{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T23:38:00Z","timestamp":1791848280895,"version":"4.3.4"},"reference-count":156,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2018,10,16]],"date-time":"2018-10-16T00:00:00Z","timestamp":1539648000000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"DOI":"10.3389\/fimmu.2018.02382","type":"journal-article","created":{"date-parts":[[2018,10,16]],"date-time":"2018-10-16T01:57:03Z","timestamp":1539655023000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":71,"title":["The Pentraxins 1975\u20132018: Serendipity, Diagnostics and Drugs"],"prefix":"10.3389","volume":"9","author":[{"given":"Mark. B.","family":"Pepys","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2018,10,16]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1038\/newbio237157a0","article-title":"Role of complement in induction of the allergic response","volume":"237","author":"Pepys","year":"1972","journal-title":"Nature New Biol."},{"key":"B2","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1038\/249159a0","article-title":"Role of C3 in in vitro lymphocyte cooperation","volume":"249","author":"Feldmann","year":"1974","journal-title":"Nature"},{"key":"B3","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1084\/jem.140.1.126","article-title":"Role of complement in induction of antibody production in vivo","volume":"140","author":"Pepys","year":"1974","journal-title":"J Exp Med."},{"key":"B4","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1038\/249051a0","article-title":"Complement-mediated mixed aggregation of murine spleen cells","volume":"249","author":"Pepys","year":"1974","journal-title":"Nature"},{"key":"B5","first-page":"93","article-title":"Role of complement in the induction of immunological responses","volume":"32","author":"Pepys","year":"1976","journal-title":"Transplant Rev."},{"key":"B6","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1111\/j.1365-3083.1974.tb01244.x","article-title":"Enumeration of absolute numbers of T and B lymphocytes in human blood","volume":"3","author":"Brown","year":"1974","journal-title":"Scand J Immunol."},{"key":"B7","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1084\/jem.141.4.821","article-title":"Effects of C-reactive protein on the lymphoid system","volume":"141","author":"Mortensen","year":"1975","journal-title":"J Exp Med."},{"key":"B8","doi-asserted-by":"publisher","first-page":"21","DOI":"10.3109\/00365517209102748","article-title":"Electroimmunoassay","volume":"29","author":"Laurell","year":"1972","journal-title":"Scand J Clin Lab Invest."},{"key":"B9","first-page":"32","article-title":"Isolation of C-reactive protein by affinity chromatography","volume":"30","author":"Pepys","year":"1977","journal-title":"Clin Exp Immunol."},{"key":"B10","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1056\/NEJM196507152730306","article-title":"Immunologic studies on a protein extracted from human secondary amyloid","volume":"273","author":"Cathcart","year":"1965","journal-title":"N Engl J Med."},{"key":"B11","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1016\/S0022-5320(66)80075-8","article-title":"The ultrastructure of human amyloid as revealed by the negative staining technique","volume":"14","author":"Bladen","year":"1966","journal-title":"J Ultrastruct Res."},{"key":"B12","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1016\/0005-2795(67)90420-5","article-title":"Isolation and identification of a plasma component of amyloid","volume":"147","author":"Cathcart","year":"1967","journal-title":"Biochim Biophys Acta"},{"key":"B13","doi-asserted-by":"crossref","first-page":"376","DOI":"10.4049\/jimmunol.99.2.376","article-title":"Plasma protein constituents of amyloid fibrils","volume":"99","author":"Cathcart","year":"1967","journal-title":"J Immunol."},{"key":"B14","doi-asserted-by":"publisher","first-page":"1090","DOI":"10.1038\/2281090b0","article-title":"Antigenic determinants in amyloid deposits","volume":"228","author":"Cathcart","year":"1970","journal-title":"Nature"},{"key":"B15","doi-asserted-by":"publisher","first-page":"482","DOI":"10.1007\/BF03401789","article-title":"Human serum amyloid P component is a single uncomplexed pentamer in whole serum","volume":"6","author":"Hutchinson","year":"2000","journal-title":"Mol Med."},{"key":"B16","doi-asserted-by":"crossref","first-page":"225","DOI":"10.4049\/jimmunol.113.1.225","article-title":"A simple method for the isolation of the subcomponents of the first component of complement by affinity chromatography","volume":"113","author":"Assimeh","year":"1974","journal-title":"J Immunol."},{"key":"B17","doi-asserted-by":"crossref","first-page":"482","DOI":"10.4049\/jimmunol.115.2.482","article-title":"The identification of a previously unrecognized subcomponent of the first component of complement","volume":"115","author":"Assimeh","year":"1975","journal-title":"J Immunol."},{"key":"B18","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.4049\/jimmunol.116.6.1745.c","article-title":"Ultrastructure and chemistry of Clt subcomponent of Cl: similarities to amyloid P component","volume":"116","author":"Painter","year":"1976","journal-title":"J Immunol."},{"key":"B19","doi-asserted-by":"publisher","first-page":"739","DOI":"10.1073\/pnas.74.2.739","article-title":"Characterisation of C-reactive protein and the complement subcomponent Clt as homologous proteins displaying cyclic pentameric symmetry (pentraxins)","volume":"74","author":"Osmand","year":"1977","journal-title":"Proc Natl Acad Sci USA."