{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T21:26:51Z","timestamp":1786742811027,"version":"build-2736575974"},"reference-count":54,"publisher":"American Chemical Society (ACS)","issue":"16","license":[{"start":{"date-parts":[[2020,4,10]],"date-time":"2020-04-10T00:00:00Z","timestamp":1586476800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2020,4,10]],"date-time":"2020-04-10T00:00:00Z","timestamp":1586476800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2020,4,10]],"date-time":"2020-04-10T00:00:00Z","timestamp":1586476800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM126296"],"award-info":[{"award-number":["GM126296"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM132024"],"award-info":[{"award-number":["GM132024"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,4,28]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Chlamydia trachomatis is the cause of several diseases such as sexually transmitted urogenital disease and ocular trachoma. The pathogen contains a small genome yet, upon infection, expresses two enzymes with deubiquitinating activity, termed ChlaDUB1 and ChlaDUB2, presumed to have redundant deubiquitinase (DUB) function because of the similarity of the primary structure of their catalytic domain. Previous studies have led to structural characterization of the enzymatic properties of ChlaDUB1; however, ChlaDUB2 has yet to be investigated thoroughly. In this study, we investigated the deubiquitinase properties of ChlaDUB2 and compared them to those of ChlaDUB1. This revealed a distinct difference in hydrolytic activity with regard to di- and polyubiquitin chains while showing similar ability to cleave a monoubiquitin-based substrate, ubiquitin aminomethylcoumarin (Ub-AMC). ChlaDUB2 was unable to cleave a diubiquitin substrate efficiently, whereas ChlaDUB1 could rapidly hydrolyze this substrate like a prototypical prokaryotic DUB, SdeA. With polyubiquitinated green fluorescent protein substrate (GFP-Ubn), whereas ChlaDUB1 efficiently disassembled the polyubiquitin chains into the monoubiquitin product, the deubiquitination activity of ChlaDUB2, while showing depletion of the substrate, did not produce appreciable levels of the monoubiquitin product. We report the structures of a catalytic construct of ChlaDUB2 and its complex with ubiquitin propargyl amide. These structures revealed differences in residues involved in substrate recognition between the two Chlamydia DUBs. On the basis of the structures, we conclude that the distal ubiquitin binding is equivalent between the two DUBs, consistent with the Ub-AMC activity result. Therefore, the difference in activity with longer ubiquitinated substrates may be due to the differential recognition of these substrates involving additional ubiquitin binding sites.<\/jats:p>","DOI":"10.1021\/acs.biochem.9b01107","type":"journal-article","created":{"date-parts":[[2020,4,10]],"date-time":"2020-04-10T11:50:55Z","timestamp":1586519455000},"page":"1604-1617","source":"Crossref","is-referenced-by-count":19,"title":["The Two Deubiquitinating Enzymes from\n                    <i>Chlamydia\ntrachomatis<\/i>\n                    Have Distinct Ubiquitin Recognition Properties"],"prefix":"10.1021","volume":"59","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5600-0304","authenticated-orcid":true,"given":"John M.","family":"Hausman","sequence":"first","affiliation":[{"name":"Purdue University , , 560 Oval Drive , , ,","place":["West Lafayette, Indiana, United States, 47907"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sebastian","family":"Kenny","sequence":"additional","affiliation":[{"name":"Purdue University , , 560 Oval Drive , , ,","place":["West Lafayette, Indiana, United States, 47907"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shalini","family":"Iyer","sequence":"additional","affiliation":[{"name":"Purdue University , , 560 Oval Drive , , ,","place":["West Lafayette, Indiana, United States, 47907"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aditya","family":"Babar","sequence":"additional","affiliation":[{"name":"Purdue University , , 560 Oval Drive , , ,","place":["West Lafayette, Indiana, United States, 47907"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiazhang","family":"Qiu","sequence":"additional","affiliation":[{"name":"Jilin University , , Xi\u2019an Road 5333 , , ,","place":["Changchun, Jilin, China, 