Protein Deimination in Human Health and Disease

Nonfiction, Health & Well Being, Medical, Medical Science, Immunology, Specialties, Internal Medicine, Neuroscience, Science & Nature, Science
Cover of the book Protein Deimination in Human Health and Disease by , Springer New York
View on Amazon View on AbeBooks View on Kobo View on B.Depository View on eBay View on Walmart
Author: ISBN: 9781461483175
Publisher: Springer New York Publication: December 3, 2013
Imprint: Springer Language: English
Author:
ISBN: 9781461483175
Publisher: Springer New York
Publication: December 3, 2013
Imprint: Springer
Language: English

Deimination is a relatively new post-translational modification of proteins, whose recognition is ever-increasing. First linked to the pathology of rheumatoid arthritis (RA), deimination is a process by which selected positively charged arginine amino acids are converted to neutral citrulline amino acids by the peptidyl arginine deiminase (PAD) family of enzymes.

Although the medical literature is rich with articles about the possible significance of deiminated proteins in RA, Protein Deimination in Human Health and Disease is the first publication to compile this knowledge and the growing amount of new information now known about the presence of deiminated proteins in the eye, skin, hair, gums, lung and nervous system, as well. As a result, this process has now been linked to numerous additional conditions besides RA, including cancer, glaucoma, Alzheimer's disease, Parkinson's disease, multiple sclerosis, spinal cord and peripheral nerve injury, Creutzfeldt-Jakob disease, among many others.

Chronicling the earliest studies of deimination up to the present, this volume distills what is currently known about citrullination of proteins in the human body and is the first book of its kind on the topic.

View on Amazon View on AbeBooks View on Kobo View on B.Depository View on eBay View on Walmart

Deimination is a relatively new post-translational modification of proteins, whose recognition is ever-increasing. First linked to the pathology of rheumatoid arthritis (RA), deimination is a process by which selected positively charged arginine amino acids are converted to neutral citrulline amino acids by the peptidyl arginine deiminase (PAD) family of enzymes.

Although the medical literature is rich with articles about the possible significance of deiminated proteins in RA, Protein Deimination in Human Health and Disease is the first publication to compile this knowledge and the growing amount of new information now known about the presence of deiminated proteins in the eye, skin, hair, gums, lung and nervous system, as well. As a result, this process has now been linked to numerous additional conditions besides RA, including cancer, glaucoma, Alzheimer's disease, Parkinson's disease, multiple sclerosis, spinal cord and peripheral nerve injury, Creutzfeldt-Jakob disease, among many others.

Chronicling the earliest studies of deimination up to the present, this volume distills what is currently known about citrullination of proteins in the human body and is the first book of its kind on the topic.

More books from Springer New York

Cover of the book Indoor Location Technologies by
Cover of the book Cognitive Pearls in General Surgery by
Cover of the book Applied Pharmacometrics by
Cover of the book Android Malware by
Cover of the book Individual and Small Group Decisions by
Cover of the book Biofilm Infections by
Cover of the book Handbook of Single-Molecule Biophysics by
Cover of the book Contract Research and Development Organizations by
Cover of the book Handbook of Practical Immunohistochemistry by
Cover of the book Nitroazoles: Synthesis, Structure and Applications by
Cover of the book Domains in Ferroic Crystals and Thin Films by
Cover of the book Fast Compact Algorithms and Software for Spline Smoothing by
Cover of the book Molecular Surgical Pathology by
Cover of the book Convection in Porous Media by
Cover of the book Micro and Nano Flow Systems for Bioanalysis by
We use our own "cookies" and third party cookies to improve services and to see statistical information. By using this website, you agree to our Privacy Policy