The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.
Protein Arginine Deiminases and Associated Citrullination: Physiological Functions and Diseases Associated with Dysregulation
Open accessAbstract
Human proteins are subjected to more than 200 known post-translational modifications (PTMs) (e.g., phosphorylation, glycosylation, ubiquitination, S-nitrosylation, methylation, Nacetylation, and citrullination) and these PTMs can alter protein structure and function with consequent effects on the multitude of pathways necessary for maintaining the physiological homeostasis. When dysregulated, however, the enzymes that catalyze these PTMs can impact the genesis of countless diseases. In this review, we will focus on protein citrullination, a PTM catalyzed by the Protein Arginine Deiminase (PAD) family of enzymes. Specifically, we will describe the roles of the PADs in both normal human physiology and disease. The development of PAD inhibitors and their efficacy in a variety of autoimmune disorders and cancer will also be discussed.
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Cancer Vaccines, Adjuvants, and Delivery Systems
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Kriebel, K., Hieke, C., Müller-Hilke, B., Nakata, M., & Kreikemeyer, B. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00053 · Cited by 118
“Physiologically, citrullination impacts gene regulation, terminal differentiation, and apoptosis, thus dysregulated citrullination is associated with numerous disorders, including autoimmune and neurodegenerative diseases (Witalison et al., 2015).”
BackgroundProximity-Dependent Labeling of Cysteines
Sen, S., Sultana, N., Shaffer, S. A., & Thompson, P. R. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c07069 · Cited by 11
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Metadata
- Authors
- Witalison, E., Thompson, P., & Hofseth, L.
- Venue
- Current Drug Targets
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2015-07-27
- Volume
- 16
- Issue
- 7
- Pages
- 700-710
- ISSN
- 1389-4501 (ISSN-L)
- OpenAlex
- W2160128879
- Cited by
- 310
- References
- 90
- FWCI
- 6.30
- Type
- journal article
- Language
- en
- Open access
- green
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