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dc.contributor.authorJones, Justin E.
dc.contributor.authorCausey, Corey P.
dc.contributor.authorKnuckley, Bryan
dc.contributor.authorSlack-Noyes, Jessica L.
dc.contributor.authorThompson, Paul R
dc.date2022-08-11T08:11:00.000
dc.date.accessioned2022-08-23T17:28:19Z
dc.date.available2022-08-23T17:28:19Z
dc.date.issued2009-09-01
dc.date.submitted2015-06-03
dc.identifier.citationCurr Opin Drug Discov Devel. 2009 Sep;12(5):616-27.
dc.identifier.issn1367-6733 (Linking)
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50055
dc.description<p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p>
dc.description.abstractThe protein arginine deiminases (PADs), and in particular PAD4, have emerged as potential therapeutic targets for the treatment of rheumatoid arthritis (RA). In this review, evidence linking dysregulated PAD activity to the onset and progression of RA is presented, and the potential role of such aberrant activity in other human diseases, such as multiple sclerosis and cancer, is discussed. The known physiological roles of the PADs, particularly PAD4, and current knowledge regarding PAD structure, catalysis and inhibition are also described.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=19736621&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3771078/
dc.subjectAnimals
dc.subjectAntineoplastic Agents
dc.subjectAntirheumatic Agents
dc.subjectArthritis, Rheumatoid
dc.subjectCatalysis
dc.subjectDrug Design
dc.subject*Drug Discovery
dc.subjectEnzyme Inhibitors
dc.subjectHumans
dc.subjectHydrolases
dc.subjectImmunologic Factors
dc.subjectIsoenzymes
dc.subjectModels, Molecular
dc.subjectMolecular Structure
dc.subjectMultiple Sclerosis
dc.subjectNeoplasms
dc.subjectProtein Conformation
dc.subjectStructure-Activity Relationship
dc.subjectProtein Arginine Deiminase
dc.subjectRheumatoid Arthritis
dc.subjectMultiple Sclerosis
dc.subjectCancer
dc.subjectTreatment
dc.subjectInhibitors
dc.subjectBiochemistry
dc.subjectEnzymes and Coenzymes
dc.subjectMedicinal-Pharmaceutical Chemistry
dc.subjectTherapeutics
dc.titleProtein arginine deiminase 4 (PAD4): Current understanding and future therapeutic potential
dc.typeJournal Article
dc.source.journaltitleCurrent opinion in drug discovery and development
dc.source.volume12
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/thompson/62
dc.identifier.contextkey7172280
html.description.abstract<p>The protein arginine deiminases (PADs), and in particular PAD4, have emerged as potential therapeutic targets for the treatment of rheumatoid arthritis (RA). In this review, evidence linking dysregulated PAD activity to the onset and progression of RA is presented, and the potential role of such aberrant activity in other human diseases, such as multiple sclerosis and cancer, is discussed. The known physiological roles of the PADs, particularly PAD4, and current knowledge regarding PAD structure, catalysis and inhibition are also described.</p>
dc.identifier.submissionpaththompson/62
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages616-27


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