NAP1L1 Antibody

1. In summary, the authors identified NAP1L1 as a novel binding partner of hepatitis c virus NS3 and found that the protease domain of NS3 is responsible for interactions with NAP1L1. They demonstrated the functional role of NAP1L1 in hepatitis c virus entry through regulating the protein expression of SR-B1. PMID: 29541944
2. knockdown of NAP1L1 suppresses IkappaBalpha degradation and nuclear transport of p65 subunit after treatment with TNF-a stimulation, leading to attenuation of the NF-kappaB transcriptional activity, whereas NAP1L4 knockdown remains silent.results of this study suggest that NAP1L1 downregulation renders the cell vulnerable to apoptotic cell death through attenuation of NF-kappaB transcriptional activity on the anti-apop... PMID: 28687276
3. NAP1L1 increases CSB processivity by decreasing the pausing probability during translocation. Our study, therefore, uncovers the different steps of CSB-mediated chromatin remodeling that can be regulated by NAP1L1. PMID: 28369616
4. Here the authors confirmed the hepatitis C virus NS5A-NAP1L1 interaction and mapped it to the C terminus of NS5A of both hepatitis C virus genotype 1 and 2. PMID: 28659470
5. Nap1 binds to RAD54. PMID: 24798879
6. TAF-Ibeta promotes BZLF1 expression and subsequent lytic infection by affecting chromatin at the BZLF1 promoter PMID: 23691099
7. NAP1L1 was down-expressed following antiproliferative agent treatment in AuL12-treated cells in comparison with control and with Au(2)Phen-treated ovarian cancer cells. PMID: 22134777
8. Results identified several proteins interacting with NAP1L2, including the ubiquitously expressed members of the nucleosome assembly protein family, NAP1L1 and NAP1L4. PMID: 21333655
9. The biochemical properties of two human NAP1-like proteins, hNAP1L1 and hNAP1L4, were characterized. PMID: 20002496
10. These results suggest that the binding of sequence-specific DNA binding proteins to human nucleosome assembly protein 1 may be an important step contributing to the activation of transcription. PMID: 14966293
11. both the acidic nature of nucleosome assembly protein I and its other functional structure(s) may be essential to mediate the assembly and disassembly of the dimers in nucleosome core particles PMID: 16287874
12. Data show that Alien binds in vivo and in vitro to NAP1 and modulates its activity by enhancing NAP1-mediated nucleosome assembly on DNA. PMID: 17339334

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HGNC: 7637

OMIM: 164060

KEGG: hsa:4673

STRING: 9606.ENSP00000261182

UniGene: Hs.524599