},{"key":"B20","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1016\/S0065-2776(08)60379-X","article-title":"Acute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein","volume":"34","author":"Pepys","year":"1983","journal-title":"Adv Immunol."},{"key":"B21","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1016\/S0140-6736(77)91260-0","article-title":"Isolation of amyloid P component (protein AP) from normal serum as a calcium-dependent binding protein","volume":"1","author":"Pepys","year":"1977","journal-title":"Lancet"},{"key":"B22","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.4049\/jimmunol.112.6.2135","article-title":"Interaction of C-reactive protein complexes with the complement system","volume":"112","author":"Kaplan","year":"1974","journal-title":"J Immunol."},{"key":"B23","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1084\/jem.140.3.631","article-title":"Interactions of C-reactive protein with the complement system","volume":"140","author":"Siegel","year":"1974","journal-title":"J Exp Med."},{"key":"B24","doi-asserted-by":"publisher","first-page":"1733","DOI":"10.1084\/jem.190.12.1733","article-title":"C-reactive protein and complement are important mediators of tissue damage in acute myocardial infarction","volume":"190","author":"Griselli","year":"1999","journal-title":"J Exp Med."},{"key":"B25","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1432-1033.1993.tb17900.x","article-title":"Molecular characterization of Limulus polyphemus C-reactive protein","volume":"214","author":"Tennent","year":"1993","journal-title":"Eur J Biochem."},{"key":"B26","first-page":"55","article-title":"Isolation and characterisation of C-reactive protein and serum amyloid P component in the rat","volume":"45","author":"de Beer","year":"1982","journal-title":"Immunology"},{"key":"B27","doi-asserted-by":"publisher","first-page":"623","DOI":"10.1152\/physrev.00016.2017","article-title":"PTX3, a humoral pattern recognition molecule, in innate immunity, tissue repair, and cancer","volume":"98","author":"Garlanda","year":"2018","journal-title":"Physiol Rev."},{"key":"B28","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1038\/367338a0","article-title":"Structure of pentameric human serum amyloid P component","volume":"367","author":"Emsley","year":"1994","journal-title":"Nature"},{"key":"B29","doi-asserted-by":"publisher","first-page":"408","DOI":"10.1006\/jmbi.1997.1271","article-title":"Pentameric and decameric structures in solution of serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses","volume":"272","author":"Ashton","year":"1997","journal-title":"J Mol Biol."},{"key":"B30","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1038\/nsb0496-346","article-title":"Three-dimensional structure of human C-reactive protein","volume":"3","author":"Shrive","year":"1996","journal-title":"Nat Struct Biol."},{"key":"B31","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1016\/S0969-2126(99)80023-9","article-title":"The physiological structure of human C-reactive protein and its complex with phosphocholine","volume":"7","author":"Thompson","year":"1999","journal-title":"Structure"},{"key":"B32","doi-asserted-by":"publisher","first-page":"1217","DOI":"10.1038\/nature04672","article-title":"Targeting C-reactive protein for the treatment of cardiovascular disease","volume":"440","author":"Pepys","year":"2006","journal-title":"Nature"},{"key":"B33","doi-asserted-by":"publisher","first-page":"9840","DOI":"10.1021\/bi00451a044","article-title":"Elucidation of a protease-sensitive site involved in the binding of calcium to C-reactive protein","volume":"28","author":"Kinoshita","year":"1989","journal-title":"Biochemistry"},{"key":"B34","doi-asserted-by":"publisher","first-page":"700","DOI":"10.1002\/pro.5560010602","article-title":"A protease-sensitive site in the proposed Ca2+-binding region of human serum amyloid P component and other pentraxins","volume":"1","author":"Kinoshita","year":"1992","journal-title":"Protein Sc"},{"key":"B35","doi-asserted-by":"publisher","first-page":"1091","DOI":"10.1161\/01.ATV.0000169644.88847.28","article-title":"CRP or not CRP? That is the question","volume":"25","author":"Pepys","year":"2005","journal-title":"Arterioscler Thromb Vasc Biol."},{"key":"B36","doi-asserted-by":"publisher","first-page":"e97","DOI":"10.1161\/01.RES.0000193595.03608.08","article-title":"Proinflammatory effects of bacterial recombinant human C-reactive protein are caused by contamination with bacterial products, not by C-reactive protein itself","volume":"97","author":"Pepys","year":"2005","journal-title":"Circ Res."},{"key":"B37","first-page":"64","article-title":"The crystal structure of the calcium-free serum amyloid P component decamer","volume-title":"From Misfolded Proteins to Well-Designed Treatment XIIth International Symposiumon Amyloidosis","author":"Coker","year":"2012"},{"key":"B38","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1016\/0167-4838(82)90118-2","article-title":"Calcium-dependent aggregation of human serum amyloid P component","volume":"701","author":"Baltz","year":"1982","journal-title":"Biochim Biophys Acta"},{"key":"B39","doi-asserted-by":"publisher","first-page":"1134","DOI":"10.1084\/jem.154.4.1134","article-title":"Fibronectin and C4-binding protein are selectively bound by aggregated amyloid P component","volume":"154","author":"de Beer","year":"1981","journal-title":"J Exp Med."