GAPDH: Biological Properties and Diversity

Nonfiction, Science & Nature, Science, Biological Sciences, Biochemistry, Chemistry, General Chemistry, Health & Well Being, Medical
Cover of the book GAPDH: Biological Properties and Diversity by Norbert W. Seidler, Springer Netherlands
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Author: Norbert W. Seidler ISBN: 9789400747166
Publisher: Springer Netherlands Publication: July 31, 2012
Imprint: Springer Language: English
Author: Norbert W. Seidler
ISBN: 9789400747166
Publisher: Springer Netherlands
Publication: July 31, 2012
Imprint: Springer
Language: English

The book represents a comprehensive review and synthesis of the biomedical literature that spans over a half-century on a single protein called glyceraldehyde 3-phosphate dehydrogenase (or, GAPDH). Due to the protein’s involvement in a vast array of cellular activities, GAPDH is of interest to the cell biologist, immunologist, virologist, biochemist etc. The protein has a significant role in fertility, cancer and neurodegeneration, suggesting that this book can be a vital resource for drug development. GAPDH function may provide insight into anesthesia. Furthermore, GAPDH is highly conserved meaning that the protein found in microorganisms, such as pathogens, remained relatively unchanged in evolution. Pathogens use GAPDH as a virulence factor, offering a unique challenge in developing anti-microbial agents that target this protein. To the evolutionary biologist, a book on the multi-functionality of GAPDH provides a focal point for a cogent discussion on the very origin of life.

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The book represents a comprehensive review and synthesis of the biomedical literature that spans over a half-century on a single protein called glyceraldehyde 3-phosphate dehydrogenase (or, GAPDH). Due to the protein’s involvement in a vast array of cellular activities, GAPDH is of interest to the cell biologist, immunologist, virologist, biochemist etc. The protein has a significant role in fertility, cancer and neurodegeneration, suggesting that this book can be a vital resource for drug development. GAPDH function may provide insight into anesthesia. Furthermore, GAPDH is highly conserved meaning that the protein found in microorganisms, such as pathogens, remained relatively unchanged in evolution. Pathogens use GAPDH as a virulence factor, offering a unique challenge in developing anti-microbial agents that target this protein. To the evolutionary biologist, a book on the multi-functionality of GAPDH provides a focal point for a cogent discussion on the very origin of life.

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