ArticleJournal of virology1997
Functional identification of nucleotides conferring substrate specificity to retroviral integrase reactions.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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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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
18 citing papers in PubMed, 42 citations in OpenAlex.
- Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication.FEMS microbiology reviews · 2026Review
- Brief Histories of Retroviral Integration Research and Associated International Conferences.Viruses · 2024Review
- Histone deacetylase 1 interacts with HIV-1 Integrase and modulates viral replication.Virology journal · 2019Article
- Inhibition of HTLV-1 Infection by HIV-1 First- and Second-Generation Integrase Strand Transfer Inhibitors.Frontiers in microbiology · 2019Article
- B'-protein phosphatase 2A is a functional binding partner of delta-retroviral integrase.Nucleic acids research · 2016Article
- Zinc finger protein designed to target 2-long terminal repeat junctions interferes with human immunodeficiency virus integration.Human gene therapy · 2012Article
- Designed zinc finger protein interacting with the HIV-1 integrase recognition sequence at 2-LTR-circle junctions.Protein science : a publication of the Protein Society · 2009Article
- Integration of rous sarcoma virus DNA: a CA dinucleotide is not required for integration of the U3 end of viral DNA.Journal of virology · 2008Article
- Inhibitors of strand transfer that prevent integration and inhibit human T-cell leukemia virus type 1 early replication.Antimicrobial agents and chemotherapy · 2008Article
- Ebola virus VP30 is an RNA binding protein.Journal of virology · 2007Article
- A high-throughput method for cloning and sequencing human immunodeficiency virus type 1 integration sites.Journal of virology · 2006Article
- The protease and reverse transcriptase of the tobacco LTR retrotransposon Tnt1 are enzymatically active when expressed in Escherichia coli.Plant molecular biology · 2001Article
- The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits.The EMBO journal · 2001Article
- Substrate sequence selection by retroviral integrase.Journal of virology · 2001Article
- Avian retrovirus DNA internal attachment site requirements for full-site integration in vitro.Journal of virology · 2000Article
- Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction.The EMBO journal · 1998Article
- Specific and independent recognition of U3 and U5 att sites by human immunodeficiency virus type 1 integrase in vivo.Journal of virology · 1998Article
- Human T-cell leukemia virus type 1 reverse transcriptase (RT) originates from the pro and pol open reading frames and requires the presence of RT-RNase H (RH) and RT-RH-integrase proteins for its activity.Journal of virology · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The long terminal repeats (LTRs) that flank the retroviral DNA genome play a distinct role in the integration process by acting as specific substrates for the integrase (IN). The role of LTR sequences in providing substrate recognition and specificity to integration reactions was investigated for INs from human immunodeficiency virus type 1 (HIV-1), Moloney murine leukemia virus (M-MuLV), human T-cell leukemia virus type 1 (HTLV-1), and human T-cell leukemia virus type 2 (HTLV-2). Overall, these INs required specific LTR sequences for optimal catalysis of 3'-processing reactions, as opposed to strand transfer and disintegration reactions. It is of particular note that in strand transfer reactions the sites of integration were similar among the four INs. In the 3'-processing reaction, sequence specificity for each IN was traced to the three nucleotides proximal to the conserved CA. Reactions catalyzed by M-MuLV IN were additionally influenced by upstream regions. The nucleotide requirements for optimal catalysis differed for each IN. HIV-1 IN showed a broad range of substrate specificities, while HTLV-1 IN and HTLV-2 IN had more defined sequence requirements. M-MuLV IN exhibited greater activity with the heterologous LTR substrates than with its own wild-type substrate. This finding was further substantiated by the high levels of activity catalyzed by the IN on modified M-MuLV LTRs. This work suggests that unlike the other INs examined, M-MuLV IN has evolved with an IN-LTR interaction that is suboptimal.
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