{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T06:13:09Z","timestamp":1792735989158,"version":"4.5.0"},"reference-count":29,"publisher":"Springer Science and Business Media LLC","issue":"7357","license":[{"start":{"date-parts":[[2011,7,1]],"date-time":"2011-07-01T00:00:00Z","timestamp":1309478400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2011,7]]},"DOI":"10.1038\/nature10307","type":"journal-article","created":{"date-parts":[[2011,7,5]],"date-time":"2011-07-05T09:54:59Z","timestamp":1309859699000},"page":"506-509","source":"Crossref","is-referenced-by-count":225,"title":["Legionella pneumophila SidD is a deAMPylase that modifies Rab1"],"prefix":"10.1038","volume":"475","author":[{"given":"Yunhao","family":"Tan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhao-Qing","family":"Luo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2011,7,6]]},"reference":[{"key":"BFnature10307_CR1","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.mib.2008.12.004","volume":"12","author":"AW Ensminger","year":"2009","unstructured":"Ensminger, A. W. & Isberg, R. R. Legionella pneumophila Dot\/Icm translocated substrates: a sum of parts. Curr. Opin. Microbiol. 12, 67\u201373 (2009)","journal-title":"Curr. Opin. Microbiol."},{"key":"BFnature10307_CR2","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1016\/j.devcel.2006.05.013","volume":"11","author":"MP Machner","year":"2006","unstructured":"Machner, M. P. & Isberg, R. R. Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila . Dev. Cell 11, 47\u201356 (2006)","journal-title":"Dev. Cell"},{"key":"BFnature10307_CR3","doi-asserted-by":"publisher","first-page":"971","DOI":"10.1038\/ncb1463","volume":"8","author":"T Murata","year":"2006","unstructured":"Murata, T. et al. The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nature Cell Biol. 8, 971\u2013977 (2006)","journal-title":"Nature Cell Biol."},{"key":"BFnature10307_CR4","doi-asserted-by":"publisher","first-page":"946","DOI":"10.1126\/science.1192276","volume":"329","author":"MP Muller","year":"2010","unstructured":"Muller, M. P. et al. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329, 946\u2013949 (2010)","journal-title":"Science"},{"key":"BFnature10307_CR5","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1038\/nrmicro1967","volume":"7","author":"RR Isberg","year":"2009","unstructured":"Isberg, R. R., O'Connor, T. J. & Heidtman, M. The Legionella pneumophila replication vacuole: making a cosy niche inside host cells. Nature Rev. Microbiol. 7, 13\u201324 (2009)","journal-title":"Nature Rev. Microbiol."},{"key":"BFnature10307_CR6","doi-asserted-by":"publisher","first-page":"e1001216","DOI":"10.1371\/journal.ppat.1001216","volume":"6","author":"T Kubori","year":"2010","unstructured":"Kubori, T., Shinzawa, N., Kanuka, H. & Nagai, H. Legionella metaeffector exploits host proteasome to temporally regulate cognate effector. PLoS Pathog. 6, e1001216 (2010)","journal-title":"PLoS Pathog."},{"key":"BFnature10307_CR7","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1038\/nature06336","volume":"450","author":"A Ingmundson","year":"2007","unstructured":"Ingmundson, A., Delprato, A., Lambright, D. G. & Roy, C. R. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450, 365\u2013369 (2007)","journal-title":"Nature"},{"key":"BFnature10307_CR8","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.molcel.2009.03.008","volume":"34","author":"CA Worby","year":"2009","unstructured":"Worby, C. A. et al. The fic domain: regulation of cell signaling by adenylylation. Mol. Cell 34, 93\u2013103 (2009)","journal-title":"Mol. Cell"},{"key":"BFnature10307_CR9","doi-asserted-by":"publisher","first-page":"e5818","DOI":"10.1371\/journal.pone.0005818","volume":"4","author":"LN Kinch","year":"2009","unstructured":"Kinch, L. N., Yarbrough, M. L., Orth, K. & Grishin, N. V. Fido, a novel AMPylation domain common to Fic, Doc, and AvrB. PLoS ONE 4, e5818 (2009)","journal-title":"PLoS ONE"},{"key":"BFnature10307_CR10","doi-asserted-by":"publisher","first-page":"1651","DOI":"10.1126\/science.1158160","volume":"320","author":"X Pan","year":"2008","unstructured":"Pan, X., Luhrmann, A., Satoh, A., Laskowski-Arce, M. A. & Roy, C. R. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science 320, 1651\u20131654 (2008)","journal-title":"Science"},{"key":"BFnature10307_CR11","doi-asserted-by":"publisher","first-page":"3026","DOI":"10.1128\/JB.01798-07","volume":"190","author":"Y Belyi","year":"2008","unstructured":"Belyi, Y., Tabakova, I., Stahl, M. & Aktories, K. Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila . J. Bacteriol. 190, 3026\u20133035 (2008)","journal-title":"J. Bacteriol."},{"key":"BFnature10307_CR12","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1111\/j.1462-5822.2009.01301.x","volume":"11","author":"X Shen","year":"2009","unstructured":"Shen, X. et al. Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response. Cell. Microbiol. 11, 911\u2013926 (2009)","journal-title":"Cell. Microbiol."},{"key":"BFnature10307_CR13","doi-asserted-by":"publisher","first-page":"841","DOI":"10.1073\/pnas.0304916101","volume":"101","author":"ZQ Luo","year":"2004","unstructured":"Luo, Z. Q. & Isberg, R. R. Multiple substrates of the Legionella pneumophila Dot\/Icm system identified by interbacterial protein transfer. Proc. Natl Acad. Sci. USA 101, 841\u2013846 (2004)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature10307_CR14","doi-asserted-by":"publisher","first-page":"1966","DOI":"10.1126\/science.1099776","volume":"305","author":"M Chien","year":"2004","unstructured":"Chien, M. et al. The genomic sequence of the accidental pathogen Legionella pneumophila . Science 305, 1966\u20131968 (2004)","journal-title":"Science"},{"key":"BFnature10307_CR15","doi-asserted-by":"publisher","first-page":"pe14","DOI":"10.1126\/scisignal.262pe14","volume":"2","author":"CR Roy","year":"2009","unstructured":"Roy, C. R. & Mukherjee, S. Bacterial FIC proteins AMP up infection. Sci. Signal. 2, pe14 (2009)","journal-title":"Sci. Signal."},{"key":"BFnature10307_CR16","doi-asserted-by":"publisher","first-page":"4846","DOI":"10.1074\/jbc.M807505200","volume":"284","author":"E Brombacher","year":"2009","unstructured":"Brombacher, E. et al. Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila . J. Biol. Chem. 284, 4846\u20134856 (2009)","journal-title":"J. Biol. Chem."},{"key":"BFnature10307_CR17","doi-asserted-by":"publisher","first-page":"951","DOI":"10.1093\/bioinformatics\/bti125","volume":"21","author":"J Soding","year":"2005","unstructured":"Soding, J. Protein homology detection by HMM\u2013HMM comparison. Bioinformatics 21, 951\u2013960 (2005)","journal-title":"Bioinformatics"},{"key":"BFnature10307_CR18","doi-asserted-by":"publisher","first-page":"3128","DOI":"10.1111\/j.1742-4658.2007.05845.x","volume":"274","author":"MK Rantanen","year":"2007","unstructured":"Rantanen, M. K., Lehtio, L., Rajagopal, L., Rubens, C. E. & Goldman, A. Structure of Streptococcus agalactiae serine\/threonine phosphatase. The subdomain conformation is coupled to the binding of a third metal ion. FEBS J. 274, 3128\u20133137 (2007)","journal-title":"FEBS J."},{"key":"BFnature10307_CR19","doi-asserted-by":"publisher","first-page":"570","DOI":"10.1016\/j.jmb.2007.11.097","volume":"376","author":"C Schlicker","year":"2008","unstructured":"Schlicker, C. et al. Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: a flexible flap subdomain controls access to the catalytic site. J. Mol. Biol. 376, 570\u2013581 (2008)","journal-title":"J. Mol. Biol."},{"key":"BFnature10307_CR20","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1016\/j.ceb.2004.06.014","volume":"16","author":"MC Seabra","year":"2004","unstructured":"Seabra, M. C. & Wasmeier, C. Controlling the location and activation of Rab GTPases. Curr. Opin. Cell Biol. 16, 451\u2013457 (2004)","journal-title":"Curr. Opin. Cell Biol."