},{"key":"B40","first-page":"23","article-title":"Analysis of autoaggregation and ligand binding sites of serum amyloid P component by in vitro mutagenesis","volume-title":"Amyloid and Amyloidosis 1998","author":"Booth","year":"1999"},{"key":"B41","doi-asserted-by":"publisher","first-page":"168","DOI":"10.1038\/273168a0","article-title":"Analogues in other mammals and in fish of human plasma proteins C-reactive protein and amyloid P component","volume":"273","author":"Pepys","year":"1978","journal-title":"Nature"},{"key":"B42","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1038\/278259a0","article-title":"Serum amyloid P-component is an acute-phase reactant in the mouse","volume":"278","author":"Pepys","year":"1979","journal-title":"Nature"},{"key":"B43","first-page":"325","article-title":"The effect of inflammatory agents on C-reactive protein and serum amyloid P component levels in plaice (Pleuronectes platessa L.) serum","author":"White","year":"1981","journal-title":"Comp Biochem Physiol."},{"key":"B44","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1111\/j.1749-6632.1982.tb22125.x","article-title":"Phylogenetic aspects of C-reactive protein and related proteins","volume":"389","author":"Baltz","year":"1982","journal-title":"Ann NY Acad Sci."},{"key":"B45","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0167-4838(82)90139-X","article-title":"C-reactive protein and serum amyloid P component in the plaice (Pleuronectes platessa L.), a marine teleost, are homologous with their human counterparts","volume":"704","author":"Pepys","year":"1982","journal-title":"Biochim Biophys Acta"},{"key":"B46","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1111\/j.1749-6632.1982.tb22177.x","article-title":"Studies of the primary structure of mouse serum amyloid P component (SAP)","volume":"389","author":"Taylor","year":"1982","journal-title":"Ann NY Acad Sci."},{"key":"B47","first-page":"307","article-title":"Isolation and characterisation of C-reactive protein from the dog","volume":"53","author":"Caspi","year":"1984","journal-title":"Immunology"},{"key":"B48","doi-asserted-by":"publisher","first-page":"903","DOI":"10.1042\/bj2210903","article-title":"Amino acid sequence homology between rat and human C-reactive protein","volume":"221","author":"Taylor","year":"1984","journal-title":"Biochem J."},{"key":"B49","first-page":"317","article-title":"Isolation and characterization of guinea-pig serum amyloid P component","volume":"59","author":"Maudsley","year":"1986","journal-title":"Immunology"},{"key":"B50","doi-asserted-by":"crossref","first-page":"919","DOI":"10.2460\/ajvr.1987.48.06.919","article-title":"C-reactive protein in dogs","volume":"48","author":"Caspi","year":"1987","journal-title":"Am J Vet Res."},{"key":"B51","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/0304-4165(87)90072-9","article-title":"Isolation and characterization of goat C-reactive protein","volume":"924","author":"Maudsley","year":"1987","journal-title":"Biochim Biophys Acta"},{"key":"B52","first-page":"17","article-title":"Immunochemical cross-reactions between pentraxins of different species","volume":"62","author":"Maudsley","year":"1987","journal-title":"Immunology"},{"key":"B53","first-page":"662","article-title":"Identification and isolation of two pentraxins from bovine serum","volume":"67","author":"Maudsley","year":"1987","journal-title":"Clin Exp Immunol."},{"key":"B54","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1111\/j.1432-1033.1993.tb17901.x","article-title":"Molecular characterization of Limulus polyphemus C-reactive protein. II. Asparagine-linked oligosaccharides","volume":"214","author":"Amatayakul-Chantler","year":"1993","journal-title":"Eur J Biochem."},{"key":"B55","first-page":"645","article-title":"Studies of the structure and binding properties of hamster female protein","volume":"80","author":"Tennent","year":"1993","journal-title":"Immunology"},{"key":"B56","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1016\/0009-8981(91)90090-Y","article-title":"Serum amyloid P component in chronic renal failure and dialysis","volume":"200","author":"Nelson","year":"1991","journal-title":"Clin Chim Acta"},{"key":"B57","first-page":"119","article-title":"Comparative clinical study of protein SAP (amyloid P component) and C-reactive protein in serum","volume":"32","author":"Pepys","year":"1978","journal-title":"Clin Exp Immunol."},{"key":"B58","doi-asserted-by":"publisher","first-page":"414","DOI":"10.1111\/imm.12266","article-title":"C-reactive protein is essential for innate resistance to pneumococcal infection","volume":"142","author":"Simons","year":"2014","journal-title":"Immunology"},{"key":"B59","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1016\/0009-8981(81)90005-X","article-title":"Solid phase radioimmunoassays for human C-reactive protein","volume":"117","author":"Shine","year":"1981","journal-title":"Clin Chim Acta"},{"key":"B60","doi-asserted-by":"publisher","first-page":"1805","DOI":"10.1172\/JCI200318921","article-title":"C-reactive protein: a critical update","volume":"111","author":"Pepys","year":"2003","journal-title":"J Clin Invest."