TDP-43 and Neurodegeneration

From Bench to Bedside

Vijay Kumar, Manoj Kumar Jaiswal

• Publisher: Academic Press
• Year: 2021
• Print ISBN:
  9780128200667
• eBook ISBN:
  9780128204405
• Topic: Medicine
• Subtopic: Medical Theory, Practice & Reference

Aggregates of the TAR DNA binding protein 43 (TDP-43), are hallmark features of the neurodegenerative diseases Amyotrophic Lateral Sclerosis (ALS) and frontotemporal dementia (FTD), with overlapping clinical, genetic and pathological features. TDP-43 and Neurodegeneration: From Bench to Bedside summarizes new findings in TDP-43 pathobiology and proteinopathies. The book summarizes TDP-43's structure, function, biology, misfolding, aggregation, pathogenesis and therapeutics. It includes autophagy-mediated therapy, role of stress granule, novel genetic, cell culture-based models, systems biology for precision medicine, development of stem cells and mechanism-based therapies that can target ALS and other related neurodegenerative diseases. This book is written for neuroscientists, neurologists, clinicians, advanced graduate students, drug discovery researchers, as well as cellular and molecular biologists involved in ALS, motor neuron disease (MND) and other neurodegenerative disorders. - Reviews TDP-43 structure, folding, function, and pathology - Identifies TDP-43 role in ALS, FTP, and other neurodegenerative diseases - Presents a systems and precision biology perspective of TDP-43 - Discusses therapeutics of TDP-43 proteinopathies - Translates bench research to application bedside

Table of contents

• Title of Book
• Cover image
• Title page
• Table of Contents
• Copyright
• List of contributors
• Preface
• Chapter 1 TDP-43 and neurodegenerative diseases: past, present, and future
• Chapter 2 Structural dissection of TDP-43: insights into physiological and pathological self-assembly
• Chapter 3 Posttranslational modifications of TDP-43
• Chapter 4 Regulation of autophagy by TDP-43: a promising therapeutic intervention in neurodegenerative diseases
• Chapter 5 Prion-like behavior of TDP-43 aggregates and its implication to disease
• Chapter 6 Search for functions of intrinsically disordered prion-like domains for FET proteins involved in amyotrophic lateral sclerosis and frontotemporal dementia
• Chapter 7 A systems biology approach to understand the role of TDP-43 in amyotrophic lateral sclerosis
• Chapter 8 TDP-43 proteinopathy mechanisms from non-mammalian model systems
• Chapter 9 New opportunities for treatment of neurodegenerative disease through the modulation of TDP-43
• Index