{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T22:25:07Z","timestamp":1790202307110,"version":"4.1.0"},"reference-count":30,"publisher":"Oxford University Press (OUP)","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEMS Microbiol Lett"],"published-print":{"date-parts":[[2014,1]]},"DOI":"10.1111\/1574-6968.12276","type":"journal-article","created":{"date-parts":[[2013,10,8]],"date-time":"2013-10-08T14:02:40Z","timestamp":1381240960000},"page":"20-24","source":"Crossref","is-referenced-by-count":15,"title":["Mycobacterial chaperonins: the tail wags the dog"],"prefix":"10.1093","volume":"350","author":[{"given":"Camilo A.","family":"Colaco","sequence":"first","affiliation":[{"name":"ImmunoBiology Limited; Babraham Research Campus Cambridge UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alistair","family":"MacDougall","sequence":"additional","affiliation":[{"name":"The European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI); Hinxton Cambridge UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2013,10,7]]},"reference":[{"key":"10.1111\/1574-6968.12276-BIB0001|fml12276-cit-0001","doi-asserted-by":"crossref","first-page":"4944","DOI":"10.1093\/nar\/gkp502","article-title":"A novel nucleoid-associated protein of Mycobacterium tuberculosis is a sequence homolog of GroEL","volume":"37","author":"Basu","year":"2009","journal-title":"Nucleic Acids Res"},{"key":"10.1111\/1574-6968.12276-BIB0002|fml12276-cit-0002","doi-asserted-by":"crossref","first-page":"e6306","DOI":"10.1371\/journal.pone.0006306","article-title":"Platensimycin activity against mycobacterial beta-ketoacyl-ACP synthases","volume":"4","author":"Brown","year":"2009","journal-title":"PLoS ONE"},{"key":"10.1111\/1574-6968.12276-BIB0003|fml12276-cit-0003","doi-asserted-by":"crossref","first-page":"2876","DOI":"10.1128\/JB.01569-08","article-title":"The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser\/Thr protein kinases","volume":"191","author":"Canova","year":"2009","journal-title":"J Bacteriol"},{"key":"10.1111\/1574-6968.12276-BIB0004|fml12276-cit-0004","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1111\/j.1365-2958.1993.tb01624.x","article-title":"Chaperonin nomenclature","volume":"8","author":"Coates","year":"1993","journal-title":"Mol Microbiol"},{"key":"10.1111\/1574-6968.12276-BIB0005|fml12276-cit-0005","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1111\/j.1365-2958.2012.08150.x","article-title":"The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function","volume":"85","author":"Fan","year":"2012","journal-title":"Mol Microbiol"},{"key":"10.1111\/1574-6968.12276-BIB0006|fml12276-cit-0006","unstructured":"First WHO Report on Neglected Tropical Diseases 2010 whqlibdoc.who.int\/publications\/2010\/9789241564090_eng.pdf"},{"key":"10.1111\/1574-6968.12276-BIB0007|fml12276-cit-0007","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1111\/j.1574-6968.2007.00989.x","article-title":"Mycobacterium smegmatis biofilm formation and sliding motility are affected by the serine\/threonine protein kinase PknF","volume":"278","author":"Gopalaswamy","year":"2008","journal-title":"FEMS Microbiol Lett"},{"key":"10.1111\/1574-6968.12276-BIB0008|fml12276-cit-0008","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1126\/science.1068408","article-title":"Molecular chaperones in the cytosol: from nascent chain to folded protein","volume":"295","author":"Hartl","year":"2002","journal-title":"Science"},{"key":"10.1111\/1574-6968.12276-BIB0009|fml12276-cit-0009","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1038\/333330a0","article-title":"Homologous plant and bacterial proteins chaperone oligomeric protein assembly","volume":"333","author":"Hemmingsen","year":"1988","journal-title":"Nature"},{"key":"10.1111\/1574-6968.12276-BIB0010|fml12276-cit-0010","doi-asserted-by":"crossref","first-page":"9957","DOI":"10.1016\/S0021-9258(18)82157-3","article-title":"The N-terminus of the molecular chaperonin GroEL is a crucial structural element for its assembly","volume":"268","author":"Horovitz","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1111\/1574-6968.12276-BIB0011|fml12276-cit-0011","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1128\/IAI.01078-07","article-title":"A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection","volume":"76","author":"Hu","year":"2008","journal-title":"Infect Immun"},{"key":"10.1111\/1574-6968.12276-BIB0012|fml12276-cit-0012","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1083\/jcb.200306132","article-title":"A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae","volume":"163","author":"Kaufman","year":"2003","journal-title":"J Cell Biol"},{"key":"10.1111\/1574-6968.12276-BIB0013|fml12276-cit-0013","doi-asserted-by":"crossref","first-page":"2608","DOI":"10.1073\/pnas.90.7.2608","article-title":"Mycobacterium tuberculosis expresses two chaperonin-60 homologs","volume":"90","author":"Kong","year":"1993","journal-title":"P Natl Acad Sci USA"},{"key":"10.1111\/1574-6968.12276-BIB0014|fml12276-cit-0014","doi-asserted-by":"crossref","first-page":"6525","DOI":"10.1128\/JB.00652-09","article-title":"Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization","volume":"191","author":"Kumar","year":"2009","journal-title":"J