(PDF) Protein Deimination in Human Health and Disease 2nd Edition by Nicholas

This is the PDF eBook version for Protein Deimination in Human Health and Disease 2nd Edition by Anthony P. Nicholas, Sanjoy K. Bhattacharya, Paul R. Thompson

Table of Contents

Chapter 1: A History of Deimination Research in Japan. The Founding Fathers. Akihito Ishigami, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan.-Chapter 2: Aspects of Peptidylarginine Deiminase Regulation That May Predispose to Autoreactivity Against Citrullinated Proteins. Indira Neeli and Marko Radic, University of Tennessee Health Science Center, Memphis, TN, USA.-Chapter 3: Structures and Functions of Peptidylarginine Deiminases. Masaki Unno, Kenji Kizawa, Hidenari Takahara, University of Ibaraki, Ibaraki, Japan.-Chapter 4: The Use PAD Knock-Out Mice in Deimination Research, Chinatsu Mukai, Brooke A. Marks and Scott A. Coonrod, Cornell University, Ithaca, NY, USA.-Chapter 5: PAD Activation in Arthritis. Dres Damgaard and Ger J.M. Pruijn, Radboud University, Nijmegen, The Netherlands and Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark.-Chapter 6: Rheumatoid Arthritis: Transition from Systemic Autoimmunity to Joint Inflammation and Bone Loss. Bence Rethi, Akilan Krishnamurthy and Anca I. Catrina, Karolinska University Hospital and Institute, Stockholm, Sweden.-Chapter 7: Porphyromonas Ginvivalis Peptidyl Arginine Deiminase: A Unique Bacterial PAD with Implications for Periodontal Disease and Rheumatoid Arthritis. Katarzyna Gawron, Anna Montgomery, Katarzyna Lazarz-Bartyzel, Grzegorz Bereta, Maria Chomyszyn-Gajewska, Patrick Venables, Jan Potempa, Jagiellonian University, Kraków, Poland and The Kennedy Institute of Rheumatology, Oxford, UK.-Chapter 8: Citrullination and Neutrophil Extracellular Traps. Nishant Dwivedi, Hui-Hsin Chang and I-Cheng Ho, Harvard Medical School, Boston, MA, USA.-Chapter 9: Citrullination and Autophagy. Guido Valesini, Cristiano Alesandri, Tania Colasanti and Fabrizio Conti, La Sapienza Università di Roma, Rome, Italy.-Chapter 10: Antigen Deimination in Human Type 1 Diabetes and Non-Obese Diabetic Mice. Hai Nguyen and Eddie A. James, Benaroya Research Institute, Seattle, Washington, USA.-Chapter 11: Citrullinated Autoantigen Targets as Risk Markers of Cardiovascular and Pulmonary Disease Phenotypes in Rheumatoid Arthritis. Vinitha Ganesan and Dana P. Ascherman, University of Miami, Miami, FL, USA.-Chapter 12: The Significance of Myofilament Protein Citrullination in Heart Failure. Citrullination in Cardiovascular Diseases, Justyna Fert-Bober, E. Crowgey, J. Sokolove, JT. Giles, J. Bathon and J. E. Van Eyk, Cedars Sinai Medical Center, Los Angeles, CA, Alfred I. duPont Hospital for Children, Wilmington, DE, AbbVie Pharmaceuticals, Redwood City, CA and Columbia University New York, NY, USA.-Chapter 13: Protein Deimination in Protein Misfolding Disorders – Modelled in Human induced Pluripotent Stem Cells (iPSCs). Sigrun Lange, Selina Wray, Mike Devine, Mar Matarin and John Hardy, University of Westminster and University College London School of Pharmacy and Institute of Neurology, London, UK.-Chapter 14: Protein Deimination in Aging and Age-Related Diseases with Ocular Manifestations. Di Ding, Mabel Enriquez-Algeciras, Sanjoy K. Bhattacharya and Vera L Bonilha. Bascom Palmer Eye Institute, University of Miami, Florida and Cole Eye Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.-Chapter 15: Chemical Modification and Mass Spectrometric Approaches for Detection of Brain Protein Deimination. Mabel Enriquez- Algeciras, Di Ding, Dana P. Ascherman and Sanjoy K. Bhattacharya, University of Miami, Miami, FL, USA.-Chapter 16: Citrullination Following Traumatic Brain Injury: A Mechanism for Ongoing Pathology Through Protein Modification. Rachel C. Lazarus John E. Buonora, Alaa Kamnaksh, Michael N. Flora, James G. Freedy, Gay R. Holstein, Giorgio P. Martinelli, David M. Jacobowitz, Denes Agoston and Gregory P Mueller, Uniformed Services University of the Health Sciences, Bethesda, MD, USA.-Chapter 17: Update on Deimination in Alzheimer’s Disease. Yoshitaka Kondo, Eun-Kyoung Choi,Yong-Sun Kim and Akihito Ishigami, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan and Hallym University, Gyeonggi-do, Republic of Korea.-Chapter 18: Deimination in Multiple Sclerosis: The Bad, the Good and the Ugly. William R. Meador, John R. Rinker and Anthony P. Nicholas, University of Alabama at Birmingham and The Birmingham VA Medical Center, Birmingham, AL, USA.-Chapter 19: Turning White Matter “Inside-Out” by Hyper-Deimination of Myelin Basic Protein (MBP). George Harauz, University of Guelph, Guelph, ON, Canada.-Chapter 20: The Significance of Deiminated GFAP in Neurodegenerative Diseases with Special Emphasis on Alexander’s Disease. Michael Brenner and Anthony P. Nicholas, University of Alabama at Birmingham, Birmingham, AL, USA.-Chapter 21: Treatment of Prostate Cancer Using Deimination Antagonists and Microvescicle Technology. Sigrun Lange, Sharad Kholia, Uchini S Kosgodage and Jameel M. Inal, University College London School of Pharmacy, University of Westminster and London Metropolitan University, London, UK.-Chapter 22: Citrullination in Inflammatory-Driven Carcinogenesis of the Colon. Erin E. Witalison and Lorne J. Hofseth, University of South Carolina, Columbia, SC, USA.-Chapter 23: Development of the Protein Arginine Deiminase (PAD) Inhibitors. Aaron Muth and Paul R. Thompson, UMASS Medical School, Worcester, MA, USA.