{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T22:09:33Z","timestamp":1790892573257,"version":"4.1.0"},"reference-count":49,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2002,6,1]],"date-time":"2002-06-01T00:00:00Z","timestamp":1022889600000},"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":[[2002,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Plasma deficiency of \u03b11-antitrypsin is most commonly due to the Z mutation (342Glu \u2192 Lys) and is associated with early-onset panlobular emphysema. The lung disease in these patients is attributed to the relative deficiency of circulating \u03b11-antitrypsin resulting in uncontrolled neutrophil-derived proteolytic activity. We have previously demonstrated that the local deficiency of Z \u03b11-antitrypsin is exacerbated by the formation of polymers within the lung and now show that this polymerization not only inactivates \u03b11-antitrypsin but also converts the molecule to a chemoattractant for human neutrophils. The chemotactic action of polymeric \u03b11-antitrypsin was substantially greater than that seen with other conformers, was of similar magnitude to C5a, and was apparent over a range of physiologically relevant concentrations (EC50 0.0045 \u00b1 0.002 mg\/ml). The biologic activity of polymeric \u03b11-antitrypsin was confirmed by the demonstration that polymers, but not native \u03b11-antitrypsin, induced neutrophil shape change and stimulated myeloperoxidase release and neutrophil adhesion. Polymeric \u03b11-antitrypsin had no effect on basal or N-formyl-Met-Leu-Phe\u2013 stimulated superoxide anion release or constitutive apoptosis. The chemotactic properties of polymeric \u03b11-antitrypsin may provide an explanation for the excessive neutrophils found in the lungs of Z \u03b11-antitrypsin homozygotes and suggests a new paradigm for the pathogenesis of emphysema in these patients.<\/jats:p>","DOI":"10.1165\/ajrcmb.26.6.4739","type":"journal-article","created":{"date-parts":[[2013,4,3]],"date-time":"2013-04-03T21:15:30Z","timestamp":1365023730000},"page":"723-730","source":"Crossref","is-referenced-by-count":126,"title":["Polymers of \u03b11-Antitrypsin Are Chemotactic for Human Neutrophils"],"prefix":"10.1093","volume":"26","author":[{"given":"Jasvir S.","family":"Parmar","sequence":"first","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ravi","family":"Mahadeva","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin J.","family":"Reed","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neda","family":"Farahi","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen A.","family":"Cadwallader","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mary T.","family":"Keogan","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Diana","family":"Bilton","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edwin R.","family":"Chilvers","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David A.","family":"Lomas","sequence":"additional","affiliation":[{"name":"Respiratory Medicine Division, Department of Medicine, University of Cambridge School of Clinical Medicine, Addenbrooke's and Papworth Hospitals, Cambridge, United Kingdom; Cambridge Institute for Medical Research, Cambridge, United Kingdom; Department of Immunology, Beaumont Hospital, Dublin, Republic of Ireland; and Cystic Fibrosis Unit, Papworth Hospital NHS Trust, Papworth Everard, Cambridge, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2002,6,1]]},"reference":[{"key":"2026030623581383900_B1","first-page":"132","article-title":"The electrophoretic \u03b11-globulin pattern of serum in \u03b11-antitrypsin deficiency.","volume":"15","author":"Laurell","year":"1963","journal-title":"Scand. J. Clin. Lab. Invest."},{"key":"2026030623581383900_B2","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1056\/NEJM197606102942404","article-title":"Liver disease in alpha1-antitrypsin deficiency detected by screening of 200,000 infants.","volume":"294","author":"Sveger","year":"1976","journal-title":"N. Engl. J. Med."},{"key":"2026030623581383900_B3","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1056\/NEJM198603203141202","article-title":"Risk of cirrhosis and primary liver cancer in alpha1-antitrypsin deficiency.","volume":"314","author":"Eriksson","year":"1986","journal-title":"N. Engl. J. Med."},{"key":"2026030623581383900_B4","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1183\/09031936.99.13224799","article-title":"Decline in FEV1 related to smoking status in individuals with severe alpha1-antitrypsin deficiency.","volume":"13","author":"Piitulainen","year":"1999","journal-title":"Eur. Respir. J."