Source:http://linkedlifedata.com/resource/entrezgene/hivinteraction/155030-3841
| Predicate | Object |
|---|---|
| rdf:type | |
| entrezgene:pubmed |
pubmed-article:10525473,
pubmed-article:10860744,
pubmed-article:10964507,
pubmed-article:11904219,
pubmed-article:17411366,
pubmed-article:20015032,
pubmed-article:2064827,
pubmed-article:7494303,
pubmed-article:7585960,
pubmed-article:7745752,
pubmed-article:7859280,
pubmed-article:8041734,
pubmed-article:8041786,
pubmed-article:8105392,
pubmed-article:8529100,
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pubmed-article:8552640,
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pubmed-article:8876228,
pubmed-article:9008157,
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pubmed-article:9593140,
pubmed-article:9603322,
pubmed-article:9918876
|
| entrezgene:interactant | |
| entrezgene:geneRifText |
HIV-1 Matrix contains two nuclear localization signals (NLS) spanning amino acids 24-33 and 110-114 that are recognized by karyopherin alpha and mediate the nuclear import of HIV-1 preintegration complexes,
HIV-1 Matrix increases intracellular ATP content, an effect hypothesized to support the ATP-dependent nuclear import of HIV-1 preintegration complexes by karyopherin alpha,
HIV-1 Vpr increases the affinity of karyopherin alpha to the HIV-1 Matrix nuclear localization signal, thereby mediating the nuclear import of HIV-1 preintegration complexes,
Hsp70 stimulates the binding of HIV-1 matrix to karyopherin alpha,
Nuclear import of HIV-1 preintegration complexes by karyopherin alpha is governed by phosphorylation of HIV-1 Matrix on tyrosine and serine, however the exact role of phosphorylation of the C-terminal tyrosine of Matrix has been debated,
The role of HIV-1 Matrix during nuclear import of the HIV-1 preintegration complex has been controversial, however recent understanding indicates HIV-1 Matrix and Vpr proteins act in concert to facilitate nuclear import by binding to karyopherin alpha
|
| entrezgene:keyphrase |
imported by
|