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"Contact of CD4+ T cells with HIV-1 infected or HIV-1 gp120-expressing cells induces PARP hydrolysis, which leads to the cleavage of 116 kDa PARP into two fragments" . "Inhibition of HIV-1 binding to CD4 by suramin is reversed by human albumin, suggesting that only free suramin has antiviral properties" . "Apoptosis induced by HIV-1 gp120/CD4 cross-linking in Th1 clones is inhibited by anti-CD95 or anti-CD95L neutralizing monoclonal antibodies, as well as by a specific interleukin-1 beta converting enzyme (ICE) inhibitor" . "HIV-1 gp120 induces CD4 association with lymphocyte surface molecules CD3, CD11a, CD27, CD45RA, CD45RB, CD45RO, CD49d, CD38, CD26, CD59, CD95 and class I MHC molecules" . "HIV-1 gp120-mediated CD4 engagement is involved in the induction of susceptibility of primary human T lymphocytes to CD95-mediated apoptosis through ezrin phosphorylation and ezrin-to-CD95 association" . "Syncytial apoptosis mediated by the fusion of cells expressing HIV-1 gp120 with cells expressing the CD4/CXCR4 receptor/coreceptor complex causes phosphorylation of p53 on serine 15 and Bax upregulation" . "Siva-1 sensitizes CD4-positive T-cells to HIV-1 gp120/gp41-induced apoptosis. The Siva-1-mediated sensitization on CD4-positive T-cells shows significant activation of caspase-3, -8, and -9" . "A point mutation (V38E) in the gp41 region of HIV-1 abolishes HIV-1-mediated apoptosis by CASP3 and minimizes CD4 loss in humanized mice without altering viral replication" . "Cell-cell contact between T cells expressing HIV-1 gp120/gp41 and other T cells expressing CD4 receptors leads to the rapid accumulation of cyclin B and tyrosine-hyperphosphorylated p34cdc2 (cdk1) kinase, indicative of cell cycle arrest at G2 phase" . "HIV-1 envelope glycoproteins gp120 and gp160 directly and specifically impair the CD3/TcR-mediated activation of phospholipase C (PLC) via the CD4 molecule in uninfected T cells" . "Binding of HIV-1 gp120 to the CD4 receptor molecule results in co-stimulation of CD3-induced T cell activation" . "Dimeric HIV-1 gp160 binds to two CD4 molecules" . "HIV-1 glycoprotein gp160 binds to both cell surface receptor and soluble CD4 and the interaction of gp160 with CD4 results in virus-cell and cell-cell fusion" . "HIV-1 gp160 molecules exist predominantly as a dimer, but higher forms corresponding to trimers and tetramers are also observed; multiple CD4 molecules bind to the gp160 oligomers" . "Interaction of HIV-1 gp160 with CD4 increases p56lck autophosphorylation and kinase activity" . "Coexpression of HIV-1 gp160 and human CD4 in HeLa cells severely impairs HIV-1 gp120 production due to the formation of intracellular gp160-CD4 complexes; this CD4-mediated inhibition of gp160 processing is alleviated by coexpression of Vpu" . "Newly synthesized CD4 and HIV-1 gp160 form a complex prior to transport from the endoplasmic reticulum (ER)" . "ICAM-1 promotes HIV-1 gp160-mediated syncytium formation, and the ICAM-1 contrareceptor LFA-1 attenuates the syncytium-inhibiting activity of virus-neutralizing monoclonal antibodies and soluble CD4" . "A complete disappearance of surface CD4 preceding single-cell death occurs in cell clones expressing gp160, in which a complex between CD4 and gp160 is formed and then accumulates intracellularly" . "Amino acid residues 257, 368, 370, and 457 of HIV-1 gp160 are critical for both cell surface and intracellular interaction between gp160 and CD4" . "Interaction of the anchoring domain of HIV-1 gp160 with the endoplasmic reticulum membrane is responsible for gp160-mediated cell surface downregulation of CD4" . "HIV-1 gp160 alone or CD4/gp160 cross-linking induces tyrosine phosphorylation of intracellular substrates p59fyn, zap 70, and