},{"key":"2026030623581383900_B5","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0014-5793(76)80478-4","article-title":"Amino acid substitution Glu\u2192 Lys in \u03b11-antitrypsin PiZ.","volume":"65","author":"Jeppsson","year":"1976","journal-title":"FEBS Lett."},{"key":"2026030623581383900_B6","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1073\/pnas.73.4.1324","article-title":"Molecular abnormality of human alpha1-antitrypsin variant (Pi-ZZ) associated with plasma activity deficiency.","volume":"73","author":"Yoshida","year":"1976","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2026030623581383900_B7","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/0022-2836(84)90298-5","article-title":"Human \u03b11-proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function.","volume":"177","author":"Loebermann","year":"1984","journal-title":"J. Mol. Biol."},{"key":"2026030623581383900_B8","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nsb0896-676","article-title":"Inhibitory conformation of the reactive loop of \u03b11-antitrypsin.","volume":"3","author":"Elliott","year":"1996","journal-title":"Nat. Struct. Biol."},{"key":"2026030623581383900_B9","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1038\/357605a0","article-title":"The mechanism of Z \u03b11-antitrypsin accumulation in the liver.","volume":"357","author":"Lomas","year":"1992","journal-title":"Nature"},{"key":"2026030623581383900_B10","doi-asserted-by":"crossref","first-page":"9548","DOI":"10.1074\/jbc.274.14.9548","article-title":"A kinetic description of the polymerisation of \u03b11-antitrypsin.","volume":"274","author":"Dafforn","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2026030623581383900_B11","doi-asserted-by":"crossref","first-page":"33663","DOI":"10.1074\/jbc.M004054200","article-title":"Pathogenic alpha 1-antitrypsin polymers are formed by reactive loop-beta-sheet A linkage.","volume":"275","author":"Sivasothy","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2026030623581383900_B12","doi-asserted-by":"crossref","first-page":"15333","DOI":"10.1016\/S0021-9258(18)82258-X","article-title":"\u03b11-antitrypsin Siiyama (Ser53\u2192 Phe); further evidence for intracellular loop-sheet polymerisation.","volume":"268","author":"Lomas","year":"1993","journal-title":"J. Biol. Chem."},{"key":"2026030623581383900_B13","doi-asserted-by":"crossref","first-page":"16864","DOI":"10.1074\/jbc.270.28.16864","article-title":"Alpha1-antitrypsin Mmalton (52Phe deleted) forms loop-sheet polymers in vivo: evidence for the C sheet mechanism of polymerisation.","volume":"270","author":"Lomas","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2026030623581383900_B14","first-page":"934","article-title":"Cirrhosis associated with alpha-1-antitrypsin deficiency: a previously unrecognised inherited disorder.","volume":"73","author":"Sharp","year":"1969","journal-title":"J. Lab. & Clin. Med."},{"key":"2026030623581383900_B15","first-page":"S101","article-title":"Protease-complexed and polymerised antithrombin and \u03b11-antitrypsin bind low density lipoprotein receptor-related protein.","volume":"3(Suppl.)","author":"Wardell","year":"1994","journal-title":"Protein Sci."},{"key":"2026030623581383900_B16","doi-asserted-by":"crossref","first-page":"1608","DOI":"10.1084\/jem.167.5.1608","article-title":"The inhibitory complex of human \u03b11-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant.","volume":"167","author":"Banda","year":"1988","journal-title":"J. Exp. Med."},{"key":"2026030623581383900_B17","doi-asserted-by":"crossref","first-page":"21023","DOI":"10.1016\/S0021-9258(17)45321-X","article-title":"Acute phase protein stimulation by \u03b11-antichymotrypsin-cathepsin G complexes: evidence for the involvement of interleukin-6.","volume":"265","author":"Kurdowska","year":"1990","journal-title":"J. Biol. Chem."},{"key":"2026030623581383900_B18","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1165\/ajrcmb.18.5.3065","article-title":"Lung polymers in Z \u03b11-antitrypsin related emphysema.","volume":"18","author":"Elliott","year":"1998","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"2026030623581383900_B19","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1021\/bi00053a014","article-title":"Effect of the Z mutation on the physical and inhibitory properties of \u03b11-antitrypsin.","volume":"32","author":"Lomas","year":"1993","journal-title":"Biochemistry"},{"key":"2026030623581383900_B20","doi-asserted-by":"crossref","first-page":"5282","DOI":"10.1074\/jbc.270.10.5282","article-title":"Preparation and characterisation of latent \u03b11-antitrypsin.","volume":"270","author":"Lomas","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2026030623581383900_B21","first-page":"101","article-title":"Modulation of multiple neutrophil functions by preparative methods or trace concentrations of bacterial lipopolysaccharide.","volume":"119","author":"Haslett","year":"1985","journal-title":"Am. J. Pathol."