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dc.contributor.authorBicker, Kevin L.
dc.contributor.authorThompson, Paul R
dc.date2022-08-11T08:11:00.000
dc.date.accessioned2022-08-23T17:28:08Z
dc.date.available2022-08-23T17:28:08Z
dc.date.issued2013-02-01
dc.date.submitted2015-05-22
dc.identifier.citationBiopolymers. 2013 Feb;99(2):155-63. doi: 10.1002/bip.22127. <a href="http://dx.doi.org/10.1002/bip.22127">Link to article on publisher's site</a>
dc.identifier.issn0006-3525 (Linking)
dc.identifier.doi10.1002/bip.22127
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50016
dc.description<p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p>
dc.description.abstractThe post-translational modification of histones has significant effects on overall chromatin function. One such modification is citrullination, which is catalyzed by the protein arginine deiminases (PADs), a unique family of enzymes that catalyzes the hydrolysis of peptidyl-arginine to form peptidyl-citrulline on histones, fibrinogen, and other biologically relevant proteins. Overexpression and/or increased PAD activity is observed in several diseases, including rheumatoid arthritis, Alzheimer's disease, multiple sclerosis, lupus, Parkinson's disease, and cancer. This review discusses the important structural and mechanistic characteristics of the PADs, as well as recent investigations into the role of the PADs in increasing disease severity in RA and colitis and the importance of PAD activity in mediating neutrophil extracellular trap formation through chromatin decondensation. Lastly, efforts to develop PAD inhibitors with excellent potency, selectivity and in vivo efficacy are discussed, highlighting the most promising inhibitors. (c) 2012 Wiley Periodicals, Inc. Biopolymers 99: 155-163, 2013.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=23175390&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3507426/
dc.subjectBiochemistry
dc.subjectEnzymes and Coenzymes
dc.subjectMedicinal-Pharmaceutical Chemistry
dc.subjectTherapeutics
dc.titleThe protein arginine deiminases: Structure, function, inhibition, and disease.
dc.typeJournal Article
dc.source.journaltitleBiopolymers
dc.source.volume99
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/thompson/27
dc.identifier.contextkey7135684
html.description.abstract<p>The post-translational modification of histones has significant effects on overall chromatin function. One such modification is citrullination, which is catalyzed by the protein arginine deiminases (PADs), a unique family of enzymes that catalyzes the hydrolysis of peptidyl-arginine to form peptidyl-citrulline on histones, fibrinogen, and other biologically relevant proteins. Overexpression and/or increased PAD activity is observed in several diseases, including rheumatoid arthritis, Alzheimer's disease, multiple sclerosis, lupus, Parkinson's disease, and cancer. This review discusses the important structural and mechanistic characteristics of the PADs, as well as recent investigations into the role of the PADs in increasing disease severity in RA and colitis and the importance of PAD activity in mediating neutrophil extracellular trap formation through chromatin decondensation. Lastly, efforts to develop PAD inhibitors with excellent potency, selectivity and in vivo efficacy are discussed, highlighting the most promising inhibitors. (c) 2012 Wiley Periodicals, Inc. Biopolymers 99: 155-163, 2013.</p>
dc.identifier.submissionpaththompson/27
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages155-63


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