derived from AAV Rep78 and Rep1 of the closely related goose parvovirus. We show that amino-terminal domain exchange efficiently redirects the specificity of Rep to the minimal origin of DNA replication. Furthermore, we establish that the amino-terminal 208 amino acids of Rep78/68 constitute a catalytic domain of Rep sufficient to mediate site-specific endonuclease 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.