130062"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiaqi","family":"Fu","sequence":"additional","affiliation":[{"name":"Purdue University , , , ,","place":["West Lafayette, Indiana, United States, 47907"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhao-Qing","family":"Luo","sequence":"additional","affiliation":[{"name":"Purdue University , , , ,","place":["West Lafayette, Indiana, United States, 47907"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0567-7753","authenticated-orcid":true,"given":"Chittaranjan","family":"Das","sequence":"additional","affiliation":[{"name":"Purdue University , , 560 Oval Drive , , ,","place":["West Lafayette, Indiana, United States, 47907"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2020,4,10]]},"reference":[{"key":"2026081416075495700_cit1","doi-asserted-by":"publisher","first-page":"754","DOI":"10.1126\/science.282.5389.754","article-title":"Genome Sequence\nof an Obligate Intracellular Pathogen of Humans: Chlamydia trachomatis","volume":"282","author":"Stephens","year":"1998","journal-title":"Science"},{"key":"2026081416075495700_cit2","doi-asserted-by":"publisher","first-page":"a010256","DOI":"10.1101\/cshperspect.a010256","article-title":"Chlamydial\nIntracellular\nSurvival Strategies","volume":"3","author":"Bastidas","year":"2013","journal-title":"Cold Spring Harbor Perspect.\nMed."},{"key":"2026081416075495700_cit3","doi-asserted-by":"publisher","first-page":"385","DOI":"10.1038\/nrmicro.2016.30","article-title":"Chlamydia cell biology and pathogenesis","volume":"14","author":"Elwell","year":"2016","journal-title":"Nat.\nRev. Microbiol."},{"key":"2026081416075495700_cit4","doi-asserted-by":"publisher","first-page":"1636","DOI":"10.1111\/j.1365-2958.2005.04647.x","article-title":"A directed screen for chlamydial\nproteins secreted by a type III mechanism identifies a translocated\nprotein and numerous other new candidates","volume":"56","author":"Subtil","year":"2005","journal-title":"Mol.\nMicrobiol."},{"key":"2026081416075495700_cit5","doi-asserted-by":"publisher","first-page":"3925","DOI":"10.1128\/IAI.00106-07","article-title":"Mechanisms of Chlamydia trachomatis Entry into Nonphagocytic\nCells","volume":"75","author":"Hybiske","year":"2007","journal-title":"Infect. Immun."},{"key":"2026081416075495700_cit6","doi-asserted-by":"publisher","first-page":"3208","DOI":"10.1128\/IAI.58.10.3208-3216.1990","article-title":"Characterization\nof the cytochalasin D-resistant (pinocytic)\nmechanisms of endocytosis utilized by chlamydiae","volume":"58","author":"Reynolds","year":"1990","journal-title":"Infect. Immun."},{"key":"2026081416075495700_cit7","doi-asserted-by":"publisher","first-page":"598","DOI":"10.1128\/IAI.19.2.598-606.1978","article-title":"Parasite-specified\nphagocytosis of Chlamydia psittaci\nand Chlamydia trachomatis by L and HeLa cells","volume":"19","author":"Byrne","year":"1978","journal-title":"Infect. Immun."},{"key":"2026081416075495700_cit8","doi-asserted-by":"publisher","first-page":"1714","DOI":"10.1111\/j.1462-5822.2005.00627.x","article-title":"Recent insights\ninto the mechanisms\nof Chlamydia entry","volume":"7","author":"Dautry-Varsat","year":"2005","journal-title":"Cell. Microbiol."},{"key":"2026081416075495700_cit9","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1016\/S1286-4579(02)01546-0","article-title":"Proteins in the\nchlamydial inclusion membrane","volume":"4","author":"Rockey","year":"2002","journal-title":"Microbes Infect."},{"key":"2026081416075495700_cit10","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.01417-16","article-title":"Chlamydia trachomatis Is Resistant to Inclusion\nUbiquitination and Associated Host Defense in Gamma Interferon-Primed\nHuman Epithelial Cells","volume":"7","author":"Haldar","year":"2016","journal-title":"mBio"},{"key":"2026081416075495700_cit11","doi-asserted-by":"publisher","first-page":"3495","DOI":"10.1016\/j.jmb.2016.04.032","article-title":"Interferon-Inducible\nGTPases in Host Resistance, Inflammation and Disease","volume":"428","author":"Pilla-Moffett","year":"2016","journal-title":"J. Mol. Biol."