},{"key":"B61","doi-asserted-by":"publisher","first-page":"92","DOI":"10.1016\/j.jim.2012.07.013","article-title":"Isolation and characterization of pharmaceutical grade human pentraxins, serum amyloid P component and C-reactive protein, for clinical use","volume":"384","author":"Pepys","year":"2012","journal-title":"J Immunol Methods"},{"key":"B62","doi-asserted-by":"publisher","first-page":"672","DOI":"10.1161\/CIRCRESAHA.114.302770","article-title":"Infusion of pharmaceutical-grade natural human C-reactive protein is not pro-inflammatory in healthy adult human volunteers","volume":"114","author":"Lane","year":"2014","journal-title":"Circ Res."},{"key":"B63","doi-asserted-by":"publisher","first-page":"612","DOI":"10.3181\/00379727-136-35323","article-title":"Specificity of C-reactive protein for choline phosphate residues of pneumococcal C-polysaccharide","volume":"136","author":"Volanakis","year":"1971","journal-title":"Proc Soc Exp Biol Med."},{"key":"B64","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1111\/j.1749-6632.1982.tb22140.x","article-title":"Complement activation by C-reactive protein complexes","volume":"389","author":"Volanakis","year":"1982","journal-title":"Ann NY Acad Sci."},{"key":"B65","doi-asserted-by":"publisher","first-page":"1703","DOI":"10.1084\/jem.154.5.1703","article-title":"C-reactive protein is protective against Streptococcus pneumoniae infection in mice","volume":"154","author":"Mold","year":"1981","journal-title":"J Exp Med."},{"key":"B66","doi-asserted-by":"crossref","first-page":"2374","DOI":"10.4049\/jimmunol.128.5.2374","article-title":"Human C-reactive protein is protective against fatal Streptococcus pneumoniae infection in mice","volume":"128","author":"Yother","year":"1982","journal-title":"J Immunol."},{"key":"B67","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.4049\/jimmunol.155.5.2557","article-title":"Human C-reactive protein is protective against fatal Streptococcus pneumoniae infection in transgenic mice","volume":"155","author":"Szalai","year":"1995","journal-title":"J Immunol."},{"key":"B68","doi-asserted-by":"publisher","first-page":"6046","DOI":"10.4049\/jimmunol.171.11.6046","article-title":"Human C-reactive protein does not protect against acute lipopolysaccharide challenge in mice","volume":"171","author":"Hirschfield","year":"2003","journal-title":"J Immunol."},{"key":"B69","doi-asserted-by":"publisher","first-page":"1369","DOI":"10.1136\/bmj.324.7350.1369","article-title":"Research pointers: association of common genetic variant with susceptibility to invasive pneumococcal disease","volume":"324","author":"Roy","year":"2002","journal-title":"BMJ"},{"key":"B70","doi-asserted-by":"publisher","first-page":"1069","DOI":"10.1080\/00365540600978922","article-title":"Polymorphism of the C-reactive protein gene is associated with mortality in bacteraemia","volume":"38","author":"Eklund","year":"2006","journal-title":"Scand J Infect Dis."},{"key":"B71","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1111\/j.1440-1843.2009.01661.x","article-title":"CRP gene variation and risk of community-acquired pneumonia","volume":"15","author":"Mukamal","year":"2010","journal-title":"Respirology"},{"key":"B72","doi-asserted-by":"publisher","first-page":"254","DOI":"10.1038\/417254a","article-title":"Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis","volume":"417","author":"Pepys","year":"2002","journal-title":"Nature"},{"key":"B73","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1111\/j.1365-2141.2009.08036.x","article-title":"Sustained pharmacological depletion of serum amyloid P component in patients with systemic amyloidosis","volume":"148","author":"Gillmore","year":"2010","journal-title":"Br J Haematol."},{"key":"B74","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1016\/0006-291X(87)91111-9","article-title":"Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum","volume":"148","author":"Pepys","year":"1987","journal-title":"Biochem Biophys Res Commun."},{"key":"B75","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1084\/jem.172.1.13","article-title":"Pentraxin-chromatin interactions: serum amyloid P component specifically displaces H1-type histones and solubilizes native long chromatin","volume":"172","author":"Butler","year":"1990","journal-title":"J Exp Med."},{"key":"B76","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1111\/1523-1747.ep12463283","article-title":"Amyloid P component binds to keratin bodies in human skin and to isolated keratin filament aggregates in vitro","volume":"91","author":"Hintner","year":"1988","journal-title":"J Invest Dermatol."},{"key":"B77","doi-asserted-by":"publisher","first-page":"1433","DOI":"10.1084\/jem.170.4.1433","article-title":"Serum amyloid P component binds to cell nuclei in vitro and to in vivo deposits of extracellular chromatin in systemic lupus erythematosus","volume":"170","author":"Breathnach","year":"1989","journal-title":"J Exp Med."},{"key":"B78","doi-asserted-by":"publisher","first-page":"694","DOI":"10.1038\/9544","article-title":"Serum amyloid P component controls chromatin degradation and prevents antinuclear autoimmunity","volume":"5","author":"Bickerstaff","year":"1999","journal-title":"Nature Med."},{"key":"B79","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1111\/j.1365-2567.2004.01860.x","article-title":"Autoimmunity and glomerulonephritis in mice with targeted deletion of the serum amyloid P component gene: SAP deficiency or strain combination?","volume":"112","author":"Gillmore","year":"2004","journal-title":"Immunology"},{"key":"B80","doi-asserted-by":"publisher","first-page":"2860","DOI":"10.4049\/jimmunol.1003641","article-title":"Human serum amyloid P functions as a negative regulator of the innate and adaptive immune responses to DNA vaccines","volume":"186","author":"Wang","year":"2011","journal-title":"J Immunol."