{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T02:49:03Z","timestamp":1787021343170,"version":"build-2736575974"},"reference-count":64,"publisher":"The Company of Biologists","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>The ubiquitously expressed glucocorticoid receptor (GR) is a major drug target for inflammatory disease, but issues of specificity, and target tissue sensitivity remain. We now identify high potency, non-steroidal GR ligands, GSK47867A and GSK47869A, which induce a novel conformation of the GR ligand binding domain (LBD) and augment the efficacy of cellular action. Despite their high potency GSK47867A and GSK47869A both induce surprisingly slow GR nuclear translocation, followed by prolonged nuclear GR retention, and transcriptional activity following washout. We reveal that GSK47867A and GSK47869A specifically alter the GR LBD structure at the HSP90 binding site. The alteration in HSP90 binding site was accompanied by resistance to HSP90 antagonism, with persisting transactivation seen after geldanamycin treatment. Taken together, our studies reveal a novel mechanism governing GR intracellular trafficking regulated by ligand binding, which relies on a specific surface charge patch within the LBD. This conformational change permits extended GR action, likely due to altered GR-HSP90 interaction. This chemical series may offer anti-inflammatory drugs with prolonged duration of action due to altered pharmacodynamics rather than altered pharmacokinetics.<\/jats:p>","DOI":"10.1242\/jcs.124784","type":"journal-article","created":{"date-parts":[[2013,5,18]],"date-time":"2013-05-18T01:32:11Z","timestamp":1368840731000},"source":"Crossref","is-referenced-by-count":11,"title":["A ligand-specific kinetic switch regulates glucocorticoid receptor trafficking and function"],"prefix":"10.1242","author":[{"given":"Peter J.","family":"Trebble","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James M.","family":"Woolven","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ken A.","family":"Saunders","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen D.","family":"Simpson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stuart N.","family":"Farrow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura C.","family":"Matthews","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David W.","family":"Ray","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2013,1,1]]},"reference":[{"key":"2021042613005797900_b1","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1111\/j.1476-5381.2010.01199.x","article-title":"Glucocorticosteroids: current and future directions.","volume":"163","author":"Barnes","year":"2011","journal-title":"Br. J. Pharmacol."},{"key":"2021042613005797900_b2","doi-asserted-by":"publisher","first-page":"D301","DOI":"10.1093\/nar\/gkl971","article-title":"The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data.","volume":"35 Database issue","author":"Berman","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"2021042613005797900_b3","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/S0092-8674(02)00817-6","article-title":"Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition.","volume":"110","author":"Bledsoe","year":"2002","journal-title":"Cell"},{"key":"2021042613005797900_b4","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/S0083-6729(04)68002-2","article-title":"Structure and function of the glucocorticoid receptor ligand binding domain.","volume":"68","author":"Bledsoe","year":"2004","journal-title":"Vitam. Horm."},{"key":"2021042613005797900_b5","doi-asserted-by":"publisher","first-page":"20473","DOI":"10.1074\/jbc.273.32.20473","article-title":"A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signaling.","volume":"273","author":"Caama\u00f1o","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b6","first-page":"1341","article-title":"Effects of glucocorticoids on the skeleton.","volume":"15","author":"Canalis","year":"2002","journal-title":"J. Pediatr. Endocrinol. Metab."