},{"key":"2026081416075495700_cit12","doi-asserted-by":"publisher","first-page":"E5628","DOI":"10.1073\/pnas.1515966112","article-title":"Ubiquitin\nsystems mark pathogen-containing vacuoles as targets for host defense\nby guanylate binding proteins","volume":"112","author":"Haldar","year":"2015","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"key":"2026081416075495700_cit13","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0004588","article-title":"IFN-\u03b3-Inducible\nIrga6Mediates\nHost Resistance against Chlamydia trachomatis via Autophagy","volume":"4","author":"Al-Zeer","year":"2009","journal-title":"PLoS One"},{"key":"2026081416075495700_cit14","doi-asserted-by":"publisher","DOI":"10.1111\/cmi.13136","article-title":"The chlamydial\ndeubiquitinase Cdu1 supports recruitment of Golgi vesicles to the\ninclusion","author":"Auer","year":"2020","journal-title":"Cell. Microbiol."},{"key":"2026081416075495700_cit15","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0086684","article-title":"The E2-Like\nConjugation Enzyme Atg3 Promotes Binding of IRG and Gbp Proteins to\nChlamydia- and Toxoplasma-Containing Vacuoles and Host Resistance","volume":"9","author":"Haldar","year":"2014","journal-title":"PLoS One"},{"key":"2026081416075495700_cit16","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1016\/j.cell.2005.11.007","article-title":"A Genomic and Functional\nInventory of Deubiquitinating Enzymes","volume":"123","author":"Nijman","year":"2005","journal-title":"Cell"},{"key":"2026081416075495700_cit17","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1038\/nrm3099","article-title":"The spatial\nand temporal organization\nof ubiquitin networks","volume":"12","author":"Grabbe","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2026081416075495700_cit18","doi-asserted-by":"publisher","first-page":"114","DOI":"10.1016\/j.bbamcr.2013.06.027","article-title":"Regulation\nof proteolysis by human deubiquitinating\nenzymes","volume":"1843","author":"Eletr","year":"2014","journal-title":"Biochim. Biophys.\nActa, Mol. Cell Res."},{"key":"2026081416075495700_cit19","doi-asserted-by":"publisher","first-page":"425","DOI":"10.1080\/10409238.2017.1325829","article-title":"Ubiquitin enzymes in\nthe regulation\nof immune responses","volume":"52","author":"Ebner","year":"2017","journal-title":"Crit. Rev.\nBiochem. Mol. Biol."},{"key":"2026081416075495700_cit20","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1146\/annurev-biochem-060310-170328","article-title":"The Ubiquitin Code","volume":"81","author":"Komander","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"2026081416075495700_cit21","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1038\/nsmb.2808","article-title":"Ubiquitin in inflammation:\nthe right linkage makes all the difference","volume":"21","author":"Corn","year":"2014","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026081416075495700_cit22","doi-asserted-by":"publisher","first-page":"550","DOI":"10.1038\/nrm2731","article-title":"Breaking the chains: structure and\nfunction of the deubiquitinases","volume":"10","author":"Komander","year":"2009","journal-title":"Nat. Rev. Mol.\nCell Biol."},{"key":"2026081416075495700_cit23","doi-asserted-by":"publisher","first-page":"499","DOI":"10.1038\/cr.2016.30","article-title":"Bacteria-host relationship:\nubiquitin ligases as weapons of invasion","volume":"26","author":"Maculins","year":"2016","journal-title":"Cell\nRes."},{"key":"2026081416075495700_cit24","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1004255","article-title":"Hell\u2019s\nBELs:\nbacterial E3 ligases that exploit the eukaryotic\nubiquitin machinery","volume":"10","author":"Huibregtse","year":"2014","journal-title":"PLoS Pathog."},{"key":"2026081416075495700_cit25","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1016\/j.jmb.2004.10.022","article-title":"Structure of a Complex\nbetween Nedd8 and the Ulp\/Senp\nProtease Family Member Den1","volume":"345","author":"Reverter","year":"2005","journal-title":"J. Mol. Biol."},{"key":"2026081416075495700_cit26","doi-asserted-by":"publisher","first-page":"1341","DOI":"10.1038\/sj.emboj.7600628","article-title":"Structural\nbasis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme\nNEDP1","volume":"24","author":"Shen","year":"2005","journal-title":"EMBO J."},{"key":"2026081416075495700_cit27","doi-asserted-by":"publisher","first-page":"15090","DOI":"10.1073\/pnas.1514568112","article-title":"Structural\nbasis of substrate recognition by a bacterial deubiquitinase important\nfor dynamics of phagosome ubiquitination","volume":"112","author":"Sheedlo","year":"2015","journal-title":"Proc.