Now showing items 1-6 of 6
Label Transfer Reagents for the Investigation of Protein Kinase Complexes
Protein kinases are essential enzymes for cellular signaling, and are often regulated by participation in protein complexes. The mitogen-activated protein kinase (MAPK) p38 is involved in multiple pathways, and its regulation depends on its interactions with other signaling proteins. However, the weak and transient nature of ...
Chemical Proteomic Tools for Studying Protein Kinase Active Sites
Protein kinases constitute one of the largest protein families in humans. These enzymes catalyze phosphorylation of serine, threonine or tyrosine residues in their protein substrates. As protein kinases regulate most signal transduction pathways in cells and play important roles in many cellular functions, deregulation of ...
Single-Molecule Studies for the Characterization of Synaptic Vesicles
Synaptic vesicles are subcellular organelles that are found in the synaptic bouton and are responsible for the propagation of signals between neurons. Synaptic vesicles undergo a fast and tightly regulated cycle in which exocytosis to release neurotransmitters and endocytosis to recycle empty vesicles take place for efficient ...
Protein Enrichment Strategies for Advanced Proteomic Studies
The intracellular environment is complex, with thousands of different proteins alongside many other types of molecules. Such complexity makes the study of individual proteins very difficult without some form of enrichment. While current methods for protein enrichment have been used successfully in many different applications, ...
Investigating Inactive Conformations of Protein Kinases
Protein kinases comprise a substantial fraction of the human genome and constitute a wide array of cell signaling pathways that control countless cellular processes. Improper kinase regulation has been implicated in a number of grievous diseases; hence, these enzymes have become prominent therapeutic targets. The crux of ...
Development and Application of Novel Methodologies for the Characterization of Phospholipase A2 Activity: Targeted Lipidomic Profiling and Interfacial Binding Analysis
Phospholipases A2 are a family of enzymes that hydrolyze membrane glycerophospholipids to yield free fatty acids and lysophospholipids. Both products serve as precursors for an array of lipid mediators that play known roles in a variety of signal transduction processes. Discussed herein is the development and application of ...