{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,5]],"date-time":"2026-06-05T05:49:42Z","timestamp":1780638582765,"version":"3.54.1"},"reference-count":42,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2003,12,1]],"date-time":"2003-12-01T00:00:00Z","timestamp":1070236800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Best Practice & Research Clinical Rheumatology"],"published-print":{"date-parts":[[2003,12]]},"DOI":"10.1016\/j.berh.2003.09.001","type":"journal-article","created":{"date-parts":[[2004,3,4]],"date-time":"2004-03-04T10:24:58Z","timestamp":1078395898000},"page":"909-927","source":"Crossref","is-referenced-by-count":101,"title":["The hereditary amyloidoses"],"prefix":"10.1016","volume":"17","author":[{"given":"Merrill D","family":"Benson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.berh.2003.09.001_BIB1","series-title":"The Metabolic and Molecular Bases of Inherited Disease","first-page":"5345","article-title":"Amyloidosis","volume":"vol IV","author":"Benson","year":"2000"},{"key":"10.1016\/j.berh.2003.09.001_BIB2","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/1040-8428(90)90021-J","article-title":"Systemic amyloidosis","volume":"10","author":"Kyle","year":"1990","journal-title":"Critical Reviews in Oncology Hematology"},{"key":"10.1016\/j.berh.2003.09.001_BIB3","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1084\/jem.138.2.373","article-title":"Immunologic studies of the major non-immunoglobulin protein of amyloid I. Identification and partial characterization of a related serum component","volume":"138","author":"Levin","year":"1973","journal-title":"Journal of Experimental Medicine"},{"key":"10.1016\/j.berh.2003.09.001_BIB4","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1093\/brain\/75.3.408","article-title":"A peculiar form of peripheral neuropathy. Familial atypical generalized amyloidosis with special involvement of the peripheral nerves","volume":"75","author":"Andrade","year":"1952","journal-title":"Brain"},{"key":"10.1016\/j.berh.2003.09.001_BIB5","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1093\/brain\/103.3.473","article-title":"Familial oculoleptomeningeal amyloidosis","volume":"103","author":"Goren","year":"1980","journal-title":"Brain"},{"key":"10.1016\/j.berh.2003.09.001_BIB6","first-page":"331","article-title":"Thyroxine binding proteins","volume":"5","author":"Robbins","year":"1976","journal-title":"Progress in Clinical and Biological Research"},{"key":"10.1016\/j.berh.2003.09.001_BIB7","doi-asserted-by":"crossref","first-page":"2375","DOI":"10.1073\/pnas.90.6.2375","article-title":"Disruption of the transthyretin gene results in mice with depressed levels of plasma retinol and thyroid hormone","volume":"90","author":"Episkopou","year":"1993","journal-title":"Proceedings of the National Academy of Sciences of the USA"},{"key":"10.1016\/j.berh.2003.09.001_BIB8","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.1073\/pnas.87.7.2843","article-title":"Fibril in senile systemic amyloidosis is derived from normal transthyretin","volume":"87","author":"Westermark","year":"1990","journal-title":"Proceedings of the National Academy of Sciences of the USA"},{"key":"10.1016\/j.berh.2003.09.001_BIB9","doi-asserted-by":"crossref","first-page":"44","DOI":"10.3109\/13506129609014354","article-title":"Review\u2014transthyretin amyloidosis","volume":"3","author":"Benson","year":"1996","journal-title":"Amyloid: International Journal of Experimental and Clinical Investigation"},{"key":"10.1016\/j.berh.2003.09.001_BIB10","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0039-6257(95)80025-5","article-title":"Major review\u2014ocular amyloidosis, with special reference to the hereditary forms with vitreous involvement","volume":"40","author":"Sandgren","year":"1995","journal-title":"Survey of Ophthalmology"},{"key":"10.1016\/j.berh.2003.09.001_BIB11","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/j.1399-0004.1992.tb03627.x","article-title":"Homozygosity for the transthyretin\u2014Met30\u2014gene in seven individuals with familial amyloidosis with polyneuropathy detected by restriction enzyme analysis of amplified genomic DNA sequences","volume":"41","author":"Holmgren","year":"1992","journal-title":"Clinical Genetics"},{"key":"10.1016\/j.berh.2003.09.001_BIB12","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1002\/art.1780261211","article-title":"Prealbumin and retinol binding protein serum concentrations in the Indiana type hereditary amyloidosis","volume":"26","author":"Benson","year":"1983","journal-title":"Arthritis and Rheumatism"},{"key":"10.1016\/j.berh.2003.09.001_BIB13","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1007\/s004390050199","article-title":"Revised