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Quantitative phosphoproteomic analysis of prion-infected neuronal cells

Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal diseases associated with the conversion of the cellular prion protein (PrPC) to the abnormal prion protein (PrPSc). Since the molecular mechanisms in pathogenesis are widely unclear, we analyzed the global phospho-proteome and detected a differential pattern of tyrosine- and threonine phosphorylated ...

Inhibition of Pre-mRNA Splicing by a Synthetic Blom7α-Interacting Small RNA

Originally the novel protein Blom7α was identified as novel pre-mRNA splicing factor that interacts with SNEVPrp19/Pso4, an essential protein involved in extension of human endothelial cell life span, DNA damage repair, the ubiquitin-proteasome system, and pre-mRNA splicing. Blom7α belongs to the heteronuclear ribonucleoprotein K homology (KH) protein family, displaying 2 KH ...

Identification of peptide inhibitors of pre‐mRNA splicing derived from the essential interaction domains of CDC5L and PLRG1

Paul Ajuh 0 Angus I. Lamond 0 0 The University of Dundee, School of Life Sciences, Wellcome Trust Biocentre , Dow Street, Dundee DD1 5EH, UK CDC5L and PLRG1 are both spliceosomal proteins that are

snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN

Judith E. Sleeman 0 Paul Ajuh 0 Angus I. Lamond ) 0 0 School of Life Sciences, University of Dundee, MSI/WTB Complex , Dow Street, Dundee, DD1 5EH , UK SUMMARY Splicing snRNPs (small nuclear

SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly

We have isolated the human protein SNEV as downregulated in replicatively senescent cells. Sequence homology to the yeast splicing factor Prp19 suggested that SNEV might be the orthologue of Prp19 and therefore might also be involved in pre-mRNA splicing. We have used various approaches including gene complementation studies in yeast using a temperature sensitive mutant with a ...

Functional coexpression of serine protein kinase SRPK1 and its substrate ASF/SF2 in Escherichia coli

Mammalian proteins expressed in Escherichia coli are used in a variety of applications. A major drawback in producing eukaryotic proteins in E.coli is that the bacteria lack most eukaryotic post-translational modification systems, including serine/threonine protein kinase(s). Here we show that a eukaryotic protein can be phosphorylated in E.coli by simul­taneous expression of a ...