},{"key":"B81","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1038\/gt.2011.67","article-title":"Serum amyloid P component facilitates DNA clearance and inhibits plasmid transfection: implications for human DNA vaccine","volume":"19","author":"Wang","year":"2011","journal-title":"Gene Ther."},{"key":"B82","doi-asserted-by":"publisher","first-page":"e0197299","DOI":"10.1371\/journal.pone.0197299","article-title":"Randomized phase I trial HIV-CORE 003: Depletion of serum amyloid P component and immunogenicity of DNA vaccination against HIV-1","volume":"13","author":"Borthwick","year":"2018","journal-title":"PLoS ONE"},{"key":"B83","doi-asserted-by":"publisher","first-page":"14584","DOI":"10.1073\/pnas.97.26.14584","article-title":"Role of serum amyloid P component in bacterial infection: protection of the host or protection of the pathogen","volume":"97","author":"Noursadeghi","year":"2000","journal-title":"Proc Natl Acad Sci USA."},{"key":"B84","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1042\/bj2250107","article-title":"Human serum amyloid P component, a circulating lectin with specificity for the cyclic 4,6-pyruvate acetal of galactose","volume":"225","author":"Hind","year":"1985","journal-title":"Biochem J."},{"key":"B85","doi-asserted-by":"publisher","first-page":"41576","DOI":"10.1074\/jbc.M107819200","article-title":"Serum amyloid P component is the Shiga toxin 2-neutralizing factor in human blood","volume":"276","author":"Kimura","year":"2001","journal-title":"J Biol Chem."},{"key":"B86","doi-asserted-by":"publisher","first-page":"6075","DOI":"10.1128\/IAI.71.10.6075-6078.2003","article-title":"Serum amyloid P component binding to Shiga toxin 2 requires both a subunit and B pentamer","volume":"71","author":"Marcato","year":"2003","journal-title":"Infect Immun."},{"key":"B87","doi-asserted-by":"publisher","first-page":"1872","DOI":"10.1128\/IAI.01591-14","article-title":"Protection of human podocytes from Shiga toxin 2-induced phosphorylation of mitogen-activated protein kinases and apoptosis by human serum amyloid P component","volume":"82","author":"Dettmar","year":"2014","journal-title":"Infect Immun."},{"key":"B88","doi-asserted-by":"publisher","first-page":"1120","DOI":"10.1086\/501472","article-title":"Human serum amyloid P component protects against Escherichia coli O157:H7 Shiga toxin 2 in vivo: therapeutic implications for hemolytic-uremic syndrome","volume":"193","author":"Armstrong","year":"2006","journal-title":"J Infect Dis."},{"key":"B89","doi-asserted-by":"publisher","first-page":"1753","DOI":"10.1128\/IAI.68.4.1753-1759.2000","article-title":"Serum amyloid P component bound to gram-negative bacteria prevents lipopolysaccharide-mediated classical pathway complement activation","volume":"68","author":"de Haas","year":"2000","journal-title":"Infect Immun."},{"key":"B90","doi-asserted-by":"publisher","first-page":"1162","DOI":"10.1084\/jem.152.5.1162","article-title":"Amyloid P-component is a constituent of normal human glomerular basement membrane","volume":"152","author":"Dyck","year":"1980","journal-title":"J Exp Med."},{"key":"B91","doi-asserted-by":"publisher","first-page":"652","DOI":"10.1038\/293652a0","article-title":"Amyloid P component is located on elastic fibre microfibrils of normal human tissues","volume":"293","author":"Breathnach","year":"1981","journal-title":"Nature"},{"key":"B92","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1038\/nm0897-855","article-title":"Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene","volume":"3","author":"Botto","year":"1997","journal-title":"Nature Med."},{"key":"B93","first-page":"284","article-title":"Binding of serum amyloid P component (SAP) by amyloid fibrils","volume":"38","author":"Pepys","year":"1979","journal-title":"Clin Exp Immunol."},{"key":"B94","first-page":"691","article-title":"Circulating serum amyloid P component is the precursor of amyloid P component in tissue amyloid deposits","volume":"66","author":"Baltz","year":"1986","journal-title":"Clin Exp Immunol."},{"key":"B95","doi-asserted-by":"publisher","first-page":"1303","DOI":"10.1002\/art.1780301115","article-title":"Imaging of experimental amyloidosis with 131I-serum amyloid P component","volume":"30","author":"Caspi","year":"1987","journal-title":"Arthritis Rheum."},{"key":"B96","doi-asserted-by":"publisher","first-page":"903","DOI":"10.1084\/jem.167.3.903","article-title":"Specific localization and imaging of amyloid deposits in vivo using 123I-labeled serum amyloid P component","volume":"167","author":"Hawkins","year":"1988","journal-title":"J Exp Med."},{"key":"B97","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1016\/S0140-6736(88)92235-0","article-title":"Diagnostic radionuclide imaging of amyloid: biological targeting by circulating human serum amyloid P component","volume":"1","author":"Hawkins","year":"1988","journal-title":"Lancet"},{"key":"B98","doi-asserted-by":"publisher","first-page":"508","DOI":"10.1056\/NEJM199008233230803","article-title":"Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component","volume":"323","author":"Hawkins","year":"1990","journal-title":"N Engl J Med."},{"key":"B99","doi-asserted-by":"publisher","first-page":"1862","DOI":"10.1172\/JCI114917","article-title":"Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis","volume":"86","author":"Hawkins","year":"1990","journal-title":"J Clin Invest."