Protein Deimination in Human Health and Disease
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...
| Συγγραφή απο Οργανισμό/Αρχή: | |
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| Άλλοι συγγραφείς: | , |
| Μορφή: | Ηλεκτρονική πηγή Ηλ. βιβλίο |
| Γλώσσα: | English |
| Έκδοση: |
New York, NY :
Springer New York : Imprint: Springer,
2014.
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| Θέματα: | |
| Διαθέσιμο Online: | Full Text via HEAL-Link |
Πίνακας περιεχομένων:
- Physiological pathways of PAD activity and citrullinated epitope generation
- from citrullination to specific immunity and disease in rheumatoid arthritis
- The role of citrullinated proteins in the pathophysiology of rheumatoid arthritis
- Protein citrullination: the link between rheumatoid arthritis and periodontitis?
- From genes and environment to anti-culture immunity in rheumatoid arthritis: The role of the lungs
- Neutrophils and their contribution to autoimmunity in rheumatoid arthritis
- Deimination in skin and regulation of PAD expression in keratinocytes
- Importance of citrullination on hair protein molecular assembly during trichocytic differentiation
- Deimination in the peripheral nervous system: A wallflower existence
- Deimination in multiple sclerosis and experimental autoimmune encephalomyelitis
- Protein hypercitrullination in CNS demyelinating disease reversed by PAD inhibition
- Deimination in prion diseases
- Deimination in Alzheimer's disease
- Ongoing studies of deimination in neurodegenerative diseases using the F95 antibody
- The role of protein deimination in epigenetics
- Identifying citrullination sites by mass spectroscopy
- Homocitrulline—an analogue and confounder related to citrulline
- Picking the PAD lock: Chemical and biological approaches to identify PAD substrates and inhibitors.
