{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T08:35:00Z","timestamp":1768811700508,"version":"3.49.0"},"reference-count":211,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2010,5,5]],"date-time":"2010-05-05T00:00:00Z","timestamp":1273017600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,5,5]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Review critically examines the hypothesis that molecular chaperones from prokaryotic and eukaryotic sources can be secreted by cells and function as intercellular signaling molecules.<\/jats:p><jats:p>This review critically examines the hypothesis that molecular chaperones and protein-folding catalysts from prokaryotes and eukaryotes can be secreted by cells and function as intercellular signals, principally but not exclusively, for leukocytes. A growing number of molecular chaperones have been reported to function as ligands for selected receptors and\/or receptors for specific ligands. Molecular chaperones initially appeared to act primarily as stimulatory signals for leukocytes and thus, were seen as proinflammatory mediators. However, evidence is now emerging that molecular chaperones can have anti-inflammatory actions or, depending on the protein and concentration, anti- and proinflammatory functions. Recasting the original hypothesis, we propose that molecular chaperones and protein-folding catalysts are \u201cmoonlighting\u201d proteins that function as homeostatic immune regulators but may also under certain circumstances, contribute to tissue pathology. One of the key issues in the field of molecular chaperone biology relates to the role of microbial contaminants in their signaling activity; this too will be evaluated critically. The most fascinating aspect of molecular chaperones probably relates to evidence for their therapeutic potential in human disease, and ongoing studies are evaluating this potential in a range of clinical settings.<\/jats:p>","DOI":"10.1189\/jlb.1209779","type":"journal-article","created":{"date-parts":[[2010,5,6]],"date-time":"2010-05-06T02:44:27Z","timestamp":1273113867000},"page":"445-462","source":"Crossref","is-referenced-by-count":107,"title":["Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation"],"prefix":"10.1093","volume":"88","author":[{"given":"Brian","family":"Henderson","sequence":"first","affiliation":[{"name":"Department of Microbial Diseases, UCL-Eastman Dental Institute, University College London , London, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A Graham","family":"Pockley","sequence":"additional","affiliation":[{"name":"Department of Oncology, The Medical School, University of Sheffield , Sheffield, United Kingdom"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2010,5,5]]},"reference":[{"key":"2023032712270669500_jlb0445-cit-b1","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/S0140-6736(06)69210-6","article-title":"Therapeutic efficacy and safety of chaperonin 10 in patients with rheumatoid arthritis: a double-blind randomized trial","volume":"368","author":"Vanags","year":"2006","journal-title":"Lancet"},{"key":"2023032712270669500_jlb0445-cit-b2","first-page":"523","article-title":"XToll, a recombinant chaperonin 10 as an anti-inflammatory immunomodulator","volume":"9","author":"Van Eden","year":"2008","journal-title":"Curr. Opin. Investig. Drugs"},{"key":"2023032712270669500_jlb0445-cit-b3","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1002\/9780470754030.ch16","article-title":"BiP, an anti-inflammatory ER protein, is a potential new therapy for the treatment of rheumatoid arthritis","volume":"291","author":"Panayi","year":"2008","journal-title":"Novartis Found. Symp."},{"key":"2023032712270669500_jlb0445-cit-b4","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1001\/archderm.144.5.683","article-title":"Efficacy and safety of chaperonin 10 in patients with moderate to severe plaque psoriasis: evidence of utility beyond a single indication","volume":"144","author":"Williams","year":"2008","journal-title":"Arch. Dermatol."},{"key":"2023032712270669500_jlb0445-cit-b5","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1111\/j.1365-2249.2008.03656.x","article-title":"Immunological efficacy of heat shock protein 60 peptide DiaPep277 therapy in clinical type I diabetes","volume":"152","author":"Huurman","year":"2008","journal-title":"Clin. Exp. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b6","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1177\/1352458508099141","article-title":"Results of a phase IIa clinical trial of an anti-inflammatory molecule, chaperonin 10, in multiple sclerosis","volume":"15","author":"Broadley","year":"2009","journal-title":"Mult. Scler."},{"key":"2023032712270669500_jlb0445-cit-b7","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1002\/9780470754030.ch14","article-title":"Extracellular functions of thioredoxin","volume":"291","author":"Nakamura","year":"2008","journal-title":"Novartis Found. Symp."},{"key":"2023032712270669500_jlb0445-cit-b8","doi-asserted-by":"crossref","DOI":"10.1017\/CBO9780511546310","volume-title":"Molecular Chaperones and Cell Signaling","author":"Henderson","year":"2005"},{"key":"2023032712270669500_jlb0445-cit-b9","volume-title":"Novartis Foundation Symposium 291","author":"Chadwick","year":"2008"},{"key":"2023032712270669500_jlb0445-cit-b10","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1189\/jlb.0109005","article-title":"Heat shock proteins and immune system","volume":"85","author":"Tsan","year":"2009","journal-title":"J. Leukoc. Biol."},{"key":"2023032712270669500_jlb0445-cit-b11","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/s12192-009-0137-6","article-title":"Caught with their PAMPs down? The extracellular signaling actions of molecular chaperones are not due to microbial contaminants","volume":"15","author":"Henderson","year":"2010","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b12","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1007\/BF02172188","article-title":"A new puffing pattern induced by temperature shock and DNP in Drosophila","volume":"18","author":"Ritossa","year":"1962","journal-title":"Experientia"},{"key":"2023032712270669500_jlb0445-cit-b13","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/0022-2836(74)90447-1","article-title":"Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs","volume":"84","author":"Tissi\u00e8res","year":"1974","journal-title":"J. Mol. Biol."},{"key":"2023032712270669500_jlb0445-cit-b14","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1007\/BF00321231","article-title":"Patterns of puffing activity in the salivary gland chromosomes of Drosophila. V. Responses to environmental treatments","volume":"31","author":"Ashburner","year":"1970","journal-title":"Chromosoma"},{"key":"2023032712270669500_jlb0445-cit-b15","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1126\/science.3083508","article-title":"Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes","volume":"232","author":"Ananthan","year":"1986","journal-title":"Science"},{"key":"2023032712270669500_jlb0445-cit-b16","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":"2023032712270669500_jlb0445-cit-b17","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1017\/CBO9780511546310.002","volume-title":"Molecular Chaperones and Cell Signaling","author":"Ellis","year":"2005"},{"key":"2023032712270669500_jlb0445-cit-b18","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/s12192-008-0068-7","article-title":"Guidelines for the nomenclature of the human heat shock proteins","volume":"14","author":"Kampinga","year":"2009","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b19","doi-asserted-by":"crossref","DOI":"10.1093\/oso\/9780198599494.001.0001","volume-title":"Guidebook to Molecular Chaperones and Protein-Folding Catalysts","author":"Gething","year":"1997"},{"key":"2023032712270669500_jlb0445-cit-b20","doi-asserted-by":"crossref","first-page":"2741","DOI":"10.1089\/ars.2009.2683","article-title":"Redox regulation of cell survival by thioredoxin super-family: an implication of redox gene therapy in the heart","volume":"11","author":"Ahsan","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"2023032712270669500_jlb0445-cit-b21","doi-asserted-by":"crossref","first-page":"4666","DOI":"10.1021\/bi9003556","article-title":"Redox-regulated chaperones","volume":"48","author":"Kumsta","year":"2009","journal-title":"Biochemistry"},{"key":"2023032712270669500_jlb0445-cit-b22","doi-asserted-by":"crossref","first-page":"101659","DOI":"10.1155\/2009\/101659","article-title":"Metallothionein as an anti-inflammatory mediator","volume":"2009","author":"Inoue","year":"2009","journal-title":"Mediators Inflamm."