p95vav and also leads to ras activation" . "HIV-1 gp160 and gp120 specifically recognize the C-terminal heparin-binding domain of fibronectin (Fn) and this binding inhibits the interaction of gp160/gp120 with soluble CD4" . "A soluble HIV-1 Env trimeric construct may better expose crucial epitopes such as the CD4 binding site and V3, as well as epitopes in the vicinity of gp41, subsequent to conjugation with the synthetic CD4-mimicking mini protein" . "Binding gp140 to the synthetic CD4-mimicking mini protein leads to an outward domain shift of the three gp120 subunits, which diminishes gp120-gp41 interactions" . "DC-SIGN increases the binding affinity of trimeric gp140 envelope glycoproteins to CD4 on permissive cell surface" . "HIV-1 Env from subtype P downregulates CD4 cell surface expression" . "CD4-linker-DC-SIGN fusion proteins enhance binding affinity to HIV-1 gp140 and gp120 in comparison to sCD4 and sDC-SIGN. These fusion proteins inhibit HIV-1 capture and transfer via DC-SIGN-expressing cells and iMDDCs" . "HIV-1 envelope glycoprotein gp120 binds to the cell surface receptor CD4 or soluble CD4; the carbohydrates present on gp120 are necessary for CD4 binding during HIV-1 entry" . "Monoclonal antibodies (MAbs) to defined peptide epitopes or N-linked glycans in HIV-1 gp120 inhibit the binding of gp120 to CD4 and exhibit neutralizing activities against HIV-1" . "Soluble CD4 can bind to HIV-1 gp120 and block HIV-1 infectivity" . "A high affinity interaction between the HIV-1 glycoprotein gp120/gp41 complex and the cellular receptor CD4 is necessary for both virus-cell and cell-cell fusion; the V3 region (amino acids 301-336) of gp120 and gp41 amino terminus are involved in fusion" . "Synthetic peptides as agonists of the HIV-1 envelope glycoprotein gp120 or CD4 receptor block the binding of gp120 and CD4" . "HIV-1 envelope protein gp120 can specifically inhibit CD4-dependent class II MHC-restricted T cell response to Antigens" . "HIV-1 gp120 suppresses T and B cell activation and the expression of cytolytic activities through its interaction with CD4" . "Removal of the N-linked sugars on HIV-1 gp120 by endoglycosidase H treatment results in deglycosylated proteins that are unable to bind to CD4, suggesting that glycosylation contributes to the ability of gp120 to bind to CD4" . "Anti-CD4 antibodies are capable of neutralizing HIV-1 strains or blocking the binding of HIV-1 envelope glycoprotein gp120 and cell surface receptor CD4" . "Amino acid residues (102-126) and (425-452) of HIV-1 gp120 contribute to the binding site for CD4 and are expected to be juxtaposed in the folded gp120 chain" . "Expression of a soluble CD4 mutant molecule lacking transmembrane and cytoplasmic domains blocks secretion of HIV-1 gp120 and surface expression of HIV-1 gp120 and gp41 from the endoplasmic reticulum" . "Pretreatment of HIV-1 infected cells with TNF alpha augments syncytia formation mediated by the interaction of HIV-1 gp120 with cell surface CD4 molecules" . "Interaction of HIV-1 gp120 with cell-associated CD4 leads to the induction of IFN alpha; preincubation of cells with anti-CD4 or the presence of soluble CD4 during incubation inhibits IFN alpha induction" . "Crosslinking of HIV-1 gp120 on human CD4+ T cells followed by signaling through the TCR results in activation-induced apoptosis" . "LFA-1 adhesion molecules are not involved in the early stages of cell membrane fusion mediated by the interaction of gp120 with CD4" . "Amino acid residues 42-49 and 54-57 in the V1 region of CD4 are involved in the interaction of CD4 with both HIV-1 gp120 and class II major histocompatibility complex molecules" . "HIV-1 gp120 induces the dissociation of p56lck from CD4 and the downregulation of CD4 from the cellular surface" . "A 