{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T02:45:43Z","timestamp":1793155543459,"version":"4.5.0"},"reference-count":51,"publisher":"Hindawi Limited","issue":"6","license":[{"start":{"date-parts":[[2015,9,1]],"date-time":"2015-09-01T00:00:00Z","timestamp":1441065600000},"content-version":"tdm","delay-in-days":1288,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2012,6]]},"DOI":"10.1111\/j.1462-5822.2012.01761.x","type":"journal-article","created":{"date-parts":[[2012,1,31]],"date-time":"2012-01-31T09:45:06Z","timestamp":1328003106000},"page":"852-868","source":"Crossref","is-referenced-by-count":80,"title":["Domain organization of Legionella effector SetA"],"prefix":"10.1155","volume":"14","author":[{"given":"Thomas","family":"Jank","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kira E.","family":"B\u00f6hmer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tina","family":"Tzivelekidis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carsten","family":"Schwan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yury","family":"Belyi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Aktories","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"98","published-online":{"date-parts":[[2012,2,21]]},"reference":[{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB1|cit1","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1038\/nrmicro1150","article-title":"Bacterial cytotoxins: targeting eukaryotic switches","volume":"3","author":"Aktories","year":"2005","journal-title":"Nat Rev Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB3|cit2","doi-asserted-by":"crossref","first-page":"16953","DOI":"10.1073\/pnas.0601562103","article-title":"Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A","volume":"103","author":"Belyi","year":"2006","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB4|cit3","doi-asserted-by":"crossref","first-page":"3026","DOI":"10.1128\/JB.01798-07","article-title":"Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila","volume":"190","author":"Belyi","year":"2008","journal-title":"J Bacteriol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB2|cit4","doi-asserted-by":"crossref","first-page":"76","DOI":"10.3389\/fmicb.2011.00076","article-title":"Effector glycosyltransferases in legionella","volume":"2","author":"Belyi","year":"2011","journal-title":"Front Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB5|cit5","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1016\/S1097-2765(01)00372-0","article-title":"The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate","volume":"8","author":"Bravo","year":"2001","journal-title":"Mol Cell"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB6|cit6","doi-asserted-by":"crossref","first-page":"4846","DOI":"10.1074\/jbc.M807505200","article-title":"Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila","volume":"284","author":"Brombacher","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB7|cit7","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1016\/j.febslet.2010.01.011","article-title":"Regulation of autophagy by phosphatidylinositol 3-phosphate","volume":"584","author":"Burman","year":"2010","journal-title":"FEBS Lett"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB8|cit8","doi-asserted-by":"crossref","first-page":"19566","DOI":"10.1074\/jbc.273.31.19566","article-title":"A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins","volume":"273","author":"Busch","year":"1998","journal-title":"J Biol Chem"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB9|cit9","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1146\/annurev.biophys.33.110502.133337","article-title":"Membrane-protein interactions in cell signaling and membrane trafficking","volume":"34","author":"Cho","year":"2005","journal-title":"Annu Rev Biophys Biomol Struct"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB10|cit10","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1172\/JCI0215420","article-title":"Rab proteins mediate Golgi transport of caveola-internalized glycosphingolipids and correct lipid trafficking in Niemann-Pick C cells","volume":"109","author":"Choudhury","year":"2002","journal-title":"J Clin Invest"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB11|cit11","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1042\/bss0720031","article-title":"Phosphoinositides and membrane traffic at the trans-Golgi network","volume":"72","author":"Choudhury","year":"2005","journal-title":"Biochem Soc Symp"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB12|cit12","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1126\/science.271.5255.1533","article-title":"Phosphoinositides as regulators in membrane traffic","volume":"271","author":"De Camilli","year":"1996","journal-title":"Science"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB14|cit13","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1038\/nature05185","article-title":"Phosphoinositides in cell regulation and membrane dynamics","volume":"443","author":"Di Paolo","year":"2006","journal-title":"Nature"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB15|cit14","doi-asserted-by":"crossref","first-page":"l6","DOI":"10.1126\/stke.2002.129.pl6","article-title":"Protein lipid overlay assay","volume":"2002","author":"Dowler","year":"2002","journal-title":"Sci STKE"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB16|cit15","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1002\/sita.200500073","article-title":"Polyethylenimine, a cost-effective transfection reagent","volume":"6","author":"Ehrhardt","year":"2006","journal-title":"Signal