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Envelope surface glycoprotein gp120
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env
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Gelsolin overexpression impairs HIV-1 gp120-induced cortical F-actin reorganization and capping and gp120-mediated CD4-CCR5 and CD4-CXCR4 redistribution in permissive lymphocytes |
PubMed
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env
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The N-terminal leucine-rich repeat fragment of Slit2 inhibits HIV-1 gp120-induced actin polymerization in T cells |
PubMed
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env
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HIV-1 gp120-CXCR4 signaling triggers cofilin activation and actin reorganization, which are important for a post entry process leading to viral nuclear localization |
PubMed
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env
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Syntenin-1 is recruited toward HIV-1 gp120/gp41-driven virus/cell and cell/cell contacts, associates with CD4, limits HIV-1-induced cell fusion and viral entry, and modulates gp120/gp41-triggered actin polymerization and PIP2 accumulation |
PubMed
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env
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HIV-1 X4-tropic gp120 upregulates alpha-SMA (ACTA2) and collagen I alpha 1 expression via the ERK1/2 pathway in a CXCR4-dependent manner in activated human hepatic stellate cells |
PubMed
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env
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Inducible T-cell kinase (ITK) affects viral entry and gp120-induced actin reorganization |
PubMed
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Envelope surface glycoprotein gp160, precursor
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env
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Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 |
PubMed
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Envelope transmembrane glycoprotein gp41
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env
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Syntenin-1 is recruited toward HIV-1 gp120/gp41-driven virus/cell and cell/cell contacts, associates with CD4, limits HIV-1-induced cell fusion and viral entry, and modulates gp120/gp41-triggered actin polymerization and PIP2 accumulation |
PubMed
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env
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The interaction of the long cytoplasmic tail of HIV-1 gp41 with the carboxy-terminal regulatory domain of p115-RhoGEF inhibits p115-mediated actin stress fiber formation and activation of serum response factor (SRF) |
PubMed
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Nef
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nef
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HIV-1 NA7 and SF2 Nefs relocalizes ACTA1 and ACTB (F-actin); dependent upon the C-terminal aspartic acids in Nef |
PubMed
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nef
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HIV-1 Nef co-localizes with F-actin and reorganizes F-actin assembly in the cortical regions of human podocyte |
PubMed
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nef
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HIV-1 Nef inhibits CXCL12 induced chemotaxis in Jurkat cells, monocytes, and PBMCs, which leads to marked downregulation of F-actin accumulation in cells |
PubMed
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nef
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HIV-1 Nef induces loss of F-actin assembly and inhibits retinoid receptor-mediated transcription |
PubMed
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nef
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HIV-1 Nef requires a PAK2 recruitment motif (F195/191I) for inhibition of actin remodeling and induction of cofilin hyperphosphorylation |
PubMed
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Pr55(Gag)
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gag
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Tec kinase chemical inhibitors diminish the recruitment of ITK to the plasma membrane perturbing HIV-1 Gag-ITK co-localization, disrupting F-actin polymerization, and inhibiting HIV-1 release and replication |
PubMed
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gag
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HIV-1 Gag, ITK, and F-actin are located in overlapping and discrete regions of T cell-T cell contact sites |
PubMed
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gag
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Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 |
PubMed
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gag
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HIV-1 Gag assembly and budding occur through an actin-driven mechanism |
PubMed
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Tat
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tat
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Treatment with cannabinoids inhibits HIV-1 Tat-enhanced attachment of U937 cells to collagen IV, laminin, or ECM1 proteins, which is linked to the cannabinoid receptor type 2 and the modulation of beta1-integrin and actin distribution |
PubMed
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tat
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Treatment of primary hippocampal neurons with HIV-1 Tat produces a significant early reduction in F-actin labeled puncta. The cysteine rich domain (residues 22-37) of Tat is required for Tat-mediated reduction of F-actin labeled puncta |
PubMed
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tat
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Uptake of the HIV-1 Tat protein is regulated by arrangement of the actin cytoskeleton in epithelial cells |
PubMed
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tat
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In Jurkat cells expressing HIV-1 Tat, decreased expression levels are found for basic cytoskeletal proteins such as actin, beta-tubulin, annexin, cofilin, gelsolin, and Rac/Rho-GDI complex |
PubMed
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tat
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HIV-1 Tat induces actin cytoskeletal rearrangements through p21-activated kinase 1 (PAK1) and downstream activation of the endothelial NADPH oxidase, an effect that is lost by introduction of mutations into the Tat cysteine-rich or basic domains |
PubMed
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Vpr
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vpr
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A stable-isotope labeling by amino acids in cell culture coupled with mass spectrometry-based proteomics identifies downregulation of actin, alpha 2 (ACTA2) expression by HIV-1 Vpr in Vpr transduced macrophages |
PubMed
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matrix
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gag
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The localization of the HIV-1 reverse transcription complex to actin microfilaments is mediated by the interaction of a reverse transcription complex component (HIV-1 Matrix) with actin, but not vimentin (intermediate filaments) or tubulin (microtubules) |
PubMed
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nucleocapsid
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gag
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HIV-1 NC-like aggregates are associated with dsDNA synthesis by HIV-1 RT and appear to efficiently bind to F-actin filaments, a property that may be involved in targeting complexes to the nuclear envelope |
PubMed
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gag
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Mature HIV-1 Nucleocapsid, as well as the nucleocapsid domain of the HIV-1 Gag polyprotein, binds filamentous actin resulting in incorporation of actin into virus particles and enhancement of cell motility |
PubMed
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retropepsin
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gag-pol
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Actin, one of the most abundant proteins of the cell, is hydrolyzed by the human immunodeficiency virus type 1 (HIV-1) protease during acute infection of cultured human T lymphocytes |
PubMed
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gag-pol
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HIV-1 protease cleaves actin in vitro at amino acid residues 66-67, 94-95, and 126-127 |
PubMed
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reverse transcriptase
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gag-pol
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HIV-1 NC-like aggregates are associated with dsDNA synthesis by HIV-1 RT and appear to efficiently bind to F-actin filaments, a property that may be involved in targeting complexes to the nuclear envelope |
PubMed
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gag-pol
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The localization of the HIV-1 reverse transcription complex to actin microfilaments is mediated by the interaction of a reverse transcription complex component (HIV-1 Matrix) with actin, but not vimentin (intermediate filaments) or tubulin (microtubules) |
PubMed
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