287 residue variant of HIV-1 gp120 (ENV59) missing 197 amino acids binds to CD4 with high affinity" . "A CD4 peptide (amino acids 74-95) inhibits the binding of gp120 to CD4+ human lymphoblastic leukemia (CEM) cells" . "Changes in two hydrophobic regions (Thr-257 and Trp-427) and two hydrophilic regions (Asp-368, Glu-370, and Asp-457) of HIV-1 gp120 result in significant reductions in CD4 binding" . "The first two domains (amino acid residues 1-177) of human CD4 bind effectively to HIV-1 gp120, and most residues interacting with gp120 lie within amino acids 21-64; the COOH-terminal half of the molecule is not necessary" . "Several polyanionic anti-HIV compounds, including dextran sulfate, pentosan polysulfate, heparin, aurintricarboxylic acid (ATA), suramin, and Evans blue, interact with HIV-1 gp120 to block the binding of gp120 to CD4" . "HIV-1 gp120 and class II MHC binding sites of CD4 are distinct and can be separated" . "The N-terminal region of HIV-1 gp120 contains conserved residues (amino acids 56-62 and 108-116) critical for binding to CD4" . "Through binding to cell surface CD4, both HIV-1 gp120 and gp160 inhibit syncytia formation between HIV-1-infected cells and CD4+ cells" . "Mutation of two basic amino acids Lys46 and Arg59 in CD4 dramatically disrupts its ability to bind HIV-1 gp120" . "Two disulfide bonds linking cysteine residues at positions 378 and 445 and positions 385 and 418 in the carboxyl terminus of HIV-1 gp120 contribute to CD4 binding" . "Antibodies to LFA-3 block the early stages of HIV-1 infection by cell-free virus following HIV-1 gp120 binding to CD4" . "Cleavage of HIV-1 gp120 with trypsin at residue 432 destroys CD4 binding" . "Binding of recombinant soluble CD4 (sCD4), the purified V1 domain of sCD4, or neutralizing antibodies to the HIV-1 surface glycoprotein gp120 on virions results in rapid dissociation of gp120 from its complex with the transmembrane glycoprotein gp41" . "HIV-1 gp120 stimulates monocytes to release TNF-alpha, IL-1 beta, IL-6, and granulocyte-macrophage-CSF, and this effect can be blocked with soluble CD4" . "12-O-tetradecanoylphorbol-13-acetate (TPA) down-modulates the expression of CD4, which is essential for syncytia formation through interaction with the HIV-1 envelope protein gp120" . "Down modulation of the interaction between HIV-1 gp120 and CD4 by TPA is blocked by protein kinase C (PKC) inhibitors, suggesting PKC may play an important role in HIV-1 infection" . "Phorbol myristate acetate (PMA) pretreatment of CD4+ cells prevents subsequent HIV-1 gp120-induced downregulation of CD4 receptor molecules" . "Cleavage at position R315 of HIV-1 gp120 by thrombin is enhanced by soluble CD4 binding" . "A single amino-acid change (cysteine 402 or tryptophan 432) in HIV-1 gp120 can abrogate CD4 binding" . "Chimpanzee CD4 molecules bearing the human amino acid at position 87 support syncytium formation, while human CD4 molecules bearing the chimpanzee residue at position 87 do not; HIV-1 gp120 binding to CD4 is not affected by the substitution at position 87" . "Small molecules, termed N-carbomethoxycarbonyl-prolyl-phenylalanyl benzyl esters (CPFs), block the binding of gp120 to CD4, but do not interfere with the binding of CD4 to class II major histocompatibility complex molecules" . "HIV-1 gp120 with substitution of cysteine's 296, 331, 418 or 445 on fails to bind to CD4" . "HIV-1 gp120/160 deglycosylated by Endo H and Endo F still binds to CD4, indicating that the carbohydrates of gp120/160 do not play a significant role in the in vitro binding to CD4" . "Mutations at four locations (amino acids 29, 59-64, 77-81, and 85) outside the antigen-complementarity-determining region (CDR2)-like sequence of CD4 markedly affect HIV-1 gp120 binding" . "Amino acid