},{"key":"2023032712270669500_jlb0445-cit-b23","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/S0140-6736(77)92605-8","article-title":"An early pregnancy factor detected in human serum by the rosette inhibition test","volume":"1","author":"Morton","year":"1977","journal-title":"Lancet"},{"key":"2023032712270669500_jlb0445-cit-b24","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1002\/j.1460-2075.1989.tb03436.x","article-title":"ATL-derived factor (ADF), an IL-2 receptor\/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction","volume":"8","author":"Tagaya","year":"1989","journal-title":"EMBO J."},{"key":"2023032712270669500_jlb0445-cit-b25","doi-asserted-by":"crossref","first-page":"2688","DOI":"10.1073\/pnas.041624998","article-title":"Chronic elevation of plasma thioredoxin: inhibition of chemotaxis and curtailment of life expectancy in AIDS","volume":"98","author":"Nakamura","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b26","doi-asserted-by":"crossref","first-page":"2170","DOI":"10.4049\/jimmunol.147.7.2170","article-title":"Human eosinophil cytotoxicity-enhancing factor. II. Multiple forms synthesized by U937 cells and their relationship to thioredoxin\/adult T cell leukemia-derived factor","volume":"147","author":"Balcewicz-Sablinska","year":"1991","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b27","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1089\/ars.2000.2.4-717","article-title":"Secretion of 10-kDa and 12-kDa thioredoxin species from blood monocytes and transformed leukocytes","volume":"2","author":"Sahaf","year":"2000","journal-title":"Antioxid. Redox Signal."},{"key":"2023032712270669500_jlb0445-cit-b28","doi-asserted-by":"crossref","first-page":"3184","DOI":"10.1182\/blood.V97.10.3184","article-title":"Truncated thioredoxin (Trx80) induces production of interleukin-12 and enhances CD14 expression in human monocytes","volume":"97","author":"Pekkari","year":"2001","journal-title":"Blood"},{"key":"2023032712270669500_jlb0445-cit-b29","doi-asserted-by":"crossref","first-page":"3511","DOI":"10.1073\/pnas.89.8.3511","article-title":"Identification of cyclophilin as a proinflammatory secretory product of lipopolysaccharide-activated macrophages","volume":"89","author":"Sherry","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b30","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1084\/jem.185.5.975","article-title":"Presence of cyclophilin A in synovial fluids of patients with rheumatoid arthritis","volume":"185","author":"Billich","year":"1997","journal-title":"J. Exp. Med."},{"key":"2023032712270669500_jlb0445-cit-b31","first-page":"791","article-title":"Serological detection of heat shock protein hsp27 in normal and breast cancer patients","volume":"7","author":"Fanelli","year":"1998","journal-title":"Cancer Epidemiol. Biomarkers Prev."},{"key":"2023032712270669500_jlb0445-cit-b32","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1379\/CSC-300.1","article-title":"Plasma heat shock protein 60 and cardiovascular disease risk: the role of psychosocial, genetic, and biological factors","volume":"12","author":"Shamaei-Tousi","year":"2007","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b33","doi-asserted-by":"crossref","first-page":"367","DOI":"10.3109\/08820139809022710","article-title":"Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals","volume":"27","author":"Pockley","year":"1998","journal-title":"Immunol. Invest."},{"key":"2023032712270669500_jlb0445-cit-b34","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1161\/01.HYP.36.2.303","article-title":"Circulating heat shock protein 60 is associated with early cardiovascular disease","volume":"36","author":"Pockley","year":"2000","journal-title":"Hypertension"},{"key":"2023032712270669500_jlb0445-cit-b35","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1097\/00004872-200209000-00027","article-title":"Circulating heat shock protein and heat shock protein antibody levels in established hypertension","volume":"20","author":"Pockley","year":"2002","journal-title":"J. Hypertens."},{"key":"2023032712270669500_jlb0445-cit-b36","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1161\/01.HYP.0000086522.13672.23","article-title":"Serum heat shock protein 70 levels predict the development of atherosclerosis in subjects with established hypertension","volume":"42","author":"Pockley","year":"2003","journal-title":"Hypertension"},{"key":"2023032712270669500_jlb0445-cit-b37","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/onc.2009.311","article-title":"Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells","volume":"29","author":"Nird\u00e9","year":"2010","journal-title":"Oncogene"},{"key":"2023032712270669500_jlb0445-cit-b38","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/ncb1131","article-title":"Functional proteomic screens reveal an essential extracellular role for hsp90 \u03b1 in cancer cell invasiveness","volume":"6","author":"Eustace","year":"2004","journal-title":"Nat. Cell Biol."},{"key":"2023032712270669500_jlb0445-cit-b39","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1038\/sj.emboj.7601579","article-title":"Extracellular heat shock protein-90\u03b1: linking hypoxia to skin cell motility and wound healing","volume":"26","author":"Li","year":"2007","journal-title":"EMBO J."},{"key":"2023032712270669500_jlb0445-cit-b40","doi-asserted-by":"crossref","first-page":"21288","DOI":"10.1073\/pnas.0908151106","article-title":"The regulatory mechanism of Hsp90\u03b1 secretion and its function in tumor malignancy","volume":"106","author":"Wang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b41","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1677\/joe.0.1470383","article-title":"Endocrine peptides \u201cmoonlighting\u201d as immune modulators: roles for somatostatin and GH-releasing factor","volume":"147","author":"Campbell","year":"1995","journal-title":"J. Endocrinol."},{"key":"2023032712270669500_jlb0445-cit-b42","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1039\/b900658n","article-title":"Moonlighting proteins\u2014an update","volume":"5","author":"Jeffery","year":"2009","journal-title":"Mol. Biosyst."},{"key":"2023032712270669500_jlb0445-cit-b43","first-page":"347","volume-title":"The Influence of Cooperative Bacteria on Animal Host Biology","author":"Henderson","year":"2005"},{"key":"2023032712270669500_jlb0445-cit-b44","doi-asserted-by":"crossref","first-page":"8561","DOI":"10.1073\/pnas.1531024100","article-title":"Glucose-6-phosphate isomerase is necessary for embryo implantation in the domestic ferret","volume":"100","author":"Schulz","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b45","doi-asserted-by":"crossref","first-page":"6034","DOI":"10.1021\/bi900569h","article-title":"A new function of GAPDH from Chlamydomonas reinhardtii: a thiol-disulfide exchange reaction with CP12","volume":"48","author":"Erales","year":"2009","journal-title":"Biochemistry"},{"key":"2023032712270669500_jlb0445-cit-b46","doi-asserted-by":"crossref","first-page":"6237","DOI":"10.1128\/IAI.73.10.6237-6248.2005","article-title":"Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties","volume":"73","author":"Bo\u00ebl","year":"2005","journal-title":"Infect. Immun."},{"key":"2023032712270669500_jlb0445-cit-b47","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1126\/science.1164551","article-title":"Function of mitochondrial Stat3 in cellular respiration","volume":"323","author":"Wegrzyn","year":"2009","journal-title":"Science"},{"key":"2023032712270669500_jlb0445-cit-b48","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1128\/MMBR.00036-07","article-title":"Moonlighting proteins in yeasts","volume":"72","author":"Gancedo","year":"2008","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"2023032712270669500_jlb0445-cit-b49","doi-asserted-by":"crossref","first-page":"3693","DOI":"10.1128\/IAI.01882-05","article-title":"Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection","volume":"74","author":"Henderson","year":"2006","journal-title":"Infect. Immun."},{"key":"2023032712270669500_jlb0445-cit-b50","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1111\/j.1365-2958.1992.tb00858.x","article-title":"Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis\/trans isomerase (PPlase) activity","volume":"6","author":"Fischer","year":"1992","journal-title":"Mol. Microbiol."