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NAP1L1 encodes a member of the nucleosome assembly protein (NAP) family. Additionally we are shipping NAP1L1 Antibodies (49) and NAP1L1 Proteins (15) and many more products for this protein.
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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.
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...
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.
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.
Nap1 binds to RAD54.
TAF-Ibeta promotes BZLF1 expression and subsequent lytic infection by affecting chromatin at the BZLF1 promoter
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.
Results identified several proteins interacting with NAP1L2, including the ubiquitously expressed members of the nucleosome assembly protein family, NAP1L1 and NAP1L4.
The biochemical properties of two human NAP1-like proteins, hNAP1L1 and hNAP1L4, were characterized.
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.
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
Data show that Alien binds in vivo and in vitro to NAP1 and modulates its activity by enhancing NAP1-mediated nucleosome assembly on DNA.
Nap1l1 promotes the proliferation of iPSC attributable to G2/M transition caused by downregulation of p27 and p21, and upregulation of cyclin B1, the activation of AKT or ERK is involved in the process.
The molecular interaction between DGKzeta and Nap1l1 was attenuated after hypoxic stress.
Downregulation of Nap1l1 significantly enhances mesodermal induction and subsequent cardiogenesis of murine induced pluripotent stem cells via inhibition of gamma-secretase-regulated Notch signaling.
Nap1l1 is a novel protein that regulates cardiomyocytes differentiation of P19CL6 cells induced by dimethyl sulfoxide.
NSN1 was found to function as a positive regulator in cell cycle progression. The interaction between NSN1 and histone chaperone AtNAP1;1, and the high resemblance in sensitivity to genotoxics between nsn1 and atnap1;1 imply the indispensability of the two nuclear proteins for cell cycle regulation.
This study highlights distinct functions for different families of histone chaperones in the maintenance of genome stability and establishes a crucial function for NAP1 family histone chaperones in somatic homologous recombination.
Data suggest that Nap1 readily dissociates histone 1 (H1) from DNA and stoichiometrically binds H1 from nucleosomes, supporting a hypothesis whereby histone chaperones contribute to regulation of H1 profile in chromatin.
role for xNAP1L in tissue-restricted gene regulation
results strongly suggest that NAP-1 functions as a chaperone for the linker histone in Xenopus eggs
Over-expression of a structural and functional domain in xNAP1 that affects axial patterning in Xenopus.
This gene encodes a member of the nucleosome assembly protein (NAP) family. This protein participates in DNA replication and may play a role in modulating chromatin formation and contribute to the regulation of cell proliferation. Alternative splicing of this gene results in several transcript variants\; however, not all have been fully described.
HSP22-like protein interacting protein
, NAP-1 related protein
, NAP-1-related protein
, nucleosome assembly protein 1-like 1
, brain protein DN38
, nucleosome assembly protein-1
, nucleosome assembly protein 1 p56A
, nucleosome assembly protein 1 p60A
, nucleosome assembly protein 1-like 1-A