transthyretin Ile122 allele frequency in African-Americans","volume":"98","author":"Jacobson","year":"1996","journal-title":"Human Genetics"},{"key":"10.1016\/j.berh.2003.09.001_BIB14","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1111\/j.1399-0004.1991.tb03085.x","article-title":"Biochemical effect of liver transplantation in two Swedish patients with familial amyloidotic polyneuropathy (FAP-met30)","volume":"40","author":"Holmgren","year":"1991","journal-title":"Clinical Genetics"},{"key":"10.1016\/j.berh.2003.09.001_BIB15","doi-asserted-by":"crossref","first-page":"12\u2008291","DOI":"10.1073\/pnas.94.23.12291","article-title":"Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation","volume":"94","author":"Borhani","year":"1997","journal-title":"Proceedings of the National Academy of Sciences of the USA"},{"key":"10.1016\/j.berh.2003.09.001_BIB16","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1212\/WNL.19.1.10","article-title":"Inherited predisposition to generalized amyloidoisis","volume":"19","author":"van Allen","year":"1969","journal-title":"Neurology"},{"key":"10.1016\/j.berh.2003.09.001_BIB17","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/0888-7543(90)90288-6","article-title":"A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic polyneuropathy","volume":"8","author":"Nichols","year":"1990","journal-title":"Genomics"},{"key":"10.1016\/j.berh.2003.09.001_BIB18","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1006\/bbrc.1999.0518","article-title":"A novel apolipoprotein A-I variant, Arg173Pro, associated with cardiac and cutaneous amyloidosis","volume":"257","author":"Hamidi","year":"1999","journal-title":"Biochemical and Biophysical Research Communications"},{"key":"10.1016\/j.berh.2003.09.001_BIB19","first-page":"173","article-title":"Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms","volume":"4","author":"Meretoja","year":"1969","journal-title":"Annals of Clinical Research"},{"key":"10.1016\/j.berh.2003.09.001_BIB20","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0014-5793(90)80510-P","article-title":"Finnish hereditary amyloidosis is caused by a single nucleotide substitution in the gelsolin gene","volume":"276","author":"Maury","year":"1990","journal-title":"Federation of European Biochemical Societies Letters"},{"key":"10.1016\/j.berh.2003.09.001_BIB21","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1038\/ng1092-157","article-title":"Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substittution for aspartic acid at residue 187","volume":"2","author":"de la Chapelle","year":"1992","journal-title":"Nature Genetics"},{"key":"10.1016\/j.berh.2003.09.001_BIB22","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/362553a0","article-title":"Human lysozyme gene mutations cause hereditary systemic amyloidosis","volume":"362","author":"Pepys","year":"1993","journal-title":"Nature"},{"key":"10.1016\/j.berh.2003.09.001_BIB23","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1093\/brain\/95.2.387","article-title":"Hereditary cerebral hemorrhage with amyloidosis","volume":"95","author":"Gudmundsson","year":"1972","journal-title":"Brain"},{"key":"10.1016\/j.berh.2003.09.001_BIB24","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/0006-291X(86)90475-4","article-title":"Hereditary cerebral amyloid angiopathy: the amyloid fibrils contain a protein which is a variant of cystatin C, an inhibitor of lysosomal cysteine proteases","volume":"136","author":"Ghiso","year":"1986","journal-title":"Biochemical and Biophysical Research Communications"},{"key":"10.1016\/j.berh.2003.09.001_BIB25","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/ng0393-252","article-title":"Hereditary renal amyloidosis associated with a mutant fibrinogen \u03b1-chain","volume":"3","author":"Benson","year":"1993","journal-title":"Nature Genetics"},{"key":"10.1016\/j.berh.2003.09.001_BIB26","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1172\/JCI117027","article-title":"Hereditary renal amyloidosis with a novel variant fibrinogen","volume":"93","author":"Uemichi","year":"1994","journal-title":"Journal of Clinical Investigation"},{"key":"10.1016\/j.berh.2003.09.001_BIB27","first-page":"4799","article-title":"Renal amyloidosis with a frame shift mutation in fibrinogen A\u03b1-chain producing a novel amyloid protein","volume":"90","author":"Hamidi","year":"1997","journal-title":"Blood"},{"key":"10.1016\/j.berh.2003.09.001_BIB28","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1093\/qjmed\/93.5.269","article-title":"Curative hepatorenal transplantation in systemic amyloidosis caused by the Glu526Val fibrinogen alpha-chain variant in an English