31 research outputs found

    Erratum: Immunoglobulin G4-related disease: Is it all the same? (Rheumatology (2020) 59 (2195–2196) DOI: 10.1093/rheumatology/keaa317)

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    The above article originally referred to 'Sex disparities in clinical characteristics and prognosis of immunoglobulin G4- related disease: a prospective study of 403 patients' by Wang et al., instead of 'Clinical phenotypes of IgG4-related disease reflect different prognostic outcomes' by Lanzillotta et al. This has now been corrected online. The Author(s) 2020. Published by Oxford University Press on behalf of the British Society for Rheumatology. All rights reserved. © 2020 Oxford University Press. All rights reserved

    Cc RNase: the Ceratitis capitata ortholog of a novel highly conserved protein family in metazoans

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    Complementary DNA encoding a protein, designa-ted Cc RNase, was isolated from the insect Ceratitis capitata. Deduced amino acid sequence analysis demonstrates that the Cc RNase has strong sequence homology with other uncharacterized proteins predicted from EST sequences belonging to different animal species, therefore de®ning a new protein family, which is conserved from Caenorhabditis elegans to humans. Phylogenetic analysis data in addition to extensive homolog searches in all available complete genomes sug-gested that all family members are true orthologs. Proteins belonging to this family are composed of 95±101 amino acids. The C.capitata orthologous protein was expressed in Escherichia coli. Despite the fact that the amino acid sequence of Cc RNase does not share any signi®cant similarities with other known ribonucleases, our data give strong evidence in support of the assignment of enzymatic activity to the recombinant protein. The expressed molecule exhibits ribonucleolytic activity against poly(C) and poly(U) synthetic substrates, as well as rRNA. It is also demonstrated that expression of Cc RNase in E.coli inhibits growth of the host cells
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