},{"key":"2021042613005797900_b7","doi-asserted-by":"publisher","first-page":"54S","DOI":"10.1378\/chest.130.1_suppl.54S","article-title":"Developing the ideal inhaled corticosteroid.","volume":"130 Suppl","author":"Cerasoli","year":"2006","journal-title":"Chest"},{"key":"2021042613005797900_b8","doi-asserted-by":"publisher","first-page":"560","DOI":"10.1210\/me.2005-0318","article-title":"MED14 and MED1 differentially regulate target-specific gene activation by the glucocorticoid receptor.","volume":"20","author":"Chen","year":"2006","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b9","doi-asserted-by":"publisher","first-page":"1754","DOI":"10.1210\/me.2007-0219","article-title":"Glucocorticoid receptor phosphorylation differentially affects target gene expression.","volume":"22","author":"Chen","year":"2008","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b10","doi-asserted-by":"publisher","first-page":"944","DOI":"10.1210\/me.2010-0073","article-title":"The HSP90 molecular chaperone cycle regulates cyclical transcriptional dynamics of the glucocorticoid receptor and its coregulatory molecules CBP\/p300 during ultradian ligand treatment.","volume":"25","author":"Conway-Campbell","year":"2011","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b11","doi-asserted-by":"publisher","first-page":"1731","DOI":"10.1210\/me.8.12.1731","article-title":"The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor.","volume":"8","author":"Czar","year":"1994","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b12","doi-asserted-by":"publisher","first-page":"4597","DOI":"10.1074\/jbc.C100531200","article-title":"A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins.","volume":"277","author":"Davies","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b13","doi-asserted-by":"publisher","first-page":"1095","DOI":"10.3748\/wjg.v17.i9.1095","article-title":"Molecular mechanism of glucocorticoid resistance in inflammatory bowel disease.","volume":"17","author":"De Iudicibus","year":"2011","journal-title":"World J. Gastroenterol."},{"key":"2021042613005797900_b14","doi-asserted-by":"publisher","first-page":"1215","DOI":"10.1210\/mend-5-9-1215","article-title":"Protein phosphatase types 1 and\/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors.","volume":"5","author":"DeFranco","year":"1991","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b15","doi-asserted-by":"publisher","first-page":"4788","DOI":"10.1128\/MCB.00649-09","article-title":"Nuclear import of the glucocorticoid receptor-hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin beta.","volume":"29","author":"Echeverr\u00eda","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"2021042613005797900_b16","doi-asserted-by":"crossref","first-page":"7182","DOI":"10.1016\/S0021-9258(20)89627-6","article-title":"The genomic structure of the human glucocorticoid receptor.","volume":"266","author":"Enc\u00edo","year":"1991","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b17","doi-asserted-by":"publisher","first-page":"18487","DOI":"10.1073\/pnas.0609163103","article-title":"Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain.","volume":"103","author":"Fang","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042613005797900_b18","doi-asserted-by":"publisher","first-page":"1467","DOI":"10.1210\/me.11.10.1467","article-title":"Involvement of the transcription factor IID protein complex in gene activation by the N-terminal transactivation domain of the glucocorticoid receptor in vitro.","volume":"11","author":"Ford","year":"1997","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b19","doi-asserted-by":"publisher","first-page":"1903","DOI":"10.1210\/me.12.12.1903","article-title":"Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton.","volume":"12","author":"Galigniana","year":"1998","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b20","doi-asserted-by":"publisher","first-page":"13602","DOI":"10.1021\/bi020399z","article-title":"Binding of hsp90-associated immunophilins to cytoplasmic dynein: direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain.","volume":"41","author":"Galigniana","year":"2002","journal-title":"Biochemistry"},{"key":"2021042613005797900_b21","doi-asserted-by":"publisher","first-page":"7309","DOI":"10.1128\/MCB.00808-08","article-title":"Glycogen synthase kinase 3beta-mediated serine phosphorylation of the human glucocorticoid receptor redirects gene expression profiles.","volume":"28","author":"Galliher-Beckley","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"2021042613005797900_b22","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1016\/j.mce.2007.05.018","article-title":"The glucocorticoid responses are shaped by molecular chaperones.","volume":"275","author":"Grad","year":"2007","journal-title":"Mol. Cell. Endocrinol."