An improved synthesis of haloaceteamidine-based inactivators of protein arginine deiminase 4 (PAD4)
| dc.contributor.author | Causey, Corey P. | |
| dc.contributor.author | Thompson, Paul R | |
| dc.date | 2022-08-11T08:11:00.000 | |
| dc.date.accessioned | 2022-08-23T17:28:21Z | |
| dc.date.available | 2022-08-23T17:28:21Z | |
| dc.date.issued | 2008-07-07 | |
| dc.date.submitted | 2015-06-03 | |
| dc.identifier.citation | Tetrahedron Lett. 2008 Jul 7;49(28):4383-4385. <a href="http://dx.doi.org/10.1016/j.tetlet.2008.05.021">Link to article on publisher's site</a> | |
| dc.identifier.issn | 0040-4039 (Linking) | |
| dc.identifier.doi | 10.1016/j.tetlet.2008.05.021 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14038/50061 | |
| dc.description | <p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p> | |
| dc.description.abstract | Protein arginine deiminase 4 (PAD4) is an enzyme that hydrolyzes peptidyl arginine residues to form citrulline and ammonia. This enzyme has been implicated in several disease states, e.g. rheumatoid arthritis, and therefore represents a unique target for the development of a novel therapeutic. A solution-phase synthesis of Cl-amidine, the most potent PAD4 inactivator described to date, has been developed. This synthesis proceeds in 80% yield over 4 steps at a significantly (12-fold) lower cost. | |
| dc.language.iso | en_US | |
| dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=19587776&dopt=Abstract">Link to Article in PubMed</a> | |
| dc.relation.url | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2597826/ | |
| dc.subject | Biochemistry | |
| dc.subject | Enzymes and Coenzymes | |
| dc.subject | Medicinal-Pharmaceutical Chemistry | |
| dc.subject | Therapeutics | |
| dc.title | An improved synthesis of haloaceteamidine-based inactivators of protein arginine deiminase 4 (PAD4) | |
| dc.type | Journal Article | |
| dc.source.journaltitle | Tetrahedron letters | |
| dc.source.volume | 49 | |
| dc.source.issue | 28 | |
| dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/thompson/68 | |
| dc.identifier.contextkey | 7172289 | |
| html.description.abstract | <p>Protein arginine deiminase 4 (PAD4) is an enzyme that hydrolyzes peptidyl arginine residues to form citrulline and ammonia. This enzyme has been implicated in several disease states, e.g. rheumatoid arthritis, and therefore represents a unique target for the development of a novel therapeutic. A solution-phase synthesis of Cl-amidine, the most potent PAD4 inactivator described to date, has been developed. This synthesis proceeds in 80% yield over 4 steps at a significantly (12-fold) lower cost.</p> | |
| dc.identifier.submissionpath | thompson/68 | |
| dc.contributor.department | Department of Biochemistry and Molecular Pharmacology | |
| dc.source.pages | 4383-4385 |
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