1,998 research outputs found
Activation of the BRLF1 promoter and lytic cycle of Epstein-Barr virus by histone acetylation.
No full textThe F-box protein Fbxo7 interacts with human inhibitor of apoptosis protein cIAP1 and promotes cIAP1 ubiquitination.
No full textTransposon mutagenesis and cloning of the genes encoding the enzymes of fengycin biosynthesis in Bacillus subtilis.
No full textAsymptotic normality of the Lk-error of the Grenander estimator
Full text linkWe investigate the limit behavior of the Lk-distance between a decreasing density f and its nonparametric maximum likelihood estimator \u88 fn for k ? 1. Due to the inconsistency of \u88 fn at zero, the case k = 2.5 turns out to be a kind of transition point.We extend asymptotic normality of the L1-distance to the Lk-distance for 1 ? k 1, we show that the Lk-distance between f and \u88 fn is asymptotically equivalent to the Lk-distance between Un and g.Delft Institute of Applied MathematicsElectrical Engineering, Mathematics and Computer Scienc
Functional and transcriptional analyses of a fengycin synthetase gene, fenC, from Bacillus subtilis.
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(One Less) Manifesto for a Theatre of Immanence
No full textThis chapter provides an introduction to the complex notion of 'immanence' as it appears in the work of Gilles Deleuze before going on to explore the implications of this concept for performance practice. In parallel, the chapter also includes a manifesto for an immanent performance practice, including images created by the author
Construction of Tn917ac1, a transposon useful for mutagenesis and cloning of Bacillus-subtilis genes.
No full textInvolvement of MCAF1 in the synergistically activation of the Epstein-Barr virus promoters by Rta and Zta
No full textMolecular Interactions of Epstein-Barr Virus Capsid Proteins
No full textABSTRACT
The capsids of herpesviruses, which comprise major and minor capsid proteins, have a common icosahedral structure with 162 capsomers. An electron microscopic study shows that Epstein-Barr virus (EBV) capsids in the nucleus are immunolabeled by anti-BDLF1 and anti-BORF1 antibodies, indicating that BDLF1 and BORF1 are the minor capsid proteins of EBV. Cross-linking and electrophoresis studies of purified BDLF1 and BORF1 revealed that these two proteins form a triplex that is similar to that formed by the minor capsid proteins, VP19C and VP23, of herpes simplex virus type 1 (HSV-1). Although the interaction between VP23, a homolog of BDLF1, and the major capsid protein VP5 could not be verified biochemically in earlier studies, the interaction between BDLF1 and the EBV major capsid protein, viral capsid antigen (VCA), can be confirmed by glutathione
S
-transferase (GST) pulldown assay and coimmunoprecipitation. Additionally, in HSV-1, VP5 interacts with only the middle region of VP19C; in EBV, VCA interacts with both the N-terminal and middle regions of BORF1, a homolog of VP19C, revealing that the proteins in the EBV triplex interact with the major capsid protein differently from those in HSV-1. A GST pulldown study also identifies the oligomerization domains in VCA and the dimerization domain in BDLF1. The results presented herein reveal how the EBV capsid proteins interact and thereby improve our understanding of the capsid structure of the virus.
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