{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T03:53:37Z","timestamp":1790481217374,"version":"4.1.0"},"reference-count":30,"publisher":"Public Library of Science (PLoS)","issue":"1","license":[{"start":{"date-parts":[[2018,1,24]],"date-time":"2018-01-24T00:00:00Z","timestamp":1516752000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01 GM111703"],"award-info":[{"award-number":["R01 GM111703"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","award":["Medical Research Fellows Program"],"award-info":[{"award-number":["Medical Research Fellows Program"]}],"id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0190255","type":"journal-article","created":{"date-parts":[[2018,1,24]],"date-time":"2018-01-24T13:28:32Z","timestamp":1516800512000},"page":"e0190255","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":19,"title":["Development of an activity-based probe for acyl-protein thioesterases"],"prefix":"10.1371","volume":"13","author":[{"given":"Megan","family":"Garland","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher J.","family":"Schulze","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian T.","family":"Foe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wouter A.","family":"van der Linden","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew A.","family":"Child","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3753-4412","authenticated-orcid":true,"given":"Matthew","family":"Bogyo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2018,1,24]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1038\/nsmb.1842","article-title":"Post-translational modifications in signal integration","volume":"17","author":"YL Deribe","year":"2010","journal-title":"Nat Struct Mol Biol"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/cr.2013.151","article-title":"Protein post-translational modifications and regulation of pluripotency in human stem cells","volume":"24","author":"YC Wang","year":"2014","journal-title":"Cell Res"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/nrm3787","article-title":"Post-translational modification: Sweetening protein quality control","volume":"15","author":"A Du Toit","year":"2014","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.3389\/fmicb.2015.01312","article-title":"Elucidating Host-Pathogen Interactions Based on Post-Translational Modifications Using Proteomics Approaches","volume":"6","author":"V Ravikumar","year":"2015","journal-title":"Front Microbiol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/nrm2084","article-title":"Palmitoylation: policing protein stability and traffic","volume":"8","author":"ME Linder","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1021\/cb300607e","article-title":"Fat chance! Getting a grip on a slippery modification","volume":"8","author":"CT Tom","year":"2013","journal-title":"ACS Chem Biol"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1083\/jcb.201008160","article-title":"The intracellular dynamic of protein palmitoylation","volume":"191","author":"C Salaun","year":"2010","journal-title":"J Cell Biol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1038\/nmeth.1769","article-title":"Global profiling of dynamic protein palmitoylation","volume":"9","author":"BR Martin","year":"2011","journal-title":"Nat Methods"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/nmeth.1293","article-title":"Large-scale profiling of protein palmitoylation in mammalian cells","volume":"6","author":"BR Martin","year":"2009","journal-title":"Nat Methods"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/nchembio.362","article-title":"Small-molecule inhibition of APT1 affects Ras localization and signaling","volume":"6","author":"FJ Dekker","year":"2010","journal-title":"Nat Chem Biol"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.chembiol.2016.12.007","article-title":"APT2 Inhibition Restores Scribble Localization and S-Palmitoylation in Snail-Transformed Cells","volume":"24","author":"JL Hernandez","year":"2017","journal-title":"Cell Chem Biol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1038\/nchembio.1315","article-title":"Small-molecule inhibition of a depalmitoylase enhances Toxoplasma host-cell invasion","volume":"9","author":"MA Child","year":"2013","journal-title":"Nat Chem Biol"},{"key":"ref13","article-title":"A fluorescent probe for cysteine depalmitoylation reveals dynamic APT signaling","author":"RS Kathayat","year":"2016","journal-title":"Nat Chem Biol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1146\/annurev-biochem-060713-035352","article-title":"Activity-based profiling of proteases","volume":"83","author":"LE Sanman","year":"2014","journal-title":"Annu Rev Biochem"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"20941","DOI":"10.1073\/pnas.1011663107","article-title":"Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screening","volume":"107","author":"DA Bachovchin","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"14694","DOI":"10.1073\/pnas.96.26.14694","article-title":"Activity-based protein profiling: the serine hydrolases","volume":"96","author":"Y Liu","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"10568","DOI":"10.1073\/pnas.1105622108","article-title":"Chemical genetic screen identifies Toxoplasma DJ-1 as a regulator of parasite secretion, attachment, and invasion","volume":"108","author":"CI Hall","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1038\/nchembio.70","article-title":"Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum","volume":"4","author":"S Arastu-Kapur","year":"2008","journal-title":"Nat Chem Biol"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"1831","DOI":"10.1021\/bi00329a005","article-title":"Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor","volume":"24","author":"JW Harper","year":"1985","journal-title":"Biochemistry"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1002\/jcb.240390105","article-title":"Mechanism-based isocoumarin inhibitors for serine proteases: use of active site structure and substrate specificity in inhibitor design","volume":"39","author":"JC Powers","year":"1989","journal-title":"J Cell Biochem"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1021\/acsinfecdis.6b00092","article-title":"Design of Selective Substrates and Activity-Based Probes for Hydrolase Important for Pathogenesis 1 (HIP1) from Mycobacterium tuberculosis","volume":"2","author":"CS Lentz","year":"2016","journal-title":"ACS Infect Dis"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"10345","DOI":"10.1021\/ja303400u","article-title":"Confirming target engagement for reversible inhibitors in vivo by kinetically tuned activity-based probes","volume":"134","author":"A Adibekian","year":"2012","journal-title":"J Am Chem Soc"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"27002","DOI":"10.1074\/jbc.M113.460709","article-title":"Characterization of a serine hydrolase targeted by acyl-protein thioesterase inhibitors in Toxoplasma gondii","volume":"288","author":"LE Kemp","year":"2013","journal-title":"J Biol Chem"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"1566","DOI":"10.1016\/j.bbalip.2013.07.008","article-title":"Cancer cells incorporate and remodel exogenous palmitate into structural and oncogenic signaling lipids","volume":"1831","author":"SM Louie","year":"2013","journal-title":"Biochim Biophys Acta"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.cell.2009.11.027","article-title":"Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis","volume":"140","author":"DK Nomura","year":"2010","journal-title":"Cell"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1038\/nature11003","article-title":"The Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity","volume":"483","author":"J Barretina","year":"2012","journal-title":"Nature"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1038\/nbt.1531","article-title":"Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes","volume":"27","author":"DA Bachovchin","year":"2009","journal-title":"Nat Biotechnol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"e11985","DOI":"10.1371\/journal.pone.0011985","article-title":"Use of activity-based probes to develop high throughput screening assays that can be performed in complex cell extracts","volume":"5","author":"E Deu","year":"2010","journal-title":"PLoS One"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/j.bmc.2011.03.014","article-title":"Alkyne derivatives of isocoumarins as clickable activity-based probes for serine proteases","volume":"20","author":"U Haedke","year":"2012","journal-title":"Bioorg Med Chem"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"3141","DOI":"10.1016\/S0968-0896(03)00235-9","article-title":"Synthesis of new 3-alkoxy-7-amino-4-chloro-isocoumarin derivatives as new beta-amyloid peptide production inhibitors and their activities on various classes of protease","volume":"11","author":"F Bihel","year":"2003","journal-title":"Bioorg Med Chem"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0190255","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,23]],"date-time":"2018-10-23T12:51:30Z","timestamp":1540299090000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0190255"}},"subtitle":[],"editor":[{"given":"Floyd","family":"Romesberg","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2018,1,24]]},"references-count":30,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2018,1,24]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0190255","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,1,24]]}}}