},{"key":"2023032712270669500_jlb0445-cit-b51","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1038\/35075148","article-title":"Protein function. Chaperonin turned insect toxin","volume":"411","author":"Yoshida","year":"2001","journal-title":"Nature"},{"key":"2023032712270669500_jlb0445-cit-b52","doi-asserted-by":"crossref","first-page":"3645","DOI":"10.1242\/jcs.01214","article-title":"Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition","volume":"117","author":"Asquith","year":"2004","journal-title":"J. Cell Sci."},{"key":"2023032712270669500_jlb0445-cit-b53","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1093\/molehr\/gam043","article-title":"Analysis of chaperone proteins associated with human spermatozoa during capacitation","volume":"13","author":"Mitchell","year":"2007","journal-title":"Mol. Hum. Reprod."},{"issue":"Suppl. 1","key":"2023032712270669500_jlb0445-cit-b54","article-title":"Protein secretion systems in bacterial-host associations, and their description in the gene ontology","volume":"9","author":"Tseng","year":"2009","journal-title":"BMC Microbiol."},{"key":"2023032712270669500_jlb0445-cit-b55","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/nrm2617","article-title":"Mechanisms of regulated unconventional protein secretion","volume":"10","author":"Nickel","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2023032712270669500_jlb0445-cit-b56","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1002\/9780470754030.ch5","article-title":"Unusual cellular disposition of the mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10","volume":"291","author":"Gupta","year":"2008","journal-title":"Novartis Found. Symp."},{"key":"2023032712270669500_jlb0445-cit-b57","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1002\/9780470754030.ch7","article-title":"Cell stress proteins in extracellular fluids: friend or foe?","volume":"291","author":"Pockley","year":"2008","journal-title":"Novartis Found. Symp."},{"key":"2023032712270669500_jlb0445-cit-b58","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1111\/j.1365-2249.1996.tb08291.x","article-title":"A synthetic 10-kD heat shock protein (hsp10) from Mycobacterium tuberculosis modulates adjuvant arthritis","volume":"103","author":"Ragno","year":"1996","journal-title":"Clin. Exp. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b59","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1111\/j.1365-2222.2004.1931.x","article-title":"Effect of Mycobacterium tuberculosis chaperonins on bronchial eosinophilia and hyper-responsiveness in a murine model of allergic inflammation","volume":"34","author":"Riffo-Vasquez","year":"2004","journal-title":"Clin. Exp. Allergy"},{"key":"2023032712270669500_jlb0445-cit-b60","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1084\/jem.186.8.1241","article-title":"Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: a potential contributory factor in Pott's disease","volume":"186","author":"Meghji","year":"1997","journal-title":"J. Exp. Med."},{"key":"2023032712270669500_jlb0445-cit-b61","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1038\/278649a0","article-title":"Early pregnancy factor is immunosuppressive","volume":"278","author":"Noonan","year":"1979","journal-title":"Nature"},{"key":"2023032712270669500_jlb0445-cit-b62","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1111\/j.1432-1033.1994.tb18897.x","article-title":"The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10","volume":"222","author":"Cavanagh","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"2023032712270669500_jlb0445-cit-b63","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1046\/j.1440-1711.2000.00951.x","article-title":"Production of a recombinant form of early pregnancy factor that can prolong allogeneic skin graft survival time in rats","volume":"78","author":"Morton","year":"2000","journal-title":"Immunol. Cell Biol."},{"key":"2023032712270669500_jlb0445-cit-b64","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0022-510X(03)00170-9","article-title":"Early pregnancy factor suppresses the infiltration of lymphocytes and macrophages in the spinal cord of rats during experimental autoimmune encephalomyelitis but has no effect on apoptosis","volume":"214","author":"Athanasas-Platsis","year":"2003","journal-title":"J. Neurol. Sci."},{"key":"2023032712270669500_jlb0445-cit-b65","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0022-510X(03)00103-5","article-title":"Early pregnancy factor treatment suppresses the inflammatory response and adhesion molecule expression in the spinal cord of SJL\/J mice with experimental autoimmune encephalomyelitis and the delayed-type hypersensitivity reaction to trinitrochlorobenzene in normal BALB\/c mice","volume":"212","author":"Zhang","year":"2003","journal-title":"J. Neurol. Sci."},{"key":"2023032712270669500_jlb0445-cit-b66","doi-asserted-by":"crossref","first-page":"4037","DOI":"10.1074\/jbc.M411569200","article-title":"Heat shock protein 10 inhibits lipopolysaccharide-induced inflammatory mediator production","volume":"280","author":"Johnson","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b67","doi-asserted-by":"crossref","first-page":"e1198","DOI":"10.1371\/journal.pone.0001198","article-title":"Differential regulation of circulating levels of molecular chaperones in patients undergoing treatment for periodontal disease","volume":"2","author":"Shamaei-Tousi","year":"2007","journal-title":"PLoS One"},{"key":"2023032712270669500_jlb0445-cit-b68","doi-asserted-by":"crossref","first-page":"2217","DOI":"10.1110\/ps.062268106","article-title":"The origami of thioredoxin-like folds","volume":"15","author":"Pan","year":"2006","journal-title":"Protein Sci."},{"key":"2023032712270669500_jlb0445-cit-b69","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1128\/iai.64.1.50-54.1996","article-title":"Immunosuppressive factor from Actinobacillus actinomycetemcomitans down regulates cytokine production","volume":"64","author":"Kurita-Ochiai","year":"1996","journal-title":"Infect. Immun."},{"key":"2023032712270669500_jlb0445-cit-b70","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1128\/IAI.69.1.154-158.2001","article-title":"Cloning and expression of the Actinobacillus actinomycetemcomitans thioredoxin (trx) gene and assessment of cytokine inhibitory activity","volume":"69","author":"Henderson","year":"2001","journal-title":"Infect. Immun."},{"key":"2023032712270669500_jlb0445-cit-b71","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1006\/dbio.1996.0208","article-title":"Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene","volume":"178","author":"Matsui","year":"1996","journal-title":"Dev. Biol."},{"key":"2023032712270669500_jlb0445-cit-b72","doi-asserted-by":"crossref","first-page":"2596","DOI":"10.1093\/emboj\/17.9.2596","article-title":"Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1","volume":"17","author":"Saitoh","year":"1998","journal-title":"EMBO J."},{"key":"2023032712270669500_jlb0445-cit-b73","doi-asserted-by":"crossref","first-page":"442","DOI":"10.4049\/jimmunol.172.1.442","article-title":"Redox-sensing release of human thioredoxin from T lymphocytes with negative feedback loops","volume":"172","author":"Kondo","year":"2004","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b74","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1084\/jem.189.11.1783","article-title":"Thioredoxin, a redox enzyme released in infection and inflammation, is a unique chemoattractant for neutrophils, monocytes, and T cells","volume":"189","author":"Bertini","year":"1999","journal-title":"J. Exp. Med."},{"key":"2023032712270669500_jlb0445-cit-b75","doi-asserted-by":"crossref","first-page":"15143","DOI":"10.1073\/pnas.191498798","article-title":"Circulating thioredoxin suppresses lipopolysaccharide-induced neutrophil chemotaxis","volume":"98","author":"Nakamura","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b76","doi-asserted-by":"crossref","first-page":"1276","DOI":"10.1161\/01.CIR.0000141803.41217.B6","article-title":"Thioredoxin-1 ameliorates myosin-induced autoimmune myocarditis by suppressing chemokine expressions and leukocyte chemotaxis in mice","volume":"110","author":"Liu","year":"2004","journal-title":"Circulation"},{"key":"2023032712270669500_jlb0445-cit-b77","doi-asserted-by":"crossref","first-page":"G772","DOI":"10.1152\/ajpgi.00425.2005","article-title":"Protective roles of redox-active protein thioredoxin-1 for severe acute pancreatitis","volume":"290","author":"Ohashi","year":"2006","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"2023032712270669500_jlb0445-cit-b78","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1164\/rccm.200209-982OC","article-title":"Redox-active protein thioredoxin prevents proinflammatory cytokine- or bleomycin-induced lung injury","volume":"168","author":"Hoshino","year":"2003","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"2023032712270669500_jlb0445-cit-b79","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1016\/j.bbrc.2005.07.007","article-title":"Thioredoxin suppresses airway hyperresponsiveness and airway inflammation in asthma","volume":"334","author":"Ichiki","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2023032712270669500_jlb0445-cit-b80","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1016\/j.lfs.2006.03.026","article-title":"Recombinant human thioredoxin suppresses lipopolysaccharide-induced bronchoalveolar neutrophil infiltration in rat","volume":"79","author":"Ueda","year":"2006","journal-title":"Life Sci."