ArticleJournal of molecular biology2010
Nucleoprotein intermediates in HIV-1 DNA integration visualized by atomic force microscopy.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Who cites it
31 citing papers in PubMed, 42 citations in OpenAlex.
- HIV-1 Integrase Assembles Multiple Species of Stable Synaptic Complex Intasomes That Are Active for Concerted DNA Integration In vitro.Journal of molecular biology · 2024Article
- Retroviral integrase: Structure, mechanism, and inhibition.The Enzymes · 2021Article
- Going beyond Integration: The Emerging Role of HIV-1 Integrase in Virion Morphogenesis.Viruses · 2020Review
- The free energy landscape of retroviral integration.Nature communications · 2019Article
- A C-terminal "Tail" Region in the Rous Sarcoma Virus Integrase Provides High Plasticity of Functional Integrase Oligomerization during Intasome Assembly.The Journal of biological chemistry · 2017Article
- Retroviral integrase protein and intasome nucleoprotein complex structures.World journal of biological chemistry · 2017Review
- Cryo-EM structures and atomic model of the HIV-1 strand transfer complex intasome.Science (New York, N.Y.) · 2017Article
- Article
- The Competitive Interplay between Allosteric HIV-1 Integrase Inhibitor BI/D and LEDGF/p75 during the Early Stage of HIV-1 Replication Adversely Affects Inhibitor Potency.ACS chemical biology · 2016Article
- Methods for the Analyses of Inhibitor-Induced Aberrant Multimerization of HIV-1 Integrase.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Interaction between Reverse Transcriptase and Integrase Is Required for Reverse Transcription during HIV-1 Replication.Journal of virology · 2015Article
- C-Terminal Domain of Integrase Binds between the Two Active Sites.Journal of chemical theory and computation · 2015Article
- HIV-1 integrase multimerization as a therapeutic target.Current topics in microbiology and immunology · 2015Review
- The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.Retrovirology · 2014Article
- A critical role of the C-terminal segment for allosteric inhibitor-induced aberrant multimerization of HIV-1 integrase.The Journal of biological chemistry · 2014Article
- Rous sarcoma virus synaptic complex capable of concerted integration is kinetically trapped by human immunodeficiency virus integrase strand transfer inhibitors.The Journal of biological chemistry · 2014Article
- A new class of multimerization selective inhibitors of HIV-1 integrase.PLoS pathogens · 2014Article
- Multimodal mechanism of action of allosteric HIV-1 integrase inhibitors.Expert reviews in molecular medicine · 2013Review
- Review
- A protein ballet around the viral genome orchestrated by HIV-1 reverse transcriptase leads to an architectural switch: from nucleocapsid-condensed RNA to Vpr-bridged DNA.Virus research · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Integration of HIV-1 (human immunodeficiency virus type 1) DNA into the genome of the host cell is an essential step in the viral replication cycle that is mediated by the virally encoded integrase protein. We have used atomic force microscopy to study stable complexes formed between HIV-1 integrase and viral DNA and their interaction with host DNA. A tetramer of integrase stably bridges a pair of viral DNA ends, consistent with previous analysis by gel electrophoresis. The intasome, composed of a tetramer of integrase bridging a pair of viral DNA ends, is highly stable to high ionic strength that would strip more loosely associated integrase from internal regions of the viral DNA. We also observed tetramers of integrase associated with single viral DNA ends; time-course experiments suggest that these may be intermediates in intasome assembly. Strikingly, integrase tetramers are only observed in tight association with viral DNA ends. The self-association properties of intasomes suggest that the integrase tetramer within the intasome is different from the integrase tetramer formed at high concentration in solution in the absence of viral DNA. Finally, the integration product remains tightly bound by the integrase tetramer, but the 3' ends of the target DNA in the complex are not restrained and are free to rotate, resulting in relaxation of initially supercoiled target DNA.
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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.