},{"key":"B100","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1146\/annurev.med.57.121304.131243","article-title":"Amyloidosis","volume":"57","author":"Pepys","year":"2006","journal-title":"Annu Rev Med."},{"key":"B101","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1084\/jem.159.4.1058","article-title":"Binding specificity of serum amyloid P component for the pyruvate acetal of galactose","volume":"159","author":"Hind","year":"1984","journal-title":"J Exp Med."},{"key":"B102","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/S0140-6736(84)90544-0","article-title":"Specific chemical dissociation of fibrillar and non-fibrillar components of amyloid deposits","volume":"2","author":"Hind","year":"1984","journal-title":"Lancet"},{"key":"B103","doi-asserted-by":"publisher","first-page":"5602","DOI":"10.1073\/pnas.91.12.5602","article-title":"Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure","volume":"91","author":"Pepys","year":"1994","journal-title":"Proc Natl Acad Sci USA."},{"key":"B104","doi-asserted-by":"publisher","first-page":"4299","DOI":"10.1073\/pnas.92.10.4299","article-title":"Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer's disease and systemic amyloidosis","volume":"92","author":"Tennent","year":"1995","journal-title":"Proc Natl Acad Sci USA."},{"key":"B105","article-title":"Pentraxin Therapeutics Limited assignee","author":"Pepys","year":"2000","journal-title":"Screening Assays to Identify Therapeutic Agents for Amyloidosis"},{"key":"B106","doi-asserted-by":"crossref","first-page":"26041","DOI":"10.1074\/jbc.270.44.26041","article-title":"Inhibition of Alzheimer \u03b2-peptide fibril formation by serum amyloid P component","volume":"270","author":"Janciauskiene","year":"1995","journal-title":"J Biol Chem."},{"key":"B107","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1016\/S0014-5793(00)01530-1","article-title":"Molecular chaperone properties of serum amyloid P component","volume":"473","author":"Coker","year":"2000","journal-title":"FEBS Lett."},{"key":"B108","doi-asserted-by":"publisher","first-page":"570","DOI":"10.1006\/jmbi.1997.1075","article-title":"Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP","volume":"269","author":"Hohenester","year":"1997","journal-title":"J Mol Biol."},{"key":"B109","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1006\/bbrc.1995.1819","article-title":"Amyloid P component promotes aggregation of Alzheimer's \u03b2-amyloid peptide","volume":"211","author":"Hamazaki","year":"1995","journal-title":"Biochem Biophys Res Commun."},{"key":"B110","doi-asserted-by":"publisher","first-page":"2311","DOI":"10.1021\/bi052434i","article-title":"A systematic study of the effect of physiological factors on \u03b22-microglobulin amyloid formation at neutral pH","volume":"45","author":"Myers","year":"2006","journal-title":"Biochemistry"},{"key":"B111","doi-asserted-by":"publisher","first-page":"875","DOI":"10.3233\/JAD-2012-120076","article-title":"Serum amyloid P component accelerates the formation and enhances the stability of amyloid fibrils in a physiologically significant under-saturated solution of amyloid- \u03b242","volume":"29","author":"Mold","year":"2012","journal-title":"J Alzheimers Dis."},{"key":"B112","doi-asserted-by":"publisher","first-page":"7619","DOI":"10.1073\/pnas.0902640106","article-title":"Molecular dissection of Alzheimer's disease neuropathology by depletion of serum amyloid P component","volume":"106","author":"Kolstoe","year":"2009","journal-title":"Proc Natl Acad Sci USA."},{"key":"B113","article-title":"Pentraxin Therapeutics Limited assignee","author":"Pepys","year":"2011","journal-title":"Combinations of SAP Depleting Agents and Anti-SAP Antibodies"},{"key":"B114","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1038\/nature09494","article-title":"Antibodies to human serum amyloid P component eliminate visceral amyloid deposits","volume":"468","author":"Bodin","year":"2010","journal-title":"Nature"},{"key":"B115","doi-asserted-by":"publisher","first-page":"1106","DOI":"10.1056\/NEJMoa1504942","article-title":"Therapeutic clearance of amyloid by antibodies to serum amyloid P component","volume":"373","author":"Richards","year":"2015","journal-title":"N Engl J Med."},{"key":"B116","doi-asserted-by":"publisher","first-page":"eaan3128","DOI":"10.1126\/scitranslmed.aan3128","article-title":"Repeat doses of antibody to serum amyloid P component clear amyloid deposits in patients with systemic amyloidosis","volume":"10","author":"Richards","year":"2018","journal-title":"Sci Transl Med."},{"key":"B117","doi-asserted-by":"publisher","first-page":"150202","DOI":"10.1098\/rsob.150202","article-title":"Pharmacological removal of serum amyloid P component from intracerebral plaques and cerebrovascular A\u03b2 amyloid deposits in vivo","volume":"6","author":"Al-Shawi","year":"2016","journal-title":"Open Biol."},{"key":"B118","doi-asserted-by":"publisher","first-page":"124","DOI":"10.1136\/jnnp-2011-301308","article-title":"Sporadic cerebral amyloid angiopathy revisited: recent insights into pathophysiology and clinical spectrum","volume":"83","author":"Charidimou","year":"2012","journal-title":"J Neurol Neurosurg Psychiatry"},{"key":"B119","first-page":"375","article-title":"Serum amyloid P component-induced cell death in primary cultures of rat cerebral cortex","volume":"270","author":"Urb\u00e1nyi","year":"1994","journal-title":"Eur J Pharmacol."