\nNatl.\nAcad. Sci. U. S. A."},{"key":"2026081416075495700_cit28","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1038\/cr.2016.38","article-title":"Substrate specificity of the ubiquitin\nand Ubl proteases","volume":"26","author":"Ronau","year":"2016","journal-title":"Cell Res."},{"key":"2026081416075495700_cit29","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1016\/j.molcel.2016.06.015","article-title":"The Molecular\nBasis for Ubiquitin\nand Ubiquitin-like Specificities in Bacterial Effector Proteases","volume":"63","author":"Pruneda","year":"2016","journal-title":"Mol. Cell"},{"key":"2026081416075495700_cit30","doi-asserted-by":"publisher","first-page":"142","DOI":"10.1111\/j.1365-2958.2006.05199.x","article-title":"Chlamydia trachomatis-derived deubiquitinating\nenzymes\nin mammalian cells during infection","volume":"61","author":"Misaghi","year":"2006","journal-title":"Mol. Microbiol."},{"key":"2026081416075495700_cit31","doi-asserted-by":"publisher","first-page":"1879","DOI":"10.1111\/j.1462-5822.2008.01178.x","article-title":"ChlaDub1 of Chlamydia\ntrachomatis suppresses NF-\u03baB activation and inhibits I\u03baB\u03b1\nubiquitination and degradation","volume":"10","author":"Le\nNegrate","year":"2008","journal-title":"Cell. Microbiol."},{"key":"2026081416075495700_cit32","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.21465","article-title":"Chlamydia\ntrachomatis-containing\nvacuole serves as deubiquitination platform to stabilize Mcl-1 and\nto interfere with host defense","volume":"6","author":"Fischer","year":"2017","journal-title":"eLife"},{"key":"2026081416075495700_cit33","doi-asserted-by":"publisher","first-page":"1377","DOI":"10.1038\/s41564-018-0271-y","article-title":"A Chlamydia effector combining deubiquitination\nand acetylation activities\ninduces\nGolgi fragmentation","volume":"3","author":"Pruneda","year":"2018","journal-title":"Nature Microbiology"},{"key":"2026081416075495700_cit34","first-page":"343","article-title":"Chapter\nFifteen - Purification and functional characterization of the DUB\ndomain of SdeA","volume-title":"Methods in Enzymology","author":"Puvar","year":"2019"},{"key":"2026081416075495700_cit35","doi-asserted-by":"publisher","first-page":"5187","DOI":"10.1093\/emboj\/20.18.5187","article-title":"A novel active site-directed\nprobe\nspecific for deubiquitylating enzymes reveals proteasome association\nof USP14","volume":"20","author":"Borodovsky","year":"2001","journal-title":"EMBO J."},{"key":"2026081416075495700_cit36","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.1016\/j.str.2011.06.010","article-title":"Preparation\nof Distinct\nUbiquitin Chain Reagents of High Purity and Yield","volume":"19","author":"Dong","year":"2011","journal-title":"Structure"},{"key":"2026081416075495700_cit37","doi-asserted-by":"publisher","first-page":"3199","DOI":"10.1021\/bi5003162","article-title":"Insights into the Mechanism\nof Deubiquitination\nby JAMM Deubiquitinases from Cocrystal Structures of the Enzyme with\nthe Substrate and Product","volume":"53","author":"Shrestha","year":"2014","journal-title":"Biochemistry"},{"key":"2026081416075495700_cit38","doi-asserted-by":"publisher","first-page":"1164","DOI":"10.1038\/nsmb.2659","article-title":"Reconstitution of the\n26S proteasome reveals functional asymmetries in its AAA+ unfoldase","volume":"20","author":"Beckwith","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026081416075495700_cit39","doi-asserted-by":"publisher","first-page":"463","DOI":"10.2144\/000113418","article-title":"Overlap extension\nPCR cloning: a simple and reliable\nway to create recombinant plasmids","volume":"48","author":"Bryksin","year":"2010","journal-title":"BioTechniques"},{"key":"2026081416075495700_cit40","first-page":"307","article-title":"[20] Processing of X-ray diffraction\ndata collected\nin oscillation mode","volume-title":"Methods in Enzymology","author":"Otwinowski","year":"1997"},{"key":"2026081416075495700_cit41","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview\nof the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr.,\nSect. D: Biol. Crystallogr."},{"key":"2026081416075495700_cit42","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1107\/S0907444909042589","article-title":"Molecular replacement with MOLREP","volume":"66","author":"Vagin","year":"2010","journal-title":"Acta Crystallogr.,\nSect. D: Biol. Crystallogr."