},{"key":"2023032712270669500_jlb0445-cit-b81","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.bbrc.2007.06.019","article-title":"Effects of thioredoxin on established airway remodeling in a chronic antigen exposure asthma model","volume":"360","author":"Imaoka","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2023032712270669500_jlb0445-cit-b82","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1124\/jpet.107.134007","article-title":"Thioredoxin-1 ameliorates cigarette smoke-induced lung inflammation and emphysema in mice","volume":"325","author":"Sato","year":"2008","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"2023032712270669500_jlb0445-cit-b83","doi-asserted-by":"crossref","first-page":"403","DOI":"10.2332\/allergolint.09-OA-0086","article-title":"Endogenous and exogenous thioredoxin 1 prevents goblet cell hyperplasia in a chronic antigen exposure asthma model","volume":"58","author":"Imaoka","year":"2009","journal-title":"Allergol. Int."},{"key":"2023032712270669500_jlb0445-cit-b84","doi-asserted-by":"crossref","first-page":"4131","DOI":"10.1073\/pnas.96.7.4131","article-title":"Overexpression of thioredoxin in transgenic mice attenuates focal ischemic brain damage","volume":"96","author":"Takagi","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b85","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1038\/labinvest.3700305","article-title":"Helicobacter felis-induced gastritis was suppressed in mice overexpressing thioredoxin-1","volume":"85","author":"Kawasaki","year":"2005","journal-title":"Lab. Invest."},{"key":"2023032712270669500_jlb0445-cit-b86","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1053\/j.gastro.2006.08.023","article-title":"Human thioredoxin-1 ameliorates experimental murine colitis in association with suppressed macrophage inhibitory factor production","volume":"131","author":"Tamaki","year":"2006","journal-title":"Gastroenterology"},{"key":"2023032712270669500_jlb0445-cit-b87","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.addr.2009.01.003","article-title":"Thioredoxin 1 delivery as new therapeutics","volume":"61","author":"Nakamura","year":"2009","journal-title":"Adv. Drug Deliv. Rev."},{"key":"2023032712270669500_jlb0445-cit-b88","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1089\/ars.2008.2340","article-title":"Thioredoxin suppresses the contact hypersensitivity response by inhibiting leukocyte recruitment during the elicitation phase","volume":"11","author":"Fukunaga","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"2023032712270669500_jlb0445-cit-b89","doi-asserted-by":"crossref","first-page":"2595","DOI":"10.1089\/ars.2009.2522","article-title":"Direct association of thioredoxin-1 (TRX) with macrophage migration inhibitory factor (MIF); regulatory role of TRX on MIF internalization and signaling","volume":"11","author":"Son","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"2023032712270669500_jlb0445-cit-b90","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1089\/ars.2007.1661","article-title":"Cell-surface thioredoxin-1: possible involvement in thiol-mediated leukocyte-endothelial cell interaction through lipid rafts","volume":"9","author":"Hara","year":"2007","journal-title":"Antioxid. Redox Signal."},{"key":"2023032712270669500_jlb0445-cit-b91","doi-asserted-by":"crossref","first-page":"5118","DOI":"10.1167\/iovs.07-1659","article-title":"Suppression of choroidal neovascularization by thioredoxin-1 via interaction with complement factor H","volume":"49","author":"Inomata","year":"2008","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"2023032712270669500_jlb0445-cit-b92","doi-asserted-by":"crossref","first-page":"3086","DOI":"10.1038\/sj.emboj.7601746","article-title":"Selective redox regulation of cytokine receptor signaling by extracellular thioredoxin-1","volume":"26","author":"Schwertassek","year":"2007","journal-title":"EMBO J."},{"key":"2023032712270669500_jlb0445-cit-b93","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1111\/j.1365-2567.2006.02354.x","article-title":"Deciphering CD30 ligand biology and its role in humoral immunity","volume":"118","author":"Kennedy","year":"2006","journal-title":"Immunology"},{"key":"2023032712270669500_jlb0445-cit-b94","doi-asserted-by":"crossref","first-page":"37474","DOI":"10.1074\/jbc.M001012200","article-title":"Truncated thioredoxin is a mitogenic cytokine for resting human peripheral blood mononuclear cells and is present in human plasma","volume":"275","author":"Pekkari","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b95","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0014-5793(03)00214-X","article-title":"Truncated thioredoxin (Trx80) exerts unique mitogenic cytokine effects via a mechanism independent of thiol oxido-reductase activity","volume":"539","author":"Pekkari","year":"2003","journal-title":"FEBS Lett."},{"key":"2023032712270669500_jlb0445-cit-b96","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1089\/152308604771978345","article-title":"Truncated thioredoxin: physiological functions and mechanism","volume":"6","author":"Pekkari","year":"2004","journal-title":"Antioxid. Redox Signal."},{"key":"2023032712270669500_jlb0445-cit-b97","doi-asserted-by":"crossref","first-page":"1598","DOI":"10.1182\/blood-2004-04-1577","article-title":"Truncated thioredoxin (Trx80) induces differentiation of human CD14+ monocytes into a novel cell type (TAMs) via activation of the MAP kinases p38, ERK, and JNK","volume":"105","author":"Pekkari","year":"2005","journal-title":"Blood"},{"key":"2023032712270669500_jlb0445-cit-b98","doi-asserted-by":"crossref","first-page":"3289","DOI":"10.1007\/s00018-009-0086-3","article-title":"Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology","volume":"66","author":"Kostenko","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"2023032712270669500_jlb0445-cit-b99","doi-asserted-by":"crossref","first-page":"3951","DOI":"10.4049\/jimmunol.165.7.3951","article-title":"Exaggerated human monocyte IL-10 concomitant to minimal TNF-\u03b1 induction by heat-shock protein 27 (Hsp27) suggests Hsp27 is primarily an anti-inflammatory stimulus","volume":"165","author":"De","year":"2000","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b100","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1161\/CIRCRESAHA.108.172155","article-title":"Extracellular release of the atheroprotective heat shock protein 27 is mediated by estrogen and competitively inhibits acLDL binding to scavenger receptor-A","volume":"103","author":"Rayner","year":"2008","journal-title":"Circ. Res."},{"key":"2023032712270669500_jlb0445-cit-b101","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1161\/01.ATV.0000220108.97208.67","article-title":"Biological significance of decreased HSP27 in human atherosclerosis","volume":"26","author":"Martin-Ventura","year":"2006","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"2023032712270669500_jlb0445-cit-b102","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.2337\/db08-0009","article-title":"Serum heat shock protein 27 and diabetes complications in the EURODIAB prospective complications study: a novel circulating marker for diabetic neuropathy","volume":"57","author":"Gruden","year":"2008","journal-title":"Diabetes"},{"key":"2023032712270669500_jlb0445-cit-b103","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev.immunol.021908.132532","article-title":"Alternative activation of macrophages: an immunologic functional perspective","volume":"27","author":"Martinez","year":"2009","journal-title":"Annu. Rev. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b104","doi-asserted-by":"crossref","first-page":"2812","DOI":"10.1002\/eji.200636993","article-title":"Exogenous heat shock protein 27 uniquely blocks differentiation of monocytes to dendritic cells","volume":"37","author":"Laudanski","year":"2007","journal-title":"Eur. J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b105","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.1073\/pnas.95.4.1758","article-title":"Role of cyclophilin A in the uptake of HIV-1 by macrophages and T lymphocytes","volume":"95","author":"Sherry","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b106","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1006\/bbrc.2001.5847","article-title":"CD147 is a signaling receptor for cyclophilin B","volume":"288","author":"Yurchenko","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2023032712270669500_jlb0445-cit-b107","doi-asserted-by":"crossref","first-page":"2714","DOI":"10.1073\/pnas.052284899","article-title":"Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix","volume":"99","author":"Allain","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b108","doi-asserted-by":"crossref","first-page":"517","DOI":"10.4049\/jimmunol.175.1.517","article-title":"Extracellular cyclophilins contribute to the regulation of inflammatory responses","volume":"175","author":"Arora","year":"2005","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b109","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1111\/j.1365-2567.2008.02877.x","article-title":"Targeting the chemotactic function of CD147 reduces collagen-induced arthritis","volume":"126","author":"Damsker","year":"2009","journal-title":"Immunology"},{"key":"2023032712270669500_jlb0445-cit-b110","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1038\/nm.1958","article-title":"Cyclophilin A enhances vascular oxidative stress and the development of angiotensin II-induced aortic aneurysms","volume":"15","author":"Satoh","year":"2009","journal-title":"Nat. Med."},{"key":"2023032712270669500_jlb0445-cit-b111","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.1097\/01.CCM.0000281858.44387.A2","article-title":"Liver proteomics for therapeutic drug discovery: inhibition of the cyclophilin receptor CD147 attenuates sepsis-induced acute renal failure","volume":"35","author":"Dear","year":"2007","journal-title":"Crit. Care Med."},{"key":"2023032712270669500_jlb0445-cit-b112","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1111\/j.1365-2249.1993.tb03354.x","article-title":"Mycobacterial 65-kD heat shock protein induces release of pro-inflammatory cytokines from human monocytic cells","volume":"91","author":"Friedland","year":"1993","journal-title":"Clin. Exp. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b113","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1111\/j.1365-3083.1994.tb03421.x","article-title":"Mycobacterial heat shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes","volume":"39","author":"Peetermans","year":"1994","journal-title":"Scand. J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b114","doi-asserted-by":"crossref","first-page":"369","DOI":"10.4049\/jimmunol.157.1.369","article-title":"Heat shock protein 65 induces CD62e, CD106 and CD54 on cultured human endothelial cells and increases their adhesiveness for monocytes and granulocytes","volume":"157","author":"Verdegaal","year":"1996","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b115","doi-asserted-by":"crossref","first-page":"865","DOI":"10.4049\/jimmunol.145.3.865","article-title":"IL-4 regulates endothelial cell activation by IL-1, tumor necrosis factor, or IFN-\u03b3","volume":"145","author":"Thornhill","year":"1990","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b116","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1172\/JCI118150","article-title":"The potent bone-resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL","volume":"96","author":"Kirby","year":"1995","journal-title":"J. Clin. Invest."},{"key":"2023032712270669500_jlb0445-cit-b117","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.4049\/jimmunol.161.3.1414","article-title":"Homogeneous Escherichia coli chaperonin 60 induces IL-1 and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation","volume":"161","author":"Tabona","year":"1998","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b118","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1074\/jbc.M307858200","article-title":"Helicobacter pylori heat shock protein 60 mediates interleukin-6 production by macrophages via a Toll-like receptor (TLR)-2-, TLR-4-, and myeloid differentiation factor 88-independent mechanism","volume":"279","author":"Gobert","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b119","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1379\/1466-1268(2002)007<0130:RLCBNC>2.0.CO;2","article-title":"Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is dependent on interaction with cell surface CD14","volume":"7","author":"Lewthwaite","year":"2002","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b120","doi-asserted-by":"crossref","first-page":"7349","DOI":"10.1128\/IAI.69.12.7349-7355.2001","article-title":"Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (hsp 65) and contains a CD14-binding domain","volume":"69","author":"Lewthwaite","year":"2001","journal-title":"Infect. Immun."},{"key":"2023032712270669500_jlb0445-cit-b121","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1359\/jbmr.1998.13.8.1260","article-title":"The Escherichia coli chaperonin 60 (groEL) is a potent stimulator of osteoclast formation","volume":"13","author":"Reddi","year":"1998","journal-title":"J. Bone Miner. Res."},{"key":"2023032712270669500_jlb0445-cit-b122","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/S8756-3282(03)00117-0","article-title":"Human chaperonin 60 (Hsp60) stimulates bone resorption: structure\/function relationships","volume":"33","author":"Meghji","year":"2003","journal-title":"Bone"},{"key":"2023032712270669500_jlb0445-cit-b123","doi-asserted-by":"crossref","first-page":"2091","DOI":"10.1111\/j.1462-5822.2008.01193.x","article-title":"The two homologous chaperonin 60 proteins of Mycobacterium tuberculosis have distinct effects on monocyte differentiation into osteoclasts","volume":"10","author":"Winrow","year":"2008","journal-title":"Cell. Microbiol."},{"key":"2023032712270669500_jlb0445-cit-b124","doi-asserted-by":"crossref","first-page":"1711","DOI":"10.1111\/j.1462-5822.2008.01161.x","article-title":"Mycobacterium tuberculosis heat shock protein 60 modulates immune response to PPD by manipulating the surface expression of TLR2 on macrophages","volume":"10","author":"Khan","year":"2008","journal-title":"Cell. Microbiol."},{"key":"2023032712270669500_jlb0445-cit-b125","doi-asserted-by":"crossref","first-page":"5300","DOI":"10.4049\/jimmunol.169.9.5300","article-title":"Effect of microbial heat shock proteins on airway inflammation and hyperresponsiveness","volume":"169","author":"Rha","year":"2002","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b126","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":"2023032712270669500_jlb0445-cit-b127","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":"2023032712270669500_jlb0445-cit-b128","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":"2023032712270669500_jlb0445-cit-b129","doi-asserted-by":"crossref","first-page":"14272","DOI":"10.1074\/jbc.M414158200","article-title":"The intercellular signaling activity of the Mycobacterium tuberculosis chaperonin 60.1 protein resides in the equatorial domain","volume":"280","author":"Tormay","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b130","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":"2023032712270669500_jlb0445-cit-b131","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":"2023032712270669500_jlb0445-cit-b132","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1128\/IAI.00143-09","article-title":"Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages","volume":"77","author":"Hickey","year":"2009","journal-title":"Infect. Immun."},{"key":"2023032712270669500_jlb0445-cit-b133","doi-asserted-by":"crossref","first-page":"3716","DOI":"10.1016\/j.febslet.2007.04.082","article-title":"Cell stress induced HSP are targets of regulatory T cells: a role for HSP inducing compounds as anti-inflammatory immuno-modulators?","volume":"581","author":"Wieten","year":"2007","journal-title":"FEBS Lett."