},{"key":"BFnature10307_CR21","doi-asserted-by":"publisher","first-page":"113","DOI":"10.3389\/fmicb.2010.00113","volume":"1","author":"AR Woolery","year":"2010","unstructured":"Woolery, A. R., Luong, P., Broberg, C. A. & Orth, K. AMPylation: something old is new again. Front. Microbiol 1, 113 (2010)","journal-title":"Front. Microbiol"},{"key":"BFnature10307_CR22","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1126\/science.1166382","volume":"323","author":"ML Yarbrough","year":"2009","unstructured":"Yarbrough, M. L. et al. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269\u2013272 (2009)","journal-title":"Science"},{"key":"BFnature10307_CR23","doi-asserted-by":"publisher","first-page":"e17638","DOI":"10.1371\/journal.pone.0017638","volume":"6","author":"W Zhu","year":"2011","unstructured":"Zhu, W. et al. Comprehensive identification of protein substrates of the Dot\/Icm type IV transporter of Legionella pneumophila . PLoS ONE 6, e17638 (2011)","journal-title":"PLoS ONE"},{"key":"BFnature10307_CR24","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1111\/j.1365-2958.1993.tb01092.x","volume":"7","author":"KH Berger","year":"1993","unstructured":"Berger, K. H. & Isberg, R. R. Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila . Mol. Microbiol. 7, 7\u201319 (1993)","journal-title":"Mol. Microbiol."},{"key":"BFnature10307_CR25","doi-asserted-by":"publisher","first-page":"305","DOI":"10.1046\/j.1365-2958.2003.03400.x","volume":"48","author":"GM Conover","year":"2003","unstructured":"Conover, G. M., Derre, I., Vogel, J. P. & Isberg, R. R. The Legionella pneumophila LidA protein: a translocated substrate of the Dot\/Icm system associated with maintenance of bacterial integrity. Mol. Microbiol. 48, 305\u2013321 (2003)","journal-title":"Mol. Microbiol."},{"key":"BFnature10307_CR26","doi-asserted-by":"publisher","first-page":"9385","DOI":"10.1073\/pnas.0801055105","volume":"105","author":"Y Liu","year":"2008","unstructured":"Liu, Y., Gao, P., Banga, S. & Luo, Z. Q. An in vivo gene deletion system for determining temporal requirement of bacterial virulence factors. Proc. Natl Acad. Sci. USA 105, 9385\u20139390 (2008)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature10307_CR27","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1093\/genetics\/142.3.749","volume":"142","author":"HY Fan","year":"1996","unstructured":"Fan, H. Y., Cheng, K. K. & Klein, H. L. Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1\u0394 of Saccharomyces cerevisiae . Genetics 142, 749\u2013759 (1996)","journal-title":"Genetics"},{"key":"BFnature10307_CR28","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1002\/yea.320110408","volume":"11","author":"RD Gietz","year":"1995","unstructured":"Gietz, R. D., Schiestl, R. H., Willems, A. R. & Woods, R. A. Studies on the transformation of intact yeast cells by the LiAc\/SS-DNA\/PEG procedure. Yeast 11, 355\u2013360 (1995)","journal-title":"Yeast"},{"key":"BFnature10307_CR29","doi-asserted-by":"publisher","first-page":"e1000822","DOI":"10.1371\/journal.ppat.1000822","volume":"6","author":"L Xu","year":"2010","unstructured":"Xu, L. et al. Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector. PLoS Pathog. 6, e1000822 (2010)","journal-title":"PLoS Pathog."}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nature10307.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature10307","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature10307.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T13:53:58Z","timestamp":1684418038000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature10307"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,7]]},"references-count":29,"journal-issue":{"issue":"7357","published-print":{"date-parts":[[2011,7]]}},"alternative-id":["BFnature10307"],"URL":"https:\/\/doi.org\/10.1038\/nature10307","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.12978956.14305054","asserted-by":"object"}]},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,7]]}}}