{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,26]],"date-time":"2026-06-26T04:31:25Z","timestamp":1782448285960,"version":"3.54.5"},"publisher-location":"New York, NY","reference-count":14,"publisher":"Springer New York","isbn-type":[{"value":"9781493995318","type":"print"},{"value":"9781493995325","type":"electronic"}],"license":[{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019]]},"DOI":"10.1007\/978-1-4939-9532-5_13","type":"book-chapter","created":{"date-parts":[[2019,5,31]],"date-time":"2019-05-31T09:02:33Z","timestamp":1559293353000},"page":"169-177","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["In Vitro Assays to Monitor the Enzymatic Activities of zDHHC Protein Acyltransferases"],"prefix":"10.1007","author":[{"given":"David A.","family":"Mitchell","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura C.","family":"Pendleton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert J.","family":"Deschenes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,6,1]]},"reference":[{"key":"13_CR1","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1038\/nrm2084","volume":"8","author":"ME Linder","year":"2007","unstructured":"Linder ME, Deschenes RJ (2007) Palmitoylation: policing protein stability and traffic. Nat Rev Mol Cell Biol 8:74\u201384","journal-title":"Nat Rev Mol Cell Biol"},{"key":"13_CR2","doi-asserted-by":"publisher","first-page":"1118","DOI":"10.1194\/jlr.R600007-JLR200","volume":"47","author":"DA Mitchell","year":"2006","unstructured":"Mitchell DA, Vasudevan A, Linder ME, Deschenes RJ (2006) Protein palmitoylation by a family of DHHC protein S-acyltransferases. J Lipid Res 47:1118\u20131127","journal-title":"J Lipid Res"},{"key":"13_CR3","doi-asserted-by":"publisher","first-page":"41268","DOI":"10.1074\/jbc.M206573200","volume":"277","author":"S Lobo","year":"2002","unstructured":"Lobo S, Greentree W, Linder M, Deschenes R (2002) Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J Biol Chem 277:41268\u201341273","journal-title":"J Biol Chem"},{"key":"13_CR4","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1083\/jcb.200206120","volume":"159","author":"AF Roth","year":"2002","unstructured":"Roth AF, Feng Y, Chen L, Davis NG (2002) The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J Cell Biol 159:23\u201328","journal-title":"J Cell Biol"},{"key":"13_CR5","doi-asserted-by":"publisher","first-page":"38104","DOI":"10.1074\/jbc.M110.169102","volume":"285","author":"DA Mitchell","year":"2010","unstructured":"Mitchell DA, Mitchell G, Ling Y, Budde C, Deschenes RJ (2010) Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes. J Biol Chem 285:38104\u201338114","journal-title":"J Biol Chem"},{"key":"13_CR6","doi-asserted-by":"publisher","first-page":"7236","DOI":"10.1074\/jbc.M111.337246","volume":"287","author":"BC Jennings","year":"2012","unstructured":"Jennings BC, Linder ME (2012) DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities. J Biol Chem 287:7236\u20137245","journal-title":"J Biol Chem"},{"key":"13_CR7","doi-asserted-by":"publisher","first-page":"34337","DOI":"10.1074\/jbc.M112.379297","volume":"287","author":"DA Mitchell","year":"2012","unstructured":"Mitchell DA, Hamel LD, Ishizuka K, Mitchell G, Schaefer LM, Deschenes RJ (2012) The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the Acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate. J Biol Chem 287:34337\u201334348","journal-title":"J Biol Chem"},{"key":"13_CR8","doi-asserted-by":"publisher","first-page":"18582","DOI":"10.1074\/jbc.M114.567420","volume":"289","author":"DA Mitchell","year":"2014","unstructured":"Mitchell DA, Hamel LD, Reddy KD, Farh L, Rettew LM, Sanchez PR, Deschenes RJ (2014) Mutations in the X-linked intellectual disability gene, zDHHC9, alter autopalmitoylation activity by distinct mechanisms. J Biol Chem 289:18582\u201318592","journal-title":"J Biol Chem"},{"key":"13_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ab.2014.05.013","volume":"460","author":"LD Hamel","year":"2014","unstructured":"Hamel LD, Deschenes RJ, Mitchell DA (2014) A fluorescence-based assay to monitor autopalmitoylation of zDHHC proteins applicable to high throughput screening. Anal Biochem 460:1\u20138","journal-title":"Anal Biochem"},{"key":"13_CR10","doi-asserted-by":"publisher","first-page":"262","DOI":"10.2174\/1386207319666160324123844","volume":"19","author":"LD Hamel","year":"2016","unstructured":"Hamel LD, Lenhart BJ, MItchell DA, Santos RG, Giulianotti MA, Deschenes RJ (2016) Identification of protein palmitoylation inhibitors from a scaffold ranking library. Comb Chem High Throughput Screen 19:262\u2013274","journal-title":"Comb Chem High Throughput Screen"},{"key":"13_CR11","doi-asserted-by":"publisher","first-page":"447","DOI":"10.1016\/0006-3002(60)91280-4","volume":"38","author":"V Massey","year":"1960","unstructured":"Massey V (1960) The composition of the ketoglutarate dehydrogenase complex. Biochim Biophys Acta 38:447\u2013460","journal-title":"Biochim Biophys Acta"},{"key":"13_CR12","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1042\/bj1410205","volume":"141","author":"AC Storer","year":"1974","unstructured":"Storer AC, Cornish-Bowden A (1974) The kinetics of coupled enzyme reactions. Applications to the assay of glucokinase, with glucose 6-phosphate dehydrogenase as coupling enzyme. Biochem J 141:205\u2013209","journal-title":"Biochem J"},{"key":"13_CR13","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1042\/bj0970587","volume":"97","author":"PB Garland","year":"1965","unstructured":"Garland PB, Shepherd D, Yates DW (1965) Steady-state concentrations of coenzyme A, acetyl-coenzyme A and long-chain fatty acyl-coenzyme A in rat-liver mitochondria oxidizing palmitate. Biochem J 97:587\u2013594","journal-title":"Biochem J"},{"key":"13_CR14","doi-asserted-by":"publisher","first-page":"454","DOI":"10.1016\/0076-6879(95)50090-1","volume":"250","author":"L Berthiaume","year":"1995","unstructured":"Berthiaume L, Peseckis SM, Resh MD (1995) Synthesis and use of iodo-fatty acid analogs. Methods Enzymol 250:454\u2013466","journal-title":"Methods Enzymol"}],"container-title":["Methods in Molecular Biology","Protein Lipidation"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-4939-9532-5_13","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,5,31]],"date-time":"2019-05-31T09:02:50Z","timestamp":1559293370000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-1-4939-9532-5_13"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019]]},"ISBN":["9781493995318","9781493995325"],"references-count":14,"URL":"https:\/\/doi.org\/10.1007\/978-1-4939-9532-5_13","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"value":"1064-3745","type":"print"},{"value":"1940-6029","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019]]},"assertion":[{"value":"1 June 2019","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}