},{"key":"2026030623581383900_B22","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/0022-1759(80)90179-9","article-title":"Rapid quantitation of neutrophil chemotaxis: use of a polyvinylpyrrolidone-free polycarbonate membrane in a multiwell assembly.","volume":"37","author":"Harvath","year":"1980","journal-title":"J. Immunol. Methods"},{"key":"2026030623581383900_B23","doi-asserted-by":"crossref","first-page":"1650","DOI":"10.4049\/jimmunol.115.6.1650","article-title":"Chemotaxis under agarose: a new and simple method for measuring chemotaxis and spontaneous migration of human polymorphonuclear leukocytes and monocytes.","volume":"115","author":"Nelson","year":"1975","journal-title":"J. Immunol"},{"key":"2026030623581383900_B24","doi-asserted-by":"crossref","first-page":"4133","DOI":"10.4049\/jimmunol.154.8.4133","article-title":"Lack of effect of recombinant platelet-derived growth factor on human neutrophil function.","volume":"154","author":"Qu","year":"1995","journal-title":"J. Immunol."},{"key":"2026030623581383900_B25","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1084\/jem.164.5.1407","article-title":"Subcellular location and properties of bactericidal factors from human neutrophils.","volume":"164","author":"Gabay","year":"1986","journal-title":"J. Exp. Med."},{"key":"2026030623581383900_B26","doi-asserted-by":"crossref","first-page":"2772","DOI":"10.1182\/blood.V90.7.2772","article-title":"Regulation of neutrophil apoptosis by tumor necrosis factor-\u03b1: requirement for TNFR55 and TNFR75 for induction of apoptosis in vitro.","volume":"90","author":"Murray","year":"1997","journal-title":"Blood"},{"key":"2026030623581383900_B27","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/0022-1759(94)00239-S","article-title":"A non-isotopic, highly sensitive, fluorimetric, cell-cell adhesion microplate assay using calcein AM-labeled lymphocytes.","volume":"13","author":"Braut-Boucher","year":"1995","journal-title":"J. Immunol. Methods."},{"key":"2026030623581383900_B28","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1172\/JCI115934","article-title":"The serpin-enzyme complex (SEC) receptor mediates the neutrophil chemotactic effect of \u03b11-antitrypsin-elastase complexes and amyloid-\u03b2-peptide.","volume":"90","author":"Joslin","year":"1992","journal-title":"J. Clin. Invest."},{"key":"2026030623581383900_B29","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1165\/ajrcmb\/1.6.451","article-title":"Chemotactic response of neutrophils.","volume":"1","author":"Zigmond","year":"1989","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"2026030623581383900_B30","doi-asserted-by":"crossref","first-page":"4330","DOI":"10.1182\/blood.V88.11.4330.bloodjournal88114330","article-title":"Demonstration of reversible priming of human neutrophils using PAF.","volume":"88","author":"Kitchen","year":"1996","journal-title":"Blood"},{"key":"2026030623581383900_B31","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/298329a0","article-title":"Structure and variation of human \u03b11-antitrypsin.","volume":"298","author":"Carrell","year":"1982","journal-title":"Nature"},{"key":"2026030623581383900_B32"},{"key":"2026030623581383900_B33","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1111\/j.0954-6820.1978.tb08452.x","article-title":"Natural history and life expectancy in severe alpha1-antitrypsin deficiency, PiZ.","volume":"204","author":"Larsson","year":"1978","journal-title":"Acta Med. Scand."},{"key":"2026030623581383900_B34","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1172\/JCI4874","article-title":"Heteropolymerisation of S, I and Z \u03b11-antitrypsin and liver cirrhosis.","volume":"103","author":"Mahadeva","year":"1999","journal-title":"J. Clin. Invest."},{"key":"2026030623581383900_B35","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1034\/j.1399-3003.2000.15e12.x","article-title":"Airways inflammation in chronic bronchitis: the effects of smoking and alpha1-antitrypsin deficiency.","volume":"15","author":"Hill","year":"2000","journal-title":"Eur. Respir. J."},{"key":"2026030623581383900_B36","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1172\/JCI115391","article-title":"Neutrophil accumulation in the lung in alpha 1-antitrypsin deficiency: spontaneous release of leukotriene B4 by alveolar macrophages.","volume":"88","author":"Hubbard","year":"1991","journal-title":"J. Clin. Invest."