TNPO3 Antibody

1. Combining these results with small-angle X-ray scattering data for the complex of TRN-SR2 with truncated integrase, we propose a molecular model of the complex. We speculate that nuclear import of the PIC may proceed concurrently with the normal nuclear transport. PMID: 28356354
2. IRF5-TNPO3 genetic variation is associated systemic lupus erythematosus. PMID: 25205108
3. Data suggest that the HIV-1 integrase (IN)/transportin-SR2 (TRN-SR2) interaction interface is a potential target for antiviral therapy. PMID: 25063804
4. Tnpo3 mutants that are not able to interact with cleavage and polyadenylation specificity factor 6 do not facilitate HIV-1 infectivity, suggesting a potential route of pharmacological intervention in the treatment of AIDS. PMID: 24449914
5. TNPO3 mutation is the cause of limb-girdle muscular dystrophy 1F, expands knowledge of the molecular basis of muscular dystrophies and bolsters the importance of defects of nuclear envelope proteins as causes of inherited myopathies. PMID: 23543484
6. The TNPO3 gene is mapped within the Limb-girdle muscular dystrophy 1F critical interval and its 923-amino acid human gene product is also expressed in skeletal muscle. PMID: 23667635
7. a model wherein one monomer of TRN-SR2 is bound to one monomer of RanGTP. PMID: 23878195
8. In skeletal muscle of limb-girdle muscular dystrophy 1F individuals, expression of transportin 3 indicates altered transportin 3 function. PMID: 23543484
9. These results suggest that TNPO3 and cyclophilin A facilitate HIV-1 infection by coordinating proper uncoating of the core in target cells. PMID: 23097435
10. Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein. PMID: 22872638
11. TNPO3 can directly engage the HIV-1 IN tetramer prebound to the cognate DNA. PMID: 22872640
12. Transportin 3 and importin alpha act as receptors and are required for effective nuclear import of HIV-1 integrase in virus-infected cells. PMID: 21326825
13. TNPO3 interacts with HIV-1 gag in the cytoplasm to assist HIV-1 infection after nuclear import. PMID: 22398280
14. TNPO3 promotes HIV-1 infectivity at a step in the virus life cycle that is detectable after the preintegration complex arrives in the nucleus and capsid is the viral determinant for TNPO3 dependence. PMID: 22145813
15. TNPO3 binds to a surface of monomeric HIV-1 integrase that remains exposed after tetramerization. PMID: 22176773
16. a novel nuclear localization signal and mechanism for serpinF1 nuclear import PMID: 22028839
17. The authors demonstrated that TNPO3 was required by several lentiviruses for nuclear import. PMID: 21976643
18. Tnp3 binds to tRNAs and capsids proteins, and is required for efficient HIV-1 integration. PMID: 21901095
19. Here the authors discover a link between the viral entry of HIV and its interaction with TRN-SR2. PMID: 21276267
20. capsid, not integrase, is the dominant viral factor that dictates transportin 3 dependency during HIV-1 infection PMID: 19846519
21. Results imply that the mechanism by which SR proteins are imported to the nucleus is conserved between Drosophila and humans and involves the nuclear import receptor transportin-SR PMID: 12134081

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HGNC: 17103

OMIM: 608423

KEGG: hsa:23534

STRING: 9606.ENSP00000265388

UniGene: Hs.193613