sequences 397-439 in HIV-1 gp120 are directly involved in the binding of gp120 to the CD4 receptor" . "Deletion analysis shows that amino acid regions 82-95, 386-389, 424-432, and 487-499 constitute a part of the HIV-1 gp120 binding region to CD4" . "95- and 25-kDa peptides derived from the disulfide bond reduction of HIV-1 gp120 bind to human CD4" . "A specific interaction between CD4 and HIV-1 gp120 is required for phosphorylation of CD4, which could involve protein kinase C" . "Binding of HIV-1 gp120 to CD4 receptor induces p56lck activation and zeta-chain (TCR) associated protein kinase 70kDa desensitization independent of TCR tyrosine phosphorylation" . "The binding of HIV-1 gp120 to CD4 molecules on T cells interrupts the sequential cascade of intercellular interactions involving antigen/MHC class II-TCR/CD4, CD40L-CD40, and B71-CD28" . "Expression of the HIV-1 envelope gene in CD4+ T cell lines and binding of HIV-1 gp120 to CD4 is sufficient for the induction of apoptosis" . "Calcium ions are required for cell fusion mediated by interactions between CD4 and HIV-1 gp120/gp41; EDTA and EGTA block cell fusion in culture media containing calcium ions" . "Apoptosis of CD4+ lymphocytes induced by HIV-1 gp120 cross-linking to CD4 is inhibited by IL-12" . "CD26 (dipeptidyl peptidase IV) cleaves the highly conserved V3 loop of HIV-1 gp120 and functions as a cofactor for entry of HIV-1 in CD4+ human cells; coexpression of human CD4 and CD26 in murine NIH 3T3 cells renders them permissive to HIV-1" . "Mutants with amino acid changes in the V1/V2 region (residues 131-196) of the HIV-1 gp120 are able to bind CD4 but are deficient in syncytium formation and/or virus entry" . "Combinations of CD4-based molecules and antibodies to HIV-1 gp120 and/or gp41 inhibit cell fusion formation mediated by the interaction of CD4 to gp120" . "Cells expressing a chimeric molecule consisting of the first 177 residues of CD4 attached to residues from the hinge, transmembrane, and cytoplasmic domains of CD8 are susceptible to fusion with cells expressing HIV-1 gp120" . "The third complementarity-determining region (CDR3; residues 79-96) within domain 1 of the human CD4 molecule plays a critical role in membrane fusion mediated by the interaction of CD4 with HIV-1 gp120" . "Release of neurotoxins from monocytes through HIV-1 gp120 stimulation involves CD4 receptors; toxin production can be inhibited either by a monoclonal antibody to the CD4-binding region of gp120 or by soluble CD4 receptors" . "Following incubation with a soluble form of CD4, gp120 of highly purified HIV-1 preparations is cleaved without addition of exogenous proteinase, yielding two proteins of 50 and 70 kDa; this cleavage likely occurs in the gp120 V3 loop" . "IL-16 induces rapid translocation of PKC from the cytosol to the membrane in CD4+ cells; PKC inhibitors completely block IL-16-induced lymphocyte migration as well as the motile response induced by HIV-1 gp120 and anti-CD4 antibody binding to CD4" . "Small molecules exhibit strong anti-HIV-1 activity by binding specifically to both HIV-1 gp120 and/or cell surface receptors (CD4, CCR5, CXCR4) and prevent gp120/CD4/CCR5 and gp120/CD4/CXCR4 complex formation and cell-cell fusion" . "CXCR4, a 45kDa cellular membrane protein, interacts with the cell surface HIV-1 gp120-CD4 complex and acts as a coreceptor to preferentially support T cell line-tropic HIV-1 Env-mediated cell fusion and HIV-1 infection" . "HIV-1 gp120-CD4 interaction is necessary to repress HIV-1 long terminal repeat-dependent luciferase activity; the cytoplasmic domain of CD4 is found to be required for this effect to occur" . "The CCR5 chemokine receptor is required for the entry of macrophage-tropic HIV-1 into target cells; the HIV-1 gp120-CD4 complex