Автор: Anthony P. Nicholas, Sanjoy K. Bhattacharya, Paul R. Thompson Название: Protein Deimination in Human Health and Disease, 2nd Edition Издательство: Springer Год: 2017 ISBN: 3319582437 Язык: English Формат: pdf Размер: 16,2 mb Страниц: 474
Published in 2014, Protein Deimination in Human Health and Disease was the first book on this novel post-translational modification, in which selected positively-charged arginine amino acids are converted to neutral citrulline amino acids by the peptidyl-arginine deiminase (PAD) family of enzymes. This area of research continues to expand rapidly, necessitating the need for this second edition.
The first edition outlined what was known about citrullinated proteins in normal tissues such as skin and hair, as well as in maladies such as rheumatoid arthritis (RA), multiple sclerosis (MS), Alzheimer’s disease (AD), glaucoma, peripheral nerve injury, neonatal hypoxic brain damage, and breast cancer. This second edition addresses numerous additional disorders such as diabetes, asthma, traumatic brain injury, inflammatory bowel disease, lupus, bone disease, heart failure, fronto-temporal dementia, and prostate and colon cancer. It also provides updates on the deimination research covering the three seminal diseases first linked to this process (RA, MS and AD), and details how auto-antibodies against citrullinated proteins contribute to disease. In addition, new hypotheses on the possible pathologic mechanisms of citrullinated myelin basic protein and glial fibrillary acidic protein are also proposed. This second edition also outlines the latest developments in therapeutic strategies, including the use of new PAD antagonists and innovative techniques such as micro-vescicles and stem cells as possible mechanisms to treat these conditions.
A History of Deimination Research in Japan: The Founding Fathers Takahara, Hidenari Pages 1-10
Aspects of Peptidylarginine Deiminase Regulation that May Predispose to Autoreactivity Against Citrullinated Proteins Neeli, Indira (et al.) Pages 11-32
Structures and Functions of Peptidylarginine Deiminases Unno, Masaki (et al.) Pages 33-46
The Use of Genetically Engineered Mice to Study PAD Biology and Pathology Mukai, Chinatsu (et al.) Pages 47-61
PAD Activation in Arthritis Damgaard, Dres (et al.) Pages 63-83
Rheumatoid Arthritis: Transition from Systemic Autoimmunity to Joint Inflammation and Bone Loss Rethi, Bence (et al.) Pages 85-97
Porphyromonas gingivalis Peptidyl Arginine Deiminase: A Unique Bacterial PAD with Implications for Periodontal Disease and Rheumatoid Arthritis Gawron, Katarzyna (et al.) Pages 99-135
Citrullination and Neutrophil Extracellular Traps Dwivedi, Nishant (et al.) Pages 137-159
Citrullination and Autophagy Valesini, Guido (et al.) Pages 161-172
Antigen Deimination in Human Type 1 Diabetes and Nonobese Diabetic Mice Nguyen, Hai (et al.) Pages 173-189
Citrullinated Autoantigen Targets as Markers of Extra-Articular Disease in Rheumatoid Arthritis Ganesan, Vinitha (et al.) Pages 191-203
The Significance of Myofilament Protein Citrullination in Heart Failure: Citrullination in Cardiovascular Diseases Fert-Bober, J. (et al.) Pages 205-225
Protein Deimination in Protein Misfolding Disorders: Modeled in Human Induced Pluripotent Stem Cells (iPSCs) Lange, Sigrun (et al.) Pages 227-239
Protein Deimination in Aging and Age-Related Diseases with Ocular Manifestations Ding, Di (et al.) Pages 241-251
Chemical Modification and Mass Spectrometric Approaches for Detection of Brain Protein Deimination Enriquez-Algeciras, Mabel (et al.) Pages 253-273
Citrullination Following Traumatic Brain Injury: A Mechanism for Ongoing Pathology Through Protein Modification Lazarus, Rachel C. (et al.) Pages 275-291
Update on Deimination in Alzheimer’s Disease Kondo, Yoshitaka (et al.) Pages 293-315
Deimination in Multiple Sclerosis: The Bad, the Good, and the Ugly Meador, William R. (et al.) Pages 317-336
Turning White Matter “Inside-Out” by Hyper-deimination of Myelin Basic Protein (MBP) Harauz, George Pages 337-389
The Significance of Deiminated GFAP in Neurodegenerative Diseases with Special Emphasis on Alexander Disease Brenner, Michael (et al.) Pages 391-412
Treatment of Prostate Cancer Using Deimination Antagonists and Microvesicle Technology Lange, Sigrun (et al.) Pages 413-425
Citrullination in Inflammatory-Driven Carcinogenesis of the Colon Witalison, Erin E. (et al.) Pages 427-443
Development of the Protein Arginine Deiminase (PAD) Inhibitors Muth, Aaron (et al.) Pages 445-466
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Protein Deimination in Human Health and Disease, 2nd Edition 
