The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Inhibitors and Inactivators of Protein Arginine Deiminase 4: Functional and Structural Characterization,
Open accessAbstract
Protein arginine deiminase 4 (PAD4) is a transcriptional coregulator that catalyzes the calcium-dependent conversion of specific arginine residues in proteins to citrulline. Recently, we reported the synthesis and characterization of F-amidine, a potent and bioavailable irreversible inactivator of PAD4. Herein, we report our efforts to identify the steric and leaving group requirements for F-amidine-induced PAD4 inactivation, the structure of the PAD4-F-amidine x calcium complex, and in vivo studies with N-alpha-benzoyl-N5-(2-chloro-1-iminoethyl)-L-ornithine amide (Cl-amidine), a PAD4 inactivator with enhanced potency. The PAD4 inactivators described herein will be useful pharmacological probes in characterizing the incompletely defined physiological role(s) of this enzyme. In addition, they represent potential lead compounds for the treatment of rheumatoid arthritis because a growing body of evidence supports a role for PAD4 in the onset and progression of this chronic autoimmune disorder.
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Self-citationPAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
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Cited by
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Diabetes primes neutrophils to undergo NETosis, which impairs wound healing
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Regulation of histone methylation by demethylimination and demethylation
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Chemical mechanisms of histone lysine and arginine modifications
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Metadata
- Authors
- Luo, Y., Arita, K., Bhatia, M., Knuckley, B., Lee, Y.-H., Stallcup, M. R., Sato, M., & Thompson, P. R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-09-09
- Volume
- 45
- Issue
- 39
- Pages
- 11727-11736
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1979179968
- Cited by
- 290
- References
- 28
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- green
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