binds CCR5, which inhibits the binding of the natural CCR5 ligands macrophage inflammatory protein (MIP)-1alpha and MIP-1beta" . "CD4 downregulation by the treatment of macrophages with HIV-1 gp120 is mediated through the induction of endogenous TNF-alpha" . "Binding of HIV-1 gp120 to CD4 molecules in cells results in the association of Lck and Raf-1, which is abolished by preincubation of the virus with soluble CD4" . "Antibodies to specific epitopes of HIV-1 gp120 block the interaction of CCR5 with the gp120/CD4 complex, suggesting that a CD4-mediated conformational change in gp120 is required for subsequent binding to CCR5" . "HIV-1 gp120 induces a specific phospholipase A2 (PLA2) activation in lymphocytes through binding to CD4, but this effect is not sufficient to accomplish virus/cell fusion" . "CD4-expressing human T cell lines induce significant and rapid conformational changes in gp120-gp41 from T cell-tropic HIV-1 strains, and little conformational changes in gp120-gp41 from macrophage-tropic HIV-1 strains" . "HIV-1 gp120 specifically recognizes the C-terminal heparin-binding domain of fibronectin (Fn) and this binding inhibits the interaction of gp120 with soluble CD4" . "Glycolipids such as galactosylceramides, sulfogalactoceramides, globotriosylceramide, and gangliosides play an important role as HIV-1 fusion cofactors following the interaction of CD4 and HIV-1 gp120" . "CD4-p56Lck interaction is required for HIV-1 gp120-induced nuclear translocation of NF-kappaB in HeLa cells" . "The inhibition of IL-2R expression and proliferation induced by the interaction of CD4 with HIV-1 envelope glycoprotein gp120 is correlated with the inhibition of expression and activation of Janus kinase JAK3" . "Gross cystic disease fluid protein-15 (GCDFP-15) binds to CD4, a T-cell co-receptor involved in antigen recognition, thereby inhibiting the ability of the receptor to interact with the HIV-1 envelope protein gp120" . "The chemokine receptor CCR5 is posttranslationally modified by sulfation of its N-terminal tyrosines; sulfated tyrosines contribute to the binding of CCR5 to MIP-1 alpha, MIP-1 beta, and HIV-1 gp120/CD4 complexes and to the ability of HIV-1 to enter cells" . "The interaction between exposed cyclophilin A (CypA) and cell surface heparans represents the initial step of HIV-1 attachment and is a necessary step for HIV-1 gp120 binding to CD4" . "CD38 expression blocks lymphocyte susceptibility to HIV-1 infection by inhibiting HIV-1 gp120/CD4-dependent viral binding to target cells" . "Human C\" beta strand (amino acids 42-47) of CD4, particularly Phe-43, plays a crucial role in HIV-1 coreceptor function as well as in HIV-1 gp120-CD4 binding capacity" . "T-tropic HIV-1 gp120s are capable of priming phorbol ester (PMA) induced co-down-modulation of gp120 complexes with tailless CD4 by interacting with CXCR4, whereas M-tropic gp120 are not, even in the presence of CCR5" . "Antibodies to specific epitopes of the CCR5 or CXCR4 chemokine receptors inhibit the entry of M-tropic, T-tropic, or dual-tropic HIV-1 into target cells by blocking the interaction of the receptors with the HIV-1 gp120/CD4 complex" . "The level of HIV-1 gp120-mediated syncytium formation and infectivity is enhanced in the presence of neuraminidase (NA) and involves the interaction between gp120, CD4, and chemokine coreceptors" . "A fusion protein between HIV-1 gp120 hepatitis B surface antigen (HBsAg) is capable of spontaneous assembly into virus-like particles and exhibits high affinity binding to CD4" . "The physiological levels of cell-surface CD4 interfere with HIV-1 replication in T cells by a mechanism that inhibits HIV-1 gp120 envelope incorporation into viral membranes" . "The cis expression of DC-SIGN on multiple lymphoid