Skip to main content

4 Result(s)

within Vera Bilan Remove this filter English Remove this filter

and

  1. No Access

    Protocol

    Identification of ADP-Ribose Acceptor Sites on In Vitro Modified Proteins by Liquid Chromatography–Tandem Mass Spectrometry

    Protein ADP-ribosylation is a covalent, reversible posttranslational modification (PTM) catalyzed by ADP-ribosyltransferases (ARTs). Proteins can be either mono- or poly-ADP-ribosylated under a variety of phys...

    Mario Leutert, Vera Bilan, Peter Gehrig, Michael O. Hottiger in Poly(ADP-Ribose) Polymerase (2017)

  2. No Access

    Protocol

    Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography–Tandem Mass Spectrometry

    ADP-ribosylation is a posttranslational modification (PTM) that affects a variety of cellular processes. In recent years, mass spectrometry (MS)-based proteomics has become a valuable tool for studying ADP-rib...

    Sara C. Larsen, Mario Leutert, Vera Bilan, Rita Martello… in Poly(ADP-Ribose) Polymerase (2017)

  3. Article

    Open Access

    Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue

    Although protein ADP-ribosylation is involved in diverse biological processes, it has remained a challenge to identify ADP-ribose acceptor sites. Here, we present an experimental workflow for sensitive and unb...

    Rita Martello, Mario Leutert, Stephanie Jungmichel, Vera Bilan… in Nature Communications (2016)

    Download PDF (854 KB) View Article

  4. No Access

    Protocol

    In Vivo Processing Assay Based on a Dual-Luciferase Reporter System to Evaluate DROSHA Enzymatic Activity

    Luciferase reporter assays are widely used to study promoter activity, transcription factors, intracellular signaling, protein interactions (Jia et al., PloS One 6:e26414), miRNA processing (Allegra and Merten...

    Vera Bilan, Danilo Allegra, Florian Kuchenbauer, Daniel Mertens in miRNA Maturation (2014)