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PMID: 18178131
TNF binds to the cell transmembrane receptors TNFR1 and TNFR2, mainly to modulate immunity
PMID: 18178131
TNFalpha binds to two distinct cell transmembrane receptors, 55 kDa TNFR1 (also called TNF R55, TNF Rbeta, p55, or CD120a) and 75 kDa TNFR2 (also called TNF R75, TNF Ralpha, p75, and CD120b).
PMID: 18178131
TNF binds to the cell transmembrane receptors TNFR1 and TNFR2, mainly to modulate immunity
PMID: 18178131
TNFalpha binds to two distinct cell transmembrane receptors, 55 kDa TNFR1 (also called TNF R55, TNF Rbeta, p55, or CD120a) and 75 kDa TNFR2 (also called TNF R75, TNF Ralpha, p75, and CD120b).
indirect
PMID: 18178131,12419805,12574335
Recombinant Nef protein stimulates NF-κB activation in promonocytic U937 cells and monocyte-derived macrophages, leading to sustained LTR activation
indirect
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
indirect
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
indirect
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
indirect
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
indirect
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
indirect
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
indirect
PMID: 18178131,12419805,17182689
Moreover, recombinant Nef protein activates AP-1, and induces the rapid phosphorylation of mitogen-activated protein kinase (MAPK)-family members (i.e. ERK1/2, p38, and JNK), interferon regulatory factor 3 (IRF-3), and both the alpha and beta subunits of the IKappaB kinase (IKK) complex, required for the activation of the NF-KappaB pathway in monocyte-derived macrophages
indirect
PMID: 18178131
Both exogenous Nef and TNF activate NF-KappaB, AP-1, and MAPK, suggesting that they might modulate the cellular machinery in a similar way, and therefore might have the same effect on HIV-1 replication in mononuclear phagocytes.
indirect
PMID: 18178131
Both exogenous Nef and TNF activate NF-KappaB, AP-1, and MAPK, suggesting that they might modulate the cellular machinery in a similar way, and therefore might have the same effect on HIV-1 replication in mononuclear phagocytes.
indirect
PMID: 18178131
Both exogenous Nef and TNF activate NF-KappaB, AP-1, and MAPK, suggesting that they might modulate the cellular machinery in a similar way, and therefore might have the same effect on HIV-1 replication in mononuclear phagocytes.
PMID: 18178131,15638722
An interaction between Vpr and the transcription factors Sp1 and TFIIB is required for Vpr-mediated transcriptional enhancement of the HIV-1 LTR in lymphoid and myeloid cells
PMID: 18178131,15638722
An interaction between Vpr and the transcription factors Sp1 and TFIIB is required for Vpr-mediated transcriptional enhancement of the HIV-1 LTR in lymphoid and myeloid cells
indirect
PMID: 18178131,12208951
The ability of Vpr to activate HIV transcription is mediated by the p300/CBP transcriptional coactivator, which, in turn, enhances the ability of Vpr to activate NF-KappaB and the HIV enhancer
indirect
PMID: 18178131,12208951
The ability of Vpr to activate HIV transcription is mediated by the p300/CBP transcriptional coactivator, which, in turn, enhances the ability of Vpr to activate NF-KappaB and the HIV enhancer
indirect
PMID: 18178131,16243842
Synthetic Vpr protein activates NF-KappaB, AP-1, and JNK in promonocytic U937 cells and in primary macrophages, resulting in enhanced HIV replication
indirect
PMID: 18178131,16243842
Synthetic Vpr protein activates NF-KappaB, AP-1, and JNK in promonocytic U937 cells and in primary macrophages, resulting in enhanced HIV replication
indirect
PMID: 18178131,16243842
Synthetic Vpr protein activates NF-KappaB, AP-1, and JNK in promonocytic U937 cells and in primary macrophages, resulting in enhanced HIV replication
PMID: 18178131,10931842
A structural and functional interaction between Vpr and Tat synergistically enhances the transcriptional activity of the HIV-1 LTR
indirect
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
indirect
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
indirect
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
indirect
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
indirect
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
indirect
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
indirect
PMID: 18178131,16920714 ,9670954,16280076
In fact, Tat by itself displays biological activities that mimic those mediated by TNF. Like TNF, Tat activates NF-KappaB, AP-1, and MAPK, as well as c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK), p38, and ERK1/2; however, unlike TNF, signalling does not modify the activation of MEK
PMID: 18178131
At more advanced stages of the disease, when TNF expression (plasma and membrane-bound) becomes more pronounced, Nef prevents TNFR-mediated death in HIV-infected T cells via interaction with the apoptosis signal-regulating kinase-1 (ASK-1)
PMID: 18178131,11298454
Nef inhibits ASK-1, caspase 3, and caspase 8 activation, resulting in the blockade of apoptosis in HIV-infected cells
PMID: 18178131,11298454
Nef inhibits ASK-1, caspase 3, and caspase 8 activation, resulting in the blockade of apoptosis in HIV-infected cells
PMID: 18178131,11298454
Nef inhibits ASK-1, caspase 3, and caspase 8 activation, resulting in the blockade of apoptosis in HIV-infected cells
PMID: 18178131,11689886
In addition, Nef coprecipitates phosphatidylinositol-3-kinase (PI3K) in 293T cells, especially its p85 subunit, via sequences present within the N and C termini of Ne
PMID: 18178131
This interaction leads to the activation of PI3K, which, in turn, phosphorylates Bad, the proapoptotic member of the Bcl-2 family.
indirect
PMID: 18178131
This interaction leads to the activation of PI3K, which, in turn, phosphorylates Bad, the proapoptotic member of the Bcl-2 family.