Transduct"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB17|cit16","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1016\/S0960-9822(01)00447-X","article-title":"Phosphatidylinositol 3-phosphate is generated in phagosomal membranes","volume":"11","author":"Ellson","year":"2001","journal-title":"Curr Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB18|cit17","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.mib.2008.12.004","article-title":"Legionella pneumophila Dot\/Icm translocated substrates: a sum of parts","volume":"12","author":"Ensminger","year":"2009","journal-title":"Curr Opin Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB13|cit18","doi-asserted-by":"crossref","first-page":"7716","DOI":"10.1128\/JB.187.22.7716-7726.2005","article-title":"Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer","volume":"187","author":"de Felipe","year":"2005","journal-title":"J Bacteriol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB19|cit19","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1007\/s00418-003-0591-7","article-title":"Phosphatidylinositol 3-phosphate is found in microdomains of early endosomes","volume":"120","author":"Gillooly","year":"2003","journal-title":"Histochem Cell Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB20|cit20","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1111\/j.1462-5822.2008.01249.x","article-title":"Large-scale identification of Legionella pneumophila Dot\/Icm substrates that modulate host cell vesicle trafficking pathways","volume":"11","author":"Heidtman","year":"2009","journal-title":"Cell Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB21|cit21","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev-cellbio-100109-104034","article-title":"Modulation of host cell function by Legionella pneumophila type IV effectors","volume":"26","author":"Hubber","year":"2010","journal-title":"Annu Rev Cell Dev Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB22|cit22","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1016\/j.bbalip.2006.02.020","article-title":"Membrane binding domains","volume":"1761","author":"Hurley","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB23|cit23","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/nature06336","article-title":"Legionella pneumophila proteins that regulate Rab1 membrane cycling","volume":"450","author":"Ingmundson","year":"2007","journal-title":"Nature"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB24|cit24","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/nrmicro1967","article-title":"The Legionella pneumophila replication vacuole: making a cosy niche inside host cells","volume":"7","author":"Isberg","year":"2009","journal-title":"Nat Rev Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB25|cit25","doi-asserted-by":"crossref","first-page":"35222","DOI":"10.1074\/jbc.M703138200","article-title":"Clostridium difficile glucosyltransferase toxin B - essential amino acids for substrate-binding","volume":"282","author":"Jank","year":"2007","journal-title":"J Biol Chem"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB26|cit26","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1038\/375500a0","article-title":"Glucosylation of Rho proteins by Clostridium difficile toxin B","volume":"375","author":"Just","year":"1995a","journal-title":"Nature"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB27|cit27","doi-asserted-by":"crossref","first-page":"13932","DOI":"10.1074\/jbc.270.23.13932","article-title":"The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins","volume":"270","author":"Just","year":"1995b","journal-title":"J Biol Chem"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB28|cit28","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1038\/35083070","article-title":"The PX domains of p47phox and p40phox bind to lipid products of PI(3)K","volume":"3","author":"Kanai","year":"2001","journal-title":"Nat Cell Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB29|cit29","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1038\/nrm2328","article-title":"Membrane recognition by phospholipid-binding domains","volume":"9","author":"Lemmon","year":"2008","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB30|cit30","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.devcel.2006.05.013","article-title":"Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila","volume":"11","author":"Machner","year":"2006","journal-title":"Dev Cell"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB31|cit31","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1126\/science.1149121","article-title":"A bifunctional bacterial protein links GDI displacement to Rab1 activation","volume":"318","author":"Machner","year":"2007","journal-title":"Science"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB32|cit32","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1016\/j.semcdb.2009.03.016","article-title":"Regulation of Golgi function via phosphoinositide lipids","volume":"20","author":"Mayinger","year":"2009","journal-title":"Semin Cell Dev Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB33|cit33","article-title":"The intracellular trafficking pathway of transferrin","author":"Mayle","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB34|cit34","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature10335","article-title":"Modulation of Rab GTPase function by a protein phosphocholine