cell lines enables more efficient entry and replication of CXCR4-tropic and CCR5/CXCR4 dual-tropic HIV-1 through its binding to the HIV-1 gp120-CD4-CXCR4 complex" . "Adsorption of multivalent gp120-containing HIV-1 virion particles into CD4+ T lymphocytes results in segregation of CD4 and CXCR4 into distinct lipid micro domains" . "CD4(+)CD45RO(+) cells display high HIV-1 gp120-binding capacity, whereas CD4(+)CD45RO(-) cells show undetectable HIV-1 gp120 binding" . "HIV-1 gp120 interacts with CD4 and alphavbeta3 in peripheral blood monocyte-derived macrophages; neutralizing antibodies against the alphavbeta3 integrin interfere with the coprecipitation of alphavbeta3 with an anti-gp120 antibody" . "Expression of the human CD4 receptor in murine T-cells is sufficient for syncytia formation with HIV-1 envelope expressing cells and entry of MLV/HIV pseudotyped retroviral vectors, suggesting that the murine CXCR4 is a functional coreceptor" . "Protein-disulfide isomerase (PDI) cleaves disulfide bonds in recombinant HIV-1 envelope glycoprotein gp120, and gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors" . "Retrocyclin binds to soluble CD4 and HIV-1 gp120, colocalizes with CD4, CXCR4, and CCR5, and inhibits replication of CCR5-tropic and CXCR4-tropic strains of HIV-1 in human cells, presumably through inhibition of gp120-CD4 binding" . "The fusion of insulin-like growth factor I (IGF I) with stromal cell-derived factor I or alpha1 proteinase inhibitor has the capacity to compete with the binding of HIV-1 gp120 to CD4 receptor" . "Griffithsin isolated from an aqueous extract of the red alga Griffithsia species blocks CD4-dependent HIV-1 gp120 binding to receptor-expressing cells and binds to viral coat glycoproteins (gp120, gp41, and gp160) in a glycosylation-dependent manner" . "Galectin-1, a dimeric beta-galactoside-binding protein, promotes infection with CCR5-tropic, CXCR4-tropic, and CCR5/CXCR4 dual-tropic HIV-1 variants by facilitating attachment of HIV-1 gp120 to CD4 at the cell surface" . "The binding of HIV-1 gp120 to CD4+-permissive cells increases the level of acetylated alpha-tubulin in a CD4-dependent manner; overexpression of Histone Deacetylase 6 (HDAC6) inhibits the acetylation of alpha-tubulin and prevents HIV-1-cell fusion" . "The ability of thioredoxin, a protein disulfide isomerase (PDI), to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 gp120" . "The V3 domain of HIV-1 gp120 induces associations between CD4 and CCR5 receptors in cholesterol-rich microenvironments" . "Bile salt-stimulated lipase (BSSL), a Lewis X (LeX)-containing glycoprotein found in human milk, binds to DC-SIGN and inhibits the interaction of gp120 with CD4" . "Genistein, tyrosine kinase inhibitor, inhibits cell fusion between macrophages and HIV-1 Env expressing cells. Genistein treatment does not change CD4 or CCR5 surface expression and has no effect on gp120-CD4-CCR5 complex formation" . "Tick salivary protein Salp15 prevents gp120-CD4 interaction at least partially through its direct interaction with the envelope glycoprotein in the C1 domain of gp120" . "HIV-1 gp120-induced Ca(2+) fluxing is CD4 dependent and coreceptor specific, and is mediated by the CCR5 and CXCR4 coreceptors" . "Alpha-defensins inhibit the binding of HIV-1 gp120 to CD4 through interaction with the D1 domain of CD4" . "Co-expression of CD4 and DC-SIGN in Raji cells promotes internalization and intracellular retention of HIV-1 through interaction with HIV-1 gp120" . "Expression of CD4 on Raji B cells strongly inhibits DC-SIGN-mediated HIV-1 transmission to T cells, presumably through interaction with HIV-1 gp120" . "Epigallocatechin gallate (EGCG) purified from the green tea catechin inhibits attachment of HIV-1 glycoprotein 120 to the CD4 