Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) 1st Edition by Michael A. Sirover – Ebook PDF Instant Download/Delivery: 0128098988, 9780128098981
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Product details:
ISBN 10: 0128098988
ISBN 13: 9780128098981
Author: Michael A. Sirover
Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) 1st Edition:
Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH): The Quintessential Moonlighting Protein in Normal Cell Function and in Human Disease examines the biochemical protein interactions of the multi-dimensional protein GAPDH, further considering the regulatory mechanisms through which cells control their functional diversity.
This protein’s diverse activities range from nuclear tRNA export and the maintenance of genomic integrity, to cytoplasmic post-transcriptional control of gene expression and receptor mediated cell signaling, to membrane facilitation of iron metabolism, trafficking and fusion.
This book will be of great interest to basic scientists, clinicians and students, including molecular and cell biologists, immunologists, pathologists and clinical researchers who are interested in the biochemistry of GAPDH in health and disease.
- Contextualizes how GAPDH is utilized by cells in vivo
- Provides detailed insight into GAPDH post-translational modifications, including functional diversity and its subcellular localization
- Includes forward-thinking exposition on tough topics, such as the exploration of how GAPDG performs functions, how it decides where it should be present and requisite structural requirements
Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) 1st Edition Table of contents:
Section I. The Role of Moonlighting GAPDH in Normal Cell Function
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Chapter 1. The role of moonlighting GAPDH in cell proliferation: the dynamic nature of GAPDH expression and subcellular localization
- Subcellular localization of moonlighting GAPDH during cell proliferation
- Proliferative-dependent expression of the GAPDH gene
- GAPDH—a cell cycle checkpoint in mammalian cells?
- Mechanisms of GAPDH nuclear translocalization and export
- The role of moonlighting GAPDH in cell senescence
- Summary
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Chapter 2. Moonlighting GAPDH and the transcriptional regulation of gene expression: multiprotein complex formation and mechanisms of nuclear translocation
- GAPDH as a DNA-binding protein
- Moonlighting GAPDH and gene transcription
- Summary
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Chapter 3. The diversity of moonlighting GAPDH function in posttranscriptional RNA regulation: mRNA stability, tRNA processing, and viral pathogenesis
- Initial identification of GAPDH–RNA interactions
- Role of moonlighting GAPDH in nuclear transfer RNA export
- Role of moonlighting GAPDH in the determination of mRNA stability
- Role of moonlighting GAPDH in the transcriptional or the translational control of viral pathogenesis
- Summary
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Chapter 4. The role of moonlighting GAPDH in membrane structure and function: membrane fusion and iron metabolism
- Initial identification of GAPDH–membrane association
- Physiological significance of membrane-bound GAPDH-I: fusogenic activity of moonlighting GAPDH
- Physiological significance of membrane-bound GAPDH-II: the functional diversity of GAPDH in iron uptake, transport, and sequestration
- Summary
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Chapter 5. The role of moonlighting GAPDH in intracellular membrane trafficking: tubulin regulation and modulation of cytoskeletal structure
- Initial identification of GAPDH–tubulin binding
- Role of GAPDH–tubulin interactions in membrane trafficking
- Summary
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Chapter 6. Moonlighting GAPDH and the maintenance of DNA integrity: preservation of genetic information and cancer facilitation
- GAPDH as a DNA damage recognition and DNA repair protein
- GAPDH and the maintenance of telomere structure
- Summary
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Chapter 7. Moonlighting GAPDH in neuronal structure and function: regulation of ion channels and signal transduction
- GAPDH as a component of neuronal structure
- The role of moonlighting GAPDH as a protein phosphorylase in neuronal structure and function
