ArticleJournal of virology2004
Characterization of Nef-CXCR4 interactions important for apoptosis induction.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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.
The trial behind it
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- Characterization of a CXCR4 antagonist TIQ-15 with dual tropic HIV entry inhibition properties.PLoS pathogens · 2024Article
- Impact of human immunodeficiency virus on pulmonary vascular disease.Global cardiology science & practice · 2021Review
- Small molecule CXCR4 antagonists block the HIV-1 Nef/CXCR4 axis and selectively initiate the apoptotic program in breast cancer cells.Oncotarget · 2018Article
- Secretion modification region-derived peptide blocks exosome release and mediates cell cycle arrest in breast cancer cells.Oncotarget · 2017Article
- Isolation of Exosomes from the Plasma of HIV-1 Positive Individuals.Journal of visualized experiments : JoVE · 2016Article
- HIV-1 Nef promotes migration and chemokine synthesis of human basophils and mast cells through the interaction with CXCR4.Clinical and molecular allergy : CMA · 2016Article
- Nef-M1, a peptide antagonist of CXCR4, inhibits tumor angiogenesis and epithelial‑to‑mesenchymal transition in colon and breast cancers.Oncotarget · 2015Article
- HIV inhibits endothelial reverse cholesterol transport through impacting subcellular Caveolin-1 trafficking.Retrovirology · 2015Article
- Pyrazolo-Piperidines Exhibit Dual Inhibition of CCR5/CXCR4 HIV Entry and Reverse Transcriptase.ACS medicinal chemistry letters · 2015Article
- Hallmarks of HIV-1 pathogenesis are modulated by Nef's Secretion Modification Region.Journal of AIDS & clinical research · 2015Article
- HIV protein Nef causes dyslipidemia and formation of foam cells in mouse models of atherosclerosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- High levels of anti-Nef antibodies may prevent AIDS disease progression in vertically HIV-1-infected infants.Journal of the International AIDS Society · 2014Article
- Peptide-based identification of functional motifs and their binding partners.Journal of visualized experiments : JoVE · 2013Article
- Nef-M1, a CXCR4 Peptide Antagonist, Enhances Apoptosis and Inhibits Primary Tumor Growth and Metastasis in Breast Cancer.Journal of cancer therapy · 2013Article
- HIV-1 Nef and T-cell activation: a history of contradictions.Future virology · 2013Article
- Astrocytic expression of HIV-1 Nef impairs spatial and recognition memory.Neurobiology of disease · 2013Article
- Validation of a novel secretion modification region (SMR) of HIV-1 Nef using cohort sequence analysis and molecular modeling.Journal of molecular modeling · 2012Article
- Secretion modification region-derived peptide disrupts HIV-1 Nef's interaction with mortalin and blocks virus and Nef exosome release.Journal of virology · 2012Article
- HIV Type 1 Nef is released from infected cells in CD45(+) microvesicles and is present in the plasma of HIV-infected individuals.AIDS research and human retroviruses · 2011Article
- Paracrine modulation of CXCR4 by IGF-1 and VEGF: implications for choroidal neovascularization.Investigative ophthalmology & visual science · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The HIV-1 Nef protein was analyzed for apoptotic structural motifs that interact with the CXCR4 receptor and induce apoptosis in CD4(+) lymphocytes. Two apoptotic motifs were identified. One centered on Nef amino acids (aa) 50 to 60, with the overlapping 20-mer peptides retaining about 82% of the activity of the full Nef protein. The second centered on aa 170 to 180, with the overlapping 20-mer peptides retaining about 30% of the activity of the full protein. Significant apoptotic abilities were observed for 11-mer motif peptides spanning aa 50 to 60 and aa 170 to 180, with a scrambled version of the 11-mer motif peptide corresponding to aa 50 to 60 showing no apoptotic ability. Hallmarks of apoptosis, such as the formation of DNA ladders and caspase activation, that were observed with the full-length protein were equally evident upon exposure of cells to these motif peptides. A CXCR4 antibody and the endogenous ligand SDF-1alpha were effective in blocking Nef peptide-induced apoptosis as well as the physical binding of a fluorescently tagged Nef protein, while CCR5 antibodies were ineffective. The CXCR4-negative cell line MDA-MB-468 was resistant to the apoptotic peptides and became sensitive to the apoptotic peptides upon transfection with a CXCR4-expressing vector. A fluorescently tagged motif peptide and Nef protein displayed physical binding to CXCR4-transfected MDA-MB-468 cells, but not to CCR5-transfected cells. The removal of the apoptotic motif sequences from the full-length protein completely eliminated the ability of Nef to induce apoptosis. However, these modified Nef proteins still retained the ability to enhance viral infectivity. Thus, specific sequences in the Nef protein appear to be necessary for Nef protein-induced apoptosis as well as for physical interaction with CXCR4 receptors.
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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.