Sökning: "mutant library"
Visar resultat 1 - 5 av 37 avhandlingar innehållade orden mutant library.
1. Directed Evolution of Glutathione Transferases Guided by Multivariate Data Analysis
Sammanfattning : Evolution of enzymes with novel functional properties has gained much attention in recent years. Naturally evolved enzymes are adapted to work in living cells under physiological conditions, circumstances that are not always available for industrial processes calling for novel and better catalysts. LÄS MER
2. Pharmacological targeting of nonsense mutant TP53 and PTEN in cancer
Sammanfattning : The TP53 tumor suppressor gene encodes p53 and is inactivated by mutations in around half of all human tumors. Approximately 11% of TP53 mutations are nonsense mutations, resulting in the premature termination of translation and the production of truncated and non-functional p53 proteins. LÄS MER
3. Translational readthrough of nonsense mutant TP53, RB1 and PTEN tumor suppressor genes as a strategy for novel cancer therapy
Sammanfattning : A nonsense mutation causes a premature termination codon in the coding sequence of an mRNA. This leads to termination of translation and release of a truncated and in most cases non-functional protein. LÄS MER
4. Directed Enzyme Evolution of Theta Class Glutathione Transferase : Studies of Recombinant Libraries and Enhancement of Activity toward the Anticancer Drug 1,3-bis(2-Chloroethyl)-1-nitrosourea
Sammanfattning : Glutathione transferases (GSTs) are detoxication enzymes involved in the cellular protection against a wide range of reactive substances. The role of GSTs is to catalyze the conjugation of glutathione with electrophilic compounds, which generally results in less toxic products. LÄS MER
5. Redesign of substrate specificity of glutathione transferase and glutathione reductase : Enzyme engineering by directed mutagenesis, phage-display selection and DNA shuffling
Sammanfattning : Human glutathione transferase (GST) A1-1 was expressed in fusion with the phage gene IIIproduct and a library of phage-displayed GST mutants was constructed by randomization of fouractive-site residues. Variant GSTs were isolated by mechanism-based phage display selection, using an immobilized transition-state analog of a nucleophilic aromatic substitution (SNAr) reaction. LÄS MER