- Moonlighting GAPDH and the regulation of ligand-gated ion channel signaling
- Summary
Section II. Physiological Stress and GAPDH Functional Diversity
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Chapter 8. The significance of nitric oxide–modified GAPDH: regulation of apoptosis, cell signaling, and heme metabolism
- GAPDH regulation in apoptosis
- Nuclear translocation of GAPDH in apoptosis
- Role of nitric oxide in GAPDH-mediated apoptosis
- SNO-GAPDH as a transnitrosylase
- SNO-GAPDH as a checkpoint for apoptosis
- SNO-GAPDH and the regulation of heme metabolism
- Moonlighting GAPDH and apoptosis: an alternative mechanism
- GAPDH and autophagy: the duality of moonlighting GAPDH function
- Summary
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Chapter 9. GAPDH and hypoxia: mechanisms of cell survival during oxygen deprivation
- Upregulation of GAPDH expression during hypoxia
- Subcellular localization of hypoxia-induced GAPDH
- Role of nitric oxide in hypoxic regulation of GAPDH expression
- Role of Ca++ in hypoxia GAPDH expression
- Misuse of GAPDH as an internal standard
- Transcriptional regulation of GAPDH in hypoxia
- Genetic regulation of hypoxic GAPDH expression
- Summary
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Chapter 10. Moonlighting GAPDH and ischemia: cellular and molecular effects of oxygen deprivation and reperfusion
- Significance of glycolysis and GAPDH in ischemia and reperfusion
- GAPDH and AMPAR excitotoxicity in ischemia
- GAPDH and nitric oxide-mediated ischemic changes in cell structure and function
- GAPDH and poly (ADP) ribose polymerase in ischemia
- GAPDH and the regulation of mitophagy during ischemia/reperfusion
- Summary
Section III. The Pathology of GAPDH Functional Diversity
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Chapter 11. GAPDH and tumorigenesis: molecular mechanisms of cancer development and survival
- GAPDH and the Warburg effect
- GAPDH and cancer cell survival
- GAPDH and cancer gene regulation
- GAPDH in ovarian cancer: effect on mRNA stability and cancer development
- GAPDH and tumor angiogenesis
- GAPDH and the prevention of tumor development
- Summary
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Chapter 12. Moonlighting GAPDH and age-related neurodegenerative disease: diversity of protein interactions and complexity of function
- GAPDH protein–protein interactions in age-related neurodegenerative disease-I: identification and characterization of neuroprotein binding
- GAPDH protein–protein interactions in age-related neurodegenerative disease-II: amyloid plaques, neurofibrillary tangles, and Lewy bodies
- Functional consequences of GAPDH protein–protein interactions in age-related neurodegenerative disease-I: determination of GAPDH glycolytic activity in vivo
- Functional consequences of GAPDH protein–protein interactions in age-related neurodegenerative disease-II: formation in vivo of GAPDH–neurodegenerative protein complexes
- Functional consequences of GAPDH protein–protein interactions in age-related neurodegenerative disease-III: role of GAPDH: neurodegenerative protein complexes in Huntingtin toxicity
- Summary
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Chapter 13. Functional diversity of GAPDH in infection and immunity: the complexity of “simple” organisms
- The role of moonlighting GAPDH in infection
- The role of GAPDH in the evasion of host defensive measures
- Summary
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Chapter 14. Moonlighting GAPDH and diabetes: pleiotropic effects of perturbations in GAPDH structure and function
- Insulin regulation of GAPDH gene expression: role of insulin response elements in the GAPDH promoter region
- Pleiotropic effects of hyperglycemic GAPDH modification
- Role of GAPDH in diabetic retinopathy-induced apoptosis
- Summary
Section IV. The Pharmacology of Moonlighting GAPDH
- GAPDH and neuropharmacology
- GAPDH and cancer pharmacology
- GAPDH and cardiovascular pharmacology
- Summary
Section V. The Unique Role of Sperm-Specific GAPDH
- Identification of spermatozoic GAPDH
- Localization of spermatozoic GAPDH
- Genetic analysis of GAPDH-S
- Purification and properties of GAPDH-S
- Formation of a glycolytic GAPDH-S fibrous sheath protein complex
- Role of GAPDH-S in human pathology
- Summary
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