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Updated: Oct 4, 2026
11:23
Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
Published on: June 30, 2019
A decade of site- and phosphorylation state-specific antibodies: recent advances in studies of spatiotemporal protein
1Division of Biochemistry, Aichi Cancer Center Research Institute, 1-1 Kanokoden, Chikusa-ku, Nagoya, Aichi 464-8681, Japan.
Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|September 5, 2001
Abstract:
From 1990 to 2001, numerous site- and phosphorylation state-specific antibodies have been developed and many are now commercially available. These antibodies have facilitated understanding of the cytoskeletal organization, signal transduction and transcriptional mechanisms as well as clinical diseases. This review is an attempt to cover all these aspects.
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02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
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During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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