Publications by authors named "R Jepras"

Article Synopsis
  • Single-cell transcriptomics often struggle to detect rare genes and can lead to inaccurate results.
  • Constellation sequencing (Constellation-Seq) improves sensitivity by making it easier to identify low-abundance transcripts and saving costs on data collection.
  • This method effectively measures gene expression changes and can help researchers study rare cell populations and their functions accurately.
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The Epstein-Barr virus induced gene 2 (EBI2) was recently identified as the first oxysterol-activated 7TM receptor. EBI2 is essential for B cell trafficking within lymphoid tissues and thus the humoral immune response in general. Here we characterize the antagonism of the non-peptide molecule GSK682753A, which blocks oxysterol-induced G-protein activation, β-arrestin recruitment and B-cell chemotaxis.

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The biological complexity associated with the regulation of histone demethylases makes it desirable to configure a cellular mechanistic assay format that simultaneously encompasses as many of the relevant cellular processes as possible. In this report, the authors describe the configuration of a JMJD3 high-content cellular mechanistic imaging assay that uses single-cell multiparameter measurements to accurately assess cellular viability and the enzyme-dependent demethylation of the H3K27(Me)3 mark by exogenously expressed JMJD3. This approach couples robust statistical analyses with the spatial resolving power of cellular imaging.

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The Epstein-Barr virus-induced receptor 2 (EBI2) is a constitutively active seven-transmembrane receptor, which was recently shown to orchestrate the positioning of B cells in the follicle. To date, no ligands, endogenously or synthetic, have been identified that modulate EBI2 activity. Here we describe an inverse agonist, GSK682753A, which selectively inhibited the constitutive activity of EBI2 with high potency and efficacy.

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Article Synopsis
  • The study focuses on isolating and characterizing different polymerized forms of the beta-amyloid (Abeta) peptide, linked to Alzheimer's disease, using a novel centrifugation method.
  • Recent findings indicated that the presence of protofibrils and fibrils (specific structures of Abeta) significantly impacted neuronal cell viability, unlike other forms like monomers or sheet structures.
  • The research confirms that both protofibrillar and fibrillar forms of Abeta are biologically active and detrimental to cell health, highlighting the complexity of its neurodegenerative effects.
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