Publications by authors named "Nadi T Wickramasekera"
Article Synopsis
- Several gene regulators typically found in the nucleus are now being detected in mitochondria, sparking interest in mitochondrial roles in cell metabolism in both healthy and disease conditions.
- Research highlights important interactions between nuclear and mitochondrial components (genomes, transcriptomes, and proteomes) that influence cell functions.
- Tumor suppressor p53 and estrogen receptor (ER) have roles in both the nucleus and mitochondria, with p53 performing transcription-independent tasks in mitochondria, while the exact functions of mitochondrial ERs are still being investigated.
The present study examined the role of the dual-specificity protein phosphatase-5 (DUSP-5) in the pressure-induced myogenic responses of organ-cultured cerebral arterial segments. In these studies, we initially compared freshly isolated and organ-cultured cerebral arterial segments with respect to responses to step increases in intravascular pressure, vasodilator and vasoconstrictor stimuli, activities of the large-conductance arterial Ca(2+)-activated K(+) (K(Ca)) single-channel current, and stable protein expression of DUSP-5 enzyme. The results demonstrate maintained pressure-dependent myogenic vasoconstriction, DUSP-5 protein expression, endothelium-dependent and -independent dilations, agonist-induced constriction, and unitary K(Ca) channel conductance in organ-cultured cerebral arterial segments similar to that in freshly isolated cerebral arteries.
View Article and Find Full Text PDFVaccinia virus, the prototypic poxvirus, efficiently and faithfully replicates its ∼200-kb DNA genome within the cytoplasm of infected cells. This intracellular localization dictates that vaccinia virus encodes most, if not all, of its own DNA replication machinery. Included in the repertoire of viral replication proteins is the I3 protein, which binds to single-stranded DNA (ssDNA) with great specificity and stability and has been presumed to be the replicative ssDNA binding protein (SSB).
View Article and Find Full Text PDFArticle Synopsis
- Poxvirus virions have a complex structure comprising at least 70 proteins, with the F18 phosphoprotein being crucial for the formation of mature virions.
- A study evaluated the importance of specific amino acid clusters in F18 through a transient complementation assay, revealing that certain hydrophobic/aromatic residues are key for interacting with other viral proteins but not necessary for complex assembly.
- Additionally, while phosphorylation sites on the F18 protein don't affect the structure, their mutation results in the production of less infectious virions.