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Titlebook: GAPDH: Biological Properties and Diversity; Norbert W. Seidler Book 2013 The Editor(s) (if applicable) and The Author(s), under exclusive

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https://doi.org/10.1007/978-3-663-01121-7ne to binding GAPDH, suggesting that GAPDH may be playing a role in these diseases. Neurodegenerative diseases that are discussed are the conformational diseases of aging, suggesting that GAPDH may be a global sensor for cellular conformational stress. In addition to GAPDH’s oxidoreductase activity,
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https://doi.org/10.1007/978-3-663-10942-6of cells and tissues to future challenges by noxious stimuli. The central thesis regarding this paradigm is that inhaled anesthetics evoke an intra-molecular protein dehydration that is recognized by the cell, eliciting a very specific burst of chaperone gene expression. The chaperones that are impl
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0065-2598 ein. 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.978-94-024-0629-0978-94-007-4716-6Series ISSN 0065-2598 Series E-ISSN 2214-8019
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GAPDH and Intermediary Metabolism,xperimental analysis of GAPDH’s enzymatic function, particularly in the use of inhibitors. The GAPDH gene is portrayed in the context of the enzyme’s role in metabolism. The observed intolerance to genetic mutation suggests that the genetic changes (i.e. those seen across species) may provide a trea
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GAPDH, as a Virulence Factor,y product of these organisms. The process by which pathogenic GAPDH, which has >40 % sequence identity to human GAPDH, is exported and attached to the outer surface of cells remains unknown. This chapter also presents a previously unpublished proposed docking sequence on GAPDH. There is also discuss
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