PMID: 18178131
Phosphorylation of Bad results in its inactivation and subsequently inhibits mitochondrial-related apoptosis.
PMID: 18178131,11689886,11160719
In fact, Nef interacts with PAK2 via its PXXP motif
PMID: 18178131
Another antiapoptotic effect of Nef in T cells involves the interaction with the tumor suppressor protein p53 via its N-terminal extremity (amino acids 1–57), both in the cytoplasm and in the nucleus of the cell.
PMID: 18178131
Another antiapoptotic effect of Nef in T cells involves the interaction with the tumor suppressor protein p53 via its N-terminal extremity (amino acids 1–57), both in the cytoplasm and in the nucleus of the cell.
indirect
PMID: 18178131,17356300
Tat can also protect lymphoid and myeloid cells from TRAIL (TNF-related apoptosis-inducing ligand)-mediated apoptosis by upregulating Bcl-2
PMID: 18178131,8996241,11861282,12767990,15990565
TNF is expressed on the surface of activated macrophages, and most of the CD4+ T lymphocyte death is mediated via TNF-mediated apoptosis and via Fas-Fas ligand and TRAIL-DR5 (death receptor) interactions
PMID: 18178131
The engagement of TNFR2 by TNF results in degradation of TRAF2 (TNFR-associated factor).
PMID: 18178131
Because TRAF2 recruits cIAP (cellular inhibitor of apoptosis proteins) to TNFR1, its degradation can facilitate apoptosis.
indirect
PMID: 18178131,14980217
TRAF2 degradation also attenuates TNFR1-mediated NF-κB activation, further promoting apoptosis
indirect
indirect
PMID: 18178131,16081599,11313374,11602715
HIV-1 gp120 has been reported to trigger the production of TNF and C-C chemokines, especially in mononuclear phagocytes
indirect
indirect
PMID: 18178131,16081599,11313374,11602715
HIV-1 gp120 has been reported to trigger the production of TNF and C-C chemokines, especially in mononuclear phagocytes PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
PMID: 18178131
Vpu is a 16 kDa viral membrane protein that regulates the release of virions from infected cells and induces the disruption of an envelope gp120-CD4 interaction in the endoplasmic reticulum.
indirect
indirectindirect
PMID: 18178131
At more advanced stages of the disease, when TNF expression (plasma and membrane-bound) becomes more pronounced, Nef prevents TNFR-mediated death in HIV-infected T cells via interaction with the apoptosis signal-regulating kinase-1 (ASK-1)
PMID: 18178131
Phosphorylation of Bad results in its inactivation and subsequently inhibits mitochondrial-related apoptosis.
PMID: 18178131,17356300
Tat can also protect lymphoid and myeloid cells from TRAIL (TNF-related apoptosis-inducing ligand)-mediated apoptosis by upregulating Bcl-2
PMID: 18178131
We observed that Nef binds directly to Akt in primary PBLs, suggesting the potential formation of a Nef-Akt-PI3K complex in HIV-infected T cells
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expressionindirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expressionindirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expressionindirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expressionindirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expressionindirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
indirect
PMID: 18178131,16081599,9621091,10704341,11698270
Interactions between HIV-1 gp120 and CD4 stimulates signal transduction pathways, such as activation of protein kinase C (PKC); the generation of PKC-dependent phosphorylation of CD4; activation of the ERK and MAPK pathways, which, in turn, stimulates transcription factors, such as NF-κB, AP-1, Elk-1; and the induction of proinflammatory cytokine and C-C chemokine gene expression
PMID: 18178131,11462036,17082816
Furthermore, the binding of a cell-associated gp120 molecule to CXCR4 induces mitochondrial transmembrane depolarization; cytochrome C release from the mitochondria to the cytosol; and, ultimately, activation of downstream caspases, resulting in T cell apoptosisindirectPMID: 18178131,11462036,17082816
Furthermore, the binding of a cell-associated gp120 molecule to CXCR4 induces mitochondrial transmembrane depolarization; cytochrome C release from the mitochondria to the cytosol; and, ultimately, activation of downstream caspases, resulting in T cell apoptosisindirectPMID: 18178131,11462036,17082816
Furthermore, the binding of a cell-associated gp120 molecule to CXCR4 induces mitochondrial transmembrane depolarization; cytochrome C release from the mitochondria to the cytosol; and, ultimately, activation of downstream caspases, resulting in T cell apoptosisPMID: 18178131,11278695,14561767
Vpu functions as a competitive inhibitor of TNFR-complex proteins, such as TRAF1PMID: 18178131,11278695,14561767
Vpu functions as a competitive inhibitor of TNFR-complex proteins, such as TRAF1indirectPMID: 18178131,16921384,16917489
PD-1 expression is upregulated by TNF and correlates with impaired, HIV-specific T cell functions as well as with predictors of disease progression: it is correlated positively with plasma viral load and inversely with CD4 T cell countindirectPMID: 18178131,16921384,16917489
PD-1 expression is upregulated by TNF and correlates with impaired, HIV-specific T cell functions as well as with predictors of disease progression: it is correlated positively with plasma viral load and inversely with CD4 T cell countindirectPMID: 18178131
Activated caspase 8 induces the release of cytochrome C from the mitochondria.
PMID: 18178131
The release of cytochrome C is usually inhibited by members of the Bcl-2 protein familyindirectPMID: 18178131,11696595
Vpu-expressing cells, the levels of these proteins are limited, resulting in increased release of cytochrome C and, subsequently, in caspase 3 activation