},{"key":"B120","doi-asserted-by":"publisher","first-page":"303","DOI":"10.1016\/S0006-8993(98)00966-4","article-title":"The in vitro neuronal toxicity of pentraxins associated with Alzheimer's disease brain lesions","volume":"813","author":"Duong","year":"1998","journal-title":"Brain Res."},{"key":"B121","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/S0006-8993(03)03345-6","article-title":"Serum amyloid P component induces neuronal apoptosis and beta-amyloid immunoreactivity","volume":"988","author":"Urb\u00e1nyi","year":"2003","journal-title":"Brain Res."},{"key":"B122","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/j.brainres.2007.01.132","article-title":"Serum amyloid P component induces TUNEL-positive nuclei in rat brain after intrahippocampal administration","volume":"1145","author":"Urb\u00e1nyi","year":"2007","journal-title":"Brain Res."},{"key":"B123","doi-asserted-by":"publisher","first-page":"696","DOI":"10.1111\/j.1471-4159.2007.05012.x","article-title":"Complement component C1q inhibits b-amyloid- and serum amyloid P-induced neurotoxicity via caspase- and calpain-independent mechanisms","volume":"104","author":"Pisalyaput","year":"2008","journal-title":"J Neurochem."},{"key":"B124","doi-asserted-by":"crossref","first-page":"3869","DOI":"10.4049\/jimmunol.145.11.3869","article-title":"Identification of a polypeptide sequence that mediates nuclear localization of the acute phase protein C-reactive protein","volume":"145","author":"Du Clos","year":"1990","journal-title":"J Immunol."},{"key":"B125","doi-asserted-by":"publisher","first-page":"152","DOI":"10.1111\/j.1365-2249.1994.tb06594.x","article-title":"Binding of pentraxins to different nuclear structures: C-reactive protein binds to small nuclear ribonucleoprotein particles, serum amyloid P component binds to chromatin and nucleoli","volume":"97","author":"Pepys","year":"1994","journal-title":"Clin Exp Immunol."},{"key":"B126","doi-asserted-by":"publisher","first-page":"795","DOI":"10.1007\/s11064-011-0674-0","article-title":"Brain serum amyloid P levels are reduced in individuals that lack dementia while having Alzheimer's disease neuropathology","volume":"37","author":"Crawford","year":"2012","journal-title":"Neurochem Res."},{"key":"B127","first-page":"283","article-title":"Immunological studies in inflammatory bowel disease","volume-title":"Immunology of the Gut, Ciba Foundation Symposium 46 (new series)","author":"Pepys","year":"1977"},{"key":"B128","doi-asserted-by":"publisher","first-page":"351","DOI":"10.1111\/j.1365-2362.1982.tb02244.x","article-title":"Serum levels of C-reactive protein in Crohn's disease and ulcerative colitis","volume":"12","author":"Fagan","year":"1982","journal-title":"Eur J Clin Invest."},{"key":"B129","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1016\/S0016-5085(83)80015-8","article-title":"Quantitative fecal indium III-labeled leukocyte excretion in the assessment of disease in Crohn's disease","volume":"85","author":"Saverymuttu","year":"1983","journal-title":"Gastroenterology"},{"key":"B130","doi-asserted-by":"publisher","first-page":"809","DOI":"10.1136\/gut.27.7.809","article-title":"Differing acute phase responses in Crohn's disease and ulcerative colitis","volume":"27","author":"Saverymuttu","year":"1986","journal-title":"Gut"},{"key":"B131","first-page":"21","author":"WHO","year":"1987","journal-title":"WHO Technical Report Series 760"},{"key":"B132","article-title":"The acute phase response and C-reactive protein","volume-title":"Oxford Textbook of Medicine, 5th Edn","author":"Pepys","year":"2014"},{"key":"B133","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1056\/NEJM199408183310701","article-title":"The prognostic value of C-reactive protein and serum amyloid A protein in severe unstable angina","volume":"331","author":"Liuzzo","year":"1994","journal-title":"N Engl J Med."},{"key":"B134","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1016\/S0140-6736(96)07591-5","article-title":"Production of C-reactive protein and risk of coronary events in stable and unstable angina","volume":"349","author":"Haverkate","year":"1997","journal-title":"Lancet"},{"key":"B135","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1007\/s12170-007-0012-x","article-title":"C-reactive protein and cardiovascular disease: weighing the evidence","volume":"1","author":"Lowe","year":"2007","journal-title":"Curr Cardiovasc Risk Rep."},{"key":"B136","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1111\/j.1365-2796.2008.02015.x","article-title":"C-reactive protein and coronary heart disease: a critical review","volume":"264","author":"Casas","year":"2008","journal-title":"J Int Med."},{"key":"B137","doi-asserted-by":"publisher","first-page":"132","DOI":"10.1016\/S0140-6736(09)61717-7","article-title":"C-reactive protein concentration and risk of coronary heart disease, stroke, and mortality: an individual participant meta-analysis","volume":"375","author":"Emerging","year":"2010","journal-title":"Lancet"},{"key":"B138","doi-asserted-by":"publisher","first-page":"1310","DOI":"10.1056\/NEJMoa1107477","article-title":"C-reactive protein, fibrinogen, and cardiovascular disease prediction","volume":"367","author":"Emerging","year":"2012","journal-title":"N Engl J Med."