Bacteriol"},{"key":"10.1111\/1574-6968.12276-BIB0015|fml12276-cit-0015","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/S0065-2911(01)44012-4","article-title":"Microbial molecular chaperones","volume":"44","author":"Lund","year":"2001","journal-title":"Adv Microb Physiol"},{"key":"10.1111\/1574-6968.12276-BIB0016|fml12276-cit-0016","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1111\/j.1574-6976.2009.00178.x","article-title":"Multiple chaperonins in bacteria-why so many?","volume":"33","author":"Lund","year":"2009","journal-title":"FEMS Microbiol Rev"},{"key":"10.1111\/1574-6968.12276-BIB0017|fml12276-cit-0017","doi-asserted-by":"crossref","first-page":"6886","DOI":"10.1074\/jbc.M708002200","article-title":"Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity","volume":"283","author":"Machida","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1111\/1574-6968.12276-BIB0018|fml12276-cit-0018","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/j.cell.2005.09.012","article-title":"GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria","volume":"123","author":"Ojha","year":"2005","journal-title":"Cell"},{"key":"10.1111\/1574-6968.12276-BIB0019|fml12276-cit-0019","doi-asserted-by":"crossref","first-page":"8105","DOI":"10.1128\/JB.186.23.8105-8113.2004","article-title":"Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis","volume":"186","author":"Qamra","year":"2004","journal-title":"J Bacteriol"},{"key":"10.1111\/1574-6968.12276-BIB0020|fml12276-cit-0020","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/j.jmb.2004.07.066","article-title":"Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins","volume":"342","author":"Qamra","year":"2004","journal-title":"J Mol Biol"},{"key":"10.1111\/1574-6968.12276-BIB0021|fml12276-cit-0021","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1128\/IAI.56.2.446-451.1988","article-title":"The Mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to common antigen and to the Escherichia coli GroEL protein","volume":"56","author":"Shinnick","year":"1988","journal-title":"Infect Immun"},{"key":"10.1111\/1574-6968.12276-BIB0022|fml12276-cit-0022","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/j.jmb.2010.11.021","article-title":"Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 is a chaperonin","volume":"405","author":"Sielaff","year":"2011","journal-title":"J Mol Biol"},{"key":"10.1111\/1574-6968.12276-BIB0023|fml12276-cit-0023","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/S1286-4579(99)80046-X","article-title":"The potential use of heat-shock proteins to vaccinate against mycobacterial infections","volume":"1","author":"Silva","year":"1999","journal-title":"Microbes Infect"},{"key":"10.1111\/1574-6968.12276-BIB0024|fml12276-cit-0024","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1016\/j.cell.2006.04.027","article-title":"Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein","volume":"125","author":"Tang","year":"2006","journal-title":"Cell"},{"key":"10.1111\/1574-6968.12276-BIB0025|fml12276-cit-0025","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1099\/mic.0.045120-0","article-title":"Biochemical and immunological characterization of a cpn60.1 knockout mutant of Mycobacterium bovis BCG","volume":"157","author":"Wang","year":"2011","journal-title":"Microbiology"},{"key":"10.1111\/1574-6968.12276-BIB0026|fml12276-cit-0026","first-page":"337","article-title":"Global leprosy situation","volume":"85","author":"WHO","year":"2010","journal-title":"Wkly Epidemiol Rec"},{"key":"10.1111\/1574-6968.12276-BIB0027|fml12276-cit-0027","unstructured":"WHO 2012 Global tuberculosis report http:\/\/apps.who.int\/iris\/bitstream\/10665\/75938\/1\/9789241564502_eng.pdf"},{"key":"10.1111\/1574-6968.12276-BIB0028|fml12276-cit-0028","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1309\/AJCPQM5ZJGO7NLSZ","article-title":"Reducing the global burden of mycobacterial infections: one more piece of the puzzle","volume":"130","author":"Wilson","year":"2008","journal-title":"Am J Clin Pathol"},{"key":"10.1111\/1574-6968.12276-BIB0029|fml12276-cit-0029","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/0167-5699(87)90168-X","article-title":"The 65\u00a0kDa antigen of mycobacteria - a common bacterial protein?","volume":"8","author":"Young","year":"1987","journal-title":"Immunol Today"},{"key":"10.1111\/1574-6968.12276-BIB0030|fml12276-cit-0030","doi-asserted-by":"crossref","first-page":"4267","DOI":"10.1073\/pnas.85.12.4267","article-title":"Stress proteins are immune targets in leprosy and tuberculosis","volume":"85","author":"Young","year":"1988","journal-title":"P Natl Acad Sci USA"}],"container-title":["FEMS Microbiology Letters"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/femsle\/article-pdf\/350\/1\/20\/19128360\/350-1-20.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,8]],"date-time":"2022-03-08T10:16:58Z","timestamp":1646734618000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/femsle\/article-lookup\/doi\/10.1111\/1574-6968.12276"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,10,7]]},"references-count":30,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2014,1]]}},"URL":"https:\/\/doi.org\/10.1111\/1574-6968.12276","relation":{},"ISSN":["0378-1097"],"issn-type":[{"value":"0378-1097","type":"print"}],"subject":[],"published":{"date-parts":[[2013,10,7]]}}}