},{"key":"2021042613005797900_b23","doi-asserted-by":"publisher","first-page":"54647","DOI":"10.1074\/jbc.M406863200","article-title":"Evidence for glucocorticoid receptor transport on microtubules by dynein.","volume":"279","author":"Harrell","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b24","doi-asserted-by":"publisher","first-page":"733","DOI":"10.1038\/42750","article-title":"A signature motif in transcriptional co-activators mediates binding to nuclear receptors.","volume":"387","author":"Heery","year":"1997","journal-title":"Nature"},{"key":"2021042613005797900_b25","doi-asserted-by":"publisher","first-page":"2358","DOI":"10.1016\/j.biocel.2007.08.010","article-title":"Protein phosphatase 5.","volume":"40","author":"Hinds","year":"2008","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"2021042613005797900_b26","doi-asserted-by":"publisher","first-page":"635","DOI":"10.1038\/318635a0","article-title":"Primary structure and expression of a functional human glucocorticoid receptor cDNA.","volume":"318","author":"Hollenberg","year":"1985","journal-title":"Nature"},{"key":"2021042613005797900_b27","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1196\/annals.1321.007","article-title":"Modulation of glucocorticoid receptor function via phosphorylation.","volume":"1024","author":"Ismaili","year":"2004","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"2021042613005797900_b28","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1084\/jem.20050466","article-title":"Histone deacetylase 2-mediated deacetylation of the glucocorticoid receptor enables NF-kappaB suppression.","volume":"203","author":"Ito","year":"2006","journal-title":"J. Exp. Med."},{"key":"2021042613005797900_b29","doi-asserted-by":"publisher","first-page":"16089","DOI":"10.1073\/pnas.2536313100","article-title":"Circadian gene expression in mammalian fibroblasts revealed by real-time luminescence reporting: temperature compensation and damping.","volume":"100","author":"Izumo","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042613005797900_b30","doi-asserted-by":"publisher","first-page":"3308","DOI":"10.1091\/mbc.E08-02-0123","article-title":"Chromatin remodeling complexes interact dynamically with a glucocorticoid receptor-regulated promoter.","volume":"19","author":"Johnson","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"2021042613005797900_b31","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1007\/978-3-642-55747-7_9","article-title":"N-CoR-HDAC corepressor complexes: roles in transcriptional regulation by nuclear hormone receptors.","volume":"274","author":"Jones","year":"2003","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"2021042613005797900_b32","doi-asserted-by":"publisher","first-page":"E718","DOI":"10.1208\/aapsj080481","article-title":"Geldanamycin, an inhibitor of Hsp90, blocks cytoplasmic retention of progesterone receptors and glucocorticoid receptors via their respective ligand binding domains.","volume":"8","author":"Kakar","year":"2006","journal-title":"AAPS J."},{"key":"2021042613005797900_b33","doi-asserted-by":"publisher","first-page":"1439","DOI":"10.1073\/pnas.96.4.1439","article-title":"The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.","volume":"96","author":"Kang","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042613005797900_b34","doi-asserted-by":"publisher","first-page":"22748","DOI":"10.1074\/jbc.M212711200","article-title":"The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism.","volume":"278","author":"Kauppi","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b35","doi-asserted-by":"publisher","first-page":"977","DOI":"10.1016\/j.amjmed.2009.02.013","article-title":"An umbrella review: corticosteroid therapy for adults with acute asthma.","volume":"122","author":"Krishnan","year":"2009","journal-title":"Am. J. Med."},{"key":"2021042613005797900_b36","doi-asserted-by":"publisher","first-page":"18146","DOI":"10.1074\/jbc.M100825200","article-title":"The conformation of the glucocorticoid receptor af1\/tau1 domain induced by osmolyte binds co-regulatory proteins.","volume":"276","author":"Kumar","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b37","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1124\/mol.62.2.297","article-title":"trans-Activation and repression properties of the novel nonsteroid glucocorticoid receptor ligand 2,5-dihydro-9-hydroxy-10-methoxy-2,2,4-trimethyl-5-(1-methylcyclohexen-3-y1)-1H-[1]benzopyrano[3,4-f]quinoline (A276575) and its four stereoisomers.","volume":"62","author":"Lin","year":"2002","journal-title":"Mol. Pharmacol."