27274-31-3Relevant articles and documents
Synthetic analogues of glycosylphosphatidylinositol-anchored proteins and their behavior in supported lipid bilayers
Paulick, Margot G.,Wise, Amber R.,Forstner, Martin B.,Groves, Jay T.,Bertozzi, Carolyn R.
, p. 11543 - 11550 (2007)
Positioned at the C-terminus of many eukaryotic proteins, the glycosylphosphatidylinositol (GPI) anchor is a posttranslational modification that anchors the modified proteins in the outer leaflet of the plasma membrane. GPI-anchored proteins play vital ro
Non-natural amino acid and application thereof Recombinant protein and recombinant protein conjugate comprising same
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Paragraph 0094; 0098; 0099-0100, (2021/10/27)
The invention provides a non-natural amino acid. A compound represented by formula (I) or an enantiomer thereof. The invention also provides application of the non-natural amino acid. Further, the present invention also provides a protein conjugate comprising the recombinant protein and of the non-natural amino acid prepared from the recombinant protein. The non-natural amino acid provided by the invention is simple and convenient to prepare, good in safety, not prone to inactivation when inserted into a protein, high in coupling ratio with a coupling part, good in stability of the obtained conjugate, and capable of being applied to various fields, especially in preparation of recombinant protein or recombinant protein conjugate.
Iterative Design and Optimization of Initially Inactive Proteolysis Targeting Chimeras (PROTACs) Identify VZ185 as a Potent, Fast, and Selective von Hippel-Lindau (VHL) Based Dual Degrader Probe of BRD9 and BRD7
Zoppi, Vittoria,Hughes, Scott J.,Maniaci, Chiara,Testa, Andrea,Gmaschitz, Teresa,Wieshofer, Corinna,Koegl, Manfred,Riching, Kristin M.,Daniels, Danette L.,Spallarossa, Andrea,Ciulli, Alessio
, p. 699 - 726 (2019/01/11)
Developing PROTACs to redirect the ubiquitination activity of E3 ligases and potently degrade a target protein within cells can be a lengthy and unpredictable process, and it remains unclear whether any combination of E3 and target might be productive for degradation. We describe a probe-quality degrader for a ligase-target pair deemed unsuitable: the von Hippel-Lindau (VHL) and BRD9, a bromodomain-containing subunit of the SWI/SNF chromatin remodeling complex BAF. VHL-based degraders could be optimized from suboptimal compounds in two rounds by systematically varying conjugation patterns and linkers and monitoring cellular degradation activities, kinetic profiles, and ubiquitination, as well as ternary complex formation thermodynamics. The emerged structure-activity relationships guided the discovery of VZ185, a potent, fast, and selective degrader of BRD9 and of its close homolog BRD7. Our findings qualify a new chemical tool for BRD7/9 knockdown and provide a roadmap for PROTAC development against seemingly incompatible target-ligase combinations.