The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
Open accessAbstract
Peptidylarginine deiminase (PAD, EC 3.5.3.15) enzymes catalyze the conversion of protein‐bound arginine to citrulline. This post‐translational modification may have a big impact on the structure and function of the target protein. In this review, we will discuss the effects of citrullination and its involvement in several human diseases, including rheumatoid arthritis and multiple sclerosis. So far, four isotypes of PAD have been described in mammals. We describe the existence of PAD in non‐mammalian vertebrates and the existence of a fifth mammalian PAD. In addition, tissue‐specific expression, genomic organization and evolutionary conservation of the different PAD isotypes will be discussed in detail. This article contains supplementary material which may be viewed at the BioEssays website at http://www.interscience.wiley.com/jpages/0265‐9247/suppmat/2003/25/v25.1106.html. BioEssays 25:1106–1118, 2003. © 2003 Wiley Periodicals, Inc.
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McGraw, W. T., Potempa, J., Farley, D., & Travis, J. (1999) · Infection and Immunity · doi:10.1128/iai.67.7.3248-3256.1999 · Cited by 378 · cited 1×
“To date only a single prokaryotic enzyme that can citrullinate proteins has been identified, in Porphyromonas gingivalis.((8)) This enzyme (AAF06719), however, is not evolutionarily related to the vertebrate PAD enzymes, can convert both peptidylarginine and free L-arginine, is not dependent on Ca2þ and shares sequenc…”
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Cited by
Nishimura, K., Sugiyama, D., Kogata, Y., Tsuji, G., Nakazawa, T., Kawano, S., Saigo, K., Morinobu, A., Koshiba, M., Kuntz, K. M., et al. (2007) · Annals of Internal Medicine · doi:10.7326/0003-4819-146-11-200706050-00008 · Cited by 873
Vossenaar, E. R., Radstake, T. R. D., van der Heijden, A., van Mansum, M. A. M., Dieteren, C., de Rooij, D.-J., Barrera, P., Zendman, A. J. W., & van Venrooij, W. J. (2004) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2003.012211 · Cited by 455
Self-citationMorris, S. M. (2016) · The Journal of Nutrition · doi:10.3945/jn.115.226621 · Cited by 435
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Chemical mechanisms of histone lysine and arginine modifications
Smith, B. C., & Denu, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.06.005 · Cited by 390
Metadata
- Authors
- Vossenaar, E. R., Zendman, A. J. W., van Venrooij, W. J., & Pruijn, G. J. M.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 2003-10-17
- Volume
- 25
- Issue
- 11
- Pages
- 1106-1118
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W2005699747
- Cited by
- 983
- References
- 1
- FWCI
- 2.30
- Type
- journal article
- Language
- en
- Open access
- green
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