ArticleJournal of virology1993
Dominant negative mutants of human T-cell leukemia virus type I Rex and human immunodeficiency virus type 1 Rev fail to multimerize in vivo.
Article in Journal of virology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 91 citations in OpenAlex.
- Structure of HIV-1 RRE stem-loop II identifies two conformational states of the high-affinity Rev binding site.Nature communications · 2024Article
- Human Retrovirus Genomic RNA Packaging.Viruses · 2022Review
- Is unphosphorylated Rex, as multifunctional protein of HTLV-1, a fully intrinsically disordered protein? An in silico study.Biochemistry and biophysics reports · 2016Article
- Nuclear export and expression of human T-cell leukemia virus type 1 tax/rex mRNA are RxRE/Rex dependent.Journal of virology · 2012Article
- DDX1 is an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication.Journal of molecular biology · 2012Article
- Comparison of the Genetic Organization, Expression Strategies and Oncogenic Potential of HTLV-1 and HTLV-2.Leukemia research and treatment · 2012Article
- Role of Nucleocytoplasmic RNA Transport during the Life Cycle of Retroviruses.Frontiers in microbiology · 2012Article
- Requirements for mouse mammary tumor virus Rem signal peptide processing and function.Journal of virology · 2012Article
- Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Phosphorylation regulates human T-cell leukemia virus type 1 Rex function.Retrovirology · 2009Article
- Mapping of the functional boundaries and secondary structure of the mouse mammary tumor virus Rem-responsive element.The Journal of biological chemistry · 2009Article
- Site-specific phosphorylation regulates human T-cell leukemia virus type 2 Rex function in vivo.Journal of virology · 2009Article
- Human T-cell leukemia virus type 2 Rex carboxy terminus is an inhibitory/stability domain that regulates Rex functional activity and viral replication.Journal of virology · 2009Article
- Rapid and efficient purification of RNA-binding proteins: application to HIV-1 Rev.Protein expression and purification · 2009Article
- Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.Protein science : a publication of the Protein Society · 2008Article
- Review
- HIV-1 Rev oligomerization is not obligatory in the presence of an extra basic domain.Retrovirology · 2005Article
- The human T-cell leukemia virus Rex protein.Frontiers in bioscience : a journal and virtual library · 2005Review
- Article
- Functional domain structure of human T-cell leukemia virus type 2 rex.Journal of virology · 2003Article
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
Human T-cell leukemia virus type I (HTLV-I) Rex and human immunodeficiency virus type 1 (HIV-1) Rev are essential gene products required for the replication of these two pathogenic human retroviruses. Both Rex and Rev act at a posttranscriptional level by binding to highly structured RNA-response elements, the Rex-response element in HTLV-I and the Rev-response element in HIV-1. Using a sensitive in vivo assay of protein-protein interaction, we now demonstrate that the HTLV-I Rex and HIV-1 Rev proteins readily form homomultimeric complexes in the absence of their cognate RNA-response elements yet fail to form heteromultimeric complexes with each other. Dominant negative mutations have been identified in both the rex and rev genes which presumably specify a critical activation or effector domain in each of these viral transactivators. Surprisingly, these dominant negative mutants of Rex and Rev fail to interact in vivo. These findings raise the possibility that the binding of nonfunctional monomers rather than functional multimers underlies the transdominant phenotype of these Rex and Rev mutants. Further, it seems likely that the assembly of functional and stable multimers of Rex and Rev in vivo may depend not only on the intrinsic multimerization domains of these proteins but also on the binding of a bridging cellular cofactor to the related activation domains present in each viral transactivator.
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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.