},{"key":"2023032712270669500_jlb0445-cit-b134","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1196\/annals.1391.020","article-title":"Stress, heat shock proteins, and autoimmunity: how immune responses to heat shock proteins are to be used for the control of chronic inflammatory diseases","volume":"1113","author":"Van Eden","year":"2007","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"2023032712270669500_jlb0445-cit-b135","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1002\/9780470754030.ch8","article-title":"HSP60 speaks to the immune system in many voices","volume":"291","author":"Quintana","year":"2008","journal-title":"Novartis Found. Symp."},{"key":"2023032712270669500_jlb0445-cit-b136","doi-asserted-by":"crossref","first-page":"e4026","DOI":"10.1371\/journal.pone.0004026","article-title":"HSP60 as a target of anti-ergotypic regulatory T cells","volume":"3","author":"Quintana","year":"2008","journal-title":"PLoS One"},{"key":"2023032712270669500_jlb0445-cit-b137","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.tibs.2007.10.005","article-title":"The dual immunoregulatory role of stress proteins","volume":"33","author":"Pockley","year":"2008","journal-title":"Trends Biochem. Sci."},{"key":"2023032712270669500_jlb0445-cit-b138","doi-asserted-by":"crossref","first-page":"13","DOI":"10.4049\/jimmunol.164.1.13","article-title":"Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells","volume":"164","author":"Kol","year":"2000","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b139","doi-asserted-by":"crossref","first-page":"3212","DOI":"10.4049\/jimmunol.162.6.3212","article-title":"Human 60-kDa heat-shock protein: a danger signal to the innate immune system","volume":"162","author":"Chen","year":"1999","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b140","doi-asserted-by":"crossref","first-page":"2340","DOI":"10.4049\/jimmunol.170.5.2340","article-title":"Human heat shock protein 60 induces maturation of dendritic cells versus a Th1-promoting phenotype","volume":"170","author":"Floh\u00e9","year":"2003","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b141","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/S1471-4906(01)02168-8","article-title":"Heat-shock proteins as activators of the innate immune system","volume":"23","author":"Wallin","year":"2002","journal-title":"Trends Immunol."},{"key":"2023032712270669500_jlb0445-cit-b142","first-page":"274","article-title":"Heat shock protein and innate immunity","volume":"1","author":"Tsan","year":"2004","journal-title":"Cell. Mol. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b143","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1038\/nri1593","article-title":"Heat shock proteins induce T-cell regulation of chronic inflammation","volume":"5","author":"van Eden","year":"2005","journal-title":"Nat. Rev. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b144","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1046\/j.1365-2249.1996.929628.x","article-title":"A 71-kD heat shock protein (hsp) from Mycobacterium tuberculosis has modulatory effects on experimental rat arthritis","volume":"103","author":"Kingston","year":"1996","journal-title":"Clin. Exp. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b145","doi-asserted-by":"crossref","first-page":"5560","DOI":"10.4049\/jimmunol.163.10.5560","article-title":"Activation of T cells recognizing an epitope of heat-shock protein 70 can protect against rat adjuvant arthritis","volume":"163","author":"Tanaka","year":"1999","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b146","doi-asserted-by":"crossref","first-page":"2711","DOI":"10.4049\/jimmunol.164.5.2711","article-title":"A conserved mycobacterial heat shock protein (hsp) 70 sequence prevents adjuvant arthritis upon nasal administration and induces IL-10-producing T cells that cross-react with the mammalian self-hsp70 homologue","volume":"164","author":"Wendling","year":"2000","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b147","doi-asserted-by":"crossref","first-page":"3712","DOI":"10.1002\/art.20635","article-title":"Inhibition of adjuvant-induced arthritis by DNA vaccination with the 70-kd or the 90-kd human heat-shock protein: immune cross-regulation with the 60-kd heat-shock protein","volume":"50","author":"Quintana","year":"2004","journal-title":"Arthritis Rheum."},{"key":"2023032712270669500_jlb0445-cit-b148","first-page":"A1312","article-title":"Reactivity of T cells from patients with rheumatoid arthritis towards human and mycobacterial hsp60","volume":"10","author":"Van Roon","year":"1996","journal-title":"FASEB J."},{"key":"2023032712270669500_jlb0445-cit-b149","doi-asserted-by":"crossref","first-page":"2001","DOI":"10.1002\/art.11174","article-title":"The spontaneous remission of juvenile idiopathic arthritis is characterized by CD30+ T cells directed to human heat-shock protein 60 capable of producing the regulatory cytokine interleukin-10","volume":"48","author":"De Kleer","year":"2003","journal-title":"Arthritis Rheum."},{"key":"2023032712270669500_jlb0445-cit-b150","doi-asserted-by":"crossref","first-page":"2022","DOI":"10.1172\/JCI28423","article-title":"Heat shock protein 60 enhances CD4+CD25+ regulatory T cell function via innate TLR2 signaling","volume":"116","author":"Zanin-Zhorov","year":"2006","journal-title":"J. Clin. Invest."},{"key":"2023032712270669500_jlb0445-cit-b151","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.1002\/art.24656","article-title":"Pan-DR-binding Hsp60 self epitopes induce an interleukin-10-mediated immune response in rheumatoid arthritis","volume":"60","author":"De Jong","year":"2009","journal-title":"Arthritis Rheum."},{"key":"2023032712270669500_jlb0445-cit-b152","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1186\/ar2674","article-title":"Heat shock protein 60 reactive T cells in juvenile idiopathic arthritis: what is new?","volume":"11","author":"Vercoulen","year":"2009","journal-title":"Arthritis Res. Ther."},{"key":"2023032712270669500_jlb0445-cit-b153","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/S0140-6736(05)66827-4","article-title":"Tolerogenic immune responses to novel T-cell epitopes from heat-shock protein 60 in juvenile idiopathic arthritis","volume":"366","author":"Kamphuis","year":"2005","journal-title":"Lancet"},{"key":"2023032712270669500_jlb0445-cit-b154","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1084\/jem.181.3.943","article-title":"Activation of T cells recognizing self 60-kD heat shock protein can protect against experimental arthritis","volume":"181","author":"Anderton","year":"1995","journal-title":"J. Exp. Med."},{"key":"2023032712270669500_jlb0445-cit-b155","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1007\/BF02678298","article-title":"Nasal administration of arthritis related T cell epitopes of hsp60 as a promising way for immunotherapy in chronic arthritis","volume":"10","author":"Prakken","year":"1998","journal-title":"Biotherapy"},{"key":"2023032712270669500_jlb0445-cit-b156","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1002\/dmrr.691","article-title":"Therapy with the hsp60 peptide DiaPep277 in C-peptide positive type 1 diabetes patients","volume":"23","author":"Huurman","year":"2007","journal-title":"Diabetes Metab. Res. Rev."},{"key":"2023032712270669500_jlb0445-cit-b157","doi-asserted-by":"crossref","first-page":"1968","DOI":"10.1161\/CIRCULATIONAHA.106.615609","article-title":"Induction of oral tolerance to oxidized low-density lipoprotein ameliorates atherosclerosis","volume":"114","author":"Van Puijvelde","year":"2006","journal-title":"Circulation"},{"key":"2023032712270669500_jlb0445-cit-b158","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1084\/jem.20021633","article-title":"Regulatory T cells selectively express Toll-like receptors and are activated by lipopolysaccharide","volume":"197","author":"Caramalho","year":"2003","journal-title":"J. Exp. Med."},{"key":"2023032712270669500_jlb0445-cit-b159","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1096\/fj.02-1139fje","article-title":"T cells respond to heat shock protein 60 via TLR2: activation of adhesion and inhibition of chemokine receptors","volume":"17","author":"Zanin-Zhorov","year":"2003","journal-title":"FASEB J."