},{"key":"2026030623581383900_B37"},{"key":"2026030623581383900_B38","doi-asserted-by":"crossref","first-page":"3601","DOI":"10.4049\/jimmunol.162.6.3601","article-title":"Soluble Fas ligand is chemotactic for human neutrophilic polymorphonuclear leukocytes.","volume":"162","author":"Ottonello","year":"1999","journal-title":"J. Immunol."},{"key":"2026030623581383900_B39","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1126\/science.181.4094.70","article-title":"\u03b11-antitrypsin deficiency: a variant with no detectable \u03b11-antitrypsin.","volume":"181","author":"Talamo","year":"1973","journal-title":"Science"},{"key":"2026030623581383900_B40","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1056\/NEJM198603203141207","article-title":"Alpha1-antitrypsin deficiency and emphysema caused by homozygous inheritance of non-expressing alpha1-antitrypsin genes.","volume":"314","author":"Garver","year":"1986","journal-title":"N. Engl. J. Med."},{"key":"2026030623581383900_B41","doi-asserted-by":"crossref","first-page":"8250","DOI":"10.1074\/jbc.272.13.8250","article-title":"Biosynthesis of \u03b11-proteinase inhibitor by human lung-derived epithelial cells.","volume":"272","author":"Cichy","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2026030623581383900_B42","doi-asserted-by":"crossref","first-page":"1952","DOI":"10.1172\/JCI112524","article-title":"Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals.","volume":"77","author":"Mornex","year":"1986","journal-title":"J. Clin. Invest."},{"key":"2026030623581383900_B43","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1042\/cs0720373","article-title":"Lung lavage fluid from patients with \u03b11-proteinase inhibitor deficiency or chronic obstructive bronchitis: anti-elastase function and cell profile.","volume":"72","author":"Morrison","year":"1987","journal-title":"Clin. Sci."},{"key":"2026030623581383900_B44","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/S0140-6736(85)91916-6","article-title":"Smoking, lung function, and \u03b11-antitrypsin deficiency.","volume":"i","author":"Janus","year":"1985","journal-title":"Lancet"},{"key":"2026030623581383900_B45","first-page":"149","article-title":"Inflammatory and immune processes in the human lung in health and disease: evaluation by bronchoalveolar lavage.","volume":"97","author":"Hunninghake","year":"1979","journal-title":"Am. J. Pathol."},{"key":"2026030623581383900_B46","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1148\/radiology.199.1.8633137","article-title":"\u03b11-antitrypsin deficiency: evaluation of bronchiectasis with CT.","volume":"199","author":"King","year":"1996","journal-title":"Radiology"},{"key":"2026030623581383900_B47","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1093\/oxfordjournals.ndt.a027308","article-title":"C-antineutrophil cytoplasmic antibody positivity in vasculitis patients is associated with the Z allele of alpha-1-antitrypsin, and P-antineutrophil cytoplasmic antibody positivity with the S allele.","volume":"11","author":"Griffith","year":"1996","journal-title":"Nephrol. Dial. Transplant."},{"key":"2026030623581383900_B48","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1007\/BF00509091","article-title":"Relationship between Weber-Christian panniculitis and the ZZ phenotype of alpha1-antitrypsin.","volume":"277","author":"Bleumink","year":"1985","journal-title":"Arch. Dermatol. Res."},{"key":"2026030623581383900_B49","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1164\/ajrccm.156.1.9508014","article-title":"Atopy, asthma, and emphysema in patients with severe \u03b11-antitrypsin deficiency.","volume":"156","author":"Eden","year":"1997","journal-title":"Am. J. Respir. Crit. Care Med."}],"container-title":["American Journal of Respiratory Cell and Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/ajrcmb\/article-pdf\/26\/6\/723\/67172906\/ajrcmb_26_6_723.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/ajrcmb\/article-pdf\/26\/6\/723\/67172906\/ajrcmb_26_6_723.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,7]],"date-time":"2026-03-07T05:10:40Z","timestamp":1772860240000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/ajrcmb\/article\/26\/6\/723\/8501838"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,6,1]]},"references-count":49,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2002,6,1]]},"published-print":{"date-parts":[[2002,6,1]]}},"URL":"https:\/\/doi.org\/10.1165\/ajrcmb.26.6.4739","relation":{},"ISSN":["1535-4989","1044-1549"],"issn-type":[{"value":"1535-4989","type":"electronic"},{"value":"1044-1549","type":"print"}],"subject":[],"published-other":{"date-parts":[[2002,6]]},"published":{"date-parts":[[2002,6,1]]}}}