family","volume":"93","author":"Gillmore","year":"2000","journal-title":"Quarterly Journal of Medicine"},{"key":"10.1016\/j.berh.2003.09.001_BIB29","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1097\/01.TP.0000046526.10003.EC","article-title":"Orthotopic liver transplantation for hereditary fibrinogen amyloidosis","volume":"75","author":"Zeldenrust","year":"2003","journal-title":"Transplantation"},{"key":"10.1016\/j.berh.2003.09.001_BIB30","first-page":"447","article-title":"Amyloid nephropathy of Ostertag with special reference to renal glomerular giant cells","volume":"72","author":"Weiss","year":"1973","journal-title":"American Journal of Pathology"},{"key":"10.1016\/j.berh.2003.09.001_BIB31","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1006\/geno.2000.6499","article-title":"A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene","volume":"72","author":"Benson","year":"2001","journal-title":"Genomics"},{"key":"10.1016\/j.berh.2003.09.001_BIB32","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1016\/S0021-9258(18)53792-3","article-title":"The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-Met variant to 1.7\u00c5 resolution","volume":"268","author":"Hamilton","year":"1993","journal-title":"Journal of Biological Chemistry"},{"key":"10.1016\/j.berh.2003.09.001_BIB33","doi-asserted-by":"crossref","first-page":"175","DOI":"10.3109\/13506129809003843","article-title":"Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation","volume":"5","author":"Schormann","year":"1998","journal-title":"Amyloid: International Journal of Experimental and Clinical Investigation"},{"key":"10.1016\/j.berh.2003.09.001_BIB34","series-title":"The Nature and Origin of Amyloid Fibrils","first-page":"104","article-title":"Metabolism of amyloid proteins","author":"Benson","year":"1996"},{"key":"10.1016\/j.berh.2003.09.001_BIB35","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/S0022-2275(20)41439-7","article-title":"In vivo metabolism of a mutant apolipoprotein, apoA-IIowa, associated with hypoalphalipoproteinemia and hereditary systemic amyloidosis","volume":"33","author":"Rader","year":"1992","journal-title":"Journal of Lipid Research"},{"key":"10.1016\/j.berh.2003.09.001_BIB36","doi-asserted-by":"crossref","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":"8","author":"Botto","year":"1997","journal-title":"Nature Medicine"},{"key":"10.1016\/j.berh.2003.09.001_BIB37","first-page":"525","article-title":"Serum amyloid P component enhances induction of murine amyloidosis","volume":"5","author":"Togashi","year":"1997","journal-title":"Laboratory Investigation"},{"key":"10.1016\/j.berh.2003.09.001_BIB38","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1515\/CCLM.2002.218","article-title":"Laboratory assessment of transthyretin amyloidosis","volume":"40","author":"Benson","year":"2002","journal-title":"Clinical Chemistry and Laboratory Medicine"},{"key":"10.1016\/j.berh.2003.09.001_BIB39","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1016\/0140-6736(93)93127-M","article-title":"Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis","volume":"341","author":"Holmgren","year":"1993","journal-title":"Lancet"},{"key":"10.1016\/j.berh.2003.09.001_BIB40","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1126\/science.1079589","article-title":"Prevention of transthyretin amyloid disease by changing protein misfolding energetics","volume":"299","author":"Hammarstrom","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.berh.2003.09.001_BIB41","first-page":"2058","article-title":"Amyloidosis and other protein deposition diseases","volume":"vol 2","author":"Benson","year":"2002"},{"key":"10.1016\/j.berh.2003.09.001_BIB42","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bss0680001","article-title":"Review\u2014protein folding and its links with human disease","volume":"68","author":"Dobson","year":"2001","journal-title":"Biochemical Society Symposium"}],"container-title":["Best Practice & Research Clinical Rheumatology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1521694203001098?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1521694203001098?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,15]],"date-time":"2021-06-15T00:37:08Z","timestamp":1623717428000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1521694203001098"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,12]]},"references-count":42,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2003,12]]}},"alternative-id":["S1521694203001098"],"URL":"https:\/\/doi.org\/10.1016\/j.berh.2003.09.001","relation":{},"ISSN":["1521-6942"],"issn-type":[{"value":"1521-6942","type":"print"}],"subject":[],"published":{"date-parts":[[2003,12]]}}}