},{"key":"2023032712270669500_jlb0445-cit-b160","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1002\/1521-4141(200002)30:2<594::AID-IMMU594>3.0.CO;2-1","article-title":"Heat shock proteins generate \u03b2-chemokines which function as innate adjuvants enhancing adaptive immunity","volume":"30","author":"Lehner","year":"2000","journal-title":"Eur. J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b161","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/S1074-7613(01)00242-4","article-title":"CD40 is a cellular receptor mediating mycobacterial heat shock protein 70 stimulation of CC-chemokines","volume":"15","author":"Wang","year":"2001","journal-title":"Immunity"},{"key":"2023032712270669500_jlb0445-cit-b162","doi-asserted-by":"crossref","first-page":"2422","DOI":"10.4049\/jimmunol.169.5.2422","article-title":"Stimulation of Th1-polarizing cytokines, C-C chemokines, maturation of dendritic cells, and adjuvant function by the peptide binding fragment of heat shock protein 70","volume":"169","author":"Wang","year":"2002","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b163","doi-asserted-by":"crossref","first-page":"3306","DOI":"10.4049\/jimmunol.174.6.3306","article-title":"Identification of stimulating and inhibitory epitopes within the heat shock protein 70 molecule that modulate cytokine production and maturation of dendritic cells","volume":"174","author":"Wang","year":"2005","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b164","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/S1074-7613(03)00324-8","article-title":"CD40, but not CD40L, is required for the optimal priming of T cells and control of aerosol M. tuberculosis infection","volume":"19","author":"Lazarevic","year":"2003","journal-title":"Immunity"},{"key":"2023032712270669500_jlb0445-cit-b165","doi-asserted-by":"crossref","first-page":"2304","DOI":"10.1002\/eji.200635953","article-title":"Interaction between the CCR5 chemokine receptors and microbial HSP70","volume":"36","author":"Whittall","year":"2006","journal-title":"Eur. J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b166","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1126\/science.1133515","article-title":"Dendritic cell stimulation by mycobacterial Hsp70 is mediated through CCR5","volume":"314","author":"Floto","year":"2006","journal-title":"Science"},{"key":"2023032712270669500_jlb0445-cit-b167","doi-asserted-by":"crossref","first-page":"3354","DOI":"10.1128\/JVI.02320-06","article-title":"Inhibition of human immunodeficiency virus type 1 infection of human CD4+ T cells by microbial HSP70 and the peptide epitope 407\u2013426","volume":"81","author":"Babaahmady","year":"2007","journal-title":"J. Virol."},{"key":"2023032712270669500_jlb0445-cit-b168","doi-asserted-by":"crossref","first-page":"26477","DOI":"10.1074\/jbc.M803310200","article-title":"Calcium signaling in dendritic cells by human or mycobacterial Hsp70 is caused by contamination and is not required for Hsp70-mediated enhancement of cross-presentation","volume":"283","author":"Bendz","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b169","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1046\/j.1365-2567.2003.01725.x","article-title":"Facets of heat shock protein 70 show immunotherapeutic potential","volume":"110","author":"Todryk","year":"2003","journal-title":"Immunology"},{"key":"2023032712270669500_jlb0445-cit-b170","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12192-008-0060-2","article-title":"Computational analysis of the human HSPH\/HSPA\/DNAJ family and cloning of a human HSPH\/HSPA\/DNAJ expression library","volume":"14","author":"Hageman","year":"2009","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b171","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1111\/j.1399-0039.2004.00299.x","article-title":"The heat-shock protein receptors: some answers and more questions","volume":"64","author":"Binder","year":"2004","journal-title":"Tissue Antigens"},{"key":"2023032712270669500_jlb0445-cit-b172","doi-asserted-by":"crossref","first-page":"1951","DOI":"10.1016\/j.febslet.2005.02.046","article-title":"Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial\/epithelial cells","volume":"579","author":"Th\u00e9riault","year":"2005","journal-title":"FEBS Lett."},{"key":"2023032712270669500_jlb0445-cit-b173","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1038\/74697","article-title":"Hsp70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine","volume":"6","author":"Asea","year":"2000","journal-title":"Nat. Med."},{"key":"2023032712270669500_jlb0445-cit-b174","doi-asserted-by":"crossref","first-page":"15107","DOI":"10.1074\/jbc.M111204200","article-title":"HSP70 as endogenous stimulus of the Toll\/interleukin-1 receptor signal pathway","volume":"277","author":"Vabulas","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b175","doi-asserted-by":"crossref","first-page":"2997","DOI":"10.4049\/jimmunol.168.6.2997","article-title":"Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs","volume":"168","author":"Panjwani","year":"2002","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b176","doi-asserted-by":"crossref","first-page":"15028","DOI":"10.1074\/jbc.M200497200","article-title":"Novel signal transduction pathway utilized by extracellular HSP70. Role of Toll-like receptor (TLR) 2 and TLR4","volume":"277","author":"Asea","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b177","doi-asserted-by":"crossref","first-page":"3077","DOI":"10.1073\/pnas.91.8.3077","article-title":"Cellular requirements for tumor-specific immunity elicited by heat shock proteins: tumor rejection antigen gp96 primes CD8+ T cells in vivo","volume":"91","author":"Udono","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2023032712270669500_jlb0445-cit-b178","doi-asserted-by":"crossref","first-page":"5398","DOI":"10.4049\/jimmunol.152.11.5398","article-title":"Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90 and hsp70","volume":"152","author":"Udono","year":"1994","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b179","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1084\/jem.189.5.797","article-title":"Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity","volume":"189","author":"Basu","year":"1999","journal-title":"J. Exp. Med."},{"key":"2023032712270669500_jlb0445-cit-b180","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1126\/science.7545313","article-title":"A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides","volume":"269","author":"Suto","year":"1995","journal-title":"Science"},{"key":"2023032712270669500_jlb0445-cit-b181","doi-asserted-by":"crossref","first-page":"8142","DOI":"10.1158\/1078-0432.CCR-04-1194","article-title":"Heat shock proteins and their use as anticancer vaccines","volume":"10","author":"Parmiani","year":"2004","journal-title":"Clin. Cancer Res."},{"key":"2023032712270669500_jlb0445-cit-b182","doi-asserted-by":"crossref","first-page":"3533","DOI":"10.4049\/jimmunol.171.7.3533","article-title":"DNA fragments of the human 60-kDa heat shock protein (HSP60) vaccinate against adjuvant arthritis: identification of a regulatory HSP60 peptide","volume":"171","author":"Quintana","year":"2003","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b183","doi-asserted-by":"crossref","first-page":"1636","DOI":"10.1096\/fj.04-2088com","article-title":"Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability","volume":"18","author":"Arispe","year":"2004","journal-title":"FASEB J."},{"key":"2023032712270669500_jlb0445-cit-b184","doi-asserted-by":"crossref","first-page":"2467","DOI":"10.1096\/fj.08-125229","article-title":"Binding of heat shock protein 70 to extracellular phosphatidylserine promotes killing of normoxic and hypoxic tumor cells","volume":"23","author":"Schilling","year":"2009","journal-title":"FASEB J."},{"key":"2023032712270669500_jlb0445-cit-b185","doi-asserted-by":"crossref","first-page":"e1925","DOI":"10.1371\/journal.pone.0001925","article-title":"Tumor-specific Hsp70 plasma membrane localization is enabled by the glycophospholipid Gb3","volume":"3","author":"Gehrmann","year":"2008","journal-title":"PLoS One"},{"key":"2023032712270669500_jlb0445-cit-b186","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1007\/s12192-009-0113-1","article-title":"The atheroprotective properties of Hsp70: a role for Hsp70-endothelial interactions?","volume":"14","author":"Pockley","year":"2009","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b187","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/0021-9150(90)90080-3","article-title":"Effect of heat shock proteins on survival of isolated aortic cells from normal and atherosclerotic cynomolgus macaques","volume":"84","author":"Johnson","year":"1990","journal-title":"Atherosclerosis"},{"key":"2023032712270669500_jlb0445-cit-b188","article-title":"Exogenous Hsp70 becomes cell associated, but not internalized by stressed arterial smooth muscle cells","volume":"29A","author":"Johnson","year":"1993","journal-title":"In Vitro Cell. Dev. Biol. Anim."