Source:http://linkedlifedata.com/resource/entrezgene/interaction/5478-155030
| Predicate | Object |
|---|---|
| rdf:type | |
| entrezgene:pubmed |
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|
| entrezgene:interactant | |
| entrezgene:geneRifText |
A fusion protein CypA-Nef consisting of cyclophilin A (CypA) linked to the amino terminus of Nef enhances the infectivity of Nef-defective HIV-1 particles and is incorporated into virions via association with Gag during particle assembly,
A small molecule HIV-1 inhibitor PF74 destabilizes the viral capsid in vitro and its antiviral activity is promoted by binding of the host protein cyclophilin A to the HIV-1 capsid,
Affinity Capture-Western,
Alignment of primate lentiviral capsid protein sequences demonstrates that they have conserved the proline rich cyclophilin A binding loop on their outer surface,
Binding of HIV-1 Capsid to cyclophilin A requires HIV-1 Gag dimerization,
Binding of HIV-1 Gag to cyclophilin A requires a region within the nucleocapsid domain of Gag which is important for Gag self-association,
Cyclophilin A binding to HIV-1 Capsid modulates the sensitivity of HIV-1 to host restriction factors,
Cyclophilin A binds to HIV-1 Matrix,
Cyclophilin A catalyzes efficiently the cis/trans isomerization of the Gly-89-Pro-90 peptide bond of HIV-1 Capsid,
Cyclophilin A decreases the degree of capsid protein processing by the HIV-1 protease,
Cyclophilin A has a higher affinity for HIV-1 Gag than for the mature HIV-1 Capsid protein, as a result of additional interactions with the 12 C-terminal amino acids of HIV-1 Matrix,
Cyclophilin A is acetylated at amino acid residue Lys125 in human cells. Acetylated cyclophilin A inhibits its catalysis, inhibits cyclosporine binding, and alters HIV-1 capsid interaction,
Cyclophilin A modulates processing of HIV-1 Gag by the viral protease,
Cyclophilin A mutants, R55K, R55A, F113W, and H126A, exhibit the most pronounced decrease in PPIase activity compared to wild type. These mutants bind to HIV-1 CA with low affinity,
CypA-CA interactions dictate the use of a NUP358/NUP153 dependent nuclear entry pathway,
H219Q and H219P substitutions in the cyclophilin A binding loop of HIV-1 CA enhance HIV-1 replication by reducing viral cyclophilin A content in resulting virions as produced in cyclophilin A-rich cells,
H219Q and H219P substitutions in the viral CypA binding loop of HIV-1 Gag reduces CypA incorporation into HIV-1 and potentiates viral replication in CypA-rich MT-2 and H9 cells,
HIV-1 CA R264K mutant is impaired in generating late reverse transcription products, is inhibited by the presence of normal levels of cyclophilin A, and is rescued with the development of a rare secondary mutation S173A,
HIV-1 Capsid and Gag proteins bind to cyclophilin A, resulting in the incorporation of cyclophilin A into virions, which is important for the completion of early steps in HIV-1 replication following entry of the virus into cells,
HIV-1 N74D CA mutant has less binding affinity to CypA and less HIV-1 infectivity than wild type,
HIV-1 p6 binds to cyclophilin A, particularly, through the p6 proline residues, located at positions 5, 7, 10, 11, 24, 30, 37 and 49,
Increasing CypA levels in permissive TE671 cells restrict HIV-1 CA mutants A92E and G94D in a CypA-dependent way,
Proline-90 and Glycine-89 of HIV-1 Capsid are required for the binding of cyclophilin A to Capsid,
Reducing the binding of CypA to the A92E mutant capsid, either by cyclosporine treatment or by an additional P90A change in the CA protein, increases the amount of particulate capsids and viral infectivity in HeLa cells,
Substitution of Thr for Ala at position 105 of CA (A105T) rescues the impaired single-cycle infectivity of T54A and A92E mutants, indicating that CA determinants outside the CypA-binding loop can modulate the dependence of HIV-1 infection on CypA,
TRIM5 alpha-mediated resistance to HIV-1 in Old World monkey cells is modulated by the HIV-1 Capsid and cyclophilin A interaction,
Targeting of the catalytic HECT domain (residues 598-952) of NEDD4-2s to HIV-1 Gag via CypA is sufficient to rescue HIV-1 budding defects,
The 12 carboxy-terminal amino acids of HIV-1 Matrix (p17; amino acids 121-132) are important for optimal binding of cyclophilin to HIV-1 Gag and Capsid (p24),
The HIV-1 p2 peptide (spacer peptide in the HIV-1 Gag polyprotein between Capsid and Nucleocapsid; SP1) is involved in the interaction between HIV-1 Capsid and cyclophilin A,
The active site hydrophobic binding pocket of cyclophilin A (amino acids 54-126) binds to the N-Terminal and central portion of HIV-1 Capsid, most importantly to Capsid amino acids 85-93,
The effect of inhibition of CA-CypA interaction by TRIM5alpha is virus isolate-dependent, which can result in inhibition, no change, or an increase in viral infectivity,
The enhancement of infection of A92E and G94D HIV-1 Capsid mutants by CypA is a result of enhanced reverse transcription in HeLa-P4 cells,
The interaction between cyclophilin A and HIV-1 CA is required for the enhanced restriction of HIV-1 due to rhTRIM5alpha in non-dividing cells,
The interaction of HIV-1 Capsid to cyclophilin A can be inhibited by cyclosporin A leading to inhibition of virus replication,
V86M capsid mutant, a single amino acid change in the cyclophilin-binding loop of the HIV-1 capsid protein, can replicate in cells expressing TRIM5a(rh). This involves decreased binding to TRIM5a(rh) and retention of binding to cyclophilin A
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| entrezgene:interactionSourc... |
BioGRID
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| entrezgene:keyphrase |
interacts with,
inhibited by,
binds,
stabilizes,
modulated by,
incorporates,
isomerized by
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