106984-09-2Relevant articles and documents
Chemical Genetics Reveals a Role of dCTP Pyrophosphatase 1 in Wnt Signaling
Friese, Alexandra,Kapoor, Shobhna,Schneidewind, Tabea,Vidadala, Srinivasa Rao,Sardana, Juhi,Brause, Alexandra,F?rster, Tim,Bischoff, Matthias,Wagner, Jessica,Janning, Petra,Ziegler, Slava,Waldmann, Herbert
, p. 13009 - 13013 (2019)
Cell-based screening is a powerful approach to identify novel chemical modulators and biological components of relevant biological processes. The canonical Wnt pathway is essential for normal embryonic development and tissue homeostasis, and its deregulation plays a crucial role in carcinogenesis. Therefore, the identification of new pathway members and regulators is of significant interest. By means of a cell-based assay monitoring Wnt signaling we identified the pyrrolocoumarin Pyrcoumin as inhibitor of canonical Wnt signaling. Target identification and validation revealed that Pyrcoumin is a competitive inhibitor of dCTP pyrophosphatase 1 (dCTPP1). We demonstrate a yet unknown interaction of dCTPP1 with ubiquitin carboxyl-terminal hydrolase (USP7) that is counteracted by dCTPP1 inhibitors. These findings indicate that dCTPP1 plays a role in regulation of Wnt/β-catenin signaling most likely through a direct interaction with USP7.
A sulfur tripod glycoconjugate that releases a high-affinity copper chelator in hepatocytes
Pujol, Ana?s M.,Cuillel, Martine,Jullien, Anne-Solène,Lebrun, Colette,Cassio, Doris,Mintz, Elisabeth,Gateau, Christelle,Delangle, Pascale
, p. 7445 - 7448 (2012)
Released in the cell: Three N-acetylgalactosamine units, which recognize the asialoglycoprotein receptor, were tethered through disulfide bonds to the three coordinating thiol functions of a sulfur tripod ligand that has a high affinity for CuI (see scheme). The resulting glycoconjugate can be considered as a prodrug, because after uptake by hepatic cells the intracellular reducing glutathione (GSH) releases the high-affinity intracellular Cu I chelator. Copyright
Covalent Protein Labeling by Enzymatic Phosphocholination
Heller, Katharina,Ochtrop, Philipp,Albers, Michael F.,Zauner, Florian B.,Itzen, Aymelt,Hedberg, Christian
, p. 10327 - 10330 (2015)
We present a new protein labeling method based on the covalent enzymatic phosphocholination of a specific octapeptide amino acid sequence in intact proteins. The bacterial enzyme AnkX from Legionella pneumophila has been established to transfer functional phosphocholine moieties from synthetically produced CDP-choline derivatives to N-termini, C-termini, and internal loop regions in proteins of interest. Furthermore, the covalent modification can be hydrolytically removed by the action of the Legionella enzyme Lem3. Only a short peptide sequence (eight amino acids) is required for efficient protein labeling and a small linker group (PEG-phosphocholine) is introduced to attach the conjugated cargo.
CYP1B1 enzyme targeting probe precursor for radioactivity F labeling
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Paragraph 0027-0029, (2021/02/10)
The invention discloses a CYP1B1 enzyme targeting probe precursor for radioactivity F labeling. The probe precursor comprises an affinity ligand capable of being combined with CYP1B1 enzyme, a chelating group capable of being used for 18F rapid label