molecule on T cells" . "CCR5- or CXCR4-tropic HIV-1 induce Indoleamine 2,3-dioxygenase (IDO) in plasmacytoid dendritic cells and this induction is inhibited by the blockade of gp120/CD4 interactions with antibodies to CD4" . "Studies by sequential (SAP) and competitive (CAP) antigen panning methodologies show that some antibodies bind better to gp120-CD4 complexes than to gp120 alone" . "Sphingomyelinase inhibits viral fusion after the engagement of HIV-1 gp120 with CD4 and this inhibition is dependent on CD4 expression levels" . "HIV-1 gp120 with T257S/S375W double mutation is stabilized into the CD4-bound state, with increasing relative fixation between core, full-length monomeric, and full-length trimeric versions of gp120" . "Virological synapse-mediated cell-to-cell HIV-1 transfer is dependent upon gp120/gp41 and CD4 interactions and is more efficient than that of a cell-free mode of uptake, yet the presence of the full CD4 cytoplasmic tail is not essential for the process" . "Focal adhesion kinase (FAK), CD4, and HIV-1 gp120 co-localize in T cells. The formation of FAK-CD4 complex is induced by gp120" . "Individual gp120-CD4 bonds undergo rapid destabilization and this destabilization is significantly enhanced by the coreceptor CCR5, not by CXCR4" . "Competition assays with CD4 and mAbs suggest that SP-A inhibits infectivity by occlusion of the CD4-binding site on gp120" . "HIV-1 gp120 hydrogen bond interactions among transmembrane residues Y108, E283, and Y251, are crucial for HIV-1-gp120/sCD4 complex binding and HIV-1 fusion. HIV-1 gp120 binding to CCR5 disrupts these interhelix hydrogen bond interactions" . "CD4 binding results in a major reorganization of the gp120 trimer, causing an outward rotation and displacement of each gp120 monomer" . "The V1-V3 region of a brain-derived HIV envelope glycoprotein plays a crucial role in determining the virus' low CD4 dependence and increased macrophage tropism, as well as its augmented fusogenicity and reduced sensitivity to the inhibitor BMS-378806" . "HIV-1 gp120 isolated from southern African HIV type 1 subtype C exhibits high-affinity binding to CD4 and the Cys228-Cys239 disulfide bond of gp120 is required for the high-affinity binding to CD4" . "Association and clustering of CD4-CXCR4 induced by HIV-1 gp120 requires moesin-mediated anchoring of actin in the plasma membrane" . "Interaction of the X4-tropic protein HIV-1 gp120 with CD4 augments ezrin and moesin phosphorylation in human permissive T cells, thereby regulating ezrin-moesin activation" . "HIV-1 gp120 promotes filamin binding to both CD4 and CXCR4" . "Deletion of the HIV-1 gp120 major variable regions (V1/V2/V3) stabilizes gp120 core proteins into the conformation recognized by CD4" . "H66N change in gp120 stabilizes the HIV-1 envelope glycoprotein complex once the CD4-bound state is achieved and decreases the probability of CD4-induced inactivation" . "A synthetic CD4-mimetic peptide conjugating with a heparan sulfate dodecasaccharide binds to gp120 and induces the exposure of the coreceptor binding domain available for interaction with the oligosaccharide" . "In resting CD4 T cells, only the HIV envelope-mediated entry, but not the VSV-G-mediated endocytosis, can lead to viral DNA synthesis and nuclear migration" . "In a CD4-bound state, gp120 elements proximal to the gp41 interface complete a 7-stranded beta-sandwich, which appeared invariant in conformation" . "Two potentially flexible topological layers (layers 1 and 2) in the gp120 inner domain (layer 1-layer 2) interactions strengthen gp120-CD4 binding by reducing the off rate when CD4 makes initial contact with the gp120 outer domain" . "Maleic anhydride-modified ovalbumin inhibits HIV-1 entry by targeting both gp120 on HIV-1 virions and CD4 