Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/17756
Title: Developing chemical biology approaches for the activity-based investigations of reversible protein phosphorylation-mediating enzymes
Authors: KALESH KARUNAKARAN NAIR ANANDAMMA
Keywords: Activity-Based Protein Profiling, Activity-Based Probe, Protein Tyrosine Phosphatase, Protein Kinase, Click Chemistry, Enzyme Inhibitors
Issue Date: 18-Jan-2010
Source: KALESH KARUNAKARAN NAIR ANANDAMMA (2010-01-18). Developing chemical biology approaches for the activity-based investigations of reversible protein phosphorylation-mediating enzymes. ScholarBank@NUS Repository.
Abstract: Abstract "Developing Chemical Biology Approaches for the Activity-Based Investigations of Reversible Protein Phosphorylation Mediating Enzymes" Karunakaran Nair A. Kalesh This dissertation reports certain chemical biology approaches developed towards the activity-based investigations of some important members in the Protein Tyrosine Phosphatase (PTP) and Protein Kinase (PK) family. In Chapter 2, the development of a panel of peptide-based activity-based probes (ABPs) for target-specific profiling of PTPs has been described. Chapter 3 describes the synthesis of caged versions of the ABPs for the development of light-controllable ABPP of PTPs. Chapter 4 describes the development of a synthetic strategy using the click-reaction to rapidly assemble inhibitor libraries of Abl kinase. In Chapter 5, the synthesis and biochemical evaluation of an improved mechanism-based cross-linker, NDA-AD, for the identification of kinase-substrate interactions is described. In Chapter 6, the development of selective ABPs for the Abl kinase using a dialdehyde-based cross-linking and photo-affinity labeling are described. Chapter 7 provides a brief outlook to some of the future developments possible with the ABPP- and inhibitor-developments of PKs and PTPs discussed in the previous chapters.
URI: http://scholarbank.nus.edu.sg/handle/10635/17756
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