},{"key":"2026081416075495700_cit43","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of Macromolecular\nStructures\nby the Maximum-Likelihood Method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr.,\nSect. D: Biol. Crystallogr."},{"key":"2026081416075495700_cit44","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1107\/S090744499801405X","article-title":"Efficient\nanisotropic refinement of macromolecular structures using FFT","volume":"55","author":"Murshudov","year":"1999","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026081416075495700_cit45","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based\nsystem for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr.,\nSect. D: Biol. Crystallogr."},{"key":"2026081416075495700_cit46","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1016\/0022-2836(87)90679-6","article-title":"Structure of ubiquitin\nrefined at\n1.8\u00c5resolution","volume":"194","author":"Vijay-Kumar","year":"1987","journal-title":"J. Mol. Biol."},{"key":"2026081416075495700_cit47","doi-asserted-by":"publisher","first-page":"343","DOI":"10.1002\/cbic.201200701","article-title":"Catch-and-Release\nProbes Applied to Semi-Intact Cells\nReveal Ubiquitin-Specific Protease Expression in Chlamydia trachomatis\nInfection","volume":"14","author":"Claessen","year":"2013","journal-title":"ChemBioChem"},{"key":"2026081416075495700_cit48","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1046\/j.1462-5822.2000.00029.x","article-title":"A secondary structure motif predictive\nof protein localization to the chlamydial inclusion membrane","volume":"2","author":"Bannantine","year":"2000","journal-title":"Cell. Microbiol."},{"key":"2026081416075495700_cit49","doi-asserted-by":"publisher","first-page":"D624","DOI":"10.1093\/nar\/gkx1134","article-title":"The MEROPS database\nof proteolytic enzymes, their substrates\nand inhibitors in 2017 and a comparison with peptidases in the PANTHER\ndatabase","volume":"46","author":"Rawlings","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"2026081416075495700_cit50","doi-asserted-by":"publisher","first-page":"4675","DOI":"10.1073\/pnas.0510403103","article-title":"Structural basis for conformational\nplasticity of the\nParkinson&#039;s disease-associated ubiquitin hydrolase UCH-L1","volume":"103","author":"Das","year":"2006","journal-title":"Proc. Natl.\nAcad. Sci. U. S. A."},{"key":"2026081416075495700_cit51","doi-asserted-by":"publisher","first-page":"1106","DOI":"10.1111\/j.1742-4658.2012.08507.x","article-title":"Contribution of active\nsite glutamine to rate enhancement in ubiquitin C-terminal hydrolases","volume":"279","author":"Boudreaux","year":"2012","journal-title":"FEBS J."},{"key":"2026081416075495700_cit52","doi-asserted-by":"publisher","first-page":"2014","DOI":"10.1002\/cmdc.201800364","article-title":"Structural Basis of\nSubstrate Recognition and Covalent\nInhibition of Cdu1 from Chlamydia trachomatis","volume":"13","author":"Ramirez","year":"2018","journal-title":"ChemMedChem"},{"key":"2026081416075495700_cit53","doi-asserted-by":"publisher","first-page":"14717","DOI":"10.1021\/bi061406c","article-title":"Substrate Recognition and Catalysis\nby UCH-L1","volume":"45","author":"Luchansky","year":"2006","journal-title":"Biochemistry"},{"key":"2026081416075495700_cit54","doi-asserted-by":"publisher","first-page":"n\/a","DOI":"10.1093\/femspd\/fty011","article-title":"Direct visualization\nof the expression\nand localization of chlamydial effector proteins within infected host\ncells","volume":"76","author":"Wang","year":"2018","journal-title":"Pathog. Dis."}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.9b01107","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/59\/16\/1604\/5909564\/bi9b01107.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/59\/16\/1604\/5909564\/bi9b01107.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T20:28:01Z","timestamp":1786739281000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/59\/16\/1604\/590336\/The-Two-Deubiquitinating-Enzymes-from-Chlamydia"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,4,10]]},"references-count":54,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2020,4,10]]},"published-print":{"date-parts":[[2020,4,28]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.biochem.9b01107","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,4,10]]}}}