},{"key":"2021042613005797900_b38","doi-asserted-by":"publisher","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method.","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"2021042613005797900_b39","doi-asserted-by":"publisher","first-page":"6097","DOI":"10.1016\/j.bmcl.2008.10.021","article-title":"The first X-ray crystal structure of the glucocorticoid receptor bound to a non-steroidal agonist.","volume":"18","author":"Madauss","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"2021042613005797900_b40","doi-asserted-by":"publisher","first-page":"1320","DOI":"10.1210\/me.2007-0154","article-title":"Caveolin mediates rapid glucocorticoid effects and couples glucocorticoid action to the antiproliferative program.","volume":"22","author":"Matthews","year":"2008","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b41","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1210\/en.2008-0196","article-title":"Thiazolidinediones are partial agonists for the glucocorticoid receptor.","volume":"150","author":"Matthews","year":"2009","journal-title":"Endocrinology"},{"key":"2021042613005797900_b42","doi-asserted-by":"publisher","first-page":"e22289","DOI":"10.1371\/journal.pone.0022289","article-title":"Cell cycle phase regulates glucocorticoid receptor function.","volume":"6","author":"Matthews","year":"2011","journal-title":"PLoS ONE"},{"key":"2021042613005797900_b43","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1113\/expphysiol.2006.036194","article-title":"Modelling the glucocorticoid receptor and producing therapeutic agents with anti-inflammatory effects but reduced side-effects.","volume":"92","author":"McMaster","year":"2007","journal-title":"Exp. Physiol."},{"key":"2021042613005797900_b44","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1038\/ncpendmet0745","article-title":"Drug insight: selective agonists and antagonists of the glucocorticoid receptor.","volume":"4","author":"McMaster","year":"2008","journal-title":"Nat. Clin Pract. Endocrinol. Metab."},{"key":"2021042613005797900_b45","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1677\/JOE-07-0639","article-title":"Real-time analysis of gene regulation by glucocorticoid hormones.","volume":"197","author":"McMaster","year":"2008","journal-title":"J. Endocrinol."},{"key":"2021042613005797900_b46","doi-asserted-by":"publisher","first-page":"3629","DOI":"10.1242\/jcs.035048","article-title":"Ligand modulation of REV-ERBalpha function resets the peripheral circadian clock in a phasic manner.","volume":"121","author":"Meng","year":"2008","journal-title":"J. Cell Sci."},{"key":"2021042613005797900_b47","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1210\/me.2003-0388","article-title":"Urban renewal in the nucleus: is protein turnover by proteasomes absolutely required for nuclear receptor-regulated transcription?","volume":"18","author":"Nawaz","year":"2004","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b48","doi-asserted-by":"publisher","first-page":"1927","DOI":"10.1046\/j.1460-9568.1999.00616.x","article-title":"Real-time imaging of glucocorticoid receptor dynamics in living neurons and glial cells in comparison with non-neural cells.","volume":"11","author":"Nishi","year":"1999","journal-title":"Eur. J. Neurosci."},{"key":"2021042613005797900_b49","doi-asserted-by":"crossref","first-page":"3333","DOI":"10.1002\/j.1460-2075.1987.tb02654.x","article-title":"Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor.","volume":"6","author":"Picard","year":"1987","journal-title":"EMBO J."},{"key":"2021042613005797900_b50","volume-title":"National Institutes of Health, Bethesda, Maryland, USA. 1997. Ref Type","author":"Rasband","year":"1997"},{"key":"2021042613005797900_b51","doi-asserted-by":"publisher","first-page":"729","DOI":"10.1016\/j.jmb.2007.02.057","article-title":"A conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90.","volume":"368","author":"Ricketson","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2021042613005797900_b52","doi-asserted-by":"publisher","first-page":"2936","DOI":"10.1002\/art.23951","article-title":"How antirheumatic drugs protect joints from damage in rheumatoid arthritis.","volume":"58","author":"Schett","year":"2008","journal-title":"Arthritis Rheum."