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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.
IRF5-TNPO3 genetic variation is associated systemic lupus erythematosus.
Data suggest that the HIV-1 integrase (IN)/transportin-SR2 (TRN-SR2) interaction interface is a potential target for antiviral therapy.
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.
In skeletal muscle of limb-girdle muscular dystrophy 1F individuals, expression of transportin 3 indicates altered transportin 3 function.
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.
a model wherein one monomer of TRN-SR2 is bound to one monomer of RanGTP.
These results suggested that inhibition of HIV-1 by TNPO3-depleted cells requires CPSF6.
TNPO3 promotes HIV-1 infectivity indirectly, by shifting the CA-binding protein CPSF6 to the nucleus, thus preventing the excessive HIV-1 CA stability that would otherwise result from cytoplasmic accumulation of CPSF6.
These results suggest that TNPO3 and cyclophilin A facilitate HIV-1 infection by coordinating proper uncoating of the core in target cells.
Identification of residues in the C-terminal domain of HIV-1 integrase that mediate binding to the transportin-SR2 protein.
TNPO3 can directly engage the HIV-1 IN tetramer prebound to the cognate DNA.
Transportin 3 and importin alpha act as receptors and are required for effective nuclear import of HIV-1 integrase in virus-infected cells.
TNPO3 interacts with HIV-1 gag in the cytoplasm to assist HIV-1 infection after nuclear import.
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.
TNPO3 binds to a surface of monomeric HIV-1 integrase that remains exposed after tetramerization.
a novel nuclear localization signal and mechanism for serpinF1 nuclear import
The authors demonstrated that TNPO3 was required by several lentiviruses for nuclear import.
Tnp3 binds to tRNAs and capsids proteins, and is required for efficient HIV-1 integration.
The protein encoded by this gene is a nuclear import receptor for serine/arginine-rich (SR) proteins such as the splicing factors SFRS1 and SFRS2. The encoded protein has also been shown to be involved in HIV-1 infection, apparently through interaction with the HIV-1 capsid protein. Two transcript variants encoding different isoforms as well as a noncoding transcript have been found for this gene.
, transportin 3
, importin 12