receptor on the host cells" . "The disulfide cross-linking interaction between gp120 and PDI is enhanced by CD4 protein" . "Subtype C gp120 isolates carrying I309L enhance utilization of CD4 but do not affect the ability to use CCR5" . "Palmitic acid analog 2-bromopalmitate (2-BP) efficiently binds to CD4 leading to the inhibition of gp120-to-CD4 binding" . "HIV-1 gp120 drastically reduces the ratio of CD4 dimers/monomers" . "The ability of gp120 to inhibit SDF-1a-induced chemotaxis is mediated by the CD4 receptor and Lck signaling" . "Thioredoxin cleaves the gp120 disulfide bond (Cys296-Cys331) in the V3 domain and the cleavage is enhanced by CD4-expressing cells" . "Elimination of the CD4 domain 2 disulfide bond (Cys130-Cys159) by mutation enhances HIV-1 gp120/gp41-mediated cell-cell fusion and virus entry" . "Virions carrying both HIV-1 R5 env and VSV-G can fuse to naive CD4+ T cells because CD4 binding allows viral uptake" . "CIITA-mediated enhancement of HIV-1 infection is gp120/gp41/CD4-dependent and occurs at the early steps in the infection cycle" . "D279 in the C2 region and N362 in the C3 region of HIV-1 gp120 augment the gp120-CD4 interaction" . "HIV-1 gp120 interacts with CD4 to cause apoptosis in human mesenchymal stem cells" . "A fusion of the CD4- and CCR5-mimetic peptides, DM1, binds gp120 and neutralizes R5, R5X4, and X4 HIV-1 isolates comparably to CD4" . "Griffithsin (GRFT) interaction with gp120 exposes the CD4 binding site by binding the glycan at position 386" . "HIV-1 infections originating from cell-free virus by CD4/gp120 interactions decrease strongly in the presence of antiretrovirals tenofovir and efavirenz whereas infections involving cell-to-cell spread are markedly less sensitive to the drugs" . "Substitution of highly conserved isoleucine with methionine at position 424 in the C4 domain of gp120 confers enhanced neutralization sensitivity to plasma antibodies and increases its interaction with sCD4 but not with CCR5" . "Immature HIV-1 virions are competent for CD4-induced gp120 conformational changes" . "The N260Q gp120 mutant has a significantly lower binding to the recombinant soluble CD4 in comparison with wild-type" . "A single Y681H substitution in HIV-1 gp41 increases the gp120-CD4 binding and enhances infectivity in low CD4 expressing cells" . "The net charge of HIV-1 gp120 V3 loop influences the global structure and diversity of the interaction surface of the gp120 outer domain to CD4 binding and epitopes exposure" . "CD4 binding shifts the V1/V2 regions of HIV-1 gp120 to unmask the co-receptor binding site, and triggers profound dynamic changes in gp120 spanning from the binding site to the gp41-interactive face of gp120" . "Feglymycin, a natural Streptomyces-derived 13mer peptide, inhibits HIV-1 gp120 binding to CD4" . "The HIV-1 transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro; soluble CD4 can block the transglutaminase-catalyzed incorporation of the polyamine spermidine into HIV-1 gp41" . "HIV-1 gp120 and gp41 form a transitional complex with the CD4 receptor and CCR5/CXCR4 coreceptors during virus-cell and cell-cell membrane fusion" . "A truncated cytoplasmic domain of 27 amino acids in HIV-1 gp41 can expose highly conserved domains involved in both HIV-1 coreceptor and CD4 binding" . "Affinity Capture-Western; Reconstituted Complex" . "Interaction between CD4 (PDB ID: 1G9M_C) from Homo sapiens and Gp120 (PDB ID: 1G9M_G) from Human immunodeficiency virus type 1." . "BIND" . "BioGRID" . "inhibits" . "downregulates" . "interacts with" . "inhibited by" . "cooperates with" . "induces phosphorylation of" . "co-localizes with" . "requires" . "relocalizes" . "binds" . "stimulates" . "complexes with" . "enhanced by" . "downregulated by" . "cleavage induced by" .