},{"key":"2021042613005797900_b53","article-title":"Glide version 5.5","author":"Schrodinger","year":"2009"},{"key":"2021042613005797900_b54","article-title":"Maestro version 9.3","author":"Schrodinger","year":"2012"},{"key":"2021042613005797900_b55","doi-asserted-by":"publisher","first-page":"18694","DOI":"10.1074\/jbc.272.30.18694","article-title":"The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin.","volume":"272","author":"Segnitz","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b56","doi-asserted-by":"publisher","first-page":"16224","DOI":"10.1074\/jbc.272.26.16224","article-title":"Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.","volume":"272","author":"Silverstein","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b57","doi-asserted-by":"publisher","first-page":"2682","DOI":"10.1128\/MCB.24.7.2682-2697.2004","article-title":"Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes.","volume":"24","author":"Stavreva","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"2021042613005797900_b58","doi-asserted-by":"publisher","first-page":"845","DOI":"10.1210\/me.2002-0320","article-title":"Dissociation of steroid receptor coactivator 1 and nuclear receptor corepressor recruitment to the human glucocorticoid receptor by modification of the ligand-receptor interface: the role of tyrosine 735.","volume":"17","author":"Stevens","year":"2003","journal-title":"Mol. Endocrinol."},{"key":"2021042613005797900_b59","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/j.mce.2003.10.057","article-title":"Regulation of nuclear retention of glucocorticoid receptor by nuclear Hsp90.","volume":"213","author":"Tago","year":"2004","journal-title":"Mol. Cell. Endocrinol."},{"key":"2021042613005797900_b60","doi-asserted-by":"publisher","first-page":"e48385","DOI":"10.1371\/journal.pone.0048385","article-title":"Org 214007-0: a novel non-steroidal selective glucocorticoid receptor modulator with full anti-inflammatory properties and improved therapeutic index.","volume":"7","author":"van Lierop","year":"2012","journal-title":"PLoS ONE"},{"key":"2021042613005797900_b61","doi-asserted-by":"publisher","first-page":"26573","DOI":"10.1074\/jbc.M110530200","article-title":"Deciphering the phosphorylation \u201ccode\u201d of the glucocorticoid receptor in vivo.","volume":"277","author":"Wang","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b62","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1101\/gad.1400506","article-title":"Novel arylpyrazole compounds selectively modulate glucocorticoid receptor regulatory activity.","volume":"20","author":"Wang","year":"2006","journal-title":"Genes Dev."},{"key":"2021042613005797900_b63","doi-asserted-by":"publisher","first-page":"15014","DOI":"10.1074\/jbc.M001007200","article-title":"Architectural principles for the structure and function of the glucocorticoid receptor tau 1 core activation domain.","volume":"275","author":"W\u00e4rnmark","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021042613005797900_b64","doi-asserted-by":"publisher","first-page":"288","DOI":"10.1016\/S0076-6879(05)93012-7","article-title":"Real-time luminescence reporting of circadian gene expression in mammals.","volume":"393","author":"Yamazaki","year":"2005","journal-title":"Methods Enzymol."}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/126\/14\/3159\/1931591\/jcs-126-14-3159.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.124784\/2044991\/jcs124784.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.124784\/2044991\/jcs124784.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,5,18]],"date-time":"2021-05-18T14:30:57Z","timestamp":1621348257000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/doi\/10.1242\/jcs.124784\/263544\/A-ligand-specific-kinetic-switch-regulates"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,1,1]]},"references-count":64,"URL":"https:\/\/doi.org\/10.1242\/jcs.124784","relation":{},"ISSN":["1477-9137","0021-9533"],"issn-type":[{"value":"1477-9137","type":"electronic"},{"value":"0021-9533","type":"print"}],"subject":[],"published":{"date-parts":[[2013,1,1]]},"article-number":"jcs.124784"}}