},{"key":"B139","doi-asserted-by":"publisher","first-page":"d548","DOI":"10.1136\/bmj.d548","article-title":"Association between C reactive protein and coronary heart disease: mendelian randomisation analysis based on individual participant data","volume":"342","author":"C","year":"2011","journal-title":"BMJ"},{"key":"B140","doi-asserted-by":"publisher","first-page":"885","DOI":"10.1084\/jem.133.4.885","article-title":"The phlogistic role of C3 leukotactic fragments in myocardial infarcts of rats","volume":"133","author":"Hill","year":"1971","journal-title":"J Exp Med."},{"key":"B141","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/S0140-6736(81)91565-8","article-title":"C-reactive protein fifty years on","volume":"1","author":"Pepys","year":"1981","journal-title":"Lancet"},{"key":"B142","first-page":"208","article-title":"C-reactive protein, amyloidosis and the acute phase response","volume-title":"Advanced Medicine","author":"Pepys","year":"1982"},{"key":"B143","doi-asserted-by":"publisher","first-page":"1834","DOI":"10.1093\/oxfordjournals.eurheartj.a015180","article-title":"C-reactive protein and complement in myocardial infarction and postinfarction heart failure","volume":"18","author":"Beranek","year":"1997","journal-title":"Eur Heart J."},{"key":"B144","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1016\/S0167-5699(97)01002-5","article-title":"A role for secretory phospholipase A2 and C-reactive protein in the removal of injured cells","volume":"18","author":"Hack","year":"1997","journal-title":"Immunol Today"},{"key":"B145","doi-asserted-by":"publisher","first-page":"563","DOI":"10.1016\/S0002-8703(98)70237-6","article-title":"C-reactive protein in postinfarction heart rupture","volume":"136","author":"Beranek","year":"1998","journal-title":"Am Heart J."},{"key":"B146","doi-asserted-by":"publisher","first-page":"1214","DOI":"10.1097\/01.WCB.0000136517.61642.99","article-title":"Human C-reactive protein increases cerebral infarct size after middle cerebral artery occlusion in adult rats","volume":"24","author":"Gill","year":"2004","journal-title":"J Cereb Blood Flow Metab."},{"key":"B147","doi-asserted-by":"crossref","first-page":"S185","DOI":"10.1016\/j.clim.2007.03.174","article-title":"Human C-reactive protein augments the gut ischemia\/reperfusion injury in mice","volume":"123","author":"Lu","year":"2007","journal-title":"Clin Immunol."},{"key":"B148","doi-asserted-by":"publisher","first-page":"e103","DOI":"10.1016\/j.jss.2009.10.021","article-title":"Decay-accelerating factor attenuates C-reactive protein-potentiated tissue injury after mesenteric ischemia\/reperfusion","volume":"167","author":"Lu","year":"2011","journal-title":"J Surg Res."},{"key":"B149","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1159\/000320763","article-title":"Specific removal of C-reactive protein by apheresis in a porcine cardiac infarction model","volume":"31","author":"Slagman","year":"2011","journal-title":"Blood Purif."},{"key":"B150","doi-asserted-by":"publisher","first-page":"e52","DOI":"10.1038\/mtna.2012.44","article-title":"A selective inhibitor of human C-reactive protein translation is efficacious in vitro and in C-reactive protein transgenic mice and humans","volume":"1","author":"Jones","year":"2012","journal-title":"Mol Ther Nucleic Acids"},{"key":"B151","doi-asserted-by":"publisher","first-page":"F1358","DOI":"10.1152\/ajprenal.00476.2012","article-title":"C-reactive protein exacerbates renal ischemia-reperfusion injury","volume":"304","author":"Pegues","year":"2013","journal-title":"Am J Physiol Renal Physiol."},{"key":"B152","doi-asserted-by":"publisher","first-page":"353614","DOI":"10.1155\/2014\/353614","article-title":"Inhibiting C-reactive protein for the treatment of cardiovascular disease: promising evidence from rodent models","volume":"2014","author":"Szalai","year":"2014","journal-title":"Mediators Inflamm."},{"key":"B153","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1002\/jca.21344","article-title":"Selective apheresis of C-reactive protein: a new therapeutic option in myocardial infarction?","volume":"30","author":"Sheriff","year":"2015","journal-title":"J Clin Apher."},{"key":"B154","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/j.ebiom.2017.07.010","article-title":"C-reactive protein mediating immunopathological lesions: a potential treatment option for severe influenza A diseases","volume":"22","author":"Gao","year":"2017","journal-title":"EBioMedicine"},{"key":"B155","doi-asserted-by":"publisher","first-page":"372432","DOI":"10.1155\/2015\/372432","article-title":"Targeting C-Reactive protein in inflammatory disease by preventing conformational changes","volume":"2015","author":"Thiele","year":"2015","journal-title":"Mediators Inflamm."},{"key":"B156","doi-asserted-by":"publisher","first-page":"616","DOI":"10.1016\/j.amjmed.2006.07.039","article-title":"C-reactive protein and heart failure after myocardial infarction in the community","volume":"120","author":"Bursi","year":"2007","journal-title":"Am J Med."}],"container-title":["Frontiers in Immunology"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/article\/10.3389\/fimmu.2018.02382\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T20:08:28Z","timestamp":1775246908000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/article\/10.3389\/fimmu.2018.02382\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,10,16]]},"references-count":156,"alternative-id":["10.3389\/fimmu.2018.02382"],"URL":"https:\/\/doi.org\/10.3389\/fimmu.2018.02382","relation":{},"ISSN":["1664-3224"],"issn-type":[{"value":"1664-3224","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,10,16]]},"article-number":"2382"}}