},{"key":"2023032712270669500_jlb0445-cit-b189","doi-asserted-by":"crossref","first-page":"1556","DOI":"10.1007\/s00018-009-8745-y","article-title":"Functions and pathologies of BiP and its interaction partners","volume":"66","author":"Dudek","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"2023032712270669500_jlb0445-cit-b190","doi-asserted-by":"crossref","first-page":"1492","DOI":"10.4049\/jimmunol.166.3.1492","article-title":"The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis","volume":"166","author":"Corrigall","year":"2001","journal-title":"J. Immunol."},{"key":"2023032712270669500_jlb0445-cit-b191","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1002\/art.20134","article-title":"Inhibition of antigen-presenting cell function and stimulation of human peripheral blood mononuclear cells to express an antiinflammatory cytokine profile by the stress protein BiP: relevance to the treatment of inflammatory arthritis","volume":"50","author":"Corrigall","year":"2004","journal-title":"Arthritis Rheum."},{"key":"2023032712270669500_jlb0445-cit-b192","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1002\/art.21654","article-title":"Treatment of murine collagen-induced arthritis by the stress protein BiP via interleukin-4-producing regulatory T cells: a novel function for an ancient protein","volume":"54","author":"Brownlie","year":"2006","journal-title":"Arthritis Rheum."},{"key":"2023032712270669500_jlb0445-cit-b193","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1111\/j.1365-2567.2009.03103.x","article-title":"Binding immunoglobulin protein-treated peripheral blood monocyte-derived dendritic cells are refractory to maturation and induce regulatory T-cell development","volume":"128","author":"Corrigall","year":"2009","journal-title":"Immunology"},{"key":"2023032712270669500_jlb0445-cit-b194","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.2174\/156802609789895656","article-title":"Strategies for stalling malignancy: targeting cancer's addiction to Hsp90","volume":"9","author":"Prodromou","year":"2009","journal-title":"Curr. Top. Med. Chem."},{"key":"2023032712270669500_jlb0445-cit-b195","doi-asserted-by":"crossref","first-page":"2031","DOI":"10.1074\/jbc.M701803200","article-title":"A critical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2","volume":"283","author":"Sidera","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b196","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.4161\/cc.3.9.1088","article-title":"Extracellular roles for the molecular chaperone, hsp90","volume":"3","author":"Eustace","year":"2004","journal-title":"Cell Cycle"},{"key":"2023032712270669500_jlb0445-cit-b197","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.4161\/cc.7.11.6054","article-title":"Extracellular HSP90: conquering the cell surface","volume":"7","author":"Sidera","year":"2008","journal-title":"Cell Cycle"},{"key":"2023032712270669500_jlb0445-cit-b198","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1074\/jbc.275.1.189","article-title":"Purification and identification of secreted oxidative stress-induced factors from vascular smooth muscle cells","volume":"275","author":"Liao","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b199","doi-asserted-by":"crossref","first-page":"3344","DOI":"10.1128\/MCB.01287-07","article-title":"Transforming growth factor \u03b1 (TGF\u03b1)-stimulated secretion of HSP90\u03b1: using the receptor LRP-1\/CD91 to promote human skin cell migration against a TGF\u03b2-rich environment during wound healing","volume":"28","author":"Cheng","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"2023032712270669500_jlb0445-cit-b200","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1111\/j.1743-6109.2006.00102.x","article-title":"In vivo delivery of heat shock protein 70 accelerates wound healing by upregulating macrophage-mediated phagocytosis","volume":"14","author":"Kovalchin","year":"2006","journal-title":"Wound Repair Regen."},{"key":"2023032712270669500_jlb0445-cit-b201","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1002\/ijc.2910610222","article-title":"A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells","volume":"61","author":"Multhoff","year":"1995","journal-title":"Int. J. Cancer"},{"key":"2023032712270669500_jlb0445-cit-b202","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1007\/s002620050326","article-title":"Heat-shock protein 72 cell-surface expression on human lung carcinoma cells in association with an increased sensitivity to lysis mediated by adherent natural killer cells","volume":"43","author":"Botzler","year":"1996","journal-title":"Cancer Immunol. Immunother."},{"key":"2023032712270669500_jlb0445-cit-b203","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1515\/BC.2002.192","article-title":"Effects of antineoplastic agents on cytoplasmic and membrane-bound heat shock protein 70 (Hsp70) levels","volume":"383","author":"Gehrmann","year":"2002","journal-title":"Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b204","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1379\/1466-1268(1998)003<0006:DOELEO>2.3.CO;2","article-title":"Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response","volume":"3","author":"Botzler","year":"1998","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b205","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1515\/BC.2003.030","article-title":"Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94","volume":"384","author":"Gross","year":"2003","journal-title":"Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b206","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1379\/1466-1268(2003)008<0348:HSPRIA>2.0.CO;2","article-title":"Heat shock protein 70-reactivity is associated with increased cell surface density of CD94\/CD56 on primary natural killer cells","volume":"8","author":"Gross","year":"2003","journal-title":"Cell Stress Chaperones"},{"key":"2023032712270669500_jlb0445-cit-b207","doi-asserted-by":"crossref","first-page":"41173","DOI":"10.1074\/jbc.M302644200","article-title":"Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B","volume":"278","author":"Gross","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2023032712270669500_jlb0445-cit-b208","first-page":"5","article-title":"The dynamics of LPS recognition: complex orchestration of multiple receptors","volume":"11","author":"Triantafilou","year":"2005","journal-title":"J. Endotoxin Res."},{"key":"2023032712270669500_jlb0445-cit-b209","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1111\/j.1574-6968.2006.00140.x","article-title":"Adhesion characteristics of Listeria adhesion protein (LAP)-expressing Escherichia coli to Caco-2 cells and of recombinant LAP to eukaryotic receptor Hsp60 as examined in a surface plasmon resonance sensor","volume":"256","author":"Kim","year":"2006","journal-title":"FEMS Microbiol. Lett."},{"key":"2023032712270669500_jlb0445-cit-b210","doi-asserted-by":"crossref","first-page":"12622","DOI":"10.1128\/JVI.01201-09","article-title":"Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface","volume":"83","author":"Honda","year":"2009","journal-title":"J. Virol."},{"key":"2023032712270669500_jlb0445-cit-b211","doi-asserted-by":"crossref","first-page":"3207","DOI":"10.1002\/art.24916","article-title":"Epitope-specific immunotherapy of rheumatoid arthritis: clinical responsiveness occurs with immune deviation and relies on the expression of a cluster of molecules associated with T cell tolerance in a double-blind, placebo-controlled, pilot phase II trial","volume":"60","author":"Koffeman","year":"2009","journal-title":"Arthritis Rheum."}],"container-title":["Journal of Leukocyte Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1189%2Fjlb.1209779","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/academic.oup.com\/jleukbio\/article-pdf\/88\/3\/445\/49586853\/jlb0445.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jleukbio\/article-pdf\/88\/3\/445\/49586853\/jlb0445.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,3,26]],"date-time":"2024-03-26T12:53:20Z","timestamp":1711457600000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jleukbio\/article\/88\/3\/445\/6959792"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,5,5]]},"references-count":211,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2010,5,5]]},"published-print":{"date-parts":[[2010,5,5]]}},"URL":"https:\/\/doi.org\/10.1189\/jlb.1209779","relation":{},"ISSN":["1938-3673","0741-5400"],"issn-type":[{"value":"1938-3673","type":"electronic"},{"value":"0741-5400","type":"print"}],"subject":[],"published-other":{"date-parts":[[2010,9]]},"published":{"date-parts":[[2010,5,5]]}}}