transferase","volume":"477","author":"Mukherjee","year":"2011","journal-title":"Nature"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB35|cit35","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1126\/science.1192276","article-title":"The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b","volume":"329","author":"Muller","year":"2010","journal-title":"Science"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB36|cit36","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/ncb1463","article-title":"The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor","volume":"8","author":"Murata","year":"2006","journal-title":"Nat Cell Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB37|cit37","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1126\/science.1067025","article-title":"A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes","volume":"295","author":"Nagai","year":"2002","journal-title":"Science"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB38|cit38","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1126\/science.1207193","article-title":"De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila","volume":"333","author":"Neunuebel","year":"2011","journal-title":"Science"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB39|cit39","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1016\/j.tim.2007.06.006","article-title":"Effector proteins translocated by Legionella pneumophila: strength in numbers","volume":"15","author":"Ninio","year":"2007","journal-title":"Trends Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB40|cit40","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1111\/j.1462-5822.2008.01219.x","article-title":"The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole","volume":"10","author":"Ragaz","year":"2008","journal-title":"Cell Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB41|cit41","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/j.jmb.2005.06.071","article-title":"Structural basis for the function of Clostridium difficile Toxin B","volume":"351","author":"Reinert","year":"2005","journal-title":"J Mol Biol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB42|cit42","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1152\/physrev.00033.2003","article-title":"Phosphoinositides in constitutive membrane traffic","volume":"84","author":"Roth","year":"2004","journal-title":"Physiol Rev"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB43|cit43","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1126\/science.1065763","article-title":"Location, location, location: membrane targeting directed by PX domains","volume":"294","author":"Sato","year":"2001","journal-title":"Science"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB44|cit44","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1038\/embor.2010.97","article-title":"High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA","volume":"11","author":"Schoebel","year":"2010","journal-title":"EMBO Rep"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB45|cit45","doi-asserted-by":"crossref","first-page":"17945","DOI":"10.1073\/pnas.1113133108","article-title":"Protein LidA from Legionella is a Rab GTPase supereffector","volume":"108","author":"Schoebel","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB46|cit46","doi-asserted-by":"crossref","first-page":"4866","DOI":"10.1073\/pnas.0501315102","article-title":"Pathogen effector protein screening in yeast identifies Legionella factors that interfere with membrane trafficking","volume":"102","author":"Shohdy","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB48|cit47","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1038\/nature10307","article-title":"Legionella pneumophila SidD is a deAMPylase that modifies Rab1","volume":"475","author":"Tan","year":"2011","journal-title":"Nature"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB47|cit48","doi-asserted-by":"crossref","first-page":"21212","DOI":"10.1073\/pnas.1114023109","article-title":"Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination","volume":"108","author":"Tan","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB51|cit49","doi-asserted-by":"crossref","first-page":"e46","DOI":"10.1371\/journal.ppat.0020046","article-title":"Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole","volume":"2","author":"Weber","year":"2006","journal-title":"PLoS Pathog"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB49|cit50","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1111\/j.1365-2958.2009.06608.x","article-title":"Pathogen trafficking pathways and host phosphoinositide metabolism","volume":"71","author":"Weber","year":"2009a","journal-title":"Mol Microbiol"},{"key":"10.1111\/j.1462-5822.2012.01761.x-BIB50|cit51","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1111\/j.1462-5822.2008.01266.x","article-title":"The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE","volume":"11","author":"Weber","year":"2009b","journal-title":"Cell Microbiol"}],"container-title":["Cellular Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1111%2Fj.1462-5822.2012.01761.x","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/onlinelibrary.wiley.com\/wol1\/doi\/10.1111\/j.1462-5822.2012.01761.x\/fullpdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,28]],"date-time":"2022-01-28T06:03:02Z","timestamp":1643349782000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1111\/j.1462-5822.2012.01761.x"}},"subtitle":["Legionella glucosyltransferase SetA binds PtdIns(3)P"],"short-title":[],"issued":{"date-parts":[[2012,2,21]]},"references-count":51,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2012,6]]}},"URL":"https:\/\/doi.org\/10.1111\/j.1462-5822.2012.01761.x","relation":{},"ISSN":["1462-5814"],"issn-type":[{"value":"1462-5814